ID C1GVT7_PARBA Unreviewed; 4111 AA.
AC C1GVT7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PAAG_02632 {ECO:0000313|EMBL:EEH40656.1};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH40656.1, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH40656.1, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293997; EEH40656.1; -; Genomic_DNA.
DR RefSeq; XP_002795156.1; XM_002795110.2.
DR STRING; 502779.C1GVT7; -.
DR GeneID; 9098728; -.
DR KEGG; pbl:PAAG_02632; -.
DR VEuPathDB; FungiDB:PAAG_02632; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_1_1; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002059; Partially assembled 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; 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 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; SSF48371; ARM repeat; 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:UP000002059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3775..4111
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 210..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2106..2158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2388..2583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2725..2765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2910..3000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3076..3100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3152..3176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3374..3481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2036..2050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2106..2123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2124..2151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2388..2405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2497..2540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2554..2583
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2910..2972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3155..3173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3374..3397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3398..3421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3441..3481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4078
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4111 AA; 459354 MW; 469BD0E92145A985 CRC64;
MGRIKKVAGL KHEATISPAL ATFIQQTITV DIPELPSYLS TFPRRWPFPR GDLYHWIRVL
NRFDEILQLV VEKYDLKSGP QTKPFGRLVL QDACVSAGIA PTTVAAETHL DKLGFGPEGD
RELVEALLDF SRLLLEKCGN RTLYSSSDRL NDLLNTTSLS LLQCVLRLGI SLAQRYFSRQ
RQSNSTHFHQ SLLASHYNIE LERVEKLAAP FPKPAPAKPA DASSSFKGKE KITHIQASRR
GSVAKCNAND LIALTKEPSD TSEPDGLPAN EWEEWGSISM SYYSPPSDNN GPAPTEASGS
TPHTPATPAP LRRTSTHPGS RMSRSSATDD SPTAEAHSPA HKPEEASRGM KVREIPSSTI
VSSRIEHVLQ EHLEDLPKDS SKYDLLHRLR VAYALTSTTE TRRQILAIRV LAVTNLAYIY
PETLFQQKVL YHDADVPKRL QLSYQLAEFV HLGATGDITA STLNQTFALN CLDALAKHKT
RAADVCAALN VNVNHGILMF LTRKAVADLA VEESPDDPPE ADDWREALFT LLRTLPNCGT
RTPETLVAAG LIPLLVDILN LRTEKARRIY PRVMEFMDTF VHSVRDALAT LAAARGFHGI
SDLISYETRT SFDLVAKGQG IPVQFRTPAI DYQVPYFQQQ SLRWLFKFVN HVMQHDSGGF
ERLLRNLIDS PPLLTALRLV LENARIYGSH VWSGAVNILS HFIHNEPTSY AVIAEAGLSK
SLLESVTGRS IPSDATNNTA AAAAAAEEGG DTPTQLRPFF IPALAEPSEH ETLRSKIVRP
PDRKLAEGIL PSTEAIVCIP QAFGAICLNQ GGLELFRKSD ALESFFDIFE SPEHVKCMKT
DSNLLRVLGN SFDELVRHHP PLKSAVMSSV LLMVARVTQH CKSKAWERGM GAKLWTEGED
GKLSVAGGPS SLVGDIGSAF SNTHGEQQSS SGAEPADSEM QSTTTTPELT SPKLGNWDFN
DVDSHGLSVP NYMFPVVRFL HAFFENHTIC NTFIEAGGVE YVLDFATLQS LPFDFHNTEA
SQQLTQVIHL MVEVKPHLVL PSLTKRTQDA VDRLAPFWRH SGNAGFFSPL THSRKQQPQD
STAKIPDSED VRATGTYFAK HLVAVRTLTD ILREAYTPPN YNTRPSQQTS PFVQVNLADK
YVALIKSLGS LHSACVWEEI LLQKDMPEPW NEATRVSEYG FGGEEVIEPP NTAPADDASE
PGDVVPGNAA ERAATVVNSV AALPNGEARS QNSAPHSTLS VEKSAAFKNV KTLRYLLSSL
PSSITGFFHL LGHGLISKRR MDTYQRQKAG TVADAIASVV LEQLDLDAAK KTSCVKDRFS
YLIVILSSFS QLLFDTTAER PHSHCLTMIL SAFKKLNGIQ AMKQLCGLFL NEIKSLGPQT
PVNSNSRDVP ARLASAYGGI KIILNFFSEM TSAQYIIDSS QTQAMASTSG DRDRPDYFLP
AQFLVELRME VIPMVQEMWN SGFVEEASSS ILKSLIDILR SVLESEYEMG AFRRGETLPP
LVSVTPKIFT CHRDRLSTLK ENGHDESLAR EALYRCNNSA SASEEYCTSQ LGLRPPPRSP
IPPNDLEQTT GSSSSRRDSI FGNLGSPQQQ LDNALATPSA QTDLASLLGH IAQPSTNEES
ITSLAENPVP NQIVQGDNAI SSSSGLLAMS IDNILNDQEE PRSENSNTPS RRAENAVRSQ
PTSPPTPSPK RREVVAIEDL DMERDKVRSN LIERCLDVLN VHHDITFELS DLIGSATAKL
RDPVNFRREV GETLMHFLIS LQMEENFQSA GKKIAAYAGL LALVLQDREV YEATLEELKE
NFSSLLGFIN IPSFSSEKPT EESCPWIPQV LLILEKMLSD DATPTLIRWN PPNSDSPAAP
EEPAALEELV VSLSNKVELF EAMVDILPRI GKDETLALSV ARILVILTRE REIAVRLGEK
RNLQRLFVMI KQLAGASDEK LQNAFMVILR HIIEDDDTVR QIIRSEIVAG FESRSPRQTD
TTGYVRQFAH LILRNPALFV EVTNEKVKLQ RYDSHQRPQL LVLKSEPTND VLSGRDETSS
RQEDTETASK SETLEALTEP QDVRASEGKD VKEKGRAVEL KAPVIEHPDG VIHYLLSELL
SYRDVEDKES PVEPSERTTP RTETQGDIEM ASGPASPTST TSGNQTTKPP KKSDKPQFKA
DEHPIYIYRC FLLQCLTELL SSYNRTKVEF INFSRKADPF ATAPSKPRSG VLNYLLNSLV
PIGTLEHSES IFFKKRVNTS NWAMRVIVAL CAKTGEFSAP SRRRTIPDGD NEPDLLFVRK
FVLEHALKSY KDANASNEPL DTKYARLLSL ADLFDKMLSA TSSADGTTHY PSSTRQVAKI
MFEKHFISAF TASISDIDLN FPPAKRAVKY ILRPLNKLTQ TAVLLSESSS IQTTPGQTDE
DDISSATSVS DVEDEREETP DLFRNSTLGM FEPNHEEETS SEESEDDEEM YDDEYDEEMD
YEDDLPENDG EVVSDDEDLD ERGPIEGLPG DSGMDIEVLI EGDDDDDEDE EEDDDEDEDD
EDDEDDDDDD EDEEGSSAMD DDLIAGEITG DNDNDSLQDG DEGEWESEDI SDNDEDEDGM
NHQLENDLED FAQGDHRSNL QDVFRLLGEQ NRNRLELRRL ELDMGMGGEL HNDLLDDEMH
DDQDEDEDEE VDELEGLDAL DGDDQFLQTF DFDHPERFIM HDADPAMDHH RHHHGQFRGI
PPPPWSMFSG SLGNRHGIIP IPSYRAHRNQ VPPRGNDDGT NPLLRRNDRP ADGGPGSRGP
PEALSDWVHA IDPSHQGRLL SMDSPVTFMN AIMQALGQGG GGFGVISRPD GVHVRLDQGH
VFTNRIQDLF GLARPQTTTT RPRDDPYQAV TFALSVTSTR WQEEARLLFS SHYLEKAQRI
INSLLKILVP PAIQEEKERQ KKLEEELKRQ EEERKEKERQ EQIAKEEAER ERKQKEEEEA
ALRRQEEVER AERAAEENAQ RSAEHPESEP MDDVQPTETE QAAVENEPAA GSSEPVPRVH
TTIRGRQLDI TGMDIDPEYL EALPEDIREE VIMQQLTEQR SQAAASGEEP SEINPEFLEA
LPPDIRDELL QQEVADRRRR EREAARRNAA ANGSASAADD MDPASFIATL DPSLRQTVLA
DQPEEILASL GPEFVSEARA LTGRRLAQFA DVGRLDQRSR PDTSQRDQGA KKPQRRQIVQ
MLDKAGVATL LRLMFMPLQG NARHHINDIL HNVCQNRQNR SEVLSLLLLI LQDGSADVSA
VDRSFAHLSL RAKTPTSAQR TPQLKRTLSL PVPSGNNDVT PLIVIQQCLG ALSFLTQYNP
HIGWFFLTEH DTVSALKMKT WRKGKGKEHR ASKFAVNTLL ALLDRKSIMD SPSCMEQLSG
LLNSITQPLT LLLRKDKEKQ EKDTKEKEAK EKETEVPENT TQAAQPAQSV EDITQQNEAA
GTADEAAHLS DTPMLDVSPN EQGHDRAEGS EEVAGPSTEE KAESRKPVED DKQKKPRILE
PPVVPEHNLQ LVVRILAARE CNGKTFRETL STINNLSSIP GAKEVFGKEL IAQTQSLSNS
ILVDLDELLP HIDQAETGID VQGMALSKFS PASSDQAKLL RVLTALDYLF DPNRLDKEKF
SEPETSNKED VLKTLYEGAT FGPLWVKLSD CLHAIRQKEN MLNVATILLP LIESLMVVCK
NTTLKDAPLS RHGREYSVSS PPPESGMEGL FFNFTEDHRK ILNELVRQNP KLMSGTFSLL
VKNPKVLEFD NKRNYFNRRI HSRGTEIRHT HAPLQLSVRR EQVFLDSFKS LYFKSADEMK
YGKLNIRFHG EEGVDAGGVT REWFQVLARG MFNPNYALFI PVASDRTTFH PNRLSGVNQE
HLMFFKFIGR IIGKALYEGR VLDCHFSRAV YKRILGKSVS IKDMETLDLD YYKSLLWMLE
NDITDILTEN FSVESDDFGE KQIIDLVDNG RNIPVTQENK EEYVQRVVEY RLVGSVKDQL
DNFLKGFHDI IPADLIAIFN EQELELLISG LPEIDVDDWK NNSEYHNYSA SSPQIQWFWR
AVRSFDKEER AKLLQFVTGT SKVPLNGFKE LEGMNGFSKF NIHRDYGHKD RLPSSHTCFN
QLDLPEYDNY ETLRQRLYTA MTAGSEYFGF A
//
