ID A0A094B9Q0_9PEZI Unreviewed; 1894 AA.
AC A0A094B9Q0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=V494_04371 {ECO:0000313|EMBL:KFY38379.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY38379.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY38379.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 -!- 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:KFY38379.1}.
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DR EMBL; JPJW01001479; KFY38379.1; -; Genomic_DNA.
DR STRING; 1420907.A0A094B9Q0; -.
DR HOGENOM; CLU_000366_1_1_1; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000029288; 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; 3.30.2160.10; 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 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:UP000029288};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1538..1894
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..802
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1861
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1894 AA; 206828 MW; 216DD5903D9344E0 CRC64;
MAQERTHSQR TRSVAPSIFD ENEPTSDAFH SSTPSSLNSS LRNTRASARQ AATTSDLAPP
GTATPSQPTP TARPSRKRKA AEREPSPQPE PEPPKPSKSK RRQKRQRTSE QEPSAAPPAP
PARQRKGKST AAMSSPGASA GPANEGGSAA SSATRKSNRN KKSNPDLAAA AAATATPTAP
RKSKKQSKNV EAEVDHNEDN DVEPGDEDDD DEDDSDDNDN DDLPRGFNED DDEDDDPFGG
FGGPGGPPHG LSNTLRALSG MMSGMSSRLR EILSNLKQKE DPSMQLIALQ ELSEILLVST
EDNLSGHFSP DSFVKELVAL MQPSDFGEEN PEMMLLACRC IANLMEALPA STANVVYGGA
VPILCQKLLE IHYIDLAEQA LSTLEKISVE YPASIVREGG LTACLTYLDF FATSTQRTAV
TTAANCCRNI PEDSFPVIRD VMPILLNVLS SNDQKVVEQG SLCVSRVVES FRYQPSKLEE
LVSSDLLKAI LRLLLPGTTN LIGPSIHTQF LRVLAFTAKA SPTLSAELFK MNVVETLYQI
LTGVSPPNGV HDVASKLDSV VIMQALIHRP REQVIETLNV ICELLPGVPQ DLPSFMDDSF
ELAIATEPSS SSSRKKSLNE KRSELLEGCK EELKRFAVIL FPTLTDAFSS TVNLSVRQKV
LTAQLKMLST LDRDIIMEAL RTLPYASFLA AILSQQDHPT LVNSALQAAE LLLTRLDDVY
RYQFYREGVI TEITKLAQSA EPTEEEDKKS EAGDATEKDP EKAAAETADN AAGEPAVAND
RDEDDNSSDG DNDDENDVDM DDPQDDRSVS NGSSRTSSVS LDGQRSSLPA GVTTMQQLIA
QRAKKFLEVH ENEKNSKIMK KKATKILSNL QDLAVKIEDF YLRQQSGNGV ELFDQLAAYF
DGDVLESVTS AELLNSEVVR VLLEVFNNPD EELANDARSA FLEVFMGRTV NRKPKTATAD
SPATPFSVLI HKLQDLLSRT EHFEVVTVHQ NTFDGNRSSA ASMLAKQIRL KLVADDDSDI
PRAYRNIMVS IHAIATFKAL DDYLRPRISI SERSRSSRHR DGLSDALAAL AAAGMANPYG
PPSAASRLAE RQFAAAMAGH AAPPPPPAAP RSSRRHKSKT APAATTGSAA QSTSETPQEK
SARRSSRRRQ AQSDTIPPPP PPPRQDDDSL QGALECADER MLSDDDEMDD SAALDTIVGE
LNEEMEEDNE EDPGAVNLEV AVGGKITARK EDGTKVATPA QAPSASVAPH GSSSAQPAAS
APPAAATPTQ SNKPMSYAAA IQATPQDWHI EFSLDDKPIS NEITIYRAVH STTGQIDEQT
SRNVWSGIHA IKFKRVPGPP PAEPSSFTQA NEAAETTASG IPASLDKHPA TSSILRLLNI
LHALNANIDD VLAENKDTLK LNVEPLSQFV NTKLTAKLNR QLEEPLIVAS NCLPSWSEDL
AHLYPFLFPF ETRHLFLQST SFGYARSMTR WQNAQSADES RRDRHRDERP FLGRLQRQKV
RISRSKILES ALKVMELYGA SQSMLEVEYF DEVGTGLGPT LEFYSTVSKE FSKKKLKLWR
ETEGNDSDEY AFGLRGLFPA PMSEEQARHE NGKKILHLFK MLGKFVARSM IDSRIIDVSF
NPTFFRIGDE STTVTPSLGA VKTVDAQLAA SLKLIKKFVV AKKAVDENGS LTAAEKVAAA
ENILVAGVRI DELGLDFTMP GYSSIELIHN GAHTAVTIDN VDLYLEKVID MTLGSGVQRQ
VDAFRTGFTQ VFPYSALSAF TPNELVMLFG RVDEDWSLET LMDSIKADHG FNMDSKSVKN
LLQTMSELSA TQRRDFLQFT TGSPKLPIGG FKNLTPMFTV VCKPSEPPYT SDDYLPSVMT
CVNYLKLPDY TDLEVMKRRM DTAIKEGQGA FHLS
//
