wanglab/gogpt-training-data huggingface dataset:
Protein: Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL2 (EC 3.1.1.n2) (Isoprenylcysteine methylesterase-like protein 2) (Q1PET6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the demethylation of isoprenylcysteine methylesters (By similarity). May act as a negative regulator of ABA signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20868530}. Golgi apparatus membrane {ECO:0000269|PubMed:20868530}; Multi-pass membrane protein {ECO:0000269|PubMed:20868530}.
Interaction partners:
- Protein-S-isoprenylcysteine O-methyltransferase B
- Protein-S-isoprenylcysteine O-methyltransferase A
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1
- Isoprenylcysteine alpha-carbonyl methylesterase ICME
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
Sequence:
MQLSPERCRPMSENREAWSANSEEMELLHGSNRLSSPEHVRRRVSGNSSEDGSPRICRQQSFGRDIGHAAAETYLITRLSFNLLGYLGVGYRWITRLLALACYAMLLMPGFLQVAYLYFFSSQVRRSIVYGGHPRNRLDLYIPPTSDGLKPVVVFVTGGAWIIGYKAWGSLLGLQLAERDIIVACLDYRNFPQGTISDMVSDAAQGISFVCNNISAFGGDPNRIYLMGQSAGAHISSCALFEQAIKESRGESISWSVSQIKAYFGLSGGYNLFNLVEHFHNRGLYRSIFLSIMEGEESFKQFSPEVRLKDLNVRKAAALLPHIILFHGSADYSIPPEASKTFTDALQAAEVKAELVMYKGKTHTDLFLQDPLRGGKDELFDHIVSMIHADDSDALRNDAVAPPRKRLVPEFLLKLAGRVSPF
Protein: Caffeate CoA-transferase (EC 2.8.3.23) (Hydrocaffeyl-CoA:caffeate CoA transferase) (F1CYZ5)
Organism: Acetobacterium woodii
Function: Involved in caffeate respiration, which consists in the reduction of the C-C double bond of caffeate. CarA catalyzes an energy-saving CoA loop for caffeate activation in the steady state of caffeate respiration. It catalyzes the formation of caffeyl-CoA from caffeate with hydrocaffeyl-CoA as the CoA donor via a ping-pong mechanism. In addition to caffeate, the enzyme can utilize 4-coumarate or ferulate as CoA acceptor. Neither acetyl-CoA nor butyryl-CoA served as the CoA donor.
Interaction partners:
Sequence:
MAKFISAKEAAKLIPDGSTVGVAGMGLAGWPEEVAVAIADNFKETGHPCNLTMKQGSAMGDWRERGMTRLGLEGLVTKWSAAHIGSAFAMNDLVRAEKMACHCLPQGVIVNLWREIAAKRPGLITKVGLGTFVDPRLEGGKMNKVTTEDLVELIEFNGEEYLFYKSFKLDVAMLRGTTADENGNITFENEGPINEGLAVAQAAKNSGGIVIVQVEYQALKNTLKPKDVKIPGALVDYVVVATDKNACWQTEGVYYEPAFAGNLRKPLSAIPILPLTERKVMARRAAMELSKGDLVNLGVGIPSDVASIVSEAGYIEEITMTTEIGGFGGIPASLPNFGSSYNAEANIDHGSMFDLYDGGGIDVAVLGLAQADEAGNINVSKFTIPGLGDRLTGPGGFINITQSTQKVVFAGSFNAKCEVEISDGKLIIKKEGRGKKLLKEVEQVTFSGKYAAENGQEILYVTERCVFKLINGKMTVIEIAPGIDLQKDILDQMDFTPAISADLKEMDSGLFSEKWDGLDTIMGK
Protein: Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH) (P74132)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Involved in the heme and chlorophyll biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32131}.
Interaction partners:
- Oxygen-dependent coproporphyrinogen-III oxidase
- Protoporphyrinogen IX oxidase
- Uroporphyrinogen decarboxylase
- Heme oxygenase 2
- Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2
- Delta-aminolevulinic acid dehydratase
- Uncharacterized HTH-type transcriptional regulator sll1512
- Anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase
Sequence:
MTTTFPTVEFSAELLNKYNQGIPRYTSYPPATELNKEFDPSDFQTAINLGNYKKTPLSLYCHIPFCAKACYFCGCNTIITQHKPAVDPYLKAVAKQIALVAPLVDQQRPVQQLHWGGGTPNYLTLEQAEFLFNTITDAFPLAENAEISIEINPCYVDKDYIFALRQLGFNRISFGIQDFNSQVQQAVNRIQPEAMLFQVMDWIRQANFDSVNVDLIYGLPHQNLATFRETLRKTAQLNPDRIAVFNFAYVPWLKPVQKKMPESALPPAEEKLKIMQATIADLTEQGYVFIGMDHFAKPDDELAIAQRRGELHRNFQGYTTQPESDLLGFGITSISMLQDVYAQNHKTLKAFYNALDREVMPIEKGFKLSQDDLIRRTVIKELMCQFKLSAQELESKYNLGFDCDFNDYFAKELSALDVLEADGLLRRLGDGLEVTPRGRILIRNIAAVFDTYLQNKSKQQMFSRAI
Protein: Rho family-interacting cell polarization regulator 1 (Q6ZS17)
Organism: Homo sapiens (Human)
Function: Downstream effector protein for Rho-type small GTPases that plays a role in cell polarity and directional migration. Acts as an adapter protein, linking active Rho proteins to STK24 and STK26 kinases, and hence positively regulates Golgi reorientation in polarized cell migration upon Rho activation. Involved in the subcellular relocation of STK26 from the Golgi to cytoplasm punctae in a Rho- and PDCD10-dependent manner upon serum stimulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27807006}. Golgi apparatus {ECO:0000269|PubMed:27807006}. Note=Localizes to the podocyte major processes and cell body (By similarity). Colocalized with STK26 in the Golgi of serum-starved cells and relocated to cytoplasmic punctae, probably vesicular compartments, along with STK26 upon serum stimulation in a Rho- and PDCD10-dependent manner (PubMed:27807006). {ECO:0000250|UniProtKB:Q68FE6, ECO:0000269|PubMed:27807006}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Programmed cell death protein 10
- Serine/threonine-protein kinase 25
- Rho-related GTP-binding protein RhoC
- Rho-related GTP-binding protein RhoB
- Serine/threonine-protein kinase 26
- Serine/threonine-protein kinase 24
Sequence:
MMSLSVRPQRRLLSARVNRSQSFAGVLGSHERGPSLSFRSFPVFSPPGPPRKPPALSRVSRMFSVAHPAAKVPQPERLDLVYTALKRGLTAYLEVHQQEQEKLQGQIRESKRNSRLGFLYDLDKQVKSIERFLRRLEFHASKIDELYEAYCVQRRLRDGAYNMVRAYTTGSPGSREARDSLAEATRGHREYTESMCLLESELEAQLGEFHLRMKGLAGFARLCVGDQYEICMKYGRQRWKLRGRIEGSGKQVWDSEETIFLPLLTEFLSIKVTELKGLANHVVVGSVSCETKDLFAALPQVVAVDINDLGTIKLSLEVTWSPFDKDDQPSAASSVNKASTVTKRFSTYSQSPPDTPSLREQAFYNMLRRQEELENGTAWSLSSESSDDSSSPQLSGTARHSPAPRPLVQQPEPLPIQVAFRRPETPSSGPLDEEGAVAPVLANGHAPYSRTLSHISEASVDAALAEASVEAVGPESLAWGPSPPTHPAPTHGEHPSPVPPALDPGHSATSSTLGTTGSVPTSTDPAPSAHLDSVHKSTDSGPSELPGPTHTTTGSTYSAITTTHSAPSPLTHTTTGSTHKPIISTLTTTGPTLNIIGPVQTTTSPTHTMPSPTHTTASPTHTSTSPTHTPTSPTHKTSMSPPTTTSPTPSGMGLVQTATSPTHPTTSPTHPTTSPILINVSPSTSLELATLSSPSKHSDPTLPGTDSLPCSPPVSNSYTQADPMAPRTPHPSPAHSSRKPLTSPAPDPSESTVQSLSPTPSPPTPAPQHSDLCLAMAVQTPVPTAAGGSGDRSLEEALGALMAALDDYRGQFPELQGLEQEVTRLESLLMQRQGLTRSRASSLSITVEHALESFSFLNEDEDEDNDVPGDRPPSSPEAGAEDSIDSPSARPLSTGCPALDAALVRHLYHCSRLLLKLGTFGPLRCQEAWALERLLREARVLEAVCEFSRRWEIPASSAQEVVQFSASRPGFLTFWDQCTERLSCFLCPVERVLLTFCNQYGARLSLRQPGLAEAVCVKFLEDALGQKLPRRPQPGPGEQLTVFQFWSFVETLDSPTMEAYVTETAEEVLLVRNLNSDDQAVVLKALRLAPEGRLRRDGLRALSSLLVHGNNKVMAAVSTQLRSLSLGPTFRERALLCFLDQLEDEDVQTRVAGCLALGCIKAPEGIEPLVYLCQTDTEAVREAARQSLQQCGEEGQSAHRRLEESLDALPRIFGPGSMASTAF
Protein: Occludin (A2VE81)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|PIRNR:PIRNR005993}; Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR005993}. Cell junction, tight junction {ECO:0000256|PIRNR:PIRNR005993}.
Interaction partners:
- Junctional adhesion molecule A
- Claudin-1
- Zona occludens protein 1
- Claudin-5
- Claudin-3
- Claudin-4
- Cadherin-1
- Tyrosine-protein kinase
- Claudin-7
- Claudin
Sequence:
MSSRPFESPPPYRPDEFKPNHYTPSNDIYSGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLVIVMCIAIFACVASTLAWDRGYGTLMGAGVNYPYAGSAFGSYGSGYGYGYGYGYGYGTGYTDPRAAKGFLLAMAAFCFIAALVIFVTSVVRSGISRTRRYYLTVIIVTAVLGIMMFIATIVYIMGVNPTAQASGSLYSSQIYALCNQFYTPAATGLYVDQYLYHYCVVDPQEAIAIVLGFMVIVAFALMIFFAVKTRRKMNCYDKSNILWDKERIYDEQPPNVEEWVKNVSAGTQDMPPPLSDYVERVDSPVAYSSNGKVNEKRLYPESSYKSTPVPEVAQELPLTSPVEDFRQPHYSSSGNLETLSKRAPAKGRAGKSRRAEQDHYETDYTTGGESCDELEDDWIREYPPITSDQQRQLYKRSFDTGLQEYKSLQAELDEVNKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKRNYCKQLKSKLSHIKKMVGDYDRRKT
Protein: Homeobox protein Meis3 (Meis1-related protein 2) (P97368)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator which directly modulates PDPK1 expression, thus promoting survival of pancreatic beta-cells. Also regulates expression of NDFIP1, BNIP3, and CCNG1.
Subcellular location: Nucleus {ECO:0000269|PubMed:21059917}.
Interaction partners:
- Pre-B-cell leukemia transcription factor 4
Sequence:
MARRYDELRHYPGITEHTTALASFSEAAPSVPRAPGPYTPHRPPQLQAPGLDSDSLKREKDDIYGHPLFPLLALVFEKCELATCSPRDGASAGLGSPPGGDVCSSDSFNEDIAAFAKQIRSERPLFSSNPELDNLMVQAIQVLRFHLLELEKVHDLCDNFCHRYITCLKGKMPIDLVIEDRDGSCREDLEDYAASCPSLPDQNTTWIRDHEDSGSVHLGTPGPSSGGLASQSGDNSSDQGDGLDTSVASPSSAGEDEDLDLERRRNKKRGIFPKVATNIMRAWLFQHLSHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRTGQGASFNPEGQPMAGFTETQPQVTVRTPGSMGMNLNLEGEWHYL
Protein: Probable pectinesterase/pectinesterase inhibitor 46 [Includes: Pectinesterase inhibitor 46 (Pectin methylesterase inhibitor 46); Pectinesterase 46 (PE 46) (EC 3.1.1.11) (Pectin methylesterase 46) (AtPME46)] (Q9FF78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Proline-rich extensin-like family protein
- Protein SEED AND ROOT HAIR PROTECTIVE PROTEIN
- Expansin-A18
- Peroxidase 7
- Proline-rich extensin-like family protein
- Peroxidase 73
- Expansin-A7
- At5g05500
- Pollen Ole e 1 allergen and extensin family protein
- Xyloglucan endotransglucosylase/hydrolase protein 14
Sequence:
MSSYGRLDEHEQAKLEASRKTKKRIAIIAISSIVLVCIVVGAVVGTTARDNSKKPPTENNGEPISVSVKALCDVTLHKEKCFETLGSAPNASRSSPEELFKYAVKVTITELSKVLDGFSNGEHMDNATSAAMGACVELIGLAVDQLNETMTSSLKNFDDLRTWLSSVGTYQETCMDALVEANKPSLTTFGENHLKNSTEMTSNALAIITWLGKIADTVKFRRRRLLETGNAKVVVADLPMMEGRRLLESGDLKKKATIVVAKDGSGKYRTIGEALAEVEEKNEKPTIIYVKKGVYLENVRVEKTKWNVVMVGDGQSKTIVSAGLNFIDGTPTFETATFAVFGKGFMARDMGFINTAGPAKHQAVALMVSADLSVFYKCTMDAFQDTMYAHAQRQFYRDCVILGTVDFIFGNAAVVFQKCEILPRRPMKGQQNTITAQGRKDPNQNTGISIHNCTIKPLDNLTDIQTFLGRPWKDFSTTVIMKSFMDKFINPKGWLPWTGDTAPDTIFYAEYLNSGPGASTKNRVKWQGLKTSLTKKEANKFTVKPFIDGNNWLPATKVPFNSDF
Protein: Probable disease resistance protein At5g04720 (Q9LZ25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable disease resistance protein.
Interaction partners:
- Protein EDS1
- At1g72940/F3N23_14
- Toll/interleukin-1 receptor-like protein
- tRNA ligase 1
- Accelerated cell death 11
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Disease resistance protein CHS1
- Protein DA1-related 4
- Probable disease resistance protein At5g45490
- Similar to part of disease resistance protein domain-containing protein)
Sequence:
MADIIGGEVVTELVRQLYAVSQKTLRCRGIAKNLATMIDGLQPTIKEIQYSGVELTPHRQAQLRMFSETLDKCRKLTEKVLKSSRWNMVRQLLHVRKMENLQSKVSSFLNGQLLVHVLADVHHVRADSEFRFDRIDRKVDSLNEKLGSMKLRGSESLREALKTAEATVEMVTTDGADLGVGLDLGKRKVKEMLFKSIDGERLIGISGMSGSGKTTLAKELARDEEVRGHFGNKVLFLTVSQSPNLEELRAHIWGFLTSYEAGVGATLPESRKLVILDDVWTRESLDQLMFENIPGTTTLVVSRSKLADSRVTYDVELLNEHEATALFCLSVFNQKLVPSGFSQSLVKQVVGECKGLPLSLKVIGASLKERPEKYWEGAVERLSRGEPADETHESRVFAQIEATLENLDPKTRDCFLVLGAFPEDKKIPLDVLINVLVELHDLEDATAFAVIVDLANRNLLTLVKDPRFGHMYTSYYDIFVTQHDVLRDVALRLSNHGKVNNRERLLMPKRESMLPREWERNNDEPYKARVVSIHTGEMTQMDWFDMELPKAEVLILHFSSDKYVLPPFIAKMGKLTALVIINNGMSPARLHDFSIFTNLAKLKSLWLQRVHVPELSSSTVPLQNLHKLSLIFCKINTSLDQTELDIAQIFPKLSDLTIDHCDDLLELPSTICGITSLNSISITNCPRIKELPKNLSKLKALQLLRLYACHELNSLPVEICELPRLKYVDISQCVSLSSLPEKIGKVKTLEKIDTRECSLSSIPNSVVLLTSLRHVICDREALWMWEKVQKAVAGLRVEAAEKSFSRDWLDD
Protein: Ribose-phosphate pyrophosphokinase 4 (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase 4) (P38063)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 5
- Ribose-phosphate pyrophosphokinase 3
- Orotate phosphoribosyltransferase 2
- Amidophosphoribosyltransferase
- ADP-ribose pyrophosphatase
- Transketolase 1
- Ribose-5-phosphate isomerase
- Transketolase 2
Sequence:
MNSESREDMAINSIKLLAGNSHPDLAEQISKKLGIPLSKVGVYQYSNKETSVTIGESLRDEDVYIIQTGIGEQEINDFLMELLILIHACKIASARKITTVIPNFPYARQDKKDKSRAPITAKLVANLLQTAGADHVITMDLHASQIQGFFHIPVDNLYAEPSVLNYIRTKTDFDNAILVSPDAGGAKRVAALADKLDLNFALIHKERQKANEVSKMVLVGDVTNKSCLLVDDMADTCGTLVKACDTLMEHGAKEVIAIVTHGIFSGSAREKLRNSRLSRIVCTNTVPVDLDLPIADQIDISPTFAEAIRRLHNGESVSYLFTHAPV
Protein: T-complex protein 1 subunit epsilon (CCT-epsilon) (Q382B2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- CCT-theta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit eta
- T-complex protein 1, zeta subunit, putative
- CCT-beta
- Phosducin domain-containing protein
- Prefoldin subunit 2, putative
- 10 kDa heat shock protein, putative
Sequence:
MSLAFDEYGRPFLLVKEQANKERVTGVEAQKANILAAISVSNVLKTSLGPRGMDKILVTQDNEVVVTNDGATIMDLMDIDNEIGQLMVELSKSQDSEIGDGTTGVVCLAGALLEQASGLLDKGIHSSRISEGFEKACEIACKRLEEIADTVPVSREEYSYLLQTARSTLNSKVVNRDRDRLAKICVDAVLSVADMERRDVNLDLIKMEGKVGGCLEETCLVNGIVIDKDFSHPQMPKVLKNPKIAILTCPFEPPKPKTKHTVHISSAEHMKEIHEQEQEYFRNQVKLCKQAGADLVICQWGFDDEANYLLYRNDLPAVRWVGGVELEMIAIATGGRIIPRFEDLQSAKLGTCGTVREVGFGTTKDRMIFIEECPSSKAVTIFIRGGNKMMIEEAKRSLHDAVCMVRNLIRDNRIVYGGGSAEIAASMAVLNYADTVSTVDQYAIRRFADALESIPINLALNSGLEPIKCLSRARIEQVEGKNPYAGVDCMDSGTLDMKKQQVFETLQGKCSQLRLATQVVKMILKVDDVIVTKPEEEE
Protein: ER membrane protein complex subunit 2 (Tetratricopeptide repeat protein 35) (TPR repeat protein 35) (Q9CRD2)
Organism: Mus musculus (Mouse)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15006}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15006}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15006}. Note=May also localize to the nuclear envelope. {ECO:0000269|PubMed:11593002}.
Interaction partners:
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 8
- ER membrane protein complex subunit 9
- ER membrane protein complex subunit 5
- ER membrane protein complex subunit 10
- Endoplasmic reticulum membrane protein complex subunit 7
- Membrane magnesium transporter 2
Sequence:
MAKVTERYDVTWEEMRDKMRKWREENSRNSEQIMEVGEELINDYASKLGDDIWIIYEQVMIAALDYGRDDLALFCLQELRRQFPGSHRVKRLTGMRFEAMERYDDAIQLYDRILQEDPTNTAARKRKIAIRKAQGKTVEAIRELNEYLEQFVGDQEAWHELAELYINEHDYAKAAFCLEELMMTNPHNHLYCQQYAEVKYTQGGLENLELSRKYFAQALKLNNRNMRALFGLYMSASHIASNPKASAKMKKDNIKYASWAANQINRAYQFAGRSKKETKYSLKAVEDMLETLQITQS
Protein: Fet31p (A0A1D8PPE2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- High-affinity iron permease
- Ftr2p
- Fth1p
- Fth2p
Sequence:
MRSLSIFSLVFLFFSTLITAKTHTWYYKTGWVNANPDGGFERPMIGFNDSWPLPTLRVKKGDTVNLYLINGFDDRNTSLHFHGLFQHGTNQMDGPEMVTQCPIPPGETFLYNFTVDDQVGSYWYHSHTSGQYGDGMRGVFIIEDDDFPYDYDEEVILTLGEHYHDFSDDLHKNFMSRYNPTGAEPIPSNILFNETRNNTWKVEPGKTYFVRIINIGRFVSQYVWMEDHEFTIVEVDGIYVEKNTTDLIYITVAQRYGVLITTKNSTDKNYAFMNRVDIDMLDVIPDELELNGTNYIEYNSKADKPEPYLLDSIDDYFDDFYLKPLSKEKLLDDADYTITVDVQMDNLGNGVNYAFFNNITYTTPRVPTLLSVLSAGDDASNELVYGTNTNSFVLQSGDVVDIVLNNLDTGKHPFHLHGHVFQLIERHEEIPETEDPVGYNASDHADWPEYPMLRDTVYVRPQSYIVMRFKADNPGVWLFHCHIEWHLDQGLAIQLIEDPQGIQKNASQHITDNHKQICEKVGVSWEGNAAANSKDYLNLKGENVQHKRLPTGFTARGIVALVFSCIAGVLGLATIAYYGMNDIADVEERVARDLDVDFDEEDNEIVNEGSSSSGSNSKH
Protein: PslH (Q9I1N1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PslF
- PslJ
- PslI
- PslD
- Alginate biosynthesis protein AlgA
- PslG
- PslE
- PslA
- dTDP-Rha:alpha-D-Gal-diphosphoundecaprenol alpha-1,3-rhamnosyltransferase
- PslL
Sequence:
MRILWILPYSPWPTTSGGKTRQYHLLRSLAARGHRITVLLHSKQPVSAEDRQALEPFLERLVVLPRRPLRSLSTLLAALFAPYPLLASVNGLSAELQRTATELLREPWDVVQVEHSYSFQPYERPLRDAGQPFVLTEHNVESSLGAATYDRLPGWALPFVRYDQWRYRRWERRVMSQAAAVVAVTEKDARQLGAMLGRPVPVVVNGVDCEHFATARPTPEAQRVLFLGNYEYAPNVDAVEWMLDEILPRVWAHCPEARMSVCGYALPAEWAQRWSDPRIEWQGFVPDLLQLQSSSSVFLAALRHGGGSKLKVLEALAAGLPLASTAQGVSGLELRDGEDYLGGESAEQLANAVVRLLQDPAQARALGENGRAYVRRAHDWSVAASQLEQVYAGLAEGAPACA
Protein: Replication-associated protein G2P (Rep) (EC 3.1.21.-) (EC 6.5.1.1) (G2P) (Gene 2 protein) (P69547)
Organism: Enterobacteria phage M13 (Bacteriophage M13)
Function: Isoform G2P plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates at the 3'-OH of the cleavage site. After one round of rolling circle synthesis, protein G2P is linked to the newly synthesized ssDNA and joins the ends of the displaced strand to generate a circular single-stranded molecule ready to be packed into a virion.
Interaction partners:
Sequence:
MIDMLVLRLPFIDSLVCSRLSGNDLIAFVDLSKIATLSGMNLSARTVEYHIDGDLTVSGLSHPFESLPTHYSGIAFKIYEGSKNFYPCVEIKASPAKVLQGHNVFGTTDLALCSEALLLNFANSLPCLYDLLDVNATTISRIDATFSARAPNENIAKQVIDHLRNVSNGQTKSTRSQNWESTVTWNETSRHRTLVAYLKHVELQHQIQQLSSKPSAKMTSYQKEQLKVLSNPDLLEFASGLVRFEARIKTRYLKSFGLPLNLFDAIRFASDYNSQGKDLIFDLWSFSFSELFKAFEGDSMNIYDDSAVLDAIQSKHFTITPSGKTSFAKASRYFGFYRRLVNEGYDSVALTMPRNSFWRYVSALVECGIPKSQLMNLSTCNNVVPLVRFINVDFSSQRPDWYNEPVLKIA
Protein: Exosome complex exonuclease RRP46 homolog (EC 3.1.13.-) (Exosome component 5) (Ribosomal RNA-processing protein 46) (oRrp46) (Q84T68)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable component of the exosome 3'->5' exoribonuclease complex, a complex that degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3'-untranslated regions. May form a homodimer separately from exosome complexes and function in DNA cleavage process. Binds double-stranded DNA (dsDNA) and single-stranded RNA (ssRNA), and possesses hydrolytic DNase and phosphorolytic RNase activities in vitro.
Subcellular location: Nucleus, nucleolus {ECO:0000305}.
Interaction partners:
- Ribosomal RNA-processing protein 42
- Ribosomal RNA-processing protein 43
- Os02g0815800 protein
- Os04g0520000 protein
- Protein ECERIFERUM 7
- Nuclear nucleic acid-binding protein C1D
- Ribosomal RNA-processing protein 40
- Ribosomal RNA-processing protein 40
- Os09g0252000 protein
- 3' exoribonuclease family, domain 1 containing protein, expressed
Sequence:
MEESRADGRNPNQLRPFSCTRNPLDRAHGSARWAQGDTIVLAAVYGPKPGTRKGENPEKASIEVVWKPMTGQIGKQEKEYEMTLKRTLQSICLLTVHPNTTTSVILQVVGNDGSLLPCAINACCAALVFAGIPLKHLAVAIGCGVLEDGEVILDTNKAEEQQLKSFAHLVFPNSRKSASSKEPNQKEEDSERGLITSITHGVMSEEDYFSCIERGLAASSRISDFMRTTLQKQAPGDV
Protein: Peroxisomal acyl-coenzyme A oxidase 2 (EC 1.17.99.3) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCA-CoA oxidase) (THCCox) (Q99424)
Organism: Homo sapiens (Human)
Function: Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids. Capable of oxidizing short as well as long chain 2-methyl branched fatty acids (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:27884763, ECO:0000269|PubMed:8943006}.
Interaction partners:
- Peroxisomal multifunctional enzyme type 2
- Alpha-methylacyl-CoA racemase
- 3-ketoacyl-CoA thiolase, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 3
- Enoyl-CoA delta isomerase 2
- Peroxisomal bifunctional enzyme
- Sterol carrier protein 2
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal targeting signal 1 receptor
- Hydroxysteroid dehydrogenase-like protein 2
Sequence:
MGSPVHRVSLGDTWSRQMHPDIESERYMQSFDVERLTNILDGGAQNTALRRKVESIIHSYPEFSCKDNYFMTQNERYKAAMRRAFHIRLIARRLGWLEDGRELGYAYRALSGDVALNIHRVFVRALRSLGSEEQIAKWDPLCKNIQIIATYAQTELGHGTYLQGLETEATYDAATQEFVIHSPTLTATKWWPGDLGRSATHALVQAQLICSGARRGMHAFIVPIRSLQDHTPLPGIIIGDIGPKMDFDQTDNGFLQLNHVRVPRENMLSRFAQVLPDGTYVKLGTAQSNYLPMVVVRVELLSGEILPILQKACVIAMRYSVIRRQSRLRPSDPEAKVLDYQTQQQKLFPQLAISYAFHFLAVSLLEFFQHSYTAILNQDFSFLPELHALSTGMKAMMSEFCTQGAEMCRRACGGHGYSKLSGLPSLVTKLSASCTYEGENTVLYLQVARFLVKSYLQTQMSPGSTPQRSLSPSVAYLTAPDLARCPAQRAADFLCPELYTTAWAHVAVRLIKDSVQHLQTLTQSGADQHEAWNQTTVIHLQAAKVHCYYVTVKGFTEALEKLENEPAIQQVLKRLCDLHAIHGILTNSGDFLHDAFLSGAQVDMARTAYLDLLRLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFQWAQKSPTNTQENPAYEEYIRPLLQSWRSKL
Protein: Alanine racemase (EC 5.1.1.1) (P9WQA9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the interconversion of L-alanine and D-alanine. D-alanine plays a key role in peptidoglycan cross-linking.
Interaction partners:
- D-alanine--D-alanine ligase
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaE
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- Alanine dehydrogenase
- Uncharacterized protein Rv3421c
- N-alpha-acetyltransferase RimI
- tRNA N6-adenosine threonylcarbamoyltransferase
- Alanine aminotransferase
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Glutamate racemase
Sequence:
MTPISQTPGLLAEAMVDLGAIEHNVRVLREHAGHAQLMAVVKADGYGHGATRVAQTALGAGAAELGVATVDEALALRADGITAPVLAWLHPPGIDFGPALLADVQVAVSSLRQLDELLHAVRRTGRTATVTVKVDTGLNRNGVGPAQFPAMLTALRQAMAEDAVRLRGLMSHMVYADKPDDSINDVQAQRFTAFLAQAREQGVRFEVAHLSNSSATMARPDLTFDLVRPGIAVYGLSPVPALGDMGLVPAMTVKCAVALVKSIRAGEGVSYGHTWIAPRDTNLALLPIGYADGVFRSLGGRLEVLINGRRCPGVGRICMDQFMVDLGPGPLDVAEGDEAILFGPGIRGEPTAQDWADLVGTIHYEVVTSPRGRITRTYREAENR
Protein: Accessory gland-specific peptide 26Ab (Male accessory gland secretory protein 355B) (P10334)
Organism: Drosophila melanogaster (Fruit fly)
Function: This protein is transferred from male to female during mating and may affect egglaying and behavior after mating.
Subcellular location: Secreted, extracellular space. Cytoplasm {ECO:0000269|PubMed:2257979}.
Interaction partners:
- Accessory gland-specific peptide 26Aa
- Accessory gland protein Acp53Ea
- Accessory gland protein Acp29AB
- ACP53C14A
- Serpin 28F
- Accessory gland protein Acp62F
- GH21475p
- Serpin 38F, isoform A
- Accessory gland protein Acp36DE
- Accessory gland protein Acp63F
Sequence:
MNYFAVICIFSCICLWQFSDAAPFISVQSSSQSRSQKVMNGMLRTLYDYSVQDSVNDATGHLIQTHKADFNSDVMSPDEIESVRQQLNMA
Protein: Small ribosomal subunit protein uS3 (30S ribosomal protein S3) (P73314)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Interaction partners:
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein uL4
Sequence:
MGQKIHPVGFRLGITKDHKSCWYADPKRYPELLQEDHKIRQYIEKTLNNAGISDIRIERKAEQIELGIHTARPGVVVGRGGSGIEQLREGLQKLLGSARQIRVNVIEVPNADADAALMAEYIGQQLERRVSFRRVVRQALQRAERAEVKGIKIQVSGRLNGAEIARTEWVREGRVPLHTLRADIDYAYRTALTTYGILGIKVWIFKGEVIPGQEAAIVAPPSQPRRKSRRQQFDDRSQDG