ID A0A3N2QAI7_9PEZI Unreviewed; 4117 AA.
AC A0A3N2QAI7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=SODALDRAFT_269198 {ECO:0000313|EMBL:ROT43746.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT43746.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT43746.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT43746.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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; ML119051; ROT43746.1; -; Genomic_DNA.
DR STRING; 1314773.A0A3N2QAI7; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000272025; 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:UP000272025};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3781..4117
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 217..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1990..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2088..2133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2368..2572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2590..2627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2665..2694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2723..2760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2898..2998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3078..3097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3146..3173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3387..3486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1655..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2037..2054
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2095..2119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2421..2468
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2483..2520
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2529..2562
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2613..2627
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2898..2953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3078..3092
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3419..3450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3456..3481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4084
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4117 AA; 456810 MW; AAABD7A1F1295B71 CRC64;
MGKITKTMQP KHEETLSPWL RDFVQSASST SLPLLPARLA TFPTRWPFPR GDLYHWIPLL
NRFDNILEVF TTTYNLTDGP QTRELGCDVL LNRDSKIVDY GDQKWDMDLL RKHGYQQDGD
RQLVEVILKF TRVLLEHCGN RSIYASSGHL NDLLNTTCLP LIIATLEVGT ELAKRYQASV
KRIGSHSRHV STALLSNHYN MDLGRVQQLA SPFVKTPLAS LSEGGPSSGT PRSAKGKEKE
KEKEKEKEKE KAHHVTAQKN AAAMFANDLT AIASDDASRW KGWGDIKVTY TVTPPLRDPA
SAAATVDRAH SSSNAPSTPT PLRRSTTMGG APTHQTPRSA RHFASEESPP SSIIRSPALP
SEQPLSNQKV FDIPESVVAS SSIHDLLARC PADLPAQTRY DILNRFRIAK ALLGDAESRR
QALAVRLLAI MNLAYIHQEA TFVEKVMRPD IDEIRRFQLV YQLAELIHPS ADGSTPVPLW
LQSIALGLLG AISNFQARCQ DVLSAVNANV NHGILLYVIR KAVAGMKPDD PPDQGDQTTE
EDTWRNKLFS LTQHLAMSTR VGAEMVGAGL MDVLVEILKL RSNVARRNQS TILSFVDALI
WSYQNAFQAF FNGDGLNAIS DLVVTSVEEA KQLAESGQGT QPELHSSIVD YQVPFYQQQT
LKWLLKFMHH MMTNSYSIGG NTDRLLRNLV DKSDLLASLR EMILHSKRYG SVLWTNSVTV
LSDFINNDPT SYAAIAESRM IVAFLESITG RPVPEQPTVA RTDEAAGRDG SAAADPSQQL
DSQVTLEPDT RPHPPPEDVL DSQVGRPLAQ GILANPDAIL TIPHLFNSIS LNNAGLKMVV
SSGAFEAFFE IFESPKHVAC LEGDHRLASN VGETFDELCR HHPTLRNPIS AAVTDLVARI
RHLGKVESRT AGLGLSLGLN DVAGNFVPAD QDLLGRLSTH SAPSPGDKGK GKGKAPADDQ
DIEMTDRPAT ADGHSKNETK TTADVAPAAN KPSAFHPYIR ALCLFLSTYL SNSSLKSLFI
NRGGIEQLLD LAESPSLSLS FDVSFNDDDD VWHGLTGVIA QLVDYAPVLA IPSILTRAQA
AVDVLKPLVD ARREDRPYFA PFVASDTTVT AEQAAGWDAA TKDKIMSGSK MAKALMTLEF
YLKMLFDCVS SIPRSNIVSF YPINVFDQYL RLVKSLGPLL QAVCNEEDAI YEAIPPHWRP
TPLTALRGKL TSEQAKSMEA KDALFVDSAL PRAAAQDDTG ESKDEGSAAE PKRLTKQEEA
STRFKNYQIL RTLLHTMHPF ACPFLQQLGK AVFPRRERDP FSRQQHTEIT KAVAACILDH
LRTSVAQEDP PVNVRRQWLL QLHTLGEIII DTHPRSTERS PIHINTPVYV AFIQQGGFDV
LMTLARRCAD TLRNSEQRER PERLASVGLK KVLNIFAMVV DGKCMLDATT QYGLLPRTTE
RSAERRDPAL ISQQLLLEAR MAVFPFVREI WESPFLEKEH PDTLHKVMDI LKTISLGDNE
PSQYHPIVDD ILKKSPAPFN WVQAQPAITN LGEEYDADLT REAVYRANGN QNTASEYCRM
HSSHLAGPRN PVPPEDAYTQ PSAPAHPATE PMAIDDAPPP ELDNVLGESM LAELEDHSSR
ASDDEEDEDE DDDDEDDDGD GDGDGDGAHR GASVGDGSAQ NTTDLRTVTK QELDSQREAL
RKDLISRSLD IIRAHPASAF EVAELIRTVV FYRPNAEIRE EVGVTLASAI TSMASDSGQV
ASEADGRTVA AYAHLFALLL LDSAFMKANL DTLRSNVDAY IGFLKVSPAN SKEELPPWIP
YVLLIVEMLL SQDEKPIEAS WKPPASENEE VQPAVFPPQD AIVSSDQQSD MLDSILDLLP
RLGKNDVLAT SILRILVIMT RKRALARRVG DKKNLQRLFV MAKQLAGGSS NPLKDPKTSG
CIMNILRHVV EDEETIKQVM RAEIRNLFEN PQRSQRNLDL HTYLRNLAPV ALRAPDLFVE
VTNEMTKLTR WTPANEGSSR PHQLALKEEA SSTAETAQSK EEGVEPAVQA TEDLSLHDIK
PSTETGDKDM TDAPKPAIQR PIVENPDGVV HFLLCELLNY REVDDKEATL PKSSKDSKAE
ATASASASSS SQEKPAETQA SDNTDGKEKK SSKVTFKAEE HPIFIYRCFL LNCLSELLQS
YNRAKVEFIN FKRSAPLQTN TPVKPRSSVL NYLIHDLLCQ SGHPDGTDNV LSKKKAATSS
QAQQVLVALV TKTAEKVIDK RRERFEYDDD PDLLFVRKFV LDTILKAYER ASTPDEPLET
RHAKMQGLAE LMNHIIGEKD RDPPTSVRGM DSPQVRSQAQ LRRMMYEKGY LDKLTSSIAD
LDLNHAGVKR SLKSVLRVLR ILTGTAKELS RSSVMPSTAL PDAADDEIMS SSSVSDVDDD
REETPDLYRN SALGMLEPRG SDDESDEEDD DEEMYDDEYG DELDYGDEEI SEDDENRLSD
DDEELGEMGE IEGLRGEPGV VEVVMDDDDD EDMDDDEDLS DDDDDELGSE DMEDLEDHVE
VVEEIVDHDG NPMEDDGDSD WESETDEDDN EDEEDIDYGG EEQDFEEAHM HGMEEMEPGD
IIGSLARAVM DPEDDFAEPE GMDELDGHYL DDGRPDDEDD DEEDDDDMED EYIYDEDYPH
DVAIPVNVPG HLGWDTLVVE PFPPHGHHRH RHGQRSPFQP GFIPGGPRDP LGGRSPASIF
RALLNVIDPT SGLDANDASD FRSYLSRRPR PSGPQNAADD GVNPLLRRGD QNPDLASRPG
AGGLNFVGLT WPPEMLMPGV GGGRAGGFFD SPIALLNDIV ASLPVMRSGP PVRLQVTQPG
GRGEVREYHF GPREMRPDSR RDGIYQEPQQ AVAFNIVSTF ERYQEEARMV FGGPQCVEMV
QKLVNLILSE LVPPAMEQEK KLKAEEEERR RVREEERKKR EEEERRAREA KEAEERAERE
KKEAEERAER ERAAAAAAPP AQSDTREGGE GSQAMEGVET HGPAETSTTE ARPADVPRVV
TTLRGEEVDI TELGIDPEYL AALPDEFREE VIAQTVSSRR SQAREEAAAG EQPAVFQEFL
DALPEDIRTE IVQQERQEIR RREREEQRRQ AAGGGHEAIA ADMDAASILL TFPPELRHQV
LLEQGEEFMD QLPPDMAAQV RVAPRLGGAR SPPSGGAPRP GQQEGAAGQP QAAKVQRKTV
VQMLDKAGIA TLLRLMFITQ YGSIRNYLFS VLSDVCENRQ NRIEVVSTVL SILQEGSTDM
DAVERSFSQL SLKAKKPKEK DADPKTLQNL KRTLTSLSSV SNSQTNSEIS PLLVVHQCLD
LLQELSTKNP HIPMLFLTEH ESVGSSLKRS LSRKGKSKDS KAQKYAINSL LSLLDRDLVM
ESSVVMAYLA DLLNKITAPL AAMERRRREA AEKEKAAAAA ATAEEKGTEE APAAEGASAP
TAGSTSATCA QAAGPSSSGG ATTDAPPTSA EAQQGGDGER NKDGPESSPV AETKDSSQKK
DRQMQVPVIP AHNLTLVVKI FVARECSSKT FQNTISAIKN LSAIPGAKSI FGQELVRQAR
LLSENIVSDL DDLLPHILKA TSGTEIQGVA LSKFSPGASE QNKLLRVLTA LDHLFDSRKR
SDTAGDEEAA NSEKQDLVHS LYHNSTFSKM WEKLSACLGA IRQRENMVNV ATILLPLIES
LMVVCKNTAS TEKAAADKEK EKVLSSPPPE SRMAGLFFNF TEEHRRILNE LVRNNPKLMS
GTFALLVKNP KVLEFDNKRN FFNRSVHSRT GAQRPSFPSL QLAVRREHVF HDSFRSLYFK
SGEEMKYGKL NIRFHGEEGV DAGGVTREWF QVLARQMFDA NYALFIPVSS DRTTFHPNKL
SGINDMHLMY FKFVGRIIGK ALYEGRLLDC YFSRAVYKRI LGKSVSVKDM ESFDPDYYKS
LVWMLENDIT DIITETFSVE DDEFGVTNTI DLCPDGRNIP VTEENKHEYV RLVVEHKLLS
SVKEQMEHFL KGFHEIIPAE LISIFNEQEL ELLISGLPDI DVDDWKSNTE YQNYTPSSPQ
IQWFWRAVRS FDKEERAKLL QFVTGTSKVP LNGFKELEGM NGINRFNIHR DYGNKDRLPS
SHTCFNQLDL PEYESYEILR SQVFKAITAG SDYFGFA
//
