ID R7YS42_CONA1 Unreviewed; 4005 AA.
AC R7YS42;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=W97_03958 {ECO:0000313|EMBL:EON64725.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON64725.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR EMBL; JH767570; EON64725.1; -; Genomic_DNA.
DR RefSeq; XP_007780042.1; XM_007781852.1.
DR STRING; 1168221.R7YS42; -.
DR GeneID; 19901269; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_1_1; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016924; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016924};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3669..4005
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 214..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1941..1982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2018..2037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2301..2387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2420..2491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2802..2904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2977..3003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3283..3367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..1976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2301..2318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2353..2387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2420..2480
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2802..2859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2877..2893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2977..2993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3293..3329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3351..3365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3972
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4005 AA; 445238 MW; 7399C29EC613385E CRC64;
MGRIKKSAAP KHGATLSPYV ADFIEKTTRS VPLHELPAHL ASFPRHWPFP RGDLYHWIPV
LNRFDSILEH FVQEYGLSEP QTQPFERRLL LKGDEEQPSA VPPSEELLDN LGLSGEGDRE
LIEAVLSFTR LLLENCGNRS LYSSSSHLNS LLHTTSLSLL KNTLRLSLRL AQRYHASRIR
AAAVAMQPSY LASHYDLNLD RVLKLAQPFV RGPASTSTFA SLSTKGKGSV GAESGTPTTS
PTPSDLVSIV KTDSSAASHW EDFGNIHFTY YDASDAAPET ASKHTTQDAP SSASPGTPTP
LRRTTSLGPH QTPRQNRPSA MGESPSTKGI SPGQPSTDNR PSGPKALQIP PPRLLSEPPH
EILSSLIPEV PPSMRFELLQ RIRVAHAIVS SQATRQDIVA IRLLAIANLA YVYPAPTFQA
EIAQQDSDEP RRLQLTYQLS ELVHPPAHSG PSVPRELQTL ALETLEALTK HKEKAVDVST
ALSVNVNHGV LFYVVRKAVA ELSTDESSQD RAEEDEWREA LFSLLNSLPG SQARLGESMV
SAGLLEILVE VLTLRTHKAE RTHPKVLNFL DMFVYNLRDA FQALVNAKGL DIIADLTAYD
VETSYSEAEK GHGLPPEYKT QMTDYKIPFY KQQTLRLLFK FMNHMITHAS GNSDRAIRNL
IDSPQLLRSL RTVLGNAPVY GSTVWSMTVS ILSNFIHQEP TSYNIIAEAG LSKEFLEAVT
GKPISDDRPL PTASEGQAEP PAQSILPVAE AITTIPQTFG AICLNESGMK LFRRSGAMEG
FLEVFESPEH VKVLEADAEA ATAIGGAFDE LARHHPRLRP AIVKAVSKTV VRVVQLCFSQ
AAHHGAGSKL WVDAGEGRLK VVGGRRAVLG EEGQKHKQAR LRQEQRRASA GADVVMQDVN
ARPWTEEFLS RDVFSDEIEE ATDSKDASIT TKYVAVLARF LTGLFNNNNI CAEFASGGAL
EYALDLTTLP SLPYNFGDDV GTSDEVGRVI QFLVDAKPHL ALPPLLKRAL RAVATLEPFL
EHEEPSAFFS AFTTPSDDQD SRTGSSRADV LCNGTRYVKA LVNLHTVCNA LTMAMGVPFH
AHRSAPTVFQ QVNVADMYSL LVDGLGRLQR SCVWEEILLQ RHMPKAWEPE TRVSGASFGG
EEADDVLHIQ HNNSNVTMNT SESNGQGSPT EPSEEQDRAA VQSKLDEEKK TAQFKNTKTL
RYLLSQVPIV ITNFFQGLGK VLLSRRGSQD SYMRQNAQIV ADELALSAIN QLKFELPNTA
GNIDDKYAYQ VIILTSTLQI MLDTDLMDRA YPQTLTLVLQ SFKDRNGFEA LADILGNLIE
TLEPGDNAEN GDTPERRHVR THLVLGGIKV ILEFYSQVIS SKNVSEAPQT QYLSRNVPDR
GRAEFFSASQ FLVEIRAKVV KQVQRLWTSN LIDKATTSVV KHLVEILKIV LEGDAENGAL
RRAEENVARK PMELKPWKSR NPDTLVRLKA KGFDEELALE ALFRCYDNHH AAEEYCNAQK
LDSRASRNPV PATMIERPSK PQEAQIQTGQ SAEGAQQQNV SGGIEGPDES NQTPSSAMQD
VETAGPADPF GLDDDPFTGL PWEETHSFGQ PTPAAPSGDG SADGSANVVT LEDLDEDRSN
LRATLIDRSL DILTVHDDVT FELSELIFAA VPKGNEAAAS AMRGEIGSTL LNSLISLQTD
EVLGSEGKKI AAYAHLLALI LQDRRFYEAT LDELKDNFEN LLSFIKMPHE QRSEDTPQWI
GQVLLILERL LAEDAQPNKI DWTPSEENPQ PGTPIAELPE PLVSLEQKMQ LFSVLLEITP
RIGKDQSLAL SVIRVFVILT RNRQIATQLA EKRNIQRLFL MVKQLAGSMG ERIQSSFMIV
LRHIIEDDET IRQIMRSEIQ AMFRNRNARQ TDTTAYVRQT YHLALRAPEI FVKVTNETLM
FARYDSRGGG GPQILALKKE DKPVAERSDA QGKDAGPAAS SAEQVTTEQV QPSTEQVDND
EAEKLKAQEL KYPVVENPDG VIHYLLCELL TYKDVEDKEQ SAAPKEPHIE SEETTPVDIE
MTDEDMRSAS ATPVPTAPLS AKKSERPDFK ADQHPIFVYR CFILQCLTEL LSCYNRTKIE
FINFSRKADP HVMTPSKPRS GILNYFLNAL IPVGTLGHPE DITSRKKSST SNWAISVLVS
LCERTSEAGV PDVRTSGDTE DEPELAYVRR FVLEHALKAF RDASTSSEPQ DMKYSRLLNL
ADMFHRMLTN RNNSGHQPTQ DAFTASQKHL AKMMYDKNFI TTLTLSIADI DLNFPGAKRA
VKYILRPLKL LTKAAYELSL SGDISSSPGQ TTEDDEISTA TSVTDDTDDV REETPDLFRN
SALGMLEPGR EEESDSTSDD DDDEDMYEED YGEEMEYEEE IGHDNGEVVS DEDEEIEAMG
DIEGLPGDVD MTLEIGIDDE EIDGMSEEDD EDDDEDEDDG IEVMEEVTGD DEGGSPAEGD
DDDWASEEEE EEDYPGQDEI EDDQVLPPPL PHIVDVIQGN RDIPQILEQL EQFTQDDHAP
SQRCLLTHFL DDEDDEEEYD DEEIIYEPDY DEGLQADHLS LNQLRHLLTV LTDEEGAVWA
RAMPPPGHRH HHHIHHHRGS PWTLFGNPLH ADRLLGLPNY RSHRPGGAQR PNDDGVNPLL
QRSGRAVTSG RRNAQSDPFG DWVYDIDPIR GPGAVRAGIG EGPVSVINNL LSAMSGAPIH
ASGGALHFTI TGGPPGSAPI PPVEAFEALR HRTQRPREPA LRPSRDDLAQ VVAFVPAGTS
SRWQDEARIL FGSAAFEKAT RVVNSLMKLL VPPAIEAAKK RAQEEAERRA KERKEREERE
EKEKKEREER EAREAEEKKA QEAAEQAARE LEEAQARAEQ ARDTAGPIEA VEEDQSMEGV
EQTQPSTATA TAEAGPAEAQ PRITTTLRGR ELDITGMGID LEYLEALPDD LREEVLMAQV
AEQRSQAAAA GEEPTDISRE FLEALPAEIR EELLQQEAQD RRRREREEAR RRAAANGGPA
ARAEEMDAAS FLASLDPGLR QAVLLEQDEE MLAQLPGDIA LEARALGGDR RLNQFMDISR
VGRPRALDRT EQLDDQASKK SKPRPVVQML DKAGVATLLR LMFIPQQGSV RGTLNGVLKD
ISENRQNRAE IISILLSILQ DGTSDVNAIE KSFAHLSLRA KQPGTQKTPQ PPKRTLTGQF
PINSEISPLT VVQQCLSSLG YLVREVSHMP AFFLTEHETA VGFKSRANRK GKGKDSRANR
FPLNALLGLL DRKLIIESSS IMEQLASILQ AITTPLTLLN RKEKEKNDEQ KKVASTQQAS
SSETQTQAPA AGSTDTEMGS AQDTQAQPAA DASALDAGDN PPTASAGDGK AENQTDDKSK
KPRLLVPPEV PDANLRLVIN ILAARECSSR TFRDTLSMIN NLSVLPGAKE VFGKELVKQA
QDLGQAILKD LDDLVMQISK AETSTDVQGM ALARFSPASS DQAKLLRVIT ALDYLFDPKR
AGTEDKPVPS NTEGLPTEQN EDILTTLYEN PTFGSLWSKL SECLTAIRQR GNMFNVATIL
LPLIEVLMVV CKNTTLKDAP LSKIHHREIT LSSPPPESRM ENMFFAFTEE HRKILNDLVR
HNPKLMSGSF SLLVKNSKVL EFDNKRNYFT RRLHHRGPNE IRHSHQPLQL AVRRDQVFLD
SFKSLHFRSG DEMKFGKLSI RFQGEEGVDA GGVTREWFQV LSRQMFNPDY ALFIPVASDR
TTFHPNRLSS VNQEHLMFFK FIGRIIGKAL YENRVLDCHF SRAVYKCILG KPVSIKDMET
LDLEYYKSLL WILENDITDI ITETFSVETD DFGEKQIIDL VENGRNIPVT DENKHEYVRL
VVEYKLTGSV KDQLENFLRG FHDIVPAELV SIFDEQELEL LISGLPEIDI DDWKNNTEYH
NYTAASPQIQ WFWRAVRSFD QEEQAKLLQF VTGTSKVPLN GFKELEGMNG FSRFNIHRDY
GNKDRLPSSH TCFNQLDLPE YESYEQLRQQ VYTAMTAGSE YFGFA
//
