ID A0A452S9H2_URSAM Unreviewed; 3614 AA.
AC A0A452S9H2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=HECT and RLD domain containing E3 ubiquitin protein ligase family member 1 {ECO:0000313|Ensembl:ENSUAMP00000028924.1};
GN Name=HERC1 {ECO:0000313|Ensembl:ENSUAMP00000028924.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000028924.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000028924.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 9643.ENSUAMP00000028924; -.
DR Ensembl; ENSUAMT00000032295.1; ENSUAMP00000028924.1; ENSUAMG00000021871.1.
DR GeneTree; ENSGT00940000155907; -.
DR OMA; LAICCQN; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd12881; SPRY_HERC1; 1.
DR CDD; cd14401; UBA_HERC1; 1.
DR Gene3D; 2.60.120.920; -; 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; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035768; SPRY_HERC1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22872; BTK-BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR22872:SF6; E3 UBIQUITIN-PROTEIN LIGASE HERC1-RELATED; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 5.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00449; SPRY; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 7.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 755..946
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REPEAT 2177..2218
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2375..2406
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2496..2537
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2750..2798
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 2799..2853
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 2854..2905
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 2906..2957
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 2959..3010
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3011..3062
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3063..3114
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 3254..3601
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 104..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1988..2008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3564
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3614 AA; 395952 MW; E4510930A8B2F17D CRC64;
AVFLVYLLNN SLLDTVSRFV LAALLKHTNL LSQACGESRY QPGKSLSEVY RCVYKVRSRL
LACKNLELIQ TRSSSRDRWI SENQDSADVD PQEHSFARTI DEEAEMEEQA ERDREEGHPE
PEDEEEEREH EVMTAGKIFQ CFLSAREVAR SRDRDRMNSG AGSGARADDP PPQSQQERRV
STDLPEGQDV YTAACNSVIH RCALLILGVS PVIDELQKRK EEGQLQQPST SASEGGGLMT
RSESLTAESR LVHASPNYRL IKSRSESDLS QPESDEEGYA LSGRRNVDLD LASSHRKRGP
LHSQLESLSD SWARLKHSRD WLCNSSYSFE SDFDLTKSLG VHTLIENVVS FVSGDVGNAP
GFKEPEESMS TSPQASIIAM EQQQLRAELR LEALHQILVL LSGMEEKGSI SLAGSRSSSG
FQSSTLLTSV RLQFLAGCFG LGTVGHGGAK GESGRLHHYQ DGIRAAKRNI QIEIQVAVHK
IYQQLSATLE RALQANKHHI EAQQRLLLVT VFALSVHYQP VDVSLAISTG LLNVLSQLCG
TDTMLGQPLQ LLPKTGVSQL STALKVASTR LLQILAITTG TYADKLSPKV VQSLLDLLCS
QLKNLLSQAG VLLMASFGEG EGEEGEEEEK KVDSSGETEK KDFRAALRKQ HAAELHLGDF
LVFLRRVVSS KAIQSKMASP KWTEVLLNIA SQKCSSGIPL VGNLRTRLLA LHVLEAVLPA
CESGVEDDQM AQVVERLFSL LSDCMWETPI AQAKHAIQIK EKEQEIKSQK QGDLEEEDEN
LPIQEISFDP EKAQCCLVEN GQILTHGSGG KGYGLASTGV TSGCYQWKFY IVKENRGNEG
TCVGVSRWPV HDFNHRTTSD MWLYRAYSGN LYHNGEQTLT LSSFTQGDFI TCVLDMEART
ISFGKNGEEP KLAFEDVDAA ELYPCVMFYS SNPGEKVKIC DMQMRGTPRD LLPGDPICSP
VAAVLAEATI QLIRILHRTD RWTYCINKKM MERLHKIKIC IKESGQKLKK SRSVQSREEN
EMREEKESKE EEKGKHNRHG LADLSEPQLR TLCIEVWPVL AVIGGVDAGL RVGGRCVHKQ
TGRHATLLGV VKEGSTSAKV QWDEAEITIS FPTFWSPSDT PLYNLEPCEP LPFDVARFRG
LTASVLLDLT YLTGIHEDMG KQSTKRHEKK HRHESEEKGD VEQKTESESA VDMRAGLMSD
DVKSQGTTAS KSDSEIASFS LDSALPSVES QHQVAEGKRK NHEHISRNHD IAQSEIRAVQ
LSYLYLGAMK SLSALLGCSK YAELLLIPKV LAENGHNSDC ASSPVVHEDV EMRAALQFLM
RHMVKRAVMR SPIKRALGLA DLERAQAMIY KLVVHGLLED QFGGKIKQEI DQQAEESDQA
QQAQTPVTTS PSASSTTSFM SSSLEDTTTA TTPVTDTETV PASESPGVMP LSLLRQMFSS
YPTTTVLPTR RAQTPPISSL PTSPSDEVGR RQSLTSPDSQ SARPANRTAL SDPSSRLSTS
PPPPAIAVPL LEMGFSLRQI AKAMEATGAR GEADAQNITV LAMWMIEHPG HEDEEEPQSG
STADARPGAA VLGSGGKSND PCYLQSPGDI PSADAAEMEE GFSESPDNLD HTENAASGSG
PPARGRSAVT RRHKFDLAAR TLLARAAGLY RSVQAHRNQS RREGISLQQD PGALYDFNLD
EELEIDLDDE AMEAMFGQDL TSDNDILGMW IPEVLDWPTW HVCESEDREE VVVCELCECS
VVSFNQHMKR NHPGCGRSAN RQGYRSNGSY VDGWFGGECG SGNPYYLLCG SCREKYLALK
TKSKTTSSER YKGQAPDLIG KQDSVYEEDW DMLDVDEDEK LTGEEEFELL AGPLGLNDRR
IVPEPVQFPD SDPLGASVAM VTATNSMEET LMQIGCHGSV EKSSSGRISL GEQAAALANP
HDRVVALRRV TAAAQVLLAR TMVMRALSLL SVSGSSCSLA AGLESLGLTD IRTLVRLMCL
AAAGRAGLST SPSAMASPSE RSRGGHSKAS KPISCLAYLS TAVGCLASNT PSAAKLLVQL
CTQNLISAAT GVNLTTVDDP IQRKFLPSFL RGIAEENKLV TSPNFVVTQA LVALLADKGA
KLRPNYDKSE VEKKGPLELA NALAACCLSS RLSSQHRQWA AQQLVRTLAA HDRDNQTTPQ
TLADMGGDLR KCSFIKLEAH QNRVMTCVWC NKKGLLATSG NDGTIRVWNV TKKQYSLQQT
CVFNRLEGDA EESLGSPSDP SFSPVSWSIS GKYLAGALEK MVNIWQVNGG KGLVDIQPHW
VSALAWPEEG PATAWSGESP ELLLVGRMDG SLGLIEVVDV STMHRRELEH CYRKDVSVTC
IAWFSEDRPF AVGYFDGKLL LGTKEPLEKG GIVLIDAHKD TLVSMKWDPT GHILMTCAKE
ENVKLWGPIS GCWRCLHSLC HPSIVNGIAW CSLPGKGSKL HLLMATGCQS GLVCVWRIPQ
DITQTSVTSS EGWWDQESSC QDGYRKSTGA KCVYQLRGHI TPVRTVAFSS DGLALVSGGL
GGLMNIWSLR DGSVLQTVVI GSGAIQTTVW IPDVGVAACS NRSKDVLVVN CTAEWAAANH
VLATCRTALK QQGVLGLNMA PCMRAFLERL PVMLQEQYAY EKPHVVCGDQ LVHSPYMQCL
ASLAVGLHLD QLLCSPPVPP HHQNCLPDPA SWNPNEWAWL ECFSTTIKAA EALTNGAQFP
ESFTVPDLEP VPEDELTFLM DNSKWINGMD EQIMSWATSR PEDWHLGGKC DVYLWGAGRH
GQLAEAGRNV MVPAAAPSFS QAQQVICGQN CTFVIQANGT VLACGEGSYG RLGQGNSDDL
HVLTVISALQ GFVVTQLVTS CGSDGHSMAL TESGEVFSWG DGDYGKLGHG NSDRQRRPRQ
IEALQGEEVV QMSCGFKHSA VVTSDGKLFT FGNGDYGRLG LGNTSNKKLP ERVTALEGYQ
IGQVACGLNH TLAVSADGSM VWAFGDGDYG KLGLGNSTAK SSPQKVDVLC GIGIKKVACG
TQFSVALTKD GHVYTFGQDR LIGLPEGRAR NHNRPQQIPV LAGVVIEDVA VGAEHTLALA
STGDVYAWGS NSEGQLGLGH TNHVREPTLV TVLQGKNVRQ ISAGRCHSAA WTAPPVPPRA
PGVSVPLQLG LPDAVPPQYG ALREVSIHSA RARLRLLYHF SDLMYSSWRL LNLSPNNQSS
TSHYNAGTWG IVQGQLRPLL APRVYTLPMV RSIGKTMVQG KNYGPQITVK RISTRGRKCK
PIFVQIARQV VKLNASDLRL PSRAWKVKLV GEGADDAGGV FDDTITEMCQ ELETGIVDLL
IPSPNATAEV GYNRDRFLFN PSACLDEHLM QFKFLGILMG VAIRTKKPLD LHLAPLVWKQ
LCCVPLTLED LEEVDLLYVQ TLNSILHIED SGITEESFHE MIPLDSFVGQ SADGKMVPII
PGGNSIPLTF SNRKEYVERA IEYRLHEMDR QVAAVREGMS WIVPVPLLSL LTAKQLEQMV
CGMPEISVEV LKKVVRYREV DEQQQLVQWF WHTLEEFSNE ERVLFMRFVS GRSRLPANTA
DISQRFQIMK VDRPYDSLPT SQTCFFQLRL PPYSSQLVMA ERLRYAINNC RSIDMDNYML
SRNVDNAEGS DTDY
//
