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Database: UniProt
Entry: N4XCQ2_COCH4
LinkDB: N4XCQ2_COCH4
Original site: N4XCQ2_COCH4 
ID   N4XCQ2_COCH4            Unreviewed;      3853 AA.
AC   N4XCQ2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=COCC4DRAFT_156849 {ECO:0000313|EMBL:ENI10784.1};
OS   Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665024 {ECO:0000313|EMBL:ENI10784.1, ECO:0000313|Proteomes:UP000012338};
RN   [1] {ECO:0000313|EMBL:ENI10784.1, ECO:0000313|Proteomes:UP000012338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000012338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
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   -!- 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; KB733444; ENI10784.1; -; Genomic_DNA.
DR   RefSeq; XP_014084693.1; XM_014229218.1.
DR   GeneID; 25839473; -.
DR   HOGENOM; CLU_000215_0_0_1; -.
DR   OrthoDB; 164548at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000012338; 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   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          3517..3853
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          215..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          719..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1112..1137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1458..1531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1865..1903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1934..1976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2216..2279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2310..2405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2505..2539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2689..2781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2848..2872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2923..2946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3149..3221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1486..1500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1504..1524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1883..1903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1947..1972
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2262..2279
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2322..2385
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2689..2726
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2727..2766
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3158..3188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3196..3219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        3820
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   3853 AA;  429371 MW;  268F074A4F422AA2 CRC64;
     MKIKKQATSR HESTLSSMIA DFVKATESIP LYQLPAHLAS FPKHWPFPRG DAYHWIPALD
     RFDHILDLFN KEYGLVDGPQ TQPFQRRLLL KGDADQGSTA SDQTTTEAVL DTLHLSQDGD
     RELIEQILNF TRMLLENCGN RSLYSSSERL DKLLNTTSTS LLKATLRLGH RLAQRYAAAR
     MRHAPATLHP SALSSHYNIN LDKVQKLSSP FAKGPTAPAP VFGTPAGRGK DRAGGADRVS
     PSDLVGMYSL SDAAMKQEFG GVLISYYEPA PATEEGSSKP ATTETPASAP TTPTPVRRTS
     SMGPNRTPRQ PQPVAPAESP NTPVFTPGQP SSKTNGPKTF EFSVDKVAKG DIHDLIKEGL
     ESLPESVHYE FLHKLRIAKL FNNGAAGRDD AVAIRLLSIA NIGYVHIEKE FMAKLGQQDA
     DEPRRLQLAH QLSELVHPPS NGQGGLSLEL QTFTMNALEA LAKHKSKAAD ICAALNVNVN
     HGVLFYVVRK LVAGLGEETG DPDDLEEDAW RDALFSLLNT LPTSQTRTGE QMVAAGLLEI
     LVDVLKLRTA KAERNHPKIL NFLDTFVYNL RDAFSALVAA KGLEIIADLM QYEVDVSKKL
     AEEDKGMPKE YKTQLTDYQI PFYHQQSLRW LFKFLNHMMT HTGGNFDRLM RNLIDSPQLL
     SSLRTVLSNA KIFGSTVWSM AVTILANFIH NEPTSYQVIA EAGLSEAFLE TVAGEPASES
     TAAANANENA ATSTSRPPQE AEKPLAKGIL PVAEAISTLP QAFDAICLAE AGMKLFQSST
     ALERFFEIFE SPAHVKALDA DAEMPTMIGN SFDELVRHHP PLKGRVLSCL SELIARVVQL
     CASKAEKEGV GAKLWTEDAN GKLLVAGGRQ ALSGSGPQRT SGSTGTDVEM KDADETPNEY
     IRVLCRFLSG FFSNHAMCAA YIELDGVDSI LDISNLACLD PKSSENRSMC EQFGHVVQVL
     VEQKPHIAVP SLIRRTQQAL ERLQPLLDHT GKQAFFVPFT SSSNSPDNEH LQRGTQYVKA
     LVSAHTLVGA MTLTFQSQMY STRSAHNVSS QVNLADMYAR LVDSLGKLHR SCVWEELLLQ
     RNMPTEWEKE TRVASSGFGN DEADHVFRIG NSATESPSNA ETAPATAGAT AENPTLSHNS
     ARFKNTQTLR NLLSKIPTEI APFFQSLGKL LLFRRSLEAY QRQCATVVAD QLAQAVIDQL
     EYEGPKESDN IEDRYAYWIV ILTSLSQLII EPNLDRPQAL TLLLVSFRNL GGFDVLANIL
     NQFYESALEI TQKQSEDTSE EMKRLLNLSL GGIKIILAFF SQIINYKVIG ESPQTSSMQT
     RPDRDRERSD YFLTAQFLVE LRFAVIKPVE KIWNSNLIDK ATSSIVKTSV NILKSVLECD
     GEHGAYKSID KIPKRSKPII KPWSARNGEH LMRLKDNGYE ESLAEEALYR CCDNYNMANE
     YCRNQGRLSV SRNPIPQYEI QARGPPSSSP SRAEVVVPEH TDDASMTSSE ITRDEDEPQE
     PETQSVQMED ADTSAATESE APTSATPKRM AIGNLTEPVA LDQLDEQRSK LRQNLVDRSL
     DVLNSHEDVT FELADLISAA VLKAPEPESM RTEIGTTLVQ SLISLQSEDD FRTQSKKIAA
     SAHLLALVLQ EKDFYDVVVG ELKDNFTTLL GFLKIFPDQS AEDSSPWIGQ VLLIIERLLA
     EDQLPRQITW TPPTEETQES TSVDELPEPI VTVEEKDQLF GAIIEMLPRI GKDESLALSV
     TRVLAMLTRT RKIATRLAEK RNVQRLFLMV KQLAGISNEG LRSAFMIVLR HMIEDDEMIR
     QIMRTEIQQM FESRDRRQTD TTGYTRQMYA LAIRAPEIFV EVTNEKLQLA RFDPNQRPQT
     LVLKKVETTS TEPANTAETS DVVAEADKPK ESSEAPKQPF LERTKTSDLK VPVVENPDGV
     IHYLLCELLA YKEAEDKPEP PKPTETASGE PGTTESSSDA AAASTTASTE PAKTEKPVFK
     ADSHPIYIYR CFILKCLAEL LQSYNRTKIE FINFSRKADP YTVTPSKPRS GVLNYLLNNL
     VPIGTLNHEG DLSFKKKLAT SNCAIDVIVS LCNKTGEHTL PKTDVPLSPY AETEPDLLFV
     RKFVLEHALK AFKDANASDE PLDMKYSRLL SIADIFSRMV SQRPNGEMLT QNADLTPNLK
     QMGKIMYEKN FITILTTAIS DIDLNFPNAK RVVKYILKPL RWLCYVAMDL SMHYDTSSTP
     DSGDEYEIST ASDDDLVENI REETPDLFRN STLGMFEPPH ESESDEDSED DEGEEMMYDD
     PYADDMEYDE AEIGDDDVVS EDDEEILEME IDGMGPIEGL PGDVDDDSEE DDEDDEDDMD
     DMDDMDDEGD DDMEDMEDAL EEITADDENA SLAEDQEDEW SDEQDDFPGG VNGEAGMPPG
     IGFVIDPPQQ LLEQMRQQGG GDIEDFLDDE MGEEDIDDEE EEYDEDIHYD PGAEDDEEGL
     PELGWGGGWE DPAPAAVRHT HRLSPWMFPA GPGDRILVPA YRSHRPGAGP RATDDGINPL
     LQRGGRSTGR DGLPRNEGNS DWVHAIESRG PRIFNQTDSP VSFISNLLNA MSSGRGGPTL
     LHHGGALHVS LGNSMGMQTF DSSMRRDIAR MRETYNSRSA REDPHSAVAF VKAYTSQRWQ
     EEARILYGPA AIEKSQRVIN SILKVMVPPA IEAAKKRQEE REAEVARKLK EEQEKKEQKE
     REEREKREAQ EKEDRERRER EAAEAASRAQ DQTSEGEPKN EAGTTSGEQA MEGVQAAQTS
     GESATVESVP AAPAGPPAPR VMTTIRGHEY DITDLGIDTE YLEALPEELR EEVLMQQSGD
     LPTDINEEFL AALPEEIREE LLAQEAQERR RREREENRRR NQSSAVAPQA EEMDTASFFA
     SLDPNLRAAV LMDTDEDTLR QLPPELSAEA RAMGGDRRLH QFNEFGYRRG DRRGQPEDPN
     QKKKARPCVQ MLDKAGVATL LRLMFIPQQG SAKASLSSIL CYVCENRQNR AEVISILLSI
     LQDGSADVNA VERSFAQLSI RAKQPQQPAE KTPKLSRKNG ALSINADVSP LMVVQQCLNT
     LTQLTEKNPA VWSFFLTEHE TGVGFKNRAN RKGKAKESKA NKYPVNALLT LLDRKLIVES
     SSIMEQLTTL LKVITAPLQA LKKEKEKAAE EAKKASESSA EGQNAENQST EATSTGAAQG
     QDTEMTAAPD SGATEEGASK PDRSKAEDDK TKKHRSLTPP DVPEANLRLV AKILAARECN
     SKVFQETLSV ISNLSPIPGA KEIFGQELLG IAKDLASSTL RDLDSLTVQI SKASSSTDVQ
     GIALAKFSPA SSDQTKLLRA LTALDYLFDP SRDSKDKPEA AAEALEPAQK EDILLTLYED
     AAFAPLWEKL SECLTVIRQR GNMLNIATTL LPLIESLMVV CKNTTLKEAP LSKMLAKEFA
     LSSPPPENKM ENLFFNFTEE HRKILNDLVR QNPKLMSGTF SLLVKNSKVL EFDNKRNYFN
     RKLHSRGGDR QAHPPLQLSV RRDQVFLDSF KSLYFKSADE MKYGKLSIRF HGEEGVDAGG
     VTREWFQSIS RQMFNPDYAL FVPVASDRTT FHPNRLSSIN PEHLMFFKFI GRIIGKALYE
     GRVLDCHFSR AVYKQIMGKQ VSLKDMETLD LEYYKSLEWM IHNEITDIIT ETFSVEVEAF
     GEMQTVDLIE NGRNIPVTED NKHEYVRLIT EHRLLGAVQE QLDHFLKGFH DIVPAELVSI
     FSEQELELLI SGLPDINVDD WKNNTEYHNY TAASPQIQWF WRAVRTFEKE EQAKLLQFVT
     GTSKVPLNGF KELEGMNGFS KFNIHRDYGS KDRLPSSHTC FNQLDLPEYE TYEDLRKALY
     TAMTAGGEYF GFA
//
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