wanglab/gogpt-training-data huggingface dataset:
Protein: Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180) (Unsaturated glucuronyl hydrolase) (SpyUGL) (Q9A0T3)
Organism: Streptococcus pyogenes serotype M1
Function: Catalyzes the hydrolysis of unsaturated hyaluronate and chondroitin disaccharides. Also degrades unsaturated heparin disaccharides. Releases 4-deoxy-4,5-didehydro D-glucuronic acid or 4-deoxy-4,5-didehydro L-iduronic acid from chondroitin disaccharides, hyaluronan disaccharides and heparin disaccharides and cleaves both glycosidic (1->3) and (1->4) bonds. Prefers sulfated glycosaminoglycans compared to unsulfated glycosaminoglycans. Probably required for mammalian cells invasion through the degradation of extracellular sulfated glycosaminoglycans such as chondroitin and hyaluronan.
Interaction partners:
Sequence:
MARPLKTIALEPIKQPERFTKEDFLSQEDITQALDLALKQVRLNMDYFKEDFPTPATKDNQYAIMDNTEWTNAFWTGCLWLAYEYSGDDAIKALAQANDLSFLDRVTRDIELDHHDLGFLYTPSCMAEWKLLKTPESREAALKAADKLVQRYQDKGGFIQAWGELGKKEDYRLIIDCLLNIQLLFFASQETGDNRYRDMAINHFYASANHVIRDDASAYHTFYFDPETGDPVKGVTRQGYSDDSAWARGQAWGIYGIPLTYRFLKEPELIQLFKGMTHYFLNRLPKDQVSYWDLIFGDGSEQSRDSSATAIAVCGIHEMLKTLPDHDPDKKTYEAAMHSMLRALIKDYANKDLKPGAPLLLHGVYSWHSGKGVDEGNIWGDYYYLEALLRFYKDWNPYW
Protein: ERCC excision repair 1, endonuclease non-catalytic subunit (D3ZAQ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA repair endonuclease XPF
- DNA repair protein complementing XP-A cells homolog
- RNA helicase
- Structure-specific endonuclease subunit SLX4
- DNA repair endonuclease XPF
- DNA mismatch repair protein Msh2
- Structure-specific endonuclease subunit MUS81
- DNA excision repair protein ERCC-5
- X-ray repair cross-complementing protein 5
- DNA repair protein XRCC1
Sequence:
MDPGKDEENRPQPSGPPTRKKFVIPLEEDEAPSSGAKPLFKSSRNPTPTAASTHSAPLTYAEYAIAQPPGGAGATVPTGSEPATGDSPSQTLKAGTKSSSIIVSPRQRGNPVLKFVRSVPWEFGEVTPDYVLGQSTCALFLSLRYHNLHPDYIHERLQSLGKNFALRVLLVQVDVKDPQQALKELAKICILADCTLVLAWSAEEAGRYLETYKAYEQKPADLLMEKLEQNFLSRATECLTTVKSVNKTDSQTLLTTFGSLEQLITASREDLALCPGLGPQKARRLFEVLHEPFLKVPR
Protein: Cilia- and flagella-associated protein 53 (Q57VE0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
Sequence:
MAHVAIRRQREEEQRAREQAQAVEKRMRLAANFETRSEKVYEQKDLMRRLDLVRAKHDDALVARRQRLAAMLLREKEEHEAMLNNLTETDEQRRDRLIRKARELRAQQQHHLRVDAQKRHERLFREKIDCLRLAESRLRVMQVANARFEQLALAERRKEEQQREEEFFAQQRVEENRLANERAQKDLEEDYIRKQAVVKALAAQVEGNKMRAEQHQLEVKKENEAFCRAVEEERAAEAQKKMEARIARAALAKEMSEFNEQLRTARRQEYERLQKEDREVLDRMLAELAEQEQEEKRRKHELRANARLHLKEVERQMNQRKEDMENLDKLWEEENNKVWEKREAHWRADEEKRRKLLRNVLIVRRQQVLDKRQQEKEAVERAEVERQEFRNMIAGLADIDAMERAQRFAVAKENQKYLESQVQRRNAEKEEVRMAMKTALTAEQEKEKVHAERIKREIENLERAKPERYKDVPLLPRQRFPPI
Protein: 26S proteasome regulatory subunit rpn8 (O74440)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit rpn7
- 26S proteasome regulatory subunit rpn502
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn2
- 26S proteasome regulatory subunit rpn1
- Probable 26S proteasome regulatory subunit rpn9
- 26S proteasome regulatory subunit 6B homolog
- Probable 26S proteasome regulatory subunit rpn6
- 26S proteasome regulatory subunit rpn12
- 26S proteasome regulatory subunit rpn10
Sequence:
MPPAVSSETSTIVPQQVIVHPLVLLSAVDSYNRSAKGTKRRVVGILLGQNNGDVVNVANSYAIPFEEDEKNASVWFLDHNFMESMNEMFKKINANEKLVGWYHTGPQLRPSDLEINNLLKKYIPNPVLVIIDVKPKSVGLPTNAYFAIDEIEDDGSKSSRTFVHLPSSIEAEEAEEIGVEHLLRDTRDASVGTLATRVTQQAQSLQGLGQRLTEIADYLRKVVDGQLPINHAILAELQSVFNLLPNIFSGPVVSEQALESEAQRAFNVNSNDQLMSIYISSIVRAVIALHDLLDSLAASKAMEQQDIKPTVQNGEVSANAEQKA
Protein: DNA utilization protein HofN (P64634)
Organism: Escherichia coli (strain K12)
Function: Required for the use of extracellular DNA as a nutrient.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- DNA utilization protein HofM
- DNA utilization protein HofQ
- DNA utilization protein HofO
- DNA utilization protein HofP
- Protein transport protein HofB homolog
Sequence:
MNPPINFLPWRQQRRTAFLRFWLLMFVAPLLLAVGITLILRLTGSAEARIDAVLLQAEQQLARSLQITKPRLLEQQQLREQRSQRQRQRQFTRDWQSALEALAALLPEHAWLTTISWQQGTLEIKGLTTSITALNALETSLRQDASFHLNQRGATQQDAQGRWQFEYQLTRKVSDEHVL
Protein: LysM domain receptor-like kinase 3 (LysM-containing receptor-like kinase 3) (EC 2.7.11.-) (F4IB81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative Lysin motif (LysM) receptor kinase that may recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- LysM domain-containing GPI-anchored protein 1
- LysM domain-containing GPI-anchored protein 3
- Remorin
- LysM domain-containing GPI-anchored protein 2
- Probable ubiquitin conjugation factor E4
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Probable inactive shikimate kinase like 1, chloroplastic
- At5g62150
Sequence:
MNLTFYIFFLSLLPSFSSSKPMNCSDTTRLCSSFLAFKPNQNQSFSVIQSMFDVLPQDITADISGGYFFIKKNCSCLTTTHQYTTNTTFTIRQNVGYVYNVTVSAYSGLAFPPNTTRAARAGAVVSVQLLCGCSSGLWNYLMSYVAMAGDSVQSLSSRFGVSMDRIEDVNGILNLDNITAGDLLYIPLDSVPGEPYETSKINPPAPSPAPASSLANGNISDDQVNHTAKSGSHVPYIWIVGGLGVVLALLVLCILVCICLRSSSCSSSEEDGNGHNFQILRKSGFFCGSGRYNCCRSGDFRQTNGETQVVAIPKALGDGMFEIEKPMVFTYEEIRAATDEFSDSNLLGHGNYGSVYFGLLREQEVAVKRMTATKTKEFAAEMKVLCKVHHSNLVELIGYAATVDELFVVYEYVRKGMLKSHLHDPQSKGNTPLSWIMRNQIALDAARGLEYIHEHTKTHYVHRDIKTSNILLDEAFRAKISDFGLAKLVEKTGEGEISVTKVVGTYGYLAPEYLSDGLATSKSDIYAFGVVLFEIISGREAVIRTEAIGTKNPERRPLASIMLAVLKNSPDSMNMSSLKEFVDPNMMDLYPHDCLFKIATLAKQCVDDDPILRPNMKQVVISLSQILLSSIEWEATLAGNSQVFSGLVQGR
Protein: Splicing factor 3B subunit 3 (Q9W0M7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex, a constituent of the spliceosome. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (By similarity). May also be involved in the assembly of the 'E' complex (By similarity). Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18981222, ECO:0000269|PubMed:27185460}.
Interaction partners:
- LD21442p
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 4
- LD45152p
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 6
- PHD finger-like domain-containing protein 5A
- Splicing factor 3A subunit 1
- U5 small nuclear ribonucleoprotein 200 kDa helicase
Sequence:
MYLYNLTLQKATGVTHAVHGNFSGGKQQEVLLSRGKSLELLRPDSNTGKVHTLLSTEIFGCVRALMAFRLTGGTKDYIVVGSDSGRIVILEYNPSKNALEKVHQETFGKSGCRRIVPGQYFAIDPKGRAVMIGAVEKQKLAYIMNRDTQARLTISSPLEAHKSNTLTYHMVGVDVGFDNPMFACLEIDYEEADMDPSGDAAQRTQQTLTFYELDLGLNHVVRKYSEPLEEHANFLVSVPGGNDGPSGVLICSENYLTYKNLGDQHDIRCPIPRRRNDLDDPERGMIFICSATHRTKSMYFFLLQTEQGDIFKITLETDDDVVSEIKLKYFDTVPPATAMCVLKTGFLFVASEFGNHYLYQIAHLGDDDDEPEFSSAMPLEEGETFFFAPRALKNLVLVDELPSFAPIITSQVADLANEDTPQLYVLCGRGPRSTLRVLRHGLEVSEMAVSELPGNPNAVWTVKKRADDEFDAYIIVSFVNATLVLSIGETVEEVTDSGFLGTTPTLCCAALGDDALVQVYPDGIRHIRSDKRVNEWKAPGKKSITKCAVNQRQVVITLSGRELVYFEMDPTGELNEYTERSEMPAEIMCMALGTVPEGEQRSWFLAVGLADNTVRILSLDPNNCLTPCSMQALPSPAESLCLVEMGHTESTTQGGLDDDAPAQRSGNNKGTIYLNIGLSNGVLLRTVLDPVSGDLADTRTRYLGSRPVKLFRIKMQGSEAVLAMSSRTWLSYYHQNRFHLTPLSYETLEYASGFSSEQCSEGIVAISTNTLRILALEKLGAVFNQVAFPLQYTPRTFVIHPDTGRMLIAETDHNAYTEDTKSARKEQMAEEMRSAAGDEERELAREMANAFINEVLPEDVFSSPKAGLGLWASQIRCLDAMHGQTMFSVPLTQNEAIMSMAMLKFSIAADGRYYLAVGIAKDLQLNPRISQGGCIDIYKIDPTCSSLEFMHRTDIDEIPGALCGFQGRLLAGCGRMLRIYDFGKKKMLRKCENKHIPYQIVNIQAMGHRVYVSDVQESVFFIRYRRAENQLIIFADDTHPRWVTATTLLDYDTIAIADKFGNLSIQRLPHSVTDDVDEDPTGTKSLWDRGLLSGASQKSENICSFHVGEIIMSLQKATLIPGGSEALIYATLSGTVGAFVPFTSREDYDFFQHLEMHMRNENPPLCGRDHLSYRSSYYPVKNVLDGDLCEQYLSIEAAKQKSIAGDMFRTPNQICKKLEDIRTRYAF
Protein: EMBRYO DEFECTIVE 140 (F4JQ75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Sm-like protein LSM8
- Sm-like protein LSM5
- Sm-like protein LSM2
- Sm-like protein LSM4
- Sm-like protein LSM7
- Sm-like protein LSM3A
- Sm-like protein LSM3B
- Protein GOLVEN 6
- Sm-like protein LSM36B
- Sm-like protein LSM6A
Sequence:
MMADDTELVSNTDQKMEDASAENPARADPPSSDDSGDSDSDSEDEAESNQQIVTLESELSANPYNYDAYVQYIKLLRKTANLEKLRQAREAMSAIFPLSPSLWLEWARDEASLAASENVPEIVMLYERGLSDYQSVSLWCDYLSFMLEFDPSVRGYPSEGISKMRSLFERAIPAAGFHVTEGNRIWEGYREFEQGVLATIDEADIEERNKQIQRIRSIFHRHLSVPLENLSSTLIAYKTWELEQGIDLDIGSDDLSKVSHQVAVANKKAQQMYSERAHLEENISKQDLSDTEKFQEFMNYIKFEKTSGDPTRVQAIYERAVAEYPVSSDLWIDYTVYLDKTLKVGKAITHAYSRATRSCPWTGDLWARYLLALERGSASEKEIYDVFEKSLQCTFSSFEEYLDLYLTRVDGLRRRMLSTRMLEALDYSLIRETFQQASDYLTPHMQNTDSLLHLHTYWANLELNIGKDLAGARGVWDSFLKKSGGMLAAWHAYIDMEVHLGHIKEARSIYRRCYTRKFDGTGSEDICKGWLRFEREHGDLEHFDLAVQKVMPRLEELQLMRLQQESTPVKPSAGLKEHSSQKRKAEQNVEEESLAKRQKRKSQKEVDLGGQSATVPATKNVKAENGKTADSDKEETEDAKPLKPKVYRDECTAFISNLSVKAQEEDIRKFFGDDGGVDSIRILHHKDTGKPRGLAYADFVDDEHLAAAIAKNRKMFFGKKISIARSNPKKGKKEFTRRGNVDGSGNSKDPSLISEKAKAPLGGETEGERKGNEVEVRGKNTFAVPRNVKPLGYTTPKPSADETPKSNDEFRNMFLKK
Protein: Transmembrane protein AmpE (Q9ZG99)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MTFLVLLLALALEKFSGWRRRIQRDGAWLAWLSLVEDLPSVSRRSWLGLLLAVVLPLLPLALLLTLLQSLAYGWLSLPLHLLVVVYSLGRGDVMADLGPFRDAWRREEAQAAFHVAERDLGILGGSESELIGRVHGHLLWQGYQSFFAVIFWYALLGPVAALAYRLLALALEHARQPALREQAARVRHILDWLPVRALVLSFALVGNFLAVIRVLLHWLLAWDISAAALLGKAGRVASDVEAVELGAAGVASLDALWQLLVRAAVLWYAVFAFCALFL
Protein: ESAT-6-like protein EsxS (Q6MX18)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Secreted {ECO:0000305|PubMed:19876390}. Note=Probably secreted via the ESX-3 / type VII secretion system (T7SS). {ECO:0000305|PubMed:19876390}.
Interaction partners:
- ESAT-6-like protein EsxR
- ESAT-6-like protein EsxQ
- ESAT-6-like protein EsxH
- 6 kDa early secretory antigenic target
- ESAT-6-like protein EsxB
- Type ISP restriction-modification enzyme LLaBIII C-terminal specificity domain-containing protein
- ESAT-6-like protein EsxC
Sequence:
MSLLDAHIPQLIASHTAFAAKAGLMRHTIGQAEQQAMSAQAFHQGESAAAFQGAHARFVAAAAKVNTLLDIAQANLGEAAGTYVAADAAAASSYTGF
Protein: AlkB homolog 2, alpha-ketoglutarate dependent dioxygenase (S4R3T5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XLLRKQEEQEPTGEEPAVLGGDKESTRKRPRREAPGNGGHSAGPSWRHIRAEGLDCSYTVLFGKAEADEIFQELEKEVEYFTGALARVQVFGKWHSVPRKQATYGDAGLTYTFSGLTLSPKPWIPVLERIRDHVSGVTGQTFNFVLINR
Protein: 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) (Cytochrome P450 39A1) (mCYP39A1) (Oxysterol 7-alpha-hydroxylase) (Q9JKJ9)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in neural cholesterol clearance through bile acid synthesis. Catalyzes 7-alpha hydroxylation of (24S)-hydroxycholesterol, a neural oxysterol that is metabolized to bile acids in the liver. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q64654}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q64654}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cholesterol 24-hydroxylase
- 3 beta-hydroxysteroid dehydrogenase type 7
- Cholesterol 25-hydroxylase
- Methylsterol monooxygenase 1
- Squalene synthase
- Lanosterol synthase
Sequence:
MGIMELFSPIAIAVLGSCVLFLFSRLKNLLGPPCIQGWIPWIGAGLEFGKAPLEFIEKARIKYGPVFTIFAMGNRMTFVSEEEGINVLLKSEHVDFESAVQSPVYHTAWIPKNVFSALHERLYALMKGKMGTFNTHHFTGPLTEELHEQLEGLGTHGTMDLNDFVRYLLYPATLNTLFKKGLFLTDKRTIKEFYQQFKTYDEGFEYGSQLPEWLLRNWSKSKRWLLALFEKNIGNIKAHGSAGHSGTLLQAILEVVETETRQYSPNYGLVVLWAALANAPPIAFWTLGYILSHPDIHRTVLESISSVFGTAGKDKIKVSEDDLKKLLIIKWCILESVRLRAPGVITRKVVKPVKILNHTVPSGDLLMLSPFWLHRNPKYFPEPESFKPERWKEANLDKYIFLDYFMAFGGGKFQCPGRWFALLEIQLCIILVLYKYECSLLDPLPKQSSRHLVGVPQPAGKCRIEYKQRA
Protein: E3 ubiquitin-protein ligase MYLIP (EC 2.3.2.27) (Inducible degrader of the LDL-receptor) (Idol) (Myosin regulatory light chain-interacting protein) (MIR) (RING-type E3 ubiquitin transferase MYLIP) (Q8BM54)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR.
Subcellular location: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q8WY64}; Peripheral membrane protein.
Interaction partners:
- Low-density lipoprotein receptor
- Ubiquitin-conjugating enzyme E2 D1
- Very low-density lipoprotein receptor
- Phospholipid-transporting ATPase ABCA1
- ATP-binding cassette sub-family G member 1
- Low-density lipoprotein receptor-related protein 8
Sequence:
MLCYVTRPDAVLMEVEVEAKANGEDCLNQVCRRLGIIEVDYFGLQFTGSKGESLWLNLRNRISQQMDGLAPYRLKLRVKFFVEPHLILQEQTRHIFFLHIKESLLAGHLQCSPEQAVELSALLAQTKFGDYNQNTAQYSYEDLCEKELSSSTLNSIVAKHKELEGISQASAEYQVLQIVSAMENYGIEWHAVRDSEGQKLLIGVGPEGISICKEDFSPINRIAYPVVQMATQSGKNVYLTVTKESGNSIVLLFKMISTRAASGLYRAITETHAFYRCDTVTSAVMMQYSRDLKGHLASLFLNENINLGKKYVFDIKRTSKEVYDHARRALYNAGVVDLVSRSDQSPPSSPLKSSDSSMSCSSCEGLSCQQTRVLQEKLRKLKEAMLCMACCEEEINSTFCPCGHTVCCESCAAQLQSCPVCRSRVEHVQHVYLPTHTSLLNLTVI
Protein: Drought-responsive family protein (F4JH94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEEDLLGICGFDSSKKYRLEELAKYQSGSCIEFEDDDEMAVDYPCPFCSDDYDLVELCHHIDEEHQLDANNGFLHEAVSCKFRLFIICPVCSRRVKMHMVDHITTQHRDVFKRLYKDESYSAFSPGTRKYLQSLIDEPLSTNHTSKSVLDPLLSFIYNPPSPKKSKLVQPDSSSEASMEDNSLIRDSTEKDWESPSPLSDTELLEKAKKREFVQGLISSAIFDHIYNF
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 (Q9Y3Q4)
Organism: Homo sapiens (Human)
Function: Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih). May mediate responses to sour stimuli.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10228147, ECO:0000269|PubMed:10430953, ECO:0000269|PubMed:16407510}; Multi-pass membrane protein {ECO:0000269|Ref.10}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
- Sodium channel protein type 5 subunit alpha
- Sodium channel protein type 2 subunit alpha
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
- Gap junction alpha-5 protein
- Homeobox protein Nkx-2.5
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Sodium channel regulatory subunit beta-1
Sequence:
MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDAEEEGAGGRQDPSRRSIRLRPLPSPSPSAAAGGTESRSSALGAADSEGPARGAGKSSTNGDCRRFRGSLASLGSRGGGSGGTGSGSSHGHLHDSAEERRLIAEGDASPGEDRTPPGLAAEPERPGASAQPAASPPPPQQPPQPASASCEQPSVDTAIKVEGGAAAGDQILPEAEVRLGQAGFMQRQFGAMLQPGVNKFSLRMFGSQKAVEREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNVVSDTFFLIDLVLNFRTGIVVEDNTEIILDPQRIKMKYLKSWFMVDFISSIPVDYIFLIVETRIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIVNLIGMMLLLCHWDGCLQFLVPMLQDFPDDCWVSINNMVNNSWGKQYSYALFKAMSHMLCIGYGRQAPVGMSDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPPDTRQRIHDYYEHRYQGKMFDEESILGELSEPLREEIINFNCRKLVASMPLFANADPNFVTSMLTKLRFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKETKLADGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVALDRLDRIGKKNSILLHKVQHDLNSGVFNYQENEIIQQIVQHDREMAHCAHRVQAAASATPTPTPVIWTPLIQAPLQAAAATTSVAIALTHHPRLPAAIFRPPPGSGLGNLGAGQTPRHLKRLQSLIPSALGSASPASSPSQVDTPSSSSFHIQQLAGFSAPAGLSPLLPSSSSSPPPGACGSPSAPTPSAGVAATTIAGFGHFHKALGGSLSSSDSPLLTPLQPGARSPQAAQPSPAPPGARGGLGLPEHFLPPPPSSRSPSSSPGQLGQPPGELSLGLATGPLSTPETPPRQPEPPSLVAGASGGASPVGFTPRGGLSPPGHSPGPPRTFPSAPPRASGSHGSLLLPPASSPPPPQVPQRRGTPPLTPGRLTQDLKLISASQPALPQDGAQTLRRASPHSSGESMAAFPLFPRAGGGSGGSGSSGGLGPPGRPYGAIPGQHVTLPRKTSSGSLPPPLSLFGARATSSGGPPLTAGPQREPGARPEPVRSKLPSNL
Protein: Aminomethyltransferase folate-binding domain-containing protein (Q4QAF7)
Organism: Leishmania major
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Uncharacterized protein L7845.02
Sequence:
MKPLAPFVCRLPSRRILRVRGTDAHDFLQGIFTNDLRELHPAGSMYGCFLYFTGRVLCDAHLYQCKQVHEGQASILVDVHERSATELLDHLTEMKMRKKVHIDDVGKELVVLAALEETSADAQRSRDSASGCDARESSVTSLSPETLEERHTECFLDPRNDALFPRPPPPSSSSPPAAVTSPSFCLRKCVVPATWAPPLSSPDSYTTLLYSRGIGEGPDVFKCNKSLPFEGNLDFLKGVSFHKGCYVGQELTHRTHVMLVTRKRTVPLHFGPANVDPPAAGIITDEGAVTKTWPVEVGEPLYSAAREKIGEVTGVCGQVGIGLFRLRYVDKATHTVPGLQLKDGTPVQTHLPDWWPRKDVKKLLQNNS
Protein: Disease resistance protein (TIR-NBS-LRR class) family (F4I9F1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Defensin-like protein 71
- Disease resistance RPP8-like protein 3
- Disease resistance protein UNI
Sequence:
MASSSSSHNWLYDVFLSFRGEDVRVTFRSHFLKELDRKLITAFRDNEIERSHSLWPDLEQAIKESRIAVVVFSKNYASSSWCLNELLEIVNCNDKIVIPVFYHVDPSQVRHQIGDFGKIFENTCKRQTDEEVKNQWKKALTLVANMLGFDSAKWNDEAKMIEEIANDVLGKLLLTTPKDSEELVGIEDHIAEMSLLLQLESKEVRMVGISGSSGIGKTTIARALFKRLSRHFQGSTFIDRAFVSYSRNIYSGANPDDPNMKLQLQGHFLSEILGKKDIKIDDPAALEERLKHQKVLIIIDDLDDIMVLDTLVGQTQWFGYGSRIIVVTNDKHFLIAHGIDHIYEVSFPTDVHACQMLCQSAFKQNYAPKGFEDLVVDVVRHAGNFPLGLNLLGKYLRRRDMEYWMDMLPRLENSLRIDGKIEKILRISYDGLESEDQEIFRHIACLFNHMEVTTIKSLLADSDVSFALENLADKSLIHVRQGYVVMHRSLQEMGRKIVRIQSIDKPGEREFLVDPNDIHDILNACTGTQKVLGISLDIRNIRELDVHERAFKGMSNLRFLEIKNFGLKEDGLHLPPSFDYLPRTLKLLCWSKFPMRCMPFGFRPENLVKLEMQYSKLHKLWEGVAPLTCLKEMDLHGSSNLKVIPDLSEATNLEILNLKFCESLVELPSSIRNLNKLLNLDMLNCKSLKILPTGFNLKSLDRLNLYHCSKLKTFPKFSTNISVLNLNLTNIEDFPSNLHLENLVEFRISKEESDEKQWEEEKPLTPFLAMMLSPTLTSLHLENLPSLVELTSSFQNLNQLKDLIIINCINLETLPTGINLQSLDYLCFSGCSQLRSFPEISTNISVLYLDETAIEEVPWWIEKFSNLTELSMNSCSRLKCVFLHMSKLKHLKEALFRNCGTLTRVELSGYPSGMEVMKADNIDTASSSLPKVVLSFLDCFNLDPETVLHHQESIIFNYMLFTGKEEVPSYFTYRTTGSSSLTIPILHVHLSQPFFRFRIGALVTNKEEPVELEVKCEFKDRFGNNFDYDIYFEVNKDRYYGEDCYNIAILDCRIPLNEDNAALAQRNYYDHVDIKIEQLDKRYSDIEQWGIRLLEDCSSAETRLDNYSNSTLPHVSEAEEGNKGYTPLQGLVNEIEHSEEPGDINVETERSTKRMRLYHFI
Protein: B7.1 (O35187)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MAYSCQLMQESPLLGFPRLRFIHLFVLLLVGLFQISSGIVGQVSKSVREKALLSCDYKFCSEEQSIHRIYWQKHDKMVLSVISGVPEVWPEYKNRTVYDIANNYSFSLLGLILSDRGTYTCVVQRYEGESYVVKHLTTVELSVRADFPTPNITESGNPSADIKRITCFASGGFPKPRLSWLENGRELNGINTTISQDPESELYTISSQLDFNTTYDHFIDCFIEYGDAHVSQNFTWVKPPEDPPDEKQTIPFAWAGSDAVKAIIIFFIAITVIAVIAAIAIIIFCITVKFRRCFRRRNEASRETNKNLYIGPVEAAAEQTV
Protein: Carbamoyl dehydratase HypE (EC 4.2.1.-) (Hydrogenase maturation factor HypE) (P24193)
Organism: Escherichia coli (strain K12)
Function: Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group. The cyano group is then transferred from HypE to the HypC-HypD complex or the HybG-HypD complex.
Interaction partners:
- Hydrogenase maturation factor HypC
- Hydrogenase maturation factor HypD
- Carbamoyltransferase HypF
- Hydrogenase maturation factor HypB
- Hydrogenase maturation factor HypA
- Hydrogenase maturation factor HybG
- Hydrogenase 3 maturation protease
- Hydrogenase maturation factor HybF
- Formate hydrogenlyase subunit 5
- Hydrogenase-2 large chain
Sequence:
MNNIQLAHGSGGQAMQQLINSLFMEAFANPWLAEQEDQARLDLAQLVAEGDRLAFSTDSYVIDPLFFPGGNIGKLAICGTANDVAVSGAIPRYLSCGFILEEGLPMETLKAVVTSMAETARAAGIAIVTGDTKVVQRGAVDKLFINTAGMGAIPANIHWGAQTLTAGDVLLVSGTLGDHGATILNLREQLGLDGELVSDCAVLTPLIQTLRDIPGVKALRDATRGGVNAVVHEFAAACGCGIELSEAALPVKPAVRGVCELLGLDALNFANEGKLVIAVERNAAEQVLAALHSHPLGKDAALIGEVVERKGVRLAGLYGVKRTLDLPHAEPLPRIC
Protein: AT5g25280/F18G18_20 (Serine-rich protein-like protein) (Q93WB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT5g22320/MWD9_11
- Guanylate-binding family protein
- Probable cyclic nucleotide-gated ion channel 16
- Uncharacterized protein
- Peptidyl-prolyl cis-trans isomerase CYP18-3
- Structural maintenance of chromosomes protein 1
- Serine/threonine-protein kinase STY8
Sequence:
MAITSSRTTRSNGSASLRSKSPSGRFCGVYSNRMPSSSPSSSGFASSTSSSFSSPSTAFFSSHNQNNHHQHRSASPTRVNLFTSAPMTQSFRYSIDNRSISPNRSIAVSSNKPSNHHKIPDSRRRCMCSPTTHPGSFRCSLHKNVANPHGQGTASYTTNGLNMRRSAMTNSLVRIGGVEGEWVRRALTTLIRPSSHQLKRRSAYEPRRSRLASMSKAEDL
Protein: Secapin (AcSecapin-1) (A0A0K1YW63)
Organism: Apis cerana (Indian honeybee)
Function: Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities. Displays antimicrobial activity against bacteria and fungi. Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent. The recombinant form inhibits trypsin (IC(50)=80.02 nM, Ki=127.25 nM), chymotrypsin (IC(50)=393.78 nM, Ki=432.59 nM), the microbial serine proteases subtilisin A (IC(50)=379.20 nM, Ki=492.77 nM) and proteinase K (IC(50)=189.43 nM, Ki=271.76 nM), plasmin (IC(50)=457.98 nM, Ki=502.91 nM), human elastase (IC(50)=347.81 nM, Ki=469.90 nM) and porcine elastase (IC(50)=94.70 nM, Ki=125.62 nM). Does not inhibit thrombin. Binds to human plasmin and inhibits the plasmin-mediated degradation of fibrin to fibrin degradation products. Also binds to bacterial and fungal surfaces and exhibits antimicrobial activity against the Gram-positive bacteria B.thuringiensis (MIC=4.21 uM) and P.larvae (MIC=11.13 uM), the Gram-negative bacterium E.coli (MIC=6.50 uM), and the fungus B.bassiana (IC(50)=2.57 uM). The synthetic peptide also exhibits antimicrobial activity against the Gram-positive bacterium P.larvae (MIC=41.12 uM), the Gram-negative bacterium P.aeruginosa (MIC=65.75 uM), and the fungus B.bassiana (IC(50)=44.27 uM) (Ref.2). In vitro it does not induce an inflammatory response and has no cytotoxic activity against mouse embryo cells (Ref.2).
Subcellular location: Secreted {ECO:0000305|PubMed:27208884}.
Interaction partners:
Sequence:
MRFQVYILHLCFFILVVLTYLSQGQSYTTTTTTSTTEQPTFLQKIHETFKKVKENAKIHNLYIFDPPTWIYTTTTEKPVESTENFDITNRQLITVPVRCPPNYDFIKGRCREKIP