ID A0A0C4DLT2_MAGP6 Unreviewed; 4086 AA.
AC A0A0C4DLT2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=MAPG_00727 {ECO:0000313|EMBL:KLU81642.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_00727T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KLU81642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU81642.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU81642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU81642.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_00727T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_00727T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_00727T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_00727T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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; ADBL01000164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876966; KLU81642.1; -; Genomic_DNA.
DR STRING; 644358.A0A0C4DLT2; -.
DR EnsemblFungi; MAPG_00727T0; MAPG_00727T0; MAPG_00727.
DR VEuPathDB; FungiDB:MAPG_00727; -.
DR eggNOG; KOG0939; Eukaryota.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011715; 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:UP000011715};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3750..4086
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 289..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1984..2047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2073..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2378..2424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2436..2545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2577..2605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2850..2940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3043..3070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3367..3450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2006..2022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2023..2037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2078..2113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2408..2424
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2436..2456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2475..2506
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2520..2545
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2586..2605
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2850..2909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2915..2938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3043..3059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3379..3414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3429..3446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4053
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4086 AA; 453236 MW; 2DAAD1D0E282A6A2 CRC64;
MGKIVKPLQP KHRETLSPWL KEFVAKVADA PLPKIPQLLA EFPTTWPFSR GDLYHWIPLL
NRFDSILECF CATYHLSDGP QARDFTCEVL LNKGAPVEYC DDRTWTQADL QALGYGQDGD
SALIVTILKF SGKLLEHCGN RSVYSSSAHL NDLLNSTSLV VLRATLEVGM ELAQRYHASV
KRMAHPSRQI GAALLASHYN IDLDRVQQLS QPFAKTPIIN FSADTMSVTP ASATKGKEKE
KAQIPAAKNS ASMFANDLVS LATSEPQDEG RWHGWGDIKV VYYPRAGIQA PPPTPAQQPT
VPDRVHSTLP STPTPLRRSS TMGSVQHRSP RADRTSGEDA SSPVTPHISG LGNDEAAKSP
QKAFEITQSA VLKTPIYELL SRFPDDMPQS ARYEVLNRLR VAKALLDSPS TRQDALAVRL
LAIANLSYIH QEAYFLEKVL RQDNDEPRRY QLVYQLAELI HPVQDGRPGV PLWLQTITFQ
LLEAISHFTS KQSDVLSALN ANVNHGILLY VIRKAVAGMR EDTEDEDDTQ RTEADDWRNS
LFSLTLHMSV SARLGTEMIG AGIMENLVEI LNIRTRVADR NHSMSLAFLD GLIYSYQGAF
QSFVDAKGLD RISELTVDIV KKATEMTKAG NGTPPSLRSS VVDYEIPFYQ QQTLKWLLKF
IHHIMTSWYS FGSNTDRLLR NLVDNSELLA SLSHVIENMS CFGSVVWTNA MIIIGDFINN
DPTSFAALME AGLIKSFLQS ITGREVKAEH PNERMNATPQ AADDDAGSAE PDDSILFEPD
DRPHPPARET LEASRSEPLA RGILPSSEAM LVIPTVINSI SLNNAGMKMV VSSRVIESYF
EIFESAKHVR CLDTDLDHAA NIGSSFDELA RHHPSLRPAI SNAVLDMVAR VVHLGREKAA
KQSWGASLSV PNPAGGSLVA DTSLLDKSGP AVLQGQDTVM ATSGPDSHDS PALGDAEQSA
KNFTPYVTAV ANFLSTFTGN TSLKTTFIHK GGIELLLDVS ELPSLPHDFA DSKGAKVLQH
VVSSLVENCP ILGLPSLLKR TQAAVDALQP LVQHKGPQLF FAPFVRPDLS LVTESGEWDQ
QVIQQIAHGT QAVKALLTTQ CLVKTLYNSL PQSNRQAISF PAVNVFDYYA RLIETLGPLL
RAVLAQEMDI AKIVPSHWPN STALGEEQPA PSVDAAAGAV GGATLDNQTA SAAESAEAGG
GARPTEPLAA STSTSSSGKS VSPDEAKSIS YKNYEVLRVL LHSMMPTSYP FFQGLGKALL
PRRERDPWTR SQHLWIAEML AKTIQAKWES SKELTVKDIH YSVVMLHSVD EMLTDTPRQT
DRGSATVIIP VLVAFKEHGG FDTLHAMLRQ FAEVAAKESD AAPSDSRPRL AKIGMKKILE
LYLTVVSGKN VWDSVQQVNL AQRPDQRRDT SPIGAQLLVE LRMSILPVVR ELWDSPLIEK
ADVGVLNRVV NILKAIADVS YEANAYKKTD KQPPALFKRE AVPFPWNDHI RIMMPLIDRG
EDVDLAREAV YRSFGAPEWA EEYIKAHKAG IAGTRNPVPP QDAYQEDGPS EAVAPEVQAP
ALTGTVVVGG DPMAVDPVPE LDRLVAVSET LSERPAPSAP AANAAAEASS RAPETQEAGG
ASSSSARPSQ TPSKTPSTPQ PPAVTKEDLD AERAKLRKDL IDRCLDVIRA HPTSVYDVAD
LISITVPLKS DANEEARQEV GETLANALIS FDADDVTSAT SIAAYAHLLS ILLQDSKPFF
RACVDTIKMN VCQYLLFLKT KEEYPIPPWI PYILLIFEIV LTDDEQPFDA KWPVPSADAE
TMPKLELVQK DPIVNQDERR ELFQAVMEIL PRAGVNDMLA IAILRILLIL TRDREFAKAA
GEKKQLHRIF AMAKQLSVLG STRFKETKIG LYVMTILRHI VEDDDTIRQI LRFEIRAFFD
ASARSSRTLE LHTYLRSLSP FSMRSPRLFI EVTQEMVKIP KWPSNAEDGQ PKQFLVVLKE
PPAAAPTNEA QASKDKDAPK DDSVEPAVQQ ATQDLNINDV KPTTESGDKE MTDAPKTPGA
EAKRPIVENP DGVINFLLEQ LLSFQKVDAE PVNAAATSKD KSKETASPTA TGGGSSSSSS
SSTSPQSTSA SEQALDDAKD KKQQKTQFKA EEHPIFVYRC FLLHCLSELL YSYNRAKIEF
INFKRGAPLL TNTPVKPRSS VLNYLLNDLL CVNSLQAPSD SLAYKKKVST ADQARMVLVA
LVAKTGEKPI NRHARRFDPS DEADLNFVRK FVLDTVLRAY REAASSGESF DIRYGKMQSL
AELMYNMIDD KETKDPIRNI PDAPRSQAQL KRLMYEKGYI AALTSSIADV DLTYPGVKRT
IKYILRVLRF LTNTAILLSA DGVLPPSSAD NVEDEILSAS SLSDLDEERE ETPDLYRNSA
LGMLEPREDD DFTDDESEDD DEEMYDDGYA DEMEYDEEMS EDDDENVSDE DEELGEMGHI
EGLPGEPAVM EVIMGDQDGE DESMDEDDDE DDSSEDDDDE ISDALEEVED HHEVVDENGS
PVEDDGASEW ESDSDNENDE GEEEIDFEAE VQDLDERAQL GHFGNINYAE PRFSHDFLGD
FPPMDDRFVE EDEADDDEED EEDEMDEDVF IFDRDNMGDG QPQPNIAPGL GWDSLVIDQP
SGAHRHRHGG IRSPFPVAPQ AVVIGGPHGD RLSEFRNFFR PRNGPPTNSH DDGVNPLLRR
HRNGGRDASP RPGMGPTFRF PPSFFSGGHE NPITLINDLI TSMPQSMGGR GGVFPSFQLH
ISQEGPHGEV HEFHIPVPAG AAQMRDSRND ASRSRDIYHE PQHAVSFMPA STSERWMEEA
KMIFGPAHHE KSLKLFLTVL SRLAPQAIAD DKEAKRKEAE RKRELEEARR RHEEEERRKK
AEAEAEAKAA REKEEAERKA KEEREAAEAA EAALLQASQS ETNSATAAND NQASEPQGME
GVETAEAALS GSHVQQAGDS DSQERLVTSI RGEQIDITGL GIDPEYLAAL PEEFREEVIA
QTLTTRRSEA RQQAENTGQE TEAFNEFLDA LPEELRQEII QQEAQERRRR QREERQRDNN
ANNNNNVSVP QEMDAASILL TFDATLREEI LMDQHEELAE HLPADMVAQA RLAAERRSAT
AASAVYRNRE AVQREGQRSD HSRQVAEAVA AQAEVKPARQ PVPQMLDKAG VATLLRLMFI
SQPAAIRTHH FGILSDVCEN RQNRLEVIST LLQILQDGST DMDAVERSFG QLSLKARQPK
EKDLQKTPTS LKRSLTNINP GVVIQHNSDV SPLMIVQQCL DLLGELCRNL HIPSLFLTEH
EILGSSLKRT LSRKGKGKDL KANKYAINSL LSLLGRSLVM ESSAVMQLLA DLLNKVTYPL
QALERRRREA EEEAKKTTVS EPATNSTEAA GASTAESQAG QSSSTATDNN AEAAPTATAA
PGPAAEQADA DADKSKTEET KAAEAKKSKQ LQPPVIPFHN LTLVVNIFVA RECSSKTFQN
TISTIKNLSN IPGAKMVFGQ ELVRQARLLS ENIVRDLDDL LPHILKAESG TEIQGVALAK
FSPGASEQNK LLRVLTALDH LFDSRAKKTD DELAGKESEK QEFISSLYHN STFGTMWEKL
SACLSAIHQR ENMVNVATIL LPLIESLMVV CKNTTLSDAP TSQSQMSKEM LLSSPPPENR
MAGLFFNFTE DHRRVLNELV RNNPKLMSGT FSLLVKNPKV LEFDNKRNYF NRSVHAKSGN
QTRPSYAPLQ LSVRRDHVFH DSFKSLYFKK GEEMKYGKLN IRFHGEEGVD AGGVTREWFQ
VLSRQMFDPN YVLFIPVSSD RTTFHPNKLS SINDEHLMFF KFIGRIIGKA LYEGRVLDCY
FSRAVYKRIL GKPVSVKDME SFDPEYYKSL VWMLENDITD IITETFAVED DAFGATETVD
LCENGRHIPV TEDNKHDYVR LVVEHKLLAS VKDQMAEFLT GFHDIIPAEL IAIFNEQELE
LLISGLPDID VDDWKSHTEY HNYTPSSQQI QWFWRAVRSF DKEERAKLLQ FVTGTSKVPL
NGFKELEGMN GVSRFNIHRD YGNKERLPSS HTCFNQLDLP EYESYEILRA QIMKAITAGS
DYFGFA
//
