ID A0A1V6Z9V6_PENNA Unreviewed; 4073 AA.
AC A0A1V6Z9V6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PENNAL_c0001G09357 {ECO:0000313|EMBL:OQE96479.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE96479.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE96479.1}.
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DR EMBL; MOOB01000001; OQE96479.1; -; Genomic_DNA.
DR STRING; 60175.A0A1V6Z9V6; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000191691; 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; cd22249; UDM1_RNF168_RNF169-like; 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:UP000191691};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3737..4073
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 271..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1987..2055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2078..2097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2364..2423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2442..2528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2884..2938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3038..3074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3354..3441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1987..2013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2021..2047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2364..2378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2380..2411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2442..2456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2465..2486
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2487..2505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2506..2528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2884..2933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3038..3052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3354..3371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3413..3441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4040
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4073 AA; 452483 MW; CE59E5FAC8E5296C CRC64;
MGRIKKVASQ KHEATISPFL QEFIARATSL PVPELPSLLS TFPKLWPFPR GDLYHWINVL
DRFDEILASA VEKYFLNTGP QTQLFTRSVL EESYSADESK KPAEGVNAKL NALGYGSEGD
RELVEAVLDF SRLLLEKCGN RSLYSSSDRL GDLLNTTSLS LLQSTLRLSL CLAQRYHSRQ
RGTHQQSVLQ SHYALDIEKL QKIAAPFPRP VIASKTPFAA SPAVLAKGKE NTAQTKVNAN
ELVSLVRDDD GWEEWGDVRV LYYPSGSEQA RTTSEFGQIE QGSHVPTTPT PLRRSATHPT
PHSTQGSNGD ESPAVPGGKV EEATRGKVLE LPYSKISTAK VEDLLAANLP HLPLESKYEL
LQKLRVAKAL TASRATRQQI LSIKALAVTN LAHVQPESTF QSKVLQSDLE QPKRLQLAYQ
LAEVVHLGAS GDLVVSRSVQ TLAIQALDAL AKHKTRAVDV CAALSVNVNH GILMFLTRKM
VNELGPENND PDDAYYDEWR DALLALLRTL PSSSTRTPET LVAAGLIPMF VDILNLRTEK
SRRVYSRIME FLDTFVHAVR DALGTLTTAR GFDAMSDLID HETKTAFEKV NRGDGFPAQY
KNPSIDYQIP YFQQQTLRWM FRFVNHIMQH NGGGFDRVLR NLIDSPQLLT SLRLVFENAR
VFGSHVWSNA VNILSSFIHN EPTSYAVIAE AGLSKSLLAA VMGRELHVLE KPPAVEPEDR
ETEAGTEGEP AATQPPSAEA AIQSEEKQKD REYPIVRPQD TPLAPGIMPA ADALACIPGA
FGAICLNSSG LDLFQSSDAL DSFFEIFENP EHVKCLKDDP ELVRSLGTTF DELVRHHPAL
KTSIMSAVLV MATRVNILGR LKAWELGMGT KMWTQDVDGK TTLLGDVFSL FREIGTAVDA
PTDDPTSFGA PQLNVDTLPN GAKLVVGHLD HVLPSPGPDF EPKEKDAHGL SATDYLFPAL
RFLGAFFENQ TNCTSFILAG GTEFLLDLAT LQSLAFDFHS TNANQEITVL IHMLAETKPH
LVLPSLLRRA QAAVDNLSAF WTAPTGSGFF TELIKPGDSK KPALEPTAAA KSGTFFVRHL
NAVLLLTDVL REVFASPLYQ TRAGQPTSIF GQANLTDHYC SLISSLSNLL ASCVWEGILL
EKNIPEKWLK ATQASAEKQG SGKSKASQVT GDPQEPSATS GAEPQQESTG APETAPAQPG
QGSREDDTEV DEQCPAFKNA RTLRYLLSAL PTSITGFLHN LGLGIIGKRR TDPLQKQKAN
AMLVSDAIAE GILCQLRFDP ANSSDSTKHR FAYLIVILSH FSHLLYEVSA ERPTPNYLTS
VLISFNKNNG LKVLKDICDV FLADIKSLPS AESIPDQDKE LADRLASGYG GIKIILGLFA
DLTAGKFIVD SSQTQALTSH PERDRDRPDY FQPGQLLVEL RMEILPMAKD MWNSDFATQS
SSPIVRLLID IMRSSLDGEY ESGAARKADT PPILLEVPKK PFVVHTERAT ALLEKGYMDS
DLNKEALYRC NNILMAAEEY CKAQQWLRAP PRVPPGPGDI KTGVPEAASG IDSLEDPGLG
EVQPFNNGNP LDGAATLQML LARASRHDGM QRSPFGGGDI DSDMHDGLAR ALDNVLNDND
DMDSDDRGES SNQRQSESHN TGTSSSEPTG TSQTEPARRR HMVTVEDLDA ERQNIRSNLI
DRALDILNEH HDVSFELSDL ITSAIKKHSE PVNFRRDIGE TLVQSLVSLQ MEDFQTAGKK
IAAYAHILAL TLQDRDMYRA TLEELKDCFS TFLGFIKLPT PEKAEQETFP WVGHVLLILE
KLLSDDCRPP EVAWPLPSLD DPNPTGNEPA RLEEPFVALE KKTQLFEALV EILPRVGKDD
TLALCISRVL VILTRERSIA ARFGEKRNLQ RLFVMVKQLS SATNDKLQSA FMLILRHIVE
DEATIRQIMR SEIVAFFESK TTRQIDVSGY VRQMQHLELR APDIFVEVTN EKLRLLRYDN
QRPQVLGLKA DKDRQQKRGR PGILLEEHRS ESSAAGDTSA PEDADKGKED KGKEDKGKED
KGKAPTKGAE LKAPIVENPD GVIHYLLSEI LSYKDVDDKE AGPEIPEQAA DQSDTQTDVD
MAVDEPTPSI ASTAEAQASR GAKKAEKPQF KADDHPIYIY RCLLLQCLTE LLSSYNRTKV
EFINFSRKAD PLATTPSKPR SGVLNYMLNV LVPLGTMEHD ESLAFKKRSI TSTWTMQVLV
ALCTKTGEFG GVGKRRTEPK YEDDEPELAF VRRFVLEHAL RSYKDAMAST EPLDAKYSKL
MSLADLFDKM LSGYSFTNDA GFPTSTRQLA KTMFEKNFIP ALTSSVADVD LNFPSSRRVI
KYILRPLNKL TQTAVLLSEN SDITIQGDNE GDDISSATSV SDMEDEREET PDLFRHSTLG
MLEPRHDEEE SSTEESEGED DEMYDDEYDE EMDYDEDVAE DDGEVVSDED DDGMGPIEGL
SGDAVEVILD EDDDEDEDDD DEDHDHSDMH DDMYDGEIGG DRDNESLGDG EEDEWESEEM
TEDEEEVEMM NQFEDEMADM RQSTRHQGED QHLGDLFRAL SGSNVDNIHG DGLGGDIHEE
ILDDLDEDGS FLLILLSQIP LPQPTLLTSG PVEDEDEMDE LDEDMDDFDE EQGSYGDMEE
DDDLLEPWGW EGDEPPMARG HPQSRFRGGA PPAWATVTEI MPGRPSGLVP IQPYHRVHRN
QIPSRSNDDG INPLLVRTDR PDPAVPPRAA AADPFADWGQ TMDPAGGRVV AMDSPISFMN
AIMQAIGGQA APGFGVVTRP DGIHVHVDRR AVLPGRIQDM LGIPRGAGPP TRTRGDDPHT
AVKFGLGTTR NRWQEEARIS FSSPYSERTQ RIINTILKLL VPPAKEEEKQ RLKLAEEERK
RLQAERAEKE RQDRIAAEEK QRELKQKEEE ENARLQAEKE QQEAERQAAG VDEPMEDVQE
TDIAVETAGP SQPEAQPTEP ARRVYTNIRG RQVDITGLEI DSEYLEALPE ELREEVIMQQ
LAEHRSQAAA AGEEDTEINQ EFLEALPAEI REELLQQEAA DRRRRERETA RRQAAAAAGA
GAGAGAGATA STQPAEEMDA VSFLATLDPS LRQAVLADQP EDVLATLGPE YVTEARGMGG
SGRRMAQFGD LSAIDPRQRI EPAAGQEPKK EQRRQIVQML DKAGVATLLR LMFMPLQGNA
RHQLNDILHN VCENRQNRSE VISVLLSILQ DGSVDSTAIE RSFSHLSLRA KAPGIQKTPQ
AKRTLALQTA SSVSSEVTPI MVIQQCIAAL SFLSQFNPHI AWFFLTEHDS ASAGKLKSLR
KGKGKENRAN KFALNALLSL LDRKLIMESP NCMEQLSSLL SSITQPLTVL LRREKERQEE
GKGKDPERPQ IEAPADQAAE AADSSMDTSM TDAPLPTVET PGAPGQETAE GEEATSAEAK
KSEDSKEPAG DEKRKKRTIE PPVVPDHNFR LVVHILAARE CNGKTFRDTL STINNLSAIP
GARDVIGNEL VAQAQALSDT ILGDLEDLLP HIHQAKTGTD MQGLALAKFS PASSDQAKLL
RILTALDYLF DQARADKLKD IEPSAPKEDV LKKLYESATF GPLWNKLSDC LTVIRQKENM
LNVATILLPL IEALMVVCKN TTLKDQPLSR GSRELSVNSS APTDAGLSME NIFFRFTEEH
RKILNELVRQ NPRLMSGTFS LLVKNPKVLE FDNKRNYFTR RVHSRGAEPR HPHPPLQLSV
RRSEVFLDSF KSLYFKSADE LKYGKLNVRF HGEEGVDAGG VTREWFQVLA RGMFNPNYAL
FIPVAADRTT FHPNRLSGVN SEHLMFFKFI GRIIGKALYE GRVLDCHFSR AVYKNILGRS
VSIKDMETLD LDYYKSLLWM LENDITDIIT ETFAIETDDF GEKQVIDLKP GGRDIPVTQE
NKEEYVQRVV EYRLVESVRE QLDNFLKGFH EIIPPELISI FNEQELELLI SGLPEIDVDE
WKNNTEYHNY SASSSQIQWF WRAVRSFDKE ERAKLLQFVT GTSKVPLNGF KELEGMNGVS
KFNIHRDYGH KDRLPSSHTC FNQLDLPEYE SYEDLRQRLY TAVTTGSEYF GFA
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