ID F7VMT2_SORMK Unreviewed; 1909 AA.
AC F7VMT2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=SMAC_00686 {ECO:0000313|EMBL:CCC06661.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC06661.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC06661.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC06661.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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:CCC06661.1}.
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DR EMBL; CABT02000002; CCC06661.1; -; Genomic_DNA.
DR STRING; 771870.F7VMT2; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_1_1_1; -.
DR InParanoid; F7VMT2; -.
DR OMA; AEPLSQF; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
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:UP000001881};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1554..1909
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..828
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1876
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1909 AA; 208854 MW; CB959A0641BDB7D8 CRC64;
MSTRLTRSAA RHAASQAANN STSTAAVAAA PGAAQPTTVA TTALAAEASS APPAAAQTLA
RSSSAKKRKT AAAAEANNIP ETAAELSSSA RRSKRQRVTQ PASQSSSSIT HPAQPAAAAS
SSAASSTTKK TTTTRRKKGK APATSTIMSS PDDPAVPPNP PTNPSSASTS RRSSRHKKDA
QDQDVVMTGT DEHEKDPTPP PPPPPPPKES PPSDSDEHDE DDDDDDDDHR YDDEDDDEDD
DPFTGFGGHG RHPHSLQDTL RHLTGIMSGV SAQVRKIMAD LKRKDDPSVQ LMALHELSTL
LLMTNEDQLS GHLSPDLIVP DLVLLMGPNE ITGEENPEIQ LVACRCLANL MEALPGSTSA
LVYGGAVHIL CEKLLQISFI DLAEQALSTV MREGGLTACL TYLDFFATST QRSAVTTAAN
CCRNIPEDSF PEILGVMPIL LNVLGSSDQR IVEQASLCVS RIAESFKYHP AKLEELMSVD
LLKAILRLLL PGSTNLISPH IHTQFLRVLA LTAMASPRLS AELFKLNVVE TLYQILTGVS
PPSGNDDLAS KLDSVLIMQA LIHRPRDQII ETLNVICELL PSVPLRDPSS ISYTMELGTF
AGPVGGSAES TRRRTANEKR IEYMEGCKEE VRRFALILFP TLTDAFSSTV NLTVRQKVLA
AQLKMLSNLD QDILSEALRS VPYASFLASI LSQQDHPLLV GLALQATELL MSRLDTVYRY
QLYREGVIAE ITKLAADAPE PKRKPSLTKQ EVKEEPDQVN LGEFLAGRMK KQKVTTLNIP
NMIGDDEGGE GLDKDEPEDT EDDENDEDDE NDENDDGNEN EIQDDDQSPV SSEGETMSLD
GPPRYLTDFP TNTYKSSIRQ VAKKFLEMYE TEKQGKAMKK KASKILASLS NLATEIEEFY
LCRKPGGPAM EDGTVLFQKL VSYFDADVLE SVTSAELLGS GVVRVLEHVF SNPDEELAAT
AQNAFLQVFM GYSVKSKPKT ATADSPATPF SVLIHKLQDL LSRSEHFEVI TAHYNSFDGS
RSTAASMLAK QIRLKLVADE ESDIPRSYRN IMVSIHAITT FKSLDDYLRP RISLSDRPHG
ASRRDAVTRA LAAMGASGFM GAAAAAARLA ERGLPPSSRS TPAHPSAAAP AQASSSRPSR
KHKSKSQPTT ETPATPDPST SKEKGGLRRS ARKQAASDSS LPRQPPEEDD LENALECADE
RQLSDEDEAA DSSDLNVLRD LDEGMDDAPT PDPTAVNMEV AAGGRITARK EDGTRVPTPG
QGKPAAPPTQ NRTSALTAAL QNTPTPQPSS KPISYSGALQ AVPQDWHIEF SVDGKVIPNE
TTIYRAVHSS SLAADEHVTR SIWSAVHSIK FRRVPGPPPP EPVGFSPSSD VGVEADENGT
PGSLAKHPIT LSILRLLKRL HDLNANIDEV LVENKETLKL NVEPLSQFVN TKLTAKLNRQ
LEEPLIVASN CLPSWSEDLA RLYPFLFPFE TRHLFLQSTS FGYARSMARW NAQSQEERRN
GRDDRPYLGR LQRQKVRISR SKILESAVKV MELYGASQSI LEVEYFEEVG TGLGPTLEFY
STVSKEFSKR KLKLWRDNEL NGDDEFVSGP TGLFPRPLSD EFATSEEGEK IMQLFKVLGK
FVARSMIDSR IIDINFNALF FRVGDATATR PTLATIKSVD PVIARSLMTI KKFSLAKKEI
DEDPNRSAVQ KVTDTENIMI DNFKIDDLYL DFTLPGYPEV ELIPNGSQTR LTIENVDIYL
EKVIDMTLGS GVRRQIEAFR AGFSQVFPYS ALSSFTPDEL CSLFGRVDED WSLETLNDSI
KADHGYNMDS KSVRNLLQIM SELTLAERRD FLQFTTGSPK LPIGGFKSLN PMFTVVCKPS
EAPYTSDDYL PSVMTCVNYL KLPNYSDIHV LKKQLFTAMK EGQGAFHLS
//
