wanglab/gogpt-training-data huggingface dataset:
Protein: Histone acetyltransferase type B subunit 2 (Kinetochore protein mis16) (O94244)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of the histone acetylase B (HAT-B) complex (By similarity). The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing (By similarity). Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A. Maintains the deacetylated state of histones specifically in the central core of the centromeres.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15369671}. Nucleus {ECO:0000269|PubMed:15369671}. Chromosome, centromere {ECO:0000269|PubMed:15369671}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15369671}.
Interaction partners:
- Histone H4
- Histone acetyltransferase type B catalytic subunit
- CENP-A recruiting complex protein mis19
- CENP-A recruiting complex protein mis20
- CENP-A histone chaperone scm3
- NASP-related protein sim3
- Kinetochore protein mis18
- Histone H3-like centromeric protein cnp1
- Histone H3.1/H3.2
- Inner kinetochore subunit mis6
Sequence:
MSEEVVQDAPLENNELNAEIDLQKTIQEEYKLWKQNVPFLYDLVITHALEWPSLTIQWLPDKKTIPGTDYSIQRLILGTHTSGNDQNYLQIASVQLPNFDEDTTEFTPSTIRRAQATGSYTIEISQKIPHDGDVNRARYMPQKPEIIATMGEGGNAYIFDTTCHDALTTGEALPQAVLKGHTAEGFGLCWNPNLPGNLATGAEDQVICLWDVQTQSFTSSETKVISPIAKYHRHTDIVNDVQFHPQHEALLASVSDDCTLQIHDTRLNPEEEAPKVIQAHSKAINAVAINPFNDYLLATASADKTVALWDLRNPYQRLHTLEGHEDEVYGLEWSPHDEPILASSSTDRRVCIWDLEKIGEEQTPEDAEDGSPELLFMHGGHTNRISEFSWCPNERWVVGSLADDNILQIWSPSRVIWGRDHVQVSPRDLE
Protein: Protein sfi1 (Suppressor of fermentation induced loss of stress resistance protein 1) (O13652)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the spindle pole body (SPB) half-bridge involved in the initial steps of SPB duplication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:10620777, ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:10620777, ECO:0000269|PubMed:16823372}. Note=Spindle pole, half bridge. {ECO:0000250|UniProtKB:Q12369}.
Interaction partners:
- Cell division control protein 31
- Tubulin alpha-2 chain
- Spindle pole body protein pcp1
- Spindle pole body protein ppc89
- Spindle pole body-associated protein sad1
- Nuclear envelope protein ndc1
- Septation initiation protein sid4
Sequence:
MSKNGAPKYVDGGRKIMDEDLRRDLEILRLILLRLSHAADDTSPLDVFNAYESVLRENGLNPARHRSYIRILYRLISSKKLSWNDEWRNLMRRIGFSQVSSDLNTPLFPLNNTDMENDPFIVNGDDYRSRSNQQKSSQFASEVAQTIKSQTAMFRRADQYRSQKDKILLANSLDFMLEKYRYYKKIDAVYLRKADAVYRAFIMLKYFPRWVQKLRNIQSRIYSAGEAYRLILIGQMVNRWRQKTRERLHQKLRFQKNAFLLDVLLKWSALTVNWNRKHEYMLKRRVFTNWMSKRRRNESLIQKANVFFQHSVLAHSFKTWKANLSIKNAATLYEKKVVFMSFNRWHANYESHVLDLQKAELFSQKAYYSIALHKWKLRIEELSDLMNKADDLYEVNLLQRMLVLWRRKATTYEKIDFWMDGHDVDIVKSAFFKWKNKFIKVDRNFELADTILQNTFLTKWRLAVRVKVVQEKRNKDRLIVTFRFWYYLMKAKSFQHKRDHRLLTIAWEAWKDNYQRRIKLQKEAQELQLTRIQKIAKQYLIKWRISLLDIKELSIRAEKLHTTNEIIGVWNQWVVSYNRKVGMQQNADLFFKRKTLRVVFEHWRYLRETNMLLRLENKVVDFREVQSEKLVLRCWNAWVARLLSVSQMLDTAELSTQKVVVRAYEAWSFRYNHQKEIMSQADQFYNERLMRSAMVFWRYQLRAIKFYFNISDWKRREFNRQTLRNAFDAWHLLMFRVTSLVMQADRFHEQKKNKLLGKYFRKWLQRMQLNQEESSLLEAEATIEGNRTSRYMHTFDTTLPMQNDEFTDESVNFENRWKQELKTPISRFSKFLRPIPPNTR
Protein: Palmitoyl-protein thioesterase 1 (PPT-1) (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1) (Q9W3C7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cleaves thioester-linked long fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides.
Subcellular location: Lysosome {ECO:0000269|PubMed:18719403}.
Interaction partners:
- Battenin
- Long-chain-fatty-acid--CoA ligase
- Lysosomal thioesterase PPT2 homolog
- long-chain-fatty-acid--CoA ligase
- Very long-chain-fatty-acid--CoA ligase bubblegum
- Long-chain-fatty-acid--CoA ligase heimdall
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Choline transporter-like 2
- palmitoyl-protein hydrolase
- Uncharacterized protein, isoform A
Sequence:
MISICCSRFSCILFLLFLIFSLVLSYIWWSPTKGGTNPEVLPVVLWHGMGDTCCVPFSLGAIMNLIVEQTKGGYVRSLQIGGNVLIDWQSGFFIHPNEQVDYVCKQLLQDEHLAKGYHAIGFSQGGQFLRAVAERCPNPPMRNLITLGGQHQGIFGLPMCPTLTEKPCDYITRLLDNAAYAPEVQKALVQATYWHDPIMENKYRLGSTFLADINNELFINKFYIENLQKLKKFVMVQFLNDTIVQPKESQWFQYYTTGQNKVIQPFTESKVYQDLGLDKMHRQGQLVFLGVEGDHLAISKAWFIQNIVPLLLEK
Protein: Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) (Q9HV43)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Acts as a chaperone.
Interaction partners:
- Protein GrpE
- Chaperonin GroEL
- Chaperone protein DnaJ
- Chaperone protein HtpG
- Co-chaperonin GroES
- Chaperone protein ClpB
- ATP-dependent protease ATPase subunit HslU
- ATP-dependent protease subunit HslV
- Lon protease
- RNA polymerase sigma factor RpoH
Sequence:
MGKIIGIDLGTTNSCVAILENGNVKVIENAEGARTTPSIIAYTNDGETLVGQPAKRQAVTNPQNTLYAVKRLIGRRFEENVVQKDIQMVPYSIVKADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDSQRQATKDAGRIAGLDVKRIINEPTAAALAYGLDKAKGDHTVIVYDLGGGTFDVSVIEIAEVDGEHQFEVLATNGDTFLGGEDFDIRLIDYLVDEFKKESGINLKGDPLAMQRLKEAAEKAKIELSSTQQTDVNLPYVTADASGPKHLNVKVSRAKLESLVEDLVQRTIEPCRTALKDAGLDVSDIHEVILVGGQTRMPLVQKTVAEFFGKEARKDVNPDEAVAVGAAIQGAVLAGDVKDVLLLDVTPLTLGIETLGGVMTGLIEKNTTIPTKKSQVFSTADDNQGAVTIHVLQGERKQAAQNKSLGKFDLADIPPAPRGVPQIEVTFDIDANGILHVSAKDKATGKQQSIVIKASSGLSEDEIQQMVRDAEANAEEDRKFEELAAARNQGDALVHATRKMITEAGDKATAEDKATIEKALGELEAAVKGDDKAEIEAKMNALSQASTPLAQKMYAEQAQQGEDAPQGEQAKAADDVVDAEFEEVKDNK
Protein: V-type proton ATPase subunit E 1 (V-ATPase subunit E 1) (V-ATPase 31 kDa subunit) (P31) (Vacuolar proton pump subunit E 1) (P11019)
Organism: Bos taurus (Bovine)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P36543}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6PCU2}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit H
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMNQARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCRKQDFPLVKAAVQKAIPVYKVATKRDVDVQIDQEAYLPEEIAGGVEIYNGDRKIKVSNTLESRLDLIAQQMMPEVRGALFGANANRKFLD
Protein: Protein SOP4 (Suppressor of PMA1-7 protein 4) (P39543)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12230471, ECO:0000269|PubMed:14562095}; Single-pass type I membrane protein {ECO:0000269|PubMed:12230471, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Endoplasmic reticulum membrane protein complex subunit 10
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 5
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 4
- Purine-cytosine permease FCY2
- Oligomycin resistance ATP-dependent permease YOR1
Sequence:
MFSQIVLLLSAFIYVASATARRGTIKGRLDLAASNITGFVSTRTSFKLYQIGNFSTEYPYTSTTMFQDDEGNFEFANLPLNDGVNETTYYVMYPASMDFNLKPNRILIEFKNLENGTLQLNAFKNFFGREYFPSKDITYPEKLQSMKVHPYITVELLHKAPIRSYLQARNVSIFSTGIVGNILNSRWKLAGVITLIALVVFPIIVEKLDPETARAIREEAKRKQREKYAAVASK
Protein: Collagen alpha-1(XXVIII) chain (Q2UY11)
Organism: Mus musculus (Mouse)
Function: May act as a cell-binding protein.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:16330543}.
Interaction partners:
Sequence:
MRRRDVAFCLLLLPAFMTQAVYGQRKKGPKPNTLARKNDFQDAICFIDVVFILDSSESSKIVLFDNQKDFVDSLSEKIFQLTPGRSLKYDIKLAALQFSSSVQIDPPLSSWKDLRTFKQRVKSLNLIGQGTFSYYAISNATRLLKREGRKDGVKVALLMTDGIDHPKSPDVQSISEDARILGISFITVGLSTVVNEAKLRLISGDPSNEPVLLLSDPTLVDRIQERLGVLFERKCEHKICECEKGEPGDPGPPGTHGNPGIKGERGPKGNPGDAQKGETGERGPVGIPGYKGDKGERGECGKPGMKGDKGPEGPYGPKGPRGIQGIGGPPGDPGPKGFQGNKGEPGPPGPYGPPGAPGIGQQGVKGERGQEGRMGAPGPIGIGEPGQPGPRGPEGAPGERGLPGEGFPGPKGEKGSEGPIGPQGLQGLSIKGDKGDLGPVGPQGPAGIPGIGSQGEQGIQGPSGPPGPQGPPGQGSPGPKGEVGQMGPTGPRGPMGIGVQGPKGEPGTVGLPGQPGVPGEDGASGKKGEAGLPGTRGPEGMPGKGQPGPKGDEGKKGSKGNQGQRGFPGPEGPKGEPGVMGPFGMPGASIPGPSGPKGDRGGPGMPGLKGEPGLPVRGPKGAQGPRGPVGAPGLKGDGYPGVAGPRGLPGPPGPMGLRGVGDTGAKGEPGVRGPPGPSGPRGIGTQGPKGDTGQKGLPGPPGPPGYGSQGIKGEQGPQGFPGSKGTVGLGLPGQKGEHGDRGDVGRKGEKGETGEPGSPGKQGLQGPKGDLGLTKEEIIKLIIEICGCGPKCKETPLELVFVIDSSESVGPENFQIIQSFVKTLADRVALDLGTARIGIINYSHKVEKVASLKQFSSKDDFKLVVDNMQYLGEGTYTATALQAANDMFKEARPGVKKVALVITDGQTDSRDKKKLADVVKDANDSNVEIFVIGVVKKDDPNFEIFHKEMNLIATDAEHVYQFDDFFTLQDTLKQKLSKKICEDFDSYLIQVFGSPSFQPEFGVSEREVSVSTPKPAKEMSKSFNVSRGQNEETESYVLTEAGILAIPTPPEATNTLEPLLSSREGVETRTPNPNLLQSEKSLYKDPRCEEALKPGECGDYVVRWYYDKQVNSCARFWFSGCNGSGNRFHSEKECRETCIKQ
Protein: Mitochondrial carrier protein, putative (Q382J3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
Sequence:
MIDWALTFLPGAAQGMTTVVLGQPLDSAKTRAQACGPLAARSAWKTMLDVAREEGVRSLYRGTGPPLIMSATKRSLQYALWDSIRAERSCNKPPRATHSTPMASHPFRSLHVNELLRSVASWLGESPFRSGACAGAAGTFIGCPFHVIKLRTQYSTRRSTRNAWVCAANIFRSEGIKGYFHGFGYHLLKDTCFAGCYLGFYDVNRRWLRAWCTSSTGTESPGIEERLPTEWTFVAGCTASMVTWALLYPLDTVKTIVQARCVGTLAVVELLRRESPLVIYRGLGVSLLRAGPISGVSMVVYEYVKSRTDRWQKEWR
Protein: Chalcone--flavanone isomerase 1 (Chalcone isomerase 1) (EC 5.5.1.6) (Protein TRANSPARENT TESTA 5) (P41088)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the intramolecular cyclization of bicyclic chalcones into tricyclic (S)-flavanones. Responsible for the isomerization of 4,2',4',6'-tetrahydroxychalcone (also termed chalcone) into naringenin.
Interaction partners:
- Chalcone synthase
- Naringenin,2-oxoglutarate 3-dioxygenase
- Flavonoid 3'-monooxygenase
- Dihydroflavonol 4-reductase
- Probable chalcone--flavanone isomerase 3
- Flavonol synthase/flavanone 3-hydroxylase
- Leucoanthocyanidin dioxygenase
- Flavonol 3-O-glucosyltransferase
- Glutathione S-transferase F12
- Transcription factor MYB75
Sequence:
MSSSNACASPSPFPAVTKLHVDSVTFVPSVKSPASSNPLFLGGAGVRGLDIQGKFVIFTVIGVYLEGNAVPSLSVKWKGKTTEELTESIPFFREIVTGAFEKFIKVTMKLPLTGQQYSEKVTENCVAIWKQLGLYTDCEAKAVEKFLEIFKEETFPPGSSILFALSPTGSLTVAFSKDDSIPETGIAVIENKLLAEAVLESIIGKNGVSPGTRLSVAERLSQLMMKNKDEKEVSDHSVEEKLAKEN
Protein: Protein kinase, putative (EC 2.7.1.-) (Q384V1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Elongation initiation factor 2 alpha subunit, putative
Sequence:
MHVDEGKFEGCLSFDLISEGQTEVTNVVPDEIEFLRANYDDIHIVEREGFHPVVLLTIDSSTQPTRRVVLEVSIVGGYPFVAPRVRILFPHQAAVGLDGVLSEAEIGQLQTDIRDAISPCLLAGAPCIMQIISVVQRVISTEDSHPQTQATVEIENAKAPAGAEESVLKRDVVKLSVLALHLLNKCCHLKDPESKEEANSNFQLLVNYLLNDARLIPKGLQKCVTWKYEYVKRIFSDAIQVCIDGSDPLMKWMWSHEEGTCTFRRVSAGRYRSEFIEQCLLGSGGFAPVYVCRKKVDGRLYAVKKIAIRKNEAEKALREVQSLAALSHKHIVRYYDAWIEPGCDDELLDYVLDGDEEVEDDCVDGDGSTTHSYDSNRRSTIGGSIRVGGASDYGEGGGETTNTTCYSCSSSAEDDDGEESNLLYDLQSPMHSHKEEEFSTLYIQMELCSKHSLRHLIDQCDKEEGSLLTAGNGDKVATKIFRQLLTVVSHFHRQGIVHRDLKPDNILFEMQSSVSSDDVGTIRVADFGLARTLHRSMKHSPSNVELNDVRPLDELEVGPSPTGNLGSVVYCAPEQERGESYDFSVDEYSLGMIALEMWLAVAGQGFRERFNIMTDISRGKPIPQWFYAWNPRMAEVIASLLERDPGKRRTSEEILNKADLPGDPADVVEALETIKRHGERFSGRVLHCVKQASVKQHCKPPPQVKDAVKALTHTVTLDLIQAVNIIGMLHGAMPLASVDPLVPLNTLLSEQDVSCLIDMNSNVWAFPNQPQLATAYHLTLLTNHHIGSFYHFHYRSRPYAVFTTPSSAPGIVDEMFLDPLLSFFHLLSVAELKSKLEIIVSHADWLAATHSRTVGSVESLDHLGDLCESIEPGKSIGPILDKVDSTLSDGNHIVSSHDRLEALKTFTLRITEALQLFGKQVASNVRVCIDPRLKPAETSVDRSFIDYGVFFECRTHERGHAIAFCCGVENFTSKCGARNADVQAVCLSVDLFALGEVCEHVRFPQTDGLLLSGVAVRPQDVYSPGQKYSALTVSANLWLDNIRACFRIDQDVRGFRKAMKARGIQTLFQVGSQSASISLFHETKMNIQSVDITSREVCRVVRRHCSFERADDPVLYLKDSEKRVRAEEVKKLFAVIKRSLFHILVVDAEAKKVAECVRLYSGEVPFPAADGERSTTPELVEWLKNSMSTYGVLPIFSVPDKTVTFAVDQKLLRTASNVEQKQYKAANRGDNVRRKK
Protein: Uncharacterized protein (Q559F5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- WD repeat domain phosphoinositide-interacting protein 3
Sequence:
MYQNALNHTNSGYGGMKAEEKTNYLNQSVITGYIKGISSYIPSSIKSSIKKQIMNSPVTFEEKDTIVGTYFDECFIQGEKHKILINCYNNGFQVWDLNHTDGVKELLSCRDGLTKFCKVLTNPLEPDNESSSFYGKRPLLAVVSGEDNPKVTKNMVRIFSLQTTELISMYKFKSPIYNVLSNQQIILVVLKERIVGFNANDMSKIKGLSLPCYPSVTSLGVIALGSRWIAYTDYESSYSFIGGHHHSSHYFGGGSSNGSGSSGGGGGGIGYSQNRNPSVPQNQTFSDTAVDVASDIAKEVAQKLYYFGDIGRKKVSSYLYPENHEQSILGTSPNSTSSLAMGNAPQLGGGGSGGMNDKPDAASVIVVFDFVKQRIVSLIKPPHTHPISYLAFDPTGTLLFTSTTEGTKVNTYQIIPFTNSLTISSPLSTSVNSNNNNNNNNINNSNNSGIIINNSLSLNSNNNNNNNTNNNTNNSNNTTNNNSIIVSGNSNNNTNNNTNNNIINNNGGNNSNGIIISSNNNNNNNSSMNFEQSYRHIYILKRGITNASIQGITTSENSKWVALTTSRGTTHIFAINPLGGEVDIHSHITRSPNSKRPIDYYSSVNNLTPSLLTINAMDRIKLGNDNDEASSSTLGSVVQGCLMSGGNACFIESNQPNLENLFVCSPTGQLILYELRPLRPPISSEMAENTLCLSITPVAEWDVCRKTRSPEYKSQFIPYSLTEINKQQLQHHMSKDQEARWLYNVEITTHSQEIRAIWGVPQFTFRSSNSVSPAVSSNSMEGGSEINFFDQDYPVGEVIKFEKRKNISPRIQDGYGSGGFSTSPSNGIGMDGEYKSGSSFDNPGSYFVNIKDEDDIEIIEKLNDAMKTPISKSTIPIPINNNNSGNSFGSNNNSSNNNSFNNNNNNNNNNNNSNSGSFGNRVGQPITINNGNGFNSNNNNNNKNFNTNNGFNNNNFNNSPETGGFLMKKGIEDFGSPNHQQPPHQQQQQQFFKNSNKNLEKDLIPNPMVTRESGLKHFDDEDEEDDDGGIDKFTGLGDEDDFPAYPHLGNNDNNNNNNKFPISSTNGIPIPLVSSNNHNNNNNGLGSNNPRPISSTPAPIPVLPNTSSSSLPTLKSSSNSNPPIINNDGDSLPPPPVTPTTTTTTTTTTSPSASIPIPIAKKSPKEKNLEDNLSSSYSSSSSTQSATSPTSPKPNLSSPPKGSSKKSRK
Protein: Master replication protein (M-Rep) (EC 2.7.7.-) (EC 3.1.21.-) (EC 3.6.1.-) (ATP-dependent helicase C2) (Replication-associated protein 2) (Rep2) (O39828)
Organism: Faba bean necrotic yellows virus (isolate Syrian SV292-88) (FBNYV)
Function: Essential for the replication of all genomic viral ssDNA (trans-replication). The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-A[GT]TATTAC-3' in the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities.
Subcellular location: Host nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MARQVICWCFTLNNPLSPLSLHDSMKYLVYQTEQGEAGNIHFQGYIEMKKRTSLAGMKKLIPGAHFEKRRGTQGEARAYSMKEDTRLEGPWEYGEFVPTIEDKLREVMNDMKITGKRPIEYIEECCNTYDKSASTLREFRGELKKKKAISSWELQRKPWMGEVDALLQERDGRRIIWVYGPQGGEGKTSYAKHLVKTRDAFYSTGGKTADIAFAWDHQELVLFDFPRSFEEYVNYGVIEQLKNGIIQSGKYQSVIKYSDYVEVIVFANFTPRSGMFSEDRIVYVYA
Protein: Alpha-ketoglutaric semialdehyde dehydrogenase 1 (alphaKGSA dehydrogenase 1) (EC 1.2.1.26) (2,5-dioxovalerate dehydrogenase 1) (2-oxoglutarate semialdehyde dehydrogenase 1) (KGSADH-I) (Succinate-semialdehyde dehydrogenase [NAD(+)]) (SSDH) (EC 1.2.1.24) (Q1JUP4)
Organism: Azospirillum brasilense
Function: Catalyzes the NAD(P)(+)-dependent oxidation of alpha-ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Prefers NAD(+) to NADP(+) as a cosubstrate. Displays broad substrate specificity: exhibits the highest activity with alphaKGSA and succinic semialdehyde as substrates, but to a lesser extent, is also active with glutaraldehyde, benzaldehyde, and a number of aldehydes from C3 to C8.
Interaction partners:
Sequence:
MANVTYTDTQLLIDGEWVDAASGKTIDVVNPATGKPIGRVAHAGIADLDRALAAAQSGFEAWRKVPAHERAATMRKAAALVRERADAIAQLMTQEQGKPLTEARVEVLSAADIIEWFADEGRRVYGRIVPPRNLGAQQTVVKEPVGPVAAFTPWNFPVNQVVRKLSAALATGCSFLVKAPEETPASPAALLRAFVDAGVPAGVIGLVYGDPAEISSYLIPHPVIRKVTFTGSTPVGKQLASLAGLHMKRATMELGGHAPVIVAEDADVALAVKAAGGAKFRNAGQVCISPTRFLVHNSIRDEFTRALVKHAEGLKVGNGLEEGTTLGALANPRRLTAMASVIDNARKVGASIETGGERIGSEGNFFAPTVIANVPLDADVFNNEPFGPVAAIRGFDKLEEAIAEANRLPFGLAGYAFTRSFANVHLLTQRLEVGMLWINQPATPWPEMPFGGVKDSGYGSEGGPEALEPYLVTKSVTVMAV
Protein: Mannitol dehydrogenase (Q5AVU0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MPQQVPTASHLSDLFSLKGKVVVITGASGPRGMGIEAARGCAEMGANVAITYASRPEGGEKNAAELARDYGVKAKAYKCDVGDFKSVEKLVQDVIAEFGQIDAFIANAGRTASAGVLDGSVKDWEEVVQTDLNGTFHCAKAVGPHFKQRGKGSLVITASMSGHIANYPQEQTSYNVAKAGCIHMARSLANEWRDFARVNSISPGYIDTGLSDFVDKKTQDLWLSMIPMGRHGDAKELKGAYVYLVSDASTYTTGADLVIDGGYTCR
Protein: SAM domain-containing protein (Q57ZJ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein kinase, putative
- Serine/threonine protein phosphatase, putative
Sequence:
MPSATGNGWFTALCAAAAAVAVPSSVYLFLSRQEGRRQGRKPHTAASTPVEEWCAEEVLDWLNSLGVSPPTMKNFEENNVDGSVLFLLGETDLPALAPKVGDAVRIREGLRKLRSAHPSQRPVHQASQQVAPQKAEDILPTGDDAENRFINIVQEVDEIRALLESQDFRNARPEWQTGVRQACARRLAALCQEKEQLPAALQAKVAPLISGLQATFTCSPNQGEGATLPAPSPALEKQLKSLHDMVDDFVRVLDGTTADVESAPVMQELQNQVGVQISRVAAVARRLPAEYGEPLLNKCEAVIQRLQRRGSQSAAATADGTHGGVPTLGGVRRGLRPANFDLVLNQLRSLFTELKSSVLGEPDARRRLDKLMSIKTTLGGILQEAATWDDSEATAIINSVANRVSSVFEQMEALTREELSSHGGGGTGAPHNEGEADNVDGYRGERGDDIPVTHVVANLQAIIQVLHSDELMDAPVEVQQQTIGKLGRKLRGLHQRMERAPRDETNLQIMTMIETAQGLIGSVADGSDDGDETPDETSSNQRWSQRASMGRGSGELGPASGGAARSPGSTTNGLATSEEADLADEAVVLLEKVFEYINSGAFDALPPDEQGEAARQNLNQLQLIEQKCRACGGQQQLMGIIAHIKGILQQRARQGSNGETRSQLFLASSACVEEIQSLLDSSAFKSADAGKRKSFALCLLPQLQNVMSSLPHMEPTEAEMMHVLIAPISEALEAASTAPDSTRDVSVSASVNPLELISRMEEIRNVLESEEFRNASARQRRLIVSRLVVSIGEIREQCLSLGEIATPLLPIVQEMHTQLQNVAAYTGDEAHEESGAGGASTPAVSRVANADDGSGDDDNEESADAVPSAEEGNLNAMLSERLKLFRSVADIADRLRRSNMEKFTVSMEELEPLQGLLAMVYSVGISSNEERSLRDEFEAQLGEAMNRANAAVSTSNDVEDVRALPATLLKGTPPARVGADERVREALRSTRERANLNQGSPRHGQVQDADVVARMSYLQDMLDEATCRIHENPPQNEEELRPYLSLLREAGEEGDRLPINLLLGFKELENSVVDAAQSIPASGGPRGAREPGMQAQEDTSNGDFAEGDAEESVTLLLLDISNRLREGSVSDERLDELSAMLDCLDGRGFTESFRHAVESVRQQLELQRVVNRNNAEESSLEDEEDDNGNTSEVAGDISRDSELDTSNKGCQRAAASAASTLSKIEDVSEVAESSENSASPTSAQGPDGGCTAALSDRALKQTKPKKHSKGKLTSCLEKLQKNVVPGGKKAELTLLPRLEERLLKEEQHFIENTTLADIQNISKLILHLQANNDVKRNSGLKSQVNRLKEKFARQLVAFKGSDQQAAAVRSKLRLQCHDGDAFGRSVRNLVICTGTEAEAPGNEMRSDELLRSLTEGKAAKAEVPSDVVKEWAGRSVALIFCEANSNEGTVLCELLMLQEVLVNRYGFDVYLVNYGDPSKAGDLLQEVAALDVKRLFLYFVTGDHDPLTPHAITFRNGSTLPYQDVINTVDNIDRVVLAHCQPLRLNVVSTLVGCDAEVKDNSLLSVVITEDAAVEIRPVRCWLYDGLLTPAVTELLSLDEERVLCPEDLVMYVVTALSSHIIDFGSFMEREPLGMGFFSPIE
Protein: ATP synthase protein MI25 (Q2F937)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004304}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004304}.
Interaction partners:
Sequence:
MGLSSTDKKDRRNMLFAAIPSICASSPKKISIYNEEMIVARCFIGFLIFSRKSLGKTFKETLDGRIESIQEELQQFFNPNEVIPGESNEQQRLLRISLRICSAVVESLPTARCAPKCEKTVQALLCRNLNVKSATLLNATSSRRIRLQDDIVTGFHFSVSERFVSGSTFKASTVEQIREAFVPIDLIREGLIVLRKV
Protein: Fibrillarin (M0R1H0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKPGFSPRGGGFGGRGGFGDRGGRGGFRGRGRGGGGGGGGGGGGGRGGGGFHSGGNRGRGRGGKRGNQSGKNVMVEPHRHEGVFICRGKEDALVTKNLVPGESVYGEKRVSISEGDDKIEYRAWNPFRSKLAAAILGGVDQIHIKPGAKVLYLGAASGTTVSHVSDIVGPDGLVYAVE
Protein: Decoralin (DEC) (P85870)
Organism: Oreumenes decoratus (Potter wasp)
Function: Linear cationic alpha-helical peptide that acts as antimicrobial peptide. Has antibacterial activity against the Gram-positive bacteria S.aureus CCT 6538 (MIC=40 uM), S.saprophyticus (MIC=40 um), B.subtilis CCT 2471 (MIC=40 uM), and B.thuringiensis (MIC=40 uM), and against the Gram-negative bacteria E.coli ATCC 25922 (MIC=80), E.coli CCT 1371 (MIC=160), K.pneumonia ATCC 13883 (MIC=80), and A.faecalis ATCC 8750 (MIC=40). Has antifungal activity against C.albicans (MIC=40 uM). At high concentrations exhibits activity in stimulating degranulation from rat peritoneal mast cells. Has very weak hemolytic activity towards human and mouse erythrocytes. In vitro, inhibits the growth of L.major promastigotes (IC(50)=72 uM).
Subcellular location: Secreted {ECO:0000269|PubMed:17981364}. Target cell membrane {ECO:0000269|PubMed:17981364}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000305|PubMed:28267894}.
Interaction partners:
Sequence:
SLLSLIRKLIT
Protein: Septin-8 (Q92599)
Organism: Homo sapiens (Human)
Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in platelet secretion. Seems to participate in the process of SNARE complex formation in synaptic vesicles (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasm, cytoskeleton {ECO:0000250}. Synapse {ECO:0000250|UniProtKB:B0BNF1}. Cell projection, axon {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:B0BNF1}. Presynapse {ECO:0000250|UniProtKB:B0BNF1}. Note=Expressed in axons of immature neurons, localizes to synapses in mature neurons (By similarity). In platelets, found in areas surrounding alpha-granules (PubMed:15116257). {ECO:0000250|UniProtKB:B0BNF1, ECO:0000269|PubMed:15116257}.
Interaction partners:
- Septin-2
- Septin-5
- Septin-7
- Uncharacterized protein C17orf47
- Septin-10
- Septin-1
- Septin-6
- Neuronal-specific septin-3
- Septin-11
- Septin-12
Sequence:
MAATDLERFSNAEPEPRSLSLGGHVGFDSLPDQLVSKSVTQGFSFNILCVGETGIGKSTLMNTLFNTTFETEEASHHEACVRLRPQTYDLQESNVQLKLTIVDAVGFGDQINKDESYRPIVDYIDAQFENYLQEELKIRRSLFDYHDTRIHVCLYFITPTGHSLKSLDLVTMKKLDSKVNIIPIIAKADTISKSELHKFKIKIMGELVSNGVQIYQFPTDDEAVAEINAVMNAHLPFAVVGSTEEVKVGNKLVRARQYPWGVVQVENENHCDFVKLREMLIRVNMEDLREQTHSRHYELYRRCKLEEMGFQDSDGDSQPFSLQETYEAKRKEFLSELQRKEEEMRQMFVNKVKETELELKEKERELHEKFEHLKRVHQEEKRKVEEKRRELEEETNAFNRRKAAVEALQSQALHATSQQPLRKDKDKKNRSDIGAHQPGMSLSSSKVMMTKASVEPLNCSSWWPAIQCCSCLVRDATWREGFL
Protein: Acyl-lipid (7-3)-desaturase (EC 1.14.19.31) (Acyl-lipid 4-desaturase) (Delta-4 desaturase) (PsD4Des) (A0PJ29)
Organism: Rebecca salina (Marine microalga) (Pavlova salina)
Function: Fatty acid desaturase that introduces a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta(7) double bond, resulting in the production of delta-4 desaturated fatty acid docosahexanoic acid (DHA).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPPSAAKQMGASTGVHAGVTDSSAFTRKDVADRPDLTIVGDSVYDAKAFRSEHPGGAHFVSLFGGRDATEAFMEYHRRAWPKSRMSRFHVGSLASTEEPVAADEGYLQLCARIAKMVPSVSSGFAPASYWVKAGLILGSAIALEAYMLYAGKRLLPSIVLGWLFALIGLNIQHDANHGALSKSASVNLALGLCQDWIGGSMILWLQEHVVMHHLHTNDVDKDPDQKAHGALRLKPTDAWSPMHWLQHLYLLPGETMYAFKLLFLDISELVMWRWEGEPISKLAGYLFMPSLLLKLTFWARFVALPLYLAPSVHTAVCIAATVMTGSFYLAFFFFISHNFEGVASVGPDGSITSMTRGASFLKRQAETSSNVGGPLLATLNGGLNYQIEHHLFPRVHHGFYPRLAPLVKAELEARGIEYKHYPTIWSNLASTLRHMYALGRRPRSKAE
Protein: Protein DEEPER ROOTING 1 (PpeDRO1) (A0A251PW43)
Organism: Prunus persica (Peach) (Amygdalus persica)
Function: Involved in the development of the root system architecture by influencing lateral root angles and primary root length.
Interaction partners:
- FYVE-type domain-containing protein
- FYVE-type domain-containing protein
Sequence:
MKLFGWMQNKLNGKQGNKKPNTVPITTHPAKQEPREEFSDWPHGLLAIGTFGNNDLKENAAESQDIQEDPTSSEEILDNFTPEEVGKLHKELTKLLTRKPNIEKEIADLPLDRFLNCPSSLEVDRRNSNALCSDSADDHKDEDIEKTISVILGRCKEICGDKNKKAIGKKSISFLLKKMFVCRSGFAPQPSLRDTLQESRMEKLLRVMLNKKIINPQGSSRAASMKKYLEDRQIPTKKESNTEDDTKEKINNGCKWVKTDSEYIVLEI