ID A0A218XLW8_PUNGR Unreviewed; 3544 AA.
AC A0A218XLW8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=CDL15_Pgr012134 {ECO:0000313|EMBL:OWM85884.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM85884.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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:OWM85884.1}.
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DR EMBL; MTKT01001111; OWM85884.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000197138; 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:SF446; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1181..1222
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3212..3475
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 575..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2186..2206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2218..2332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2373..2420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2829..2879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1927..1966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2258..2272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2273..2332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2829..2873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3544 AA; 385432 MW; AF710DFDCE6A2EEC CRC64;
MQQHLSALLA STDVDVVEAC LQTLAAFLKK AIGKCSIRDS SLSSKLYALA QGWGVKEEGL
GLVACALPNG CDPIAQELGS TLHFEFYADK DSANEQQTGE GLKIIHLPSV SSCPESDLEL
LDKLIKEYKV PSSLRFSLLT RLRFARAFGS LASRQQYTSI RLYAFIVLVK ASSDADDLTS
FFNAEPEFIN ELLSLLSYEE EVPEKIRILC LLSLVALCQD RNRQASVLAA VTSGGHRGIL
SSLVQKAIES VTSGSSKWPV VFAEALLSLV TALVSSSNGC SAMREAGFIA TLLPLLKDTD
PQHLHLVSTA VHILEAFMDY SNPAAALFRE LGGLDDTVAR LKVEVSYIEN GAKQQVEATD
CGENVQAVAP AASSDLDNVQ PLYSEALVSY HRRLLMKALL RAISLGTYAT GNASSVYGSN
ENLLPQCLCI IFRRAKDFGG GVFSLAATVM SDLIHKDPTC FSLLDAVGLP SAFLDAIMDG
VLCSSEAVSC IPQCLDALCL NTAGLEAVKD RNALRCFVKI FTSRAYLRAL TGDTPGTLSS
GLDELLRHAS SLRGSGVEML LEILNTISNI GSAGETTNLS SESAPVPMET DAEGGSSVSP
DEGDSSKAVV NSEQTSETSS DASVTNIEGF LPDCVCNAAR LLETVLQNAE TCRIFVEKKG
IEAVLQLLTL PSMPLSVPLG HSLSIAFKNF SLQHSASLAH AVCSFLRQYS STTNSLLESV
AGTPLAAVES AKQAKILRNL SILEDILSLS IFLLKGTTTL FTELGAADAD SLKDLGRTYR
EVIWQVSSCN DSKVEEKKAV EQDQENADAG SSNPVARESD DDANMPVVRY MNPVSIRNGS
QSLWGGEREF FSVVRSGESL HRRSRHGFSR IRGGRTGRHL EALNLEPEVQ TSTPETSSHN
VKKKSPDVLV LEILGRLATT LRSFFTALVK GFTSSNRRRG DSASMVSASK TLGSGLAKIY
FEALSFSGHS NYQRTDLSLS VKCRYLGKIV DDMAALTFDS RRRTCYASMI NNFYVHGTFK
ELLMTFEATS QLLWTLPYSA PAPATDHDKV VEETRLSHST WLRDTLQSYC RELEYFVNSA
FLISPTSTSQ AQQLIQPVTT GLSIGLFPVP RDPEVFVQLL QSQVLDVILP VWNHQMFPNC
SPEFIASMIS LVTHVYSGVG DVKRNRAGIT GSTTQRYMPP PPDEATITTI VEMGFTRARA
EEALRRVESN SVEMAMEWLF SHAEDPVQED DELARALALS LGNSSETTKS DVADKPMDVA
TDGPQAKAPP VDDVLSALVK LFQNSDVMAF PLTDLLVTLC NRKKGEERPK VISFLIQQLK
LCRLDFSTDT SALCMISHVI ALVLSEDGSA REIAAQNGIV SAAIDILMNF RARNELADET
VVPKCISALL LILDNMLQPR PKVLSENSEG VNTGSLAEPS PEQDSLSILA PVTENKAGSE
LPDKESGTVL EKIFGNSTGY LTIDESQKLL QVACDFIKQH VPSMMMQAVL QICARLTKTH
ALALQFLEYG GLAALFSLPR ACFFPGYDTV ASAIIRHLLE DPQTLQTAME LEIKQTLSGS
RHGGRVSPRT FLTSMASVIS RDPTVFMKAA SAVCQLETSG GRTLVVLLKE RDKSKSSASE
PGLSLNESGN KMQDGSVKCS KSHKKVPANL TQVIDQLLDI VLKFPSSKGQ EDSGCDLTLM
EVDEPDTKVK GKAKVDSTRK SDSESERSAA LAKVTFVLIL LSDILLMYAH AVGVILKRDL
ELQGSNQLES SGNGGLLHHI LHHLLPLSAQ KSAGPDEWRD KLSEKASSFL VALCGRSAEG
RRRVICELVK TFSSFSNLES NSSRTTLLPD KKVSSFAELA YSILSKNSSP GNLLGSGCST
DVAKSMIDGG MVQCLASILQ VIDLDHPDAP KIVTLIVKSL ESLTRAANMS EPVFRPEALN
KKKNAISSET VNEQASAPSP AELAEENQDS FNQQEAPGTV EMQEQQHRGG SPEGEGNMHE
ENPNNSEGQD MRNEVEAMAS SPTTNLGMDF IREEMEDGGP PHGGNHIEVT FRVEGRADDD
MVRWREALDG LDHHLQVLGQ PGASGGLIEG WNMDDLFGLR RTLGFERRRQ TGRSSFDRSA
TEASGFQHPL LVRPNQAGNM VSLRDLESLP ADSFDASHFY MFDAPVLPYD HVPSSLFSTR
IGSSSVHPPL GDYSIGLDSL QLPGRRGLSD GRWTDDGQPP AGPQASAIAQ AVEEQFLSQL
QRSSPPAERQ LQSSGPQENQ LLDAATNNGS RQTAEGGIDE TQRSEDQNEE IGNEVRNQQI
NPAVESIPSQ EQINPESSAA EEPMSIQPLS LNSSPNQQDN MEIGNGDSAT ATGEGETFLE
FVISSMETGG GQADPDAEDV SARAVVRDES LESTDIGAAD GTASGMPDDG QAAAARPTTV
DVDMSSSDNE IGQADPSGAV AESLQPEAVA TVNADLPEQA AVNSEVPGGN AIDPTFLEAL
PEDLRAEVLA SQQAQPVQPP AYVPPSADEI DPEFLAALPP DIQAEVLAQQ RAQRVTQQAQ
PVDMDNASII ATFPADLREE VLLTSSEAVL SALPSPLLAE AQMLRDRAMS HYQARSLFGG
SHRLSSRRNG LGFDRQPAMD RGVGVTIGQR AASAVSDNLK FKEIEGEPLL DSSALKALIR
LLRLAQPLGK GLLQRLLLNL CAHSATRANL VHLLLGMIKP EAEGLPGGLA TINSQRLYGC
QSNIVYGRSQ LLDGLPPLVL RRIVEILTYL ATNHSAVASM LFYFDPSSLA EASSLGYLDS
KSYKGKEKVV EGVSSNGSQD AQAEVPLVIF LKLLNRPLFS RSTTHFEQVL GLIQVVVYDA
AAKLESESQS EKAIDDAKVP PEQTGDLKKE KSSNGPENTS DSNDKEAKST TDETSSSKPK
TSVNIYDVLL QLPKSDLRNL CSLLGREGLS DKVYLLASEV LKKLSRVAAP HRKLFIMELS
ELAHDLSSSA VNELVTLRNT HMLGLSAGSM AGAAILRVLQ ALSSLTAAGV GGAKGLDADK
ELEEQTTMWK LNLALESLWQ ELSDCIGVTE AQLSQSSLGP TMPNVNVVDQ VQGISASPPL
PPGTQRLLPY IEAFFVLSEK LQASSSTTVQ QDQATVTATE VKECVGASTS SSTTKSSADS
QKRLDGLVTF VKFAEKHRRL LNAFIRQNPG LLENSLSMML KAPRLVDFDN KRSYFRSRIR
QQHEQSLSGP LRISVRRAYV LEDSYNQLRM RSTQELKGRL NVQFQGEEGI DAGGLTREWY
QLLSRVIFDR GALLFTTVGN NATFQPNPNS VYQTEHLSYF KFVGRVVAKA LFDGQLLDVH
FTRSFYKHIL GIKVTYHDIE AVDPDYYKNL KWMLENDVSD IPDLTFSMDA DEEKHILYEK
NEVTDYELKP GGRNIRVTEE TKHEYVDLVA DHILTNAIRT QINSFLEGFS ELILRDLISI
FNDKELELLI SGLPEIDLDD LRANTEYTGY TAASSVVQWF WDVVKGFTKE DMARFHWRAL
ELYKVYQVLR GFRFIKLMGL PIDYPQHIHV SINSTCQNTL RKSSCKTACF LQSMKPAKGL
GLVN
//
