ID A0A178A7T9_9PLEO Unreviewed; 3978 AA.
AC A0A178A7T9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=IQ06DRAFT_261938 {ECO:0000313|EMBL:OAK93661.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK93661.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK93661.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK93661.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441730; OAK93661.1; -; Genomic_DNA.
DR STRING; 765868.A0A178A7T9; -.
DR InParanoid; A0A178A7T9; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000077206; 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:UP000077206};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3642..3978
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 211..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1922..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2003..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2313..2341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2378..2479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2599..2631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2765..2871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2909..2940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2962..2991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3309..3345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1948..1967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2378..2475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2765..2818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2844..2859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2918..2934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2962..2978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3325..3344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3945
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3978 AA; 441460 MW; 7422360942CEB09C CRC64;
MKIKKQATSR HESTLSSMIA DFVRATESIP LYQLPAHLAS FPKHWPFPRG DAYHWIPVLN
RFDRILELFN QEYGLVDGPQ TTPFQRRLLL KGDAEEGSTG TDHTTTDAVL DTLHVSQDGD
RELVENILNF TRVLLENCGN RSLYASSERL DKLLNSTSTS LLKATLRLGH RLAQRFSAAR
ARLGSPSQLH LSLLNSHYNI SLEKLQKLSA PLSKGPSAAP PVFGTPTGKG KDKALADRRS
DSDRVSPSDL VGLYTLSDSS LKQEFGGVAL SYYEPTTSPP EENTTRPAPT DVPTTPTPVR
RTSNMGPNRT PRQTQAPPTA ESPITPGFTP GQSGGKPAGP KTFEFSADKV SSSDLHELVK
QGLANLPDTV HYEFFHKLRT AKLLSGGSAG RDDAIALRML ALANSGYVYG DKDFHAKIGQ
QDADEPRRLQ LAYQLSELVH PPGNGERGIS VELQTFTLNA LEALAKHKAK AADICTALSV
NVNHGVLFYL VRKLVAGLGS ETSSVGDLEE DAWRDALFSL LNTLPGTQQR TGEGMVSAGL
LEILVGALEL RTEKAERNQP KVLNFLDTFV YNLRDAFQAL VNAKGLDVIA SMMEYEVDIA
KKLAEDGKGI PQEYKTHLTD YQIPFYHQQT LRWLFKFLNH MMTHSGANND RLMRTLIDSA
QLLTGLRTVL SNARVYGSTV WSTAVTILTS FIHNEPTSYQ VIVEAKLSQA FLETVAGEPA
AESPEALNED NGDSDPSVQR IYPPREPGTP LAAGILPIAE AISTLPLAFG AICLAESGMK
LFQSSTALKH FFEIFESPAH IKALDADTEM PTMIGNSFDE LVRHHPPLKT RVLSCLSEVI
ARVVHLCAEK AEKEGVGSKL WTEDAQGKLV VAGGRCALSG PQMHHRVGQA LSPSGSDVVM
QGADDSAPGQ ASTDVVTADQ VTETEDATKG PTTGQYIRVL CRFLSGFFSN HAMCAAYIEA
DGVESILDIS SLACLDPRSN ESRSMTEEFS RVVQVLVEQK PHIAVPSLIK RTQQALQRLE
PMLDHTGMQA FFAPFTSAGG SQDQAVLNKG TEYIKSLVTA FTLVGAMTLT FQSQMYSSRG
AHNVANQVNL ADMYAHLVYG LGKLHRSCVW EELLLQRNMP TEWEKETRVK SSGFGNIEAD
LVFGMGPGDR PTDTAGPTAA EGSNDSNAAA IDASSTGIAV IPSQDSAQFK NTQTLRTLLS
KIPTEIAPFS QSLGKLLLFR RSVEAYQRQC ATVVSDQLAQ AVIDQLQYRG PQDSASPEDR
YAYWVVILTS LSQLMIDPNM DRPQALTLLL VSFRNLGGFE VLADILDKFY QSALEITQKQ
DDKASNDSQR LLNLSLGGIK IILAFYAHIT NLKVIGESQQ TSSMQSRPDR DRERADFFST
AQFLVELRFA VVKPIEKIWN SDLIDKATTS IVKTSINILK SVLDAQGEHG AHPTADKIPK
RSKPIIKPWT PRSAEYTTRL KEAGFSEALV EEALYRCCDN LNMAREYCQN QARPNSSRNP
IPQYELEARG PPSASPSRAE VVVPEHADSV SMSSSDNTQD EEGSEAPDTR SVEMEDVSTT
PAAAQPPGDV PTSDDQAEAS APSPHDALAY QTRMRAGNKA EPVAADALDK ERGQLRQNLV
DRSLDILNSH DDVTFELADL ITAAVARATE PGSMRTEVGT TLMQSLISFQ CEDDFRSQSK
KIAASAHLLA LVLQEKDFYD VIVEELKDNF VTLLGFIKIF PDQASEDSSP WVGQVLLIIE
RLLAEDQLPQ QISWTPPTGE STEDISIDQL PEPIVSLDEK NQLFDAIMEI LPRISKDESL
ALSVTRVLVM LTRTRKIAAR LAEKRNIQRL FLMVKQLAGI TNEGLRSALM IVMRHMIEDE
AMIRQIMGTE IQQVFESRDR RQTDTTGYTR QMYAHAIRAP EIFVEVTNEK LQLARFDPNQ
RPQTLVLKRE DSPPVTSDTA SGANDTPAEE DQPKETTEPR PSILERTKTA DLKVPVVENS
DGVIHYLLCE LLAYKEIEDS PEIAKPTEGA PTDARGPSEQ ANDAESSPTS TPATPAPEPN
KPEKPVFKAD AHPIYIYRCF LLKCLAELLQ SYNRTKVEFI SFSRKADPYT TTPSKPRSGV
LNYLLNTLVP IGTLNHEGDL AFKKKLATST CAIDVIVSLC QKTGEVAVPK GEAQQMPYAE
NEPDLLFVRK FVLEHALKAF RDANASDEPL DMKYSRLLTI SDIFSRMVSQ RPTGEMIAQN
TELTSSLKQM AKVMYEKNFI TILTTAISDI DLNFPNAKRV VKYILKPLKW LTFVAMDLSM
HYDTSTAPDS ADEYEIETAS DDDLVDNTRE ETPDLFRNST LGMFELPNNS ESDDSDDEDG
EELMYDDQYA DDMEFDEGDI GDNDEVISED DDDIMEADLD EMGPMDPGDI EIEVEMPDDG
DDMGSLDDSE DDDEHDEDDE DDDGMDDDED DEMDDMDEED EEGALEALEA LEEITGDDEN
ASLGEDPEDE WSDDPGDYGG VNGEGIMPSG AVGLVLDTPS QLLEHMRHSE MGIDDFMEDD
MGEEDDEEED YDEYDEDEIH FDAGMEDEED DMHEMSGWTG AWDDPGPPTH RHAHRLSPWM
FPAGPGDRIL VPAYRSHRPG AGPRATDDGV NPLLQRGGRS QGRGNEGPFR NEGMSDWVHA
IEGRGPRVFN ADSPVSFISN LLNAMSQGSG PTLTQAGGAL QLSFNNMPLG MPHPFETNLR
RDAARMRENQ ISRSAREDPN SAIAFAKVST STRWQEEARV LYGPSAIEKS QRVVNTILKK
MVPPAMEAAK KRQEEREAEA ARKAKEEQEL KEKKEREERE AKEKEERERQ EREAAEAAAR
ATEPGTEAAP TEDSTPVTEP QAMEGVESAQ TSSDQPAESA SPAADARPRI MTTLRGHEYD
ITDLGIDLEY LDALPEELRE EVLMQQVAER RQEERAQRQQ QQQAQPQQAE PAAQGGDQPT
DIDEQFLAAL PPEIREELLQ QEAAERRRRE REENRRRNQT TAVPQAEDMD TASFLASLDP
TLRAAVLMDT DEDTLRQLPP EISAEARAYG GDRRLNQFNE YRREARRGQA DDSAQKKQSR
PCVQMLDKAG VATLLRLMFI PQQGSAKTSL SSILRYVCEN RQNRAEVISI LLSILQDGSA
DVNAVEKSFA QLSIRAKQPQ QPADKTPKLS RKNGALSINA DVSPLMVVQQ CLNTLTQLTE
KNRNVWLFFL TEHETGVGFK NRGNRKGKGK ETKASRFPIN ALLSLLDRKL IVESSSIMEQ
LTTLLHGITY PLIHLKKEKD KAAEEAKKAA EIATEPVRAA DLTAIVEQSV SAPEAQVQDT
EMNVATDTAA QPSTAAGEGE SSAAKSSEPK ADEAKAKKQR DMVPPEIPEN NLRLVAKILA
ARECNSKVFQ ETLSVISNLS PIPGAKEVFG QELLGIAKDL ASSTLQDLSS LTDQVAKAES
PTDVQGIALA KFSPASSDQT KLLRALTALD YLFDPSRDNK DKSGATAEAL EPAQKEDILL
SLYEDAAFAP LWDKLSACLT VIRQRGNMLN IATTLLPLIE SLMVVCKNTT LKEVPLSKML
PKEFALSSPP PENKMENLFF NFTEDHRKIL NDLVRQNPKL MSGTFSLLVK NSKVLEFDNK
RNYFNRKLHS RNGDRQPHPP LQLAVRRDQV FLDSFKSLYF KSADEMKFGK LSIRFHGEEG
VDAGGVTREW FQVISRQMFN ADYALFVPVA SDRTTFHPNR LSSINPEHLM FFKFIGRIIG
KALYEGRVLD CHFSRAVYKQ IMGKQVNLKD METLDLEYYK SLEWMLNNDI TDIITETFSV
EVEAFGEMQI VDLIENGRDI PVTEENKHEY IRLITEHRLT GSVKEQLENF LKGFHDIVPA
ELVSIFSEQE LELLISGLPD INVDDWKNNT EYHNYTAASP QIQWFWRAVR TFEKEEQAKL
LQFVTGTSKV PLNGFKELEG MNGFSKFNIH RDYGSKDRLP SSHTCFNQLD LPEYESYEDL
RKALYTAMTA GGEYFGFA
//
