ID K5W2F3_AGABU Unreviewed; 3600 AA.
AC K5W2F3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 28-JUN-2023, entry version 53.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=AGABI1DRAFT_56206 {ECO:0000313|EMBL:EKM80974.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM80974.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
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; JH971388; EKM80974.1; -; Genomic_DNA.
DR RefSeq; XP_007328076.1; XM_007328014.1.
DR STRING; 597362.K5W2F3; -.
DR GeneID; 18830155; -.
DR KEGG; abp:AGABI1DRAFT56206; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_0_1; -.
DR InParanoid; K5W2F3; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008493; 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 CDD; cd14297; UBA2_spUBP14_like; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; 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 InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
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; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008493};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1257..1297
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3265..3600
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 209..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2259..2282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2426..2498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2677..2699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2907..2954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2014..2029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2137..2163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2426..2463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2919..2951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3567
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3600 AA; 400036 MW; 7797595163CE4EFB CRC64;
MKITSKSKKA VTPPAAVAEF ISKILNASDD QLVHILGCVE SWKWPRSDLN AWIKVLNKFD
SILEDIINQY ELDKVQLVPF PSQTTTLVSE LLRFQRLLLE NSTNRKTFNS YDRLNSLLLC
SDLDIVLLSL QVLLRPAQQY SSQSSVTHVL SHATSRLLAL AKRWPHLREY GVSLVDLVSS
KNKAEIDGLP AEARDVSFSF YRMETSAATA RDKTRESTSD TPATPPKSQT ASVTGPINIS
LSEATLQSQP AMNILVDSVR SHRVPEEEKF ELLNRIRVSQ ALSKTGEAQR EKLVIARLLA
IAIYALTHTD SQTTATFFLY EPDLISNVAE LLHVEYDVPI AVQTAAIAVL DSLTRYRNRC
QEVLTAVNAG VNHGILMALF RKTVHDVANP SSSIPQSFIE ALLQFVTLIA THTTGVNMVV
GAGLIPLLIQ LVENRLSNRL PVVSKTLQLI DSVLYSFQNG FSLFVAARGV SILVDRIEYE
IDHDIQNYKT IAEIQDFNFA GSCLPIPRSS VLKHLLRTMH RMMQSSGTSE GLRGLIDTSL
IKSVKSIIDN RGLFGPSVLP IAINIMATFV HNEPTSLSII QEAGLPESFY KAIETGIEPS
IEVLQSIPNA LGALCLNETG QSQLSNRPSI IPAIFAIFTS ERHLKVLIDK ENAVIIGTAI
DELVRHHPLL KAAVFASLKS TLGAIEEIGR NFQVSTELLH WYRLAPAVAT TVDTDVKMED
FESIQAKAVQ AEAADFSGGD VADEAASKSH DNTVVSFIDV LCRFLEGFFQ HGPHCKDFIT
LSDGLTYIGR LTALPCLPYD FSNSVTSDSL VQVMRTLVDF ATNETLVYLS KIVHDSLRDT
TDFWNSLEPS SKLLPLLDIN DTNWAVCNDQ FRNLVTLHIR TSLLSDVFGT VGYSHGRGAI
TLLQTLMTSC GGQTIPELGA LHRATIWENM VLNAALMKRG IPQTSPVQSP FNGTPNVSTT
NLIEATNSLN TGSTANGIQG VDDGRPTGEE TARPKQDETP VSRNAAALKY LTHGMPNVLA
PFFQAIVKMF HARRNPEASQ KQQILDSAGV IASILLKHLQ IPQFDDAPSL NTYYSVIFGL
YNLLFVDERT STNTLHTVEL RAFYQIGGFD ELLRIGTSLA ESIEEITRIR EEERTDLLSK
TLIHAYGGLK VALHLLHPII SSKSLCESPQ TLLLITRDKK ETEPGFFDPN NFLVKLRLKV
LPLFRSLWEA PWLVQAPLGV SRSIVRSVLE LVNGENEQSK PETTSEAAIP TIPRPTGPDE
SRVQMLVDMG FPRSAAERAL VHTRNNVTAA TDFLLNHPFV FPPDPVPVSI PVATSSNAAG
EVEAVPSTDA QEQQASGEAV EETSAPEISS KTESESGQQK EGVKTMEEWK SALDEAREPL
RTLVSRQALL LLDEHQSLLF ELHSAFVRPS VYQSQAVRDL VDDVKSFSPY AHDVQEQPLA
NRCRLLALVL SEQPSSLDDS VRKELLDGLL ALLLSGMDIN NPPKWLASHL LVTEALLTLA
EEPRAISLSV PKVDEPIKTE ALNSGLPRAD AKNIIFEFVL RLLAIRDLPS DEFLSVLRLL
VYFTKDRKMV KHFLESEGLI HLFGRIGALE VSGGSSYIII ILRHVIEDRA TVQKVMTESI
KRFIQHQRNS IVDVNAYVRH CNAMAFRDTN VFLDVTKSLC DLDITYYDGF NPQLRLMSGQ
KDSEKTAPDE TSAKEEKRAE VSDVEMKPEP PVFEQPDDQH AENVIRLLYT ELAATVKSIN
EASTSNNLAK TSTEEMGQVE SLPTTQPSTD SASLAKVDEK PPPAARVTED KYQYACFLMQ
CMTELIISYD TCKVAFLSFV PKKKNQTPSK DSASKFRSVT LQFLFNDVIN PGTINPSSSD
SNRSHLSLCH WAMLVVVSLC VDTSTSPHEP KDISPELVAV RKYVLETLSR SLKDIPSIEN
LEVRYGKLLA FSDLCHRLLT VRFNHPNTNN RKHQDEIPTH IAKIMLEKNF VPTLTSALSD
VDLNYPHIRT LVDFILRPLQ YLTKIAIKMN RGSKNKEVTE IRVDESETTS LSSEENDSDM
SEDGAREETP DLYRNSALGM YGGEMDDGHF SGSEDMDEDE DEGDVEMDFE GTGSEDTSEA
TDDEEDELEE EEGEGEEDWD DVEEEEGHHG VDQNLVENDQ DDDEEEVLDD DEMEDEVDED
GNILWEDVPP PGDGLGSIGE DIDDEDDHGV PIQIVHHEED PDMASDDEGF RFEGGIFNAE
AGLPFGAPFI NISTGRDPPP VFLSRRNRSD SEDFQVFGRA RNAPAPPPET TTHPLLLDAS
NPSNRFTSNA RRGARHPHRN IAIGADLFQS LDDIMGPGST QFLQQILTAG GAHAFQLDMG
NGANVDRLHR RPNQGVISAA IRVERGPRTS SPKQGREFEP ILTLQRWAEE AKILNGEFVS
ERTGKLVNHV ILALLPAAAE AKKRANEAEK KKEAEEMSAA NDREEEDPGR QDTEPEKQAE
PVEEPTKLAS PILAPEETAQ VGQVAEASTE EPSTHDQRME VVTTDQDTLM TDATVHETHE
NADEAGSSRE AEVSAPQQRI TVMIHGSQVD ITDTGIDPTF LEALPDDMRE EVLNQHVRDQ
RAATVERPAD SQISAEFLDA LPPEIRAEII QQEAMERARL RADESAPTQP AHATEIDPAS
FIASLDPTLR QSVLMEQNDG FLQTLAPHVL AEAGSFAGGA RRPAQRNPPR ISGASAPPRK
FTADHDALLL LDKSGIAALV RLLFFPQVSK KSLLFKVLVN ICENTKTRAE LFNVLLSILQ
DGPGDLAAVD KSFAQLTVRN TSKPPTPKSV GKQKATSDYL AALTSTNTRI DAVPDLVVQR
CLESLTYIVS ANELASMFFL TEHELPAGLR KSSSKKGKGK EKQIPQTHYP IVLLLSLLDR
QPLIRTPAIM ESLVGLLATV TRPLASLKPK DDDRSQPAAE ETSQPQNPLS QLPVAQGESQ
GTTNISTGVP SDPVTALMDK EKKTSLEAIE ERILLANPPQ IPPTVLRLIV NILTVGECSG
RTFQQSLALI QHLSYVPDAR EVIAQELRSK TEEFGRVLHT DLDELVVALQ GPQEELNTVA
AKFSPASSLQ AKLLRVLKTI DYMYSSKTPL SRNEADVDKV QAIYESFRFT PLWRRLGDCL
SIIEERPETE HIAIVLLPLI EALMVVCKYA NIKSFNTIPR ALRGSVSPRT PTTPRESIED
LFITFTDVHR KVLNVMVRNN PSLMSGSFAL LVSNPRVLDF DNKRNYFNQQ LHRRPSSREH
YGTLQLNVRR ARVFEDSFQY LQRKSGDQIK YGKLSVRFYD EEGVDAGGVT REWFQILARQ
MFDPNNALFQ PCAADKLTYQ PNKNSWVNPE HLSFFKFVGR VIGKAIYDGR LLDAYFAKSL
YRQILGKPVD YRDVEWVDPE YYNSLCWILE NDPGVLELNF SVEADEFGVN RIVPLKDNGE
AIAVTQDNKR EFVQLSAQYR LYSSIKEQIE NLLNGFYEII PKELIAIFNE QELELLISGT
PDIDVDEWRA ATEYNGYSSS DPNIVWWWRA LKSFNREERA KVLSFATGTS RVPLSGFVDL
QGVQGVQRFS IHRAYGESDR LPQAHTCFNQ IDLPQYSSYE MLRQQLLLAI NEGGEGFAFS
//
