PharMolix/UniProtQA huggingface dataset:
Protein: NOTJ_ASPSM
Sequence: MRIMSIMLHLLATILLSSAVSAQNANAASTRRLIGEDRESGRRWGVAATDLGIPYDQHNGEIGFLFGDTVSTKWVQEAKDLRSPVMLRSGIHPGEDGGIVFESAAGVDGDGLAPRLFYNGDRGDDGTGTGTWEFTVLPNDGISFPETGEHIISYLSIMNFTTPWTPNYSGLAYSTDGNTFTRLPTKWLNNDNNTDPFQMWTMQRDGDWVYVFTVRSAPQYGPLMLQRVPWDKMTNKTEYQGWGWNGEDWGWQRPCSPILDGYFGEPSVRRLHDGTWAMVYLNASTSTPHIVSRSAKDPTGPWSEEKVQVNQEGDGSLLYGGFIHPWSTSKGNQLYLMVSNWTSTSNLSQTTEAVADYEGTVSVSQFTGTL
What is the function of this protein?
Part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2. 2. 2]diazaoctane core (PubMed:20722388).  The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F (PubMed:20722388).  The reverse prenyltransferase notF then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2. 2. 2]diazaoctane core (PubMed:20722388).  Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG, to yield 6-hydroxy-deoxybrevianamide E (Probable).  6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (PubMed:20722388).  As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH cytochrome P450 monooxygenase or the notD FAD-linked oxidoreductase (Probable).  This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D (PubMed:22188465).  On the other hand notoamide S is converted to notoamide T by notH (or notD), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (+)-notoamide T (Probable).  To generate antipodal (-)-notoaminide T, notH' (or notD') in Aspergillus versicolor is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable).  The remaining oxidoreductase notD (or notH) likely catalyzes the oxidative pyran ring formation to yield (+)-stephacidin A (Probable).  The FAD-dependent monooxygenase notI is highly similar to notB and is predicted to catalyze a similar conversion from (+)-stephacidin A to (-)-notoamide B via the 2,3-epoxidation of (+)-stephacidin A followed by a pinacol-type rearrangement (Probable).  Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable).  The fonction of notJ in the notoamide biosynthesis has not been determined yet (Probable).
What are the official names of this protein?
Notoamide biosynthesis cluster protein J.
Protein: RL20_METEP
Sequence: MARVKRGVTSHAKHKKVLKAAKGYYGRRKNTIRIAKQAVEKGLQYAYRDRKNKKRTFRALWIQRLNAAVREHGLTYSRFINALAQSGIEVDRKALSELAIHEPAAFAAVVEKAKSALPKAA
What is the function of this protein?
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit.  It is not involved in the protein synthesizing functions of that subunit.
What are the official names of this protein?
50S ribosomal protein L20.
What is the protein family that this protein belongs to?
Belongs to the bacterial ribosomal protein bL20 family.
Protein: G3OX_PEA
Sequence: MPSLSEAYRAHPVHVNHKHPDFNSLQELPESYNWTHLDDHTLIDSNNIMKESTTTVPVIDLNDPNASKLIGLACKTWGVYQVMNHGIPLSLLEDIQWLGQTLFSLPSHQKHKATRSPDGVSGYGIARISSFFPKLMWYEGFTIVGSPLDHFRELWPQDYTRFCDIVVQYDETMKKLAGTLMCLMLDSLGITKEDIKWAGSKAQFEKACAALQLNSYPSCPDPDHAMGLAPHTDSTFLTILSQNDISGLQVNREGSGWITVPPLQGGLVVNVGDLFHILSNGLYPSVLHRVLVNRTRQRFSVAYLYGPPSNVEICPHAKLIGPTKPPLYRSVTWNEYLGTKAKHFNKALSSVRLCTPINGLFDVNDSNKNSVQVG
What is the function of this protein?
Converts the inactive gibberellin (GA) precursors GA9 and GA20 in the bioactives gibberellins GA4 and GA1.  Has a small activity on GA29, producing GA8.  Unable to convert GA20 to GA5, GA5 to GA3 or GA12 to GA14.  Involved in the production of bioactive GA for vegetative growth and development, but not for the 3-beta-hydroxylation of GA in developing seeds.
What are the official names of this protein?
Gibberellin 3-beta-dioxygenase 1, GA 3-oxidase 1, Gibberellin 3 beta-hydroxylase 1.
What is the protein family that this protein belongs to?
Belongs to the iron/ascorbate-dependent oxidoreductase family. GA3OX subfamily.
Protein: HEM3_ALKMQ
Sequence: MRTIKIGSRASQLALVQAEIIINMLKEKFPQYTYEIIKITTLGDRILDKTLDKIGGKGLFVKEIQKALAEEKIDLAIHSMKDMPGETPEELVLGAITKREDPRDVLITRENKSLEELPKGAVIGSSSLRRQAQVMALRGDIKVVPIRGNVGTRLGKIETESLDGVILAAAGLNRLGLKEKISSYLEIEDFTPAVGQGALGCEARRKDIEMLEMLLAINHEETYRCVMAERAFLKLLEGGCHVPIGAYGQQQGQELHMTGMVASSDGRRVIKEQVMGDIADFQALGIQLGETLIEKGAKEILETVNTDNRIVNTEGS
What is the function of this protein?
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
What are the official names of this protein?
Porphobilinogen deaminase, PBG, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase.
What is the protein family that this protein belongs to?
Belongs to the HMBS family.
Protein: S40A1_HUMAN
Sequence: MTRAGDHNRQRGCCGSLADYLTSAKFLLYLGHSLSTWGDRMWHFAVSVFLVELYGNSLLLTAVYGLVVAGSVLVLGAIIGDWVDKNARLKVAQTSLVVQNVSVILCGIILMMVFLHKHELLTMYHGWVLTSCYILIITIANIANLASTATAITIQRDWIVVVAGEDRSKLANMNATIRRIDQLTNILAPMAVGQIMTFGSPVIGCGFISGWNLVSMCVEYVLLWKVYQKTPALAVKAGLKEEETELKQLNLHKDTEPKPLEGTHLMGVKDSNIHELEHEQEPTCASQMAEPFRTFRDGWVSYYNQPVFLAGMGLAFLYMTVLGFDCITTGYAYTQGLSGSILSILMGASAITGIMGTVAFTWLRRKCGLVRTGLISGLAQLSCLILCVISVFMPGSPLDLSVSPFEDIRSRFIQGESITPTKIPEITTEIYMSNGSNSANIVPETSPESVPIISVSLLFAGVIAARIGLWSFDLTVTQLLQENVIESERGIINGVQNSMNYLLDLLHFIMVILAPNPEAFGLLVLISVSFVAMGHIMYFRFAQNTLGNKLFACGPDAKEVRKENQANTSVV
What is the function of this protein?
Transports Fe(2+) from the inside of a cell to the outside of the cell, playing a key role for maintaining systemic iron homeostasis (PubMed:15692071, PubMed:24304836, PubMed:22178646, PubMed:29599243, PubMed:30247984, PubMed:22682227, PubMed:29237594).  Transports iron from intestinal, splenic, hepatic cells, macrophages and erythrocytes into the blood to provide iron to other tissues (By similarity).  Controls therefore dietary iron uptake, iron recycling by macrophages and erythrocytes, and release of iron stores in hepatocytes (By similarity).  When iron is in excess in serum, circulating HAMP/hepcidin levels increase resulting in a degradation of SLC40A1, thus limiting the iron efflux to plasma (PubMed:22682227, PubMed:29237594, PubMed:32814342).
What are the official names of this protein?
Solute carrier family 40 member 1, Ferroportin-1, Iron-regulated transporter 1.
What is the protein family that this protein belongs to?
Belongs to the ferroportin (FP) (TC 2.A.100) family. SLC40A subfamily.
Protein: YHV3_SCHPO
Sequence: MEVPRASPNQEPLCSISPSSLVINEIITVVTAIRKTTRWRNSGVASILGVSTLKDEFLADGLESRWKTNGEKSSSIRYPLVMEFSQLKEDLTNRASLNGYDSLKLLSPFLRTIKSPRMTGYITSLCLSAILKFFSFRIISEESPNLALSMRNLSFAITQCRFESFDASQDEAVLLRVSRLMEELLRGPGKAVLSDDSICEIVETGLSMCCQSRLSQVLRYSAELSMTSILEKIFERLKYIDVKTDSEDFWDASEEHSIKGEEFHYKKITEGDEISNEIDPFGIGSIREVFRVLVSFIDFGKQKFSDNIKAMALRFINTALEVSGSHISDFPSLRVLITDTLCKSLLQLIRSDHTALLTNSLLVMTTLLQAMPGSLKLQQELFISYLISCLHIPSTTPRERNVETSLHKVVSSLDLSEEISPDRATPTSFTERKRFAFDTRNRPPEVRELIVECLGSLSRIPYFLIDLYVNYDCDPQMSDLAIDLLKVLTRNCLVDSARYSTANVPPLCLDALLNFIYYFHEHLQPCYNDPNNTFKDDVAKTLIESKKRKAIIIEGAELFNESPSDGIAFLTQHSIIKQSDNPTCIVEFFHSTNRLSKRVLGEFLTKGSNSHILNAFISAFDFKGKRIDEALRLLLQSFRLPGESQLIERVLETFSHYYMSANPDSMSSKDAAFVLSYSIIMLNTDQHNPNIKSQRRMTLDDFCRNVRGVNDGQDFDRNFLSEIYKAIKENEIIVAEEHDTELSFLYIWSKLQQSVKITEPFKRSSSNVHDKIVFLEVWKSIMAALIYVFSTATEDTVFYRVVNGIQQATEVAAAYELNEPVDYAIERFCQFTALDPSSVPGTQLNTAIKVEDRIITVSELSVRFGRDFRAQLALLVLFWISSKFGNIIDASWPLLVQLTICLARNNLIDNSFLPGFKLFGYQWFPFPEPPLNSGKPALSKEGGLLSALSSYLSSYANDEPPCPTDEEIQHTLCTIDCISSAKIDNFLTKLVDLKQPGLNKLLDSLLSLSNPSTSLLTDENTVDDNKVSSVEALSNIQSAIVADLLTSLFLGTRESLNKLERRTQILSYLLFQIEQSGDEKVINQLSLYIFEMFMDDDLKLSENSEDWGLFSKLCNLLNDKNIVVRNQSLSLFHQLVNKYPFLLESWIGLQLVQSAVNTNTADIDDLYRLLSKIPTNLLDLPMFQVYLGCVDTLIQTIVKQIAQILSKQKKGASKGLPFDKSILDNHSAELNDAFNLFLKAAVEYKVDSNESSEHFQDTRWKIIYDHVCKLCLSRSRSLRAASLSCLQRIVVEQLDQPHEVSYTMALFHLVLLPTMENMITVLTEKPEHKIFGLAQAQMFNIICKTVLIDMNVLSAQKEMLHTLWLKLMDVAIKLSSIHGSESMAEVMESIKNVFMILHGAGALAGPTIEVDPEIPDHLIKTWNTTWNNLFIYYPELSNDLNINNEAEMKKENLKNPSQTTTV
What are the official names of this protein?
Uncharacterized protein C211.03.
What are the subcellular locations of this protein?
Cytoplasm. Golgi apparatus membrane; Single-pass membrane protein.
Protein: RL11_PSEMY
Sequence: MAKKIQAYIKLQVKAGQANPSPPVGPALGQHGVNIMEFCKAFNAKTQGMEPGLPTPVIITVYSDRSFTFETKSTPASVLLKKAAGLTSGSARPNTVKVGTVTRAQLEEIAKTKQADLTAADLDAAVRTIAGSARSMGLNVEGV
What is the function of this protein?
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
What are the official names of this protein?
50S ribosomal protein L11.
What is the protein family that this protein belongs to?
Belongs to the universal ribosomal protein uL11 family.
Protein: TM186_DANRE
Sequence: MDMMMMSTRLIHLSRHFPQYGFRCHPSGLISSARMQYNINNGLAHMGKQMPNTSTHTTRIHPASFSSDLASRKYSLIYAFPLIRGLRALSRLKLLQTGITVVLLPTVYYLHLQGQASVLVLNRSIGIALFAGVMLYSISHFVRRVVGMMYLDSTQTILKVSHLSFWGHRRDIYVPVSDVVTLGDSGDSRGESILRLKRYSTSNTMYFSTRLGRVVDRHAFGKVFGSLS
What is the function of this protein?
May be required for efficient assembly of the mitochondrial complex I.
What are the official names of this protein?
Transmembrane protein 186.
What is the protein family that this protein belongs to?
Belongs to the TMEM186 family.
What are the subcellular locations of this protein?
Mitochondrion inner membrane; Multi-pass membrane protein.
Protein: BETA_ACIB3
Sequence: MNIKEYDYIIIGAGSAGNVLAARLTEDKDTTVLLLEAGGPDYRLDFRTQMPAALAYPLQGRRYNWAYLTDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLEQWATHKGLENWTYADCLPYYKKAETRDIGGNDYHGDSGPVSVATPKNGNNVLFHAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRSSTARGYLDMAKGRPNLTILTHATTNKILFNQKQAIGVEYIIGADQNNLQRALVKREVLLCAGAIASPQILQRSGVGQSTFLKSMDIDVVHDLPGVGENLQDHLEMYLQYKCKQPVSLYPALKWYNQPAIGAEWLFNGTGIGASNQFEAGGFIRSSDEFKWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIKLKSKDPFAHPSILFNYMSTEQDWREFRDAIRITREIMHQPALDPYRGDEISPGKHLQTDAELDDFVRNHAETAYHPSCSCKMGEDEMAVVDGQGRVHGMNGLRVVDASIMPLIITGNLNATTIMIAEKIADQIRGREALPRSTAPFYVAS
What is the function of this protein?
Involved in the biosynthesis of the osmoprotectant glycine betaine.  Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate.
What are the official names of this protein?
Oxygen-dependent choline dehydrogenase, CDH, CHD, Betaine aldehyde dehydrogenase, BADH.
What is the protein family that this protein belongs to?
Belongs to the GMC oxidoreductase family.
Protein: C149A_DANRE
Sequence: MANQLRETHQSLKKKYRELIDGESSLPPEKRNQVNLAQLLMDSRERNKQLAEEVKEVTQRLSETQGDNKLLRMTITKQRLGDDEVGIRHFPAHEREDLVRQLEKAALHREELEHTLKTLSDELQDVKAERTVFKEKSKRLNLELNHILGGQEKRIIDVDALCMENKYLHERLKQVQEEVSLLKSNIQKYKTALDRRKNPEIGGKSSSRSLTGVLSPKQVHGFLSEENGCSLPATPQSISDLKSLATALLETIHEKNIIIQHQRQTNRILGNRVADLERKLKTLEISGLWSLPDDRTGRGGPSLWERDTAGDDSFPNMWRGSRPGPDGGAGEEDTPVTREESDPSGTRTNGQVGTQLKEKKTACCPVTEVIAAVEELCVVLEAEDAVLALDPAGLQLQWTQTPSVTLEQSACKNTDIKNSAGSPATDLGEISEGAAVKIEPIEESGSSFVS
What are the official names of this protein?
Coiled-coil domain-containing protein 149-A.
What is the protein family that this protein belongs to?
Belongs to the CCDC149 family.
Protein: CH10_BACTN
Sequence: MNIKPLADRVLILPAPAEEKTIGGIIIPDTAKEKPLKGEVVAVGHGTKDEEMVLKVGDTVLYGKYAGTELEVEGTKYLIMRQSDVLAILG
What is the function of this protein?
Together with the chaperonin GroEL, plays an essential role in assisting protein folding.  The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.  GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
What are the official names of this protein?
Co-chaperonin GroES, 10 kDa chaperonin, Chaperonin-10, Cpn10.
What is the protein family that this protein belongs to?
Belongs to the GroES chaperonin family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: DEF1_HEUSA
Sequence: DGVKLCDVPSGTWSGHCGSSSKCSQQCKDREHFAYGGACHYQFPSVKCFCKRQC
What is the function of this protein?
Possesses antifungal activity insensitive to inorganic cations.  Causes germ tubes and hyphae to swell and form multiple hyphal buds.  Binds to the plasma membrane of the fungus.  Has no inhibitory effect on insect gut alpha-amylase.
What are the official names of this protein?
Defensin-like protein 1, Cysteine-rich antifungal protein 1, Defensin AFP1, HsAFP1.
What is the protein family that this protein belongs to?
Belongs to the DEFL family.
What are the subcellular locations of this protein?
Secreted.
Protein: DNLJ_AERHH
Sequence: MSDILSRHRQLCELLIEYGHQYYVLDNPTVPDAEYDRLMRELIVLEAEHPELKTPASPSVRVGGQPLTAFKQVRHEIPMLSLDNVFSGEELQAFEQRMRDRLKREVSFTFCCEPKLDGLAVSLLYVAGQLVQAATRGDGTTGEEITENVRTIKAIPLSLRGEGWPARLEVRGEVFMPKAGFEAMNAKALAAGEKVFVNPRNAAAGSLRQLDSRITASRPLAFYAYGVGVGGEQLGGSHFGRLNQLKEWGLPLSPEVKLKEGAAGCQAFHDDILARRGELPYEIDGVVYKVDAIPLQEELGFVARAPRWATAHKFPAQEEMTELENVEFQVGRTGAVTPVAKLKPVFVGGVTVSNATLHNADEIERLGVMIGDTVIVRRAGDVIPQIVAVVEAQRPADARAILFPTECPVCGSAVERLEGEAVTRCSGGLFCEAQRKEAIKHFAARRAMDVDGLGDKIVEQLVDKGLVKTPADLFSLNAIQLAGLERMGQKSALNLVAAIDAARSTTLPRFLFALGIREVGEATALNLANHFLTLDALRAASVEQLLEVADVGDIVAKHVYYFLRQPHNIEVLEALLAAGIHWPAIEKKEASEQPFAGKTFVLTGTLTTLSRNDAKAALQALGAKVAGSVSAKTDVLVAGEAAGSKLVKAQELGITVWSEEELQQALQG
What is the function of this protein?
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.  It is essential for DNA replication and repair of damaged DNA.
What are the official names of this protein?
DNA ligase, Polydeoxyribonucleotide synthase [NAD(+)].
What is the protein family that this protein belongs to?
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Protein: THIC_PROMP
Sequence: MRNSWIQPRIGQKNITQMNFAKNGHITEEMNYVAKKENLPPSLIMEEVARGRLIIPANVNHVNLEPMAIGIASKCKVNANIGASPNASDINEEVEKLKLAVKYGADTVMDLSTGGVNLDEVRQAIIKESSVPIGTVPVYQALESAHGSIERLTEDDFLHIIEKHCQQGVDYQTIHAGLLIEHLPKVKGRITGIVSRGGGILAQWMLHHFKQNPLYTRFDDICEIFKKYDCTFSLGDSLRPGCLHDASDDAQLAELKTLGELTRRAWTHNVQVMVEGPGHVPMDQIEFNVRKQMEECSEAPFYVLGPLVTDISPGYDHISSAIGAAMAGWYGTAMLCYVTPKEHLGLPNAEDVREGLIAYKIAAHAADIARHRAGARDRDDELSHARYNFDWNKQFELSLDPERAKQYHDETLPEEIFKKAEFCSMCGPNHCPMNSKISDETLDELNNKLTKCDTSV
What is the function of this protein?
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
What are the official names of this protein?
Phosphomethylpyrimidine synthase, Hydroxymethylpyrimidine phosphate synthase, HMP-P synthase, HMP-phosphate synthase, HMPP synthase, Thiamine biosynthesis protein ThiC.
What is the protein family that this protein belongs to?
Belongs to the ThiC family.
Protein: NDK_WOLTR
Sequence: MAIERTLSILKPDTVKNNIIGNINSYIEKSGLRIIAQKMMLLTKKQAELFYAIHKDRPFFGGLVEFMTSGPVIVQVLVGENAISKYRQIMGATDPKQADKGTIRGDFADDVNENRVHGSDSLENAHKEIAFFFAECELV
What is the function of this protein?
Major role in the synthesis of nucleoside triphosphates other than ATP.  The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
What are the official names of this protein?
Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase.
What is the protein family that this protein belongs to?
Belongs to the NDK family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: IDI2_PYRAE
Sequence: MGIDKRKDDHIYLASSELSQIGSAWFEEVVLIHNALPEIDLSEVDLTTRFLGAPVKAPFGIGAMTGGTELAGKINAELAKAAEEFGIPIYVGSQRIALVKPEVKWTFEVVKQNAPHVPKVANLGAPQLAELGERELEEWVVQAIDMIDAYAIAIHLNAAQEVVQPEGEPRFKGVLEKLKIVKRAAGKPLIVKETGNGISKEVAARLSGIADAIDVGGFGGTSFVAIEGARAKESPLQKRLAETYKWWGIPTAASICEVKSAYAGYLIASGGIRSGLDGAKAIALGANFFTMSQPLLKAALDGRLREEIAMIIAELKTAMFLTGARTVQELALVPRVYGPRLRNWIEQRRLTC
What is the function of this protein?
Involved in the biosynthesis of isoprenoids.  Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
What are the official names of this protein?
Isopentenyl-diphosphate delta-isomerase, IPP isomerase, Isopentenyl diphosphate:dimethylallyl diphosphate isomerase, Isopentenyl pyrophosphate isomerase, Type 2 isopentenyl diphosphate isomerase, IDI-2.
What is the protein family that this protein belongs to?
Belongs to the IPP isomerase type 2 family.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: AYG1_ASPFU
Sequence: MPRWILGDKFDTVFPHKGSLKVLWESRWKSACSKSVYPFHDGSIEDFEPIFNHLISKNINDAASDEYTQAFLPTASALEEKAAQALQAGKHEEASNLLCRAAVVYRISRFPYVDITKPSSIKRVAFERQKQAYLKATSLWTQPIREVTVPHTYRTGNDGAHIPIYIRTPAGADQSNPVPIVLIMTGLDGYRSDNSQRTHEILARGWAAVVAEIPGTADCPADPADPASPDRLWDSVLSYLDQRPELNTAKMVVWGLSAGGYYAIRAAHTHRDRLLGAIAHGPGCHYYLDPEWLAKVNDHEYPFEITAAWATKHGYKTVEEFVAGAQKKFSLVETGIVDQPSCRLLLLNGVDDGVVPIEDCLVLFEHGSPKEGRFYKGLPHMGYPNSLPVSYEWLEQVLASPSKTKN
What is the function of this protein?
Heptaketide hydrolyase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:11350964, PubMed:15310761, PubMed:19156203).  The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA (PubMed:10515939).  The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayp1 though chain-length shortening (PubMed:10515939, PubMed:11350964).  1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone (PubMed:10515939, PubMed:11350964, PubMed:15310761).  The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN (PubMed:10515939).  1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone (PubMed:10515939).  Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN (PubMed:10515939).  Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin (PubMed:10515939).  DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize (PubMed:26972005).  DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins (PubMed:19703288).  DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses (PubMed:19156203, PubMed:20145078, PubMed:21501368, PubMed:21747802, PubMed:21573171, PubMed:24818666).  DHN-melanin protects also conidia against amoeba predation (PubMed:25684622).
What are the official names of this protein?
Heptaketide hydrolyase ayg1, Conidial pigment biosynthesis protein ayg1.
What is the protein family that this protein belongs to?
Belongs to the AB hydrolase superfamily.
What are the subcellular locations of this protein?
Endosome.
Protein: SPEH_THEM4
Sequence: MKSLGRHIIAEFYDCNKEILDNVEAIEKSMKEAAYETGATLVNSSFHRFLPYGVSGVVVISESHLTIHTWPEYGYAAVDLFTCGDDVDPWKAFSYLKKILKSQRVHVVEHLRGKYDEIGIPENSPHKMEV
What is the function of this protein?
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
What are the official names of this protein?
S-adenosylmethionine decarboxylase proenzyme, AdoMetDC, SAMDC.
What is the protein family that this protein belongs to?
Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
Protein: NADB_SYNY3
Sequence: MGANQFDVVVVGSGAAGLYACLCLPGHYRVALVTKAELKTGASDWAQGGIAAAIAPTDSPQSHYEDTLAAGAGLCDGEAVDFLVNHAPQAIAELVQFGVSFDRHGQHLALTLEAAHSQPRVLHAADTTGRAIVSTLMGQVQARPNVEIFSQAIALSLNIEPTTGHCRGIQVFVNQTIETFHSRAVLLATGGGGQVFAQTTNPKVSTGDGIALAWRSGAQVRDLEFFQFHPTALTKPGVPHFLISEAVRGEGAHLLDRQGKRFAFDYHPRGELAPRDVVSRAIFQHLANTEKDPTQATVFLDLSPIEPERIQRRFPNIIRRCLHWGVDIFREPIPVAPAAHYWMGGITTDINCQTTIPGLYALGETASTGVHGANRLASNSLLECIVFASQLRNLSLPPLASSDSNVNQSIKEIRLDTTNDLALLNHWRSELPRLMWQTAGICRQAETLQMAIAKLEQWQEQWQQLSSSKLLAHLPEDQKISLSGPGLNEFMQLWAETHNLLDIAQLILTSALFREESRGGHYRLDCPDTKREWQSHTVIEGTRVFLQPSQSQD
What is the function of this protein?
Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+).
What are the official names of this protein?
L-aspartate oxidase, LASPO, Quinolinate synthase B.
What is the protein family that this protein belongs to?
Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.
What are the subcellular locations of this protein?
Cytoplasm.
Protein: RNFA_PECCP
Sequence: MTEYALLFVSILLVNNFVLVKFLGLCPFMGVSKKLETAIGMGMATTFVMTVGSMFSWLVNEFILVPLDILYLRTMAFILVLAVVVQFSEMFVRKVSPELYRLLGIFLPLITTNCAVLGVVLLNINLSHGFLKSTIYGFGGAAGFSLVMVLFAAIRERLAVSDIPAPFRGSSIALITAGLMSLAFMGFTGLVKF
What is the function of this protein?
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
What are the official names of this protein?
Ion-translocating oxidoreductase complex subunit A, Rnf electron transport complex subunit A.
What is the protein family that this protein belongs to?
Belongs to the NqrDE/RnfAE family.
What are the subcellular locations of this protein?
Cell inner membrane; Multi-pass membrane protein.
Protein: WWP2_HUMAN
Sequence: MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQWQSQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPALPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRHYTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFGQE
What is the function of this protein?
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.  Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level.  Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death.  Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2.  Ubiquitinates RPB1 and promotes it to proteasomal degradation.
What are the official names of this protein?
NEDD4-like E3 ubiquitin-protein ligase WWP2, Atrophin-1-interacting protein 2, AIP2, HECT-type E3 ubiquitin transferase WWP2, WW domain-containing protein 2.
What are the subcellular locations of this protein?
Nucleus.