ID W6ZIK1_COCMI Unreviewed; 1871 AA.
AC W6ZIK1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=COCMIDRAFT_7155 {ECO:0000313|EMBL:EUC43396.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC43396.1};
RN [1] {ECO:0000313|EMBL:EUC43396.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC43396.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR EMBL; KI964030; EUC43396.1; -; Genomic_DNA.
DR RefSeq; XP_007690064.1; XM_007691874.1.
DR STRING; 930090.W6ZIK1; -.
DR GeneID; 19125194; -.
DR KEGG; bor:COCMIDRAFT_7155; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_1_1_1; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000054032; 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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1515..1871
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..800
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1838
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1871 AA; 206159 MW; 61FC948179494159 CRC64;
MSSRVTRSQR RQSGNPHTNS TPNSLPAPPP QPALPPPPTA RKRKSAARDD QSPELPDITD
APPARSARNK RSKIDLQDPP QQPKTRSNKA KGKAAAQMSS SGSVPSAYDT HEHALTANSP
PSDPIDEKST PQPSRRTRGG RKSGPDSSRR QPKPSSHTDP DPDPDTPSTS RRSSRRSNKM
ETDTTMEDAP PVNAEEDARQ SSDENSSDDE HADEHGERYD QEEDDDDDDD DDDPFTGGFL
GRNPHSLSAL RQLTGIMAGT TQRLRGILEQ LRSHDDTVQL TALNELSEVL LISTEDNLAG
HFSPDAYVKE LVKLMQPNEF TMEENPEIML LACRCLANLM EALPQATANV VYGGAVPVLC
SKLLEINFID LAEQCLSTLE KISIEFPGVI VREGGLTACL TFLDFFATST QRTAVTTAAN
CCRNIPEDSF PVVRDVMPIL ENILNNNDQK VVEQGCICVS RIVQSFKQHE SKLEELVSPG
LLKAILRLLL PGTTNMIGAN IHTMFLQVLA YTAKASPRLS AELLKMNVVD TLYQILTGVS
PPTGTEDVAA KIDSVVIMQA LIHRPKDQVF ETLNVICELL PDVPQQGLSY LDDLFDAGYP
GDDILPLSSS NKKTMNEKRI QLLEGCKAEV KRFAVILLPT LTDAYSSTVN LSVRQKVLTA
HLKMLSNLDI DILEEALRPV PYASHLASIF TQQDHPSLVT YALQAAELLL KRLESIYRYQ
FYREGVISEI QQLANRPCKT LDSRAKESKS TVGANVTALG DSIASSAEPE AESESGNPND
GVDMEMHSDD EGDEVDLDDD PNASSQNRDD DDESDSSSSS DDQREPPPMP NVEDIITLRA
KKFIETHERD SDKPTRDRAI AVLEDLKTLA NEIKACGSKG TASNFMNLFT RLASYFEGDA
LESITSYELK SSKIVDVLLE VFSKPMSSKH VDPRPIFLEA FMGGSGQSKI KTASTASPAT
PFSVLVHKLQ DLLSRSEHFD VITVHQNMYD SRGSATSMLA KQLRLKLVAD DDSGIPKTYR
NIMVSIHAIA TFKALDDYLR PRISLADRPR PAQPRDQFAR DQFEAMYAQA LAEGRAPPPP
RTPSDPASRA PKKPSRSKPG PPDSPQPGPS SATREKTRRS SRRQQQNPPL PPPPPPPAMP
RSNNGQDPVE CADESQLSDP ESVDEDSALN AIVDDLEEDL DEDMPDPSAV SVEVASTGKA
TAHQEDGTRI ATPVQGTPIA KPPSEARTPA SRLSALLQSS AMRQTLGGAA SALSYAAAVQ
STPQDWHIEF SVNDQPLSNE TTIYRAVHFT RAQPSDGPLR SVWNGIHTIK FKRVQGPPLS
ESSSLTPPPE SKSDASGMPA SLDEHPVTSG ILRLLSILHG LNSHLDDILL ANKEQIKLNA
EPLSQFVNTK LTAKLNRQLE EPLIVASNCL PSWSEDLARF YPFLFPFETR HLFLQSTSFG
YSRSMTRWQN SQPTSDSRGD RHRDERPFLG RLQRQKVRIS RSRILESAMK VMQLYGHSAS
VLEVEYFEEV GTGLGPTLEF YSTVSREFSK KKLKLWRENE SNDSDEYAFG KRGLYPAPMS
EEEANSENGE KRLELFKVLG KFVARSMLDS RIIDISFNPT FFRISDGSST AVVPSLGAIK
TVDEGLASSL LLLKQFADAK KKVEDSDLSP EEKVVALQEI VIHDCTVEDL ALDFTLPGYD
SIELIENGAN TAVTIENVDS YVDKVIDFTL GSGVERQANA FREGFTEVFP YSALKAFTPD
ELVMLFGRTD EDWSLETLVD SIKADHGYNL DSKSVRNLLS TMSQFNAQER RDFLQFITGS
PKLPIGGFKA LTPMFTVVCK PSEPPFTSDD YLPSVMTCVN YLKMPDYSSV EILREKLSVA
IREGQGAFHL S
//
