ID A0A439DB59_9PEZI Unreviewed; 4078 AA.
AC A0A439DB59;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=EKO27_g3468 {ECO:0000313|EMBL:RWA11632.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA11632.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA11632.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA11632.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWA11632.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RYZI01000074; RWA11632.1; -; Genomic_DNA.
DR STRING; 363999.A0A439DB59; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000286045; 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; IPR016024; ARM-type_fold.
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; SSF48371; ARM repeat; 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:UP000286045};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3742..4078
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 213..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2017..2037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2071..2106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2363..2521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2576..2607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2687..2740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2802..2827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2876..2976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3056..3081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3133..3162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3240..3261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3389..3450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1604..1635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2017..2035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2073..2090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2396..2443
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2457..2521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2576..2599
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2687..2711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2718..2732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2876..2924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2959..2976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3056..3072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3394..3450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4045
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4078 AA; 455620 MW; C11ED5ED06FE514E CRC64;
MGKITKAIQT KHKETLTPWL QEFVDSAASK PLPLLPRALA TFPSRWPFPR GDLYHWIPLL
NRFDELLESF NATYKLNEGP QSRDFGCEIL LKSGLEGEEA ERYRNLTELG YAKDGDVYLI
VSILRFTQML LDHCGNRSIY ASSAHLNDLL NSMDYRILIA TLQVGVELAQ RYQASVKRIH
GMATRQVHTA LLSNHYNIDL DRVQQLAQPF VKTPIVKPPD SGTVSTPNSA NKNREKSQGS
GSKNAATLFA NDLCAIAKSE PNEAHDAQTR WSGWADVKLT YYPSSGTNSH EHSQPAMPDR
GMPNTPSTPT PLRRSNSANA SHVTPRTNRQ VQGVAEDSAG STPRSPTLGR DEIIYPGQKV
LEVPQSTVIS SSPYHILEKL PKDLPKETRY EFLNRLRVAK ALTGSLESRQ QALKVRLLAI
QNLAYIHVES TFVEKVLRQD SDEPRRFQLV YQLAELIHPS ADGTTKVPLD LQSIALSLLE
AISSFGSKLP DIFSALNATV NHGVLLYVIR KAVADMKQDE VGEQWTPEDE WREQLFSLTL
HITMSMAQNS MRNTPEIISA GLLDILVEIL NLRSSIAERT HGQLVGFLDS LVYNVHTSFQ
TLAAADGLEA ITNLITHEVN LAKQLAADGR GTPSSHRSQV VDYEIPFHQQ QNLKFLLKFI
HHLMTNGFAY SGNTDRLLRN LVDKADLLYS IRDIIENVTQ FGALVWTNAV TILGDFLNND
PTSFSAVLEA GLIHSYLVAL TGHPVTTPPR EEAATPSPGH TNDNDEESQG SPPASDALEP
DNRPHPPPPD ILELPRDHPL AGGIVASADP ISTVPVVLNA ICLNNLGMKM VVSSRTFDTF
FEIFESPDHV RAMAAEETLA HSVGGSFDEL ARHHPSLRPA IANAVLDMIA RVTHLARVKA
RDCGWGAKLV VRGSERELVA DESLLGFTPD LPEKAKTNEI ITGDADVHMM DIDTQNPEDL
DKSSGLLSVH TSIGPYVDAV AGFLTHYISN QNLKMSLITN GGIEQLLDLY TSPSLPHTCR
GSFAGRSLQS VLSSLIESSP IIGLPSLLRR THDAIGVLDV FVKPGDSASY FKPFLTQDAA
LTGQTTEHLT KHLATGTSVV KALLNSQSLM RVLYHSFPFS SRTQAVTLHG INVFDYHSQL
IKSLGPLIRA VVFEEITIST IVPQQWYGKD NEGRDQQGPP AIAAPKGDDE PGPDFEDPTF
SGACSPAAVW QWAVGKKASR DQESPKNAQS SPQYRNFQTI RALFEALLPT TLPLLQTYGK
SLLLRRERDT YIRSHHMQLA EDISLTILEQ LDVPSREGTA RDFQYWYIML HATHELLVNP
TAEGRSDRAM HAQNIIPVLL AFKKHNGLKM LNAMLIKFKD EICNPHEDDE NVARSRLASL
GLKKILDIYS MFANGKLITD AVSTVNVLPQ RATSGDRRGE ASVAPNLIVE LRATILPVVQ
ELWESRLVEK GSATSVTKII EILKAISSAD AETSSYRRSD KNLPPAYLEP SNSKFPWPTH
VPDVNYLIEG SFTEGLAQEA IYRSLGNRQA ATEYCSAHEK GIAGPDNPIP EYDAPTDVEG
TSSGERTVPA DNEPMVLDLP SDDTPNILDE ELIGELRDTA AALSSSADRD TPIPSAAHQE
SNGQGSASTS PAQGSARRVK IELETTTRPS QHVAKEDLDE ERAKLRSNMI DRCLDVIGAH
PDTTYEVSEL ISSVVFRPTG DDLSTRQEIG ETLVNALMSF AMDDDLKANG RSIAAYAHLL
SLLLQDKPFL KASVNILKEN VSEFLRFLHV PGSSSTEELS PWIPYVLLVF EILLSDDEQL
GDINWKAPEV ENDAIQPLEW IDKDLNVNDG DRRTLLSAIL EILPRIGKEE SLAVSVLRIL
VILTRDRTFA RQVGDKKNLQ RLFVTAKQLS GAGALRLSET RISSYILTIL RHVIEDEEVI
KQIMRSEIRA HMDGTRNTRP LEPTGFLRHF SSLVLRDPKL FVEVCNETVK LNRWAPRDGN
TARNQVVLLQ DSQGEATKDE VAPTVRATED LTIQDIKPST EAEDKHMDDV SKTTTQDLKR
PVVETPDGVV HFLLCELLNY KEVDDKDTSQ LSKEVTEIGG QNASSSDASN EHENRTTDGK
EKKGKSSFKA DEHPIFIYRC FLLHCLTELL QGYNRTKVEF INFKRNAPLS ANTPVKPRSS
VLNYLLTDLL YPSNMDGPLD TIIYKKKYAT AMQTQNLLVA LVTRTGEKPV ERGRDKYDYE
DEPDLLFVRR FVLDTILKSY KDATTSNDPF DSRYARMLGL AEVMHLMMGD KDKDPTASSR
NNSDPLERSQ AQLRRLMYEK GYLAALTASI ADIDLAFPPV KRTIKYILRV FRVLTSTAIN
LSHANIISSI PAHDNVEDEL ISTSSLSDVE DDREETPDLY RNSALGMHEP LRDMDDDYSE
DSEDDDDEEM YDDEYDDDMP YESEDREEDV SDREEEEEDL EGMGPIEGLS GEPGVIEVTM
EDDDDVDEMD EDDEEDESDE DEDSDEIDDD EDRIEIVDDE GNPLDDNAWE SESEDMADEE
AEIDFAAETR DLREADIHDM DDADGLNRFG NMMRAIGDGD FEPLEDLNHI NDRYMEEEED
DEEDEDDDEM EDEYAYEEDY PNDPQPPRDI VAPALGWDTL VVDHGGLFGS GRRRHPPNDR
QPVSLPFMVG HRDLNNFSGM FEDLFNEFLE TMADTFTITS HDHRRFREGH TVNTNSDSRI
RGGHSRDARL PTNEDGMNPL LRRTNETSRD ASPRPGNYAG GSLVRLGLPG SLLTGIGHDN
PVSFISDLVA SLPAHFNRHG HAHALHFSIG TGPRLNELPF PFSLPSRETR SDSRRDSYQE
PVQSTSFSAE STIARWAEEM KMIFGTHNQD KACKLLPAIM FHLVPPAIDE EKKLQAERQR
IEDGQRKKRE EEERRAKEAK EAKEAEEKAA REQQEAEERE RAAEAAAAAA AAAAEAQTSS
ASEDVHDSHV EPDAMQGIES SSEAASAARE NTAVANQARS YTTIRGEQVD ITELGIDHDY
LEALPEEFRE EVIAQTVSSR RAEAREAPRG AGEQTEIFQE FLDALPEDIR EEIVRQEGAE
RRRRDREEAR RQATAAGQVP EAQDMDPASI LMTFPPALRD QVLMEQGPEI LDSLPPELVA
QARRALRTSH PIVSEDRIPP GANRGRDAVQ ASGPADEDNK PQRRAVVQML DKAGVATLLR
LMFINMKGGS IENSLKNVFK DVCENRLNRL EVISTLLQIL QDGSTDVDAV ERSFTHLSIK
AKQPKDKEAK TQTPQSLKRA STNINSHHSL QTTSDTSPLL IVQQCLDLLC YLADQNVHVP
SLFLTEHDVV VSTLKRSLSR KGKGKDNKAQ KYAINSLLSL LDRDLVMESS AIMDSLSQLL
SRVTFPLLTL DRKQKEAAES IKLLEAENVK ADDESTAAAN NTQRTVPENA NQTTASGIRH
SDQAPITTEN AEPSSSPNPS NVESKTPTTL EKRQAALRKI KQLHPPIIPD SNLTLIIKIF
VARECSSKTF KETLSTIKNL SVIPGAMLVF GQELARQAQV LSEKIVVHLD ELLPHIQNAD
TGTEIQGVAL SKFSPGASDQ NKLLRVLTAL DHLFAQKKSD TAGEPSVEET KKQDLLSTLY
RNPTFNALWE KLSACLSAIR QRESLLNVAT ILLPLIEALM VVCKESAHAD ASTSTSQNVQ
GHEDHRRILN ELVRNNPSLM KGTFANLVKN PKVLEFDNKR NWFNRSVHNK QQANHRPFPT
LQLQVRREHV FHDSFKSLYF KSGEEMKFSK LNIRFHGEEG VDAGGVTREW FQVLARQMFD
ANYALFVPVS SDRTTFHPNK LSGINDEHLL FFKFIGRIIG KALYEGRLLD CYFSRAVYKR
ILGKPVSVKD MESFDPEYYK SLSWMLNNDI TDIITETFSV EDDEFGVTKV SDLCENGRNI
PVTEDNKHDY VRLVVEHKLL SSVKEQMENF LKGFHDIIPA DMISIFNEQE LELLISGLPD
VDIDDWKSNT EYHNYTPSSP QIQWFWRALR SFDKEEVAKL LQFVTGTSKV PLNGFKELEG
MNGINRFNIH RDYGNKDRLP SSHTCFNQLD LPEYENYETL RRQLLKAITT GSDYFGFA
//
