ID A0A2G5EKI5_AQUCA Unreviewed; 3687 AA.
AC A0A2G5EKI5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=AQUCO_00700539v1 {ECO:0000313|EMBL:PIA56266.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA56266.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA56266.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; KZ305024; PIA56266.1; -; Genomic_DNA.
DR STRING; 218851.A0A2G5EKI5; -.
DR InParanoid; A0A2G5EKI5; -.
DR OrthoDB; 1214833at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000230069; 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; cd14327; UBA_atUPL1_2_like; 1.
DR Gene3D; 6.10.250.1630; -; 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 InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR PANTHER; PTHR11254:SF398; HECT-TYPE E3 UBIQUITIN TRANSFERASE; 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; 2.
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.
DR PROSITE; PS50330; UIM; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1300..1341
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3346..3687
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 717..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2040..2071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2099..2130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2151..2213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2388..2414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2513..2536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2564..2594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2613..2633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2731..2757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2967..3025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1740..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2159..2193
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2194..2209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2564..2591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2613..2627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3654
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3687 AA; 406298 MW; BAC6C8E10AEEF257 CRC64;
MTTLRSSLPS RLRQLLSGEG AVGPSLKLES EPPPAIKAFI DKVITSPLHD IAIPLSGFRW
EYNKGNFHHW RPLFLHFDTY FKEHLSNRKD LLLSDNISDA VHFPKHDVLQ ILRVMQTILE
NCHNKSSFGG LEHFKFLLAS TDPEILIATL ETLSALVKIN PSKLHVSGKL VGCGSINSCL
LSLAQGWGSK EEGLGLYSCV VANEKTQEEG LSLFPSDLEN ECGKSQYRLG STLYFEYHAV
NSQNSEDTKK PSSLCVIHIP DLHLRKEDDL SLLHHCVEQY NVPPEHRFSL LTRIRYARAF
RSPKTCRLYS RICLLAFIVL VQSNDAHDEL VSFFANEPEY TNELIRIVRS EETIPVSIRT
LAMLALGSQL AAYSSSHDRA RILSGSSVIS AGGNRMILLN VLQKAVLSLN VSSNPSSLSF
VEALLQFYLL HVISSSSSGS AIRGSGMVST LLPLLQDISS AHMHLVCFAV KALQKLMDYS
NAAVSLFKDL GGVELLSQRL QTEVNRVISE PGPSDKSVVI GELDKFDDDL LYSQKRLIKA
LLKALGSATY APANTTRSHN SQENSLPGSL SLIFQNVERF GGDIYFSAVT VMNEIIHKDP
TCFNVLHELG LPDAFISSVN AGIHPSSKAI TCVPSGLGSI CLNAKGLEAV KETMALRFLV
DLFTSRKYVL AMNEGVVPLA NAVEELLRHV SSLRGTGVDI IIEIIDKLAS LGDDACSGSS
EKGDGSNAME TDAADGENVG SSSLVTAMNS TSDGINNERF VQLCIFHVMV LVHRTMENTE
TCRIFVEKKG IEALMKLLLR PSIAQSSEGM SIALHSTVVF KGFTQHHSAP LAHAFCSFLR
DHLKKALTGF GSASGSFLLA PRTAPDRSIF SSLFIVEFLL FLAASKENRW VTALLTEFGN
GSKDVLEDIG RIHREVLWQI SLLDDSKPDI EDAGAGSTTE SQKPEPNSNE TDDQRFNSFR
QFLDPLLRRR GLSVESQFFD LLNLYRDLGR ASGAPQRFSM EGQSNLRLGS SHQLHRSISS
EAAGSITRLE GDKVRSYYSS CCDMMRSLAF HINHLFLELG KVMLLPSRRR DDSLTVSPTS
KSVVSTFASI ALDHLNFKGH VDPSRSEVPI STKCRYLGKV IDFIDGILLD KPDSCNPILV
NCFYGNGVVQ AVLTTFEATS QLLFAVNRAP TSPMETDDGN SKQAEKEEAD HSWIYGPLAS
YGTLMDHLAT SSFVFSPFTK HLLAQPLFNG SVPFPRSAET FVKVLQSMVL KVVLPIWTHP
HFTDCGQEFI TTILSILRHI YSGVEVKNVN STAVTRASPP LNESTITMIV EMGFSRSRAE
EALRQVGTNS VEMAMEWLFS HPEEVQEDDE LARALALSLG SSGTSTTDEQ VTDAVIPPEQ
EEDMVQLPPV DELLSTCMQL LHVKEPLAFP VRDFLVMISS QNDGKDRSKV LSYIIDHVKL
CSSVSESGNV TMLSALFHVL ALVLHEDSVA REVASKNGLV TIASDLLSQW DPSSVDGDKQ
VPKWVTAAFL AIDRLLQVDP KLNSEFSEQL KKDDLSNRDA SVVIEEDKPK KLQSTLGLDS
LHIDLNEQKR LVEIACRCIR NQLPSETMHV VLQLCATLTR THSVAVHFLD AGGLPSLLSL
PTRSLFSGFD NVASTVIRHI LEDPNTLQQA MESEIRHSLV ATANRHSNGR VTPRNFLLNL
ASVVSRDPVV FMQAAKSVCQ IEMVGERPYV VLLKDREKEK IKEKEKEKTS DKDKQQVTDV
KNASSDLSSM TPGNGHGKLA DSNTKNVKVH KKSPPSFASV IELLLDSVIT FVPSSKDDGV
IGEVSSSSLA DMDIDDATNK GKGKAVATVS EPDEKNNQED SASLAKTVFV LKLLTEILLT
YSSSVHVLLR RDSEVANYRG LHQRGHPGNS TGGIFHHILH KFLPYPGCFK KEKKVDGDWR
QKLSTRASQF LVASCIRSVE GRRRVFTEIS SVFNDFVDSS DGFRSPNCNI QAFIDLLNEI
LAARSPTGAS ISPEASATFI DVGLVRSLTR SLQILDLDHV DSPKVVTGLV KALELVTKEH
VHSADPSSGK GENSVKPPEQ NQSEGTETGG NRFQSLENAY QSNNDEVPAD HIEPFNAVQA
SGSSESVTDD MEPNRDIDGS FAPGTEDDFM HENSEDARDL ENGIETVGIR FDIQHNGQDN
LDEEDDEMSG DDGDEVDEEE DEDEDDDEEE HHDLEEDEVH HMSHPDTDQD DHEIDEDEID
EDMLEEEDED DEDDGDGVIL RLEEGINGIN VFDHIEVFGR ENSFPNDTLH VMPVEVFGSR
RQGRTTSIYN LLGRTGDNGA ASQHPLLTEP SSTMHPSQSR LSENAGDAIF PDRSLENASS
RLDSIFRSLR NVRHGHRFNM WSDDSQQRGG SNVPSIPQGL EEWLVSQLRR PVPEKSSETD
KTTVDSQAKV EANQSEVGVG VETHVDNNTT DGSVSLPPPN ADMMVGDGNL DNRSEADEFV
QAMDASGAHT QSVDMQYERN DGVVRDVEAV SQESGGSGAT LGESLRSLEV EIGSADGHDD
GGERQGSLER LPLGDLQPAR LRRSNVSLGN TVTANRDASL QSVTEVSENA GQDISQGVPT
EEQQTNREAD SGSIDPAFLE ALPEELRAEV LSTQHGQVAQ PSNPQPESGG DIDPEFLAAL
PPDIRAEVLA QQQVQRLQQS QELEGQPVEM DTVSIIATFP SDLREEVLLT SSDAILANLT
PALVAEANML RERFAHRYHS RTLFGMYPRN RRGEASRRGE AAGSGLGRGG GSIASRRSAG
GKVVEADGAP LVDGEALKGM IRVLRVVQPL YKGQLQRLLL NLCAHRETRA SLAHILMEML
LLDTRKRADS SSSSAEPSYR LYACQNYVMY SRPQFSDGVP PLVSRRVLET LTYLARNHPY
VAKLLLQLEM PHPPLQGLQE SDPRGKAIMV MEEDNMVRSE PKGDVAIILL LSLLNQPLYL
RSIAHLEQLL NLLEVVIDNA DNNSSLSIKP GASPTDQPSG PQTAVSDAEM NSDAGGSSSG
GETKLCKTDE PPEPSTSGSS KESDTHAILL SLPQGELRLL CSLLAREGLS ENAYVLVAEV
LKKLVAIAPV HCPLFITELA ESIKSLTGSA IKELHIFGEA EKALLSTTST DGTAVLRVLQ
ALSSLVTSLQ EKEKDIQPLP GKEHSDPLSQ VWDINAALEP LWLELSTCIS KIETYTENAP
DSNATRNVTS TATGVMPPLP GGTQNILPYI ESFFVTCEKL HPGQSGVVHD FGIATTSEVE
DATTSTGQQK SSGTTSKVDE KHIAFVKFSE KHRKLLNAFI RQNPGLLEKS FTLMLKVPRF
IDFDNKRSHF RSKIKHQHDH HHSPLRISVR RAYILEDSYN QLRMRSTQDL KGRLTVHFQG
EEGIDAGGLT REWYQLLSRV IFDKGALLFT TVGNDSTFQP NPNSVYQTEH LSYFKFVGRV
VGKALFDGQL LDVHFTRSFY KHILGVKVTY HDIEAIDPDY FKNLKWMLEN DISDVLDLTF
SMDADEEKLI LYERTEVTDY ELIPGGRNIR VTEENKHEYV DLVAEHRLTT AIRPQINAFL
EGFNELISRD LISIFNDKEL ELLISGLPDI DLDDMRANTE YSGYSAASPV IQWFWEVAQG
FSKEDKARLL QFVTGTSKVP LEGFSALQGI SGSQRFQIHK AYGSPDHLPS AHTCFNQLDL
PEYPHKQHLE ERLLLAIHEA NEGFGFG
//