ID A0A1S3RZW1_SALSA Unreviewed; 2589 AA.
AC A0A1S3RZW1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC106605930 {ECO:0000313|RefSeq:XP_014057419.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014057419.1};
RN [1] {ECO:0000313|RefSeq:XP_014057419.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014057419.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00330}.
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DR RefSeq; XP_014057419.1; XM_014201944.1.
DR OrthoDB; 4161627at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20347; BRcat_RBR_CUL9; 1.
DR CDD; cd20359; Rcat_RBR_CUL9; 1.
DR CDD; cd16624; RING-HC_RBR_CUL9; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR047561; BRcat_RBR_CUL9.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047560; Rcat_RBR_CUL9.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR047562; RING-HC_RBR_CUL9.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22771; CULLIN AND GALACTOSE-BINDING DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22771:SF4; CULLIN-9; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF11515; Cul7; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM01337; APC10; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1188..1367
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT DOMAIN 1609..1861
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT DOMAIN 2127..2345
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2298..2341
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 60..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2499..2589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2417..2447
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 67..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2499..2531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2532..2582
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2589 AA; 289942 MW; 8C6066681D25CF9F CRC64;
MRQSVAIMVG ERRNGNLLVQ LGTKLQAYPE ELIRQRRTHD GQTEYLIRWC LLAIDDGSGS
GGGSNEAGGG GGSSSGVGGS SGSTSGESKT ENILMWMSTE DVYANCPTLL GKRKADTQRP
LQEEERPSGE FPADVTFDEV ELSDMKDDVK NLVTRARKQM AKKSDFAISI THTIHVLSAY
ASIGSLVGVF KETGALDLLM ELLCNKERQT RRSAGKMLRA LASHDAGSRA YVLLSLSQQD
GIEQHMDFDN RYTLLELFAE TTSSEEHGIS FEGIHLPQIP GKLLFSLVKR YLCVTSLMDK
LNTAGVESSS ERQDAAGSSG TGHQLENLRV QREFEFTMAM ANLISELVRV MGWDRNRQPP
QSAGLAQGSA CGEDQEDEPP RRVVRSIFQP RFSASASASP AAAAASNIAA ATPPKKKTGN
GFKTRTDFAS RSAYVEYVQE NLKSGMLVRM LEDYEEVSAG DEGDFRYSND GSPPVQVYWT
SLSRTYWVHW HMVEILGTGT SGQGEKDAQE KASSLTETIK LTTVSQTLFS KPPGGLYSLP
YLAEGLQSDG ATLSRAEWWE VLFFIKKLEP KQQQEINNIL RQSLDEQMSD VDEATLIQLL
VPGEVARKLL HYLKQTLQNS CLWDLLCSHA FSKHYLRRGG GGLEDDELLP DGSLGSSGLG
GGRSNSSSDA TAAASSSSAM GSLSKKPKKE SPTDYCSDTE SELPMEDESN YPEDLKEKMK
VFNNPKVQGK KTALEKLGEV VDIMKKSGSD PVQQLAGIKF IIQVLEDEGP QERSTLRTDA
VQTIRDKVLK FLVEILSGQP KENVVSTLRL TRALMVKYEW RVSFATEGGV KAILSCMQEY
PTVPQVQQVA LATLMVITGA SKHDLGSMSS CYLPLSESGT PMMLGVFASI GSATAEGSKG
LLAAIPAGIE LMLNTPRCML SVRNGLLVII MLISSSKSLA EQLVACDVSA VLKKCLSASR
PVNMLAIIAL NHISMVHKLE KKESKDELDF KDTELKMLVV SLKEMTATKE VILTLEQLLC
DDASQLEEER NQVTRSRETY QDLVRLMDQH RADRAAQLSI LRILNKFLDN YLEDLLPWHE
SIEPCLSSMT AFINDREVVQ LLIRFLYRLA SVNKDYAVVM CRLGTKDALV KALDKHSINL
LLVTELRDLI TDCEKYASLY KKMTTSVLAG CIQMVLGQIE EHRRSHQPIN IPFFDIFLRN
LCQGSSVELK EDKCWEKVEV SSNHHRANKL TDKNPKTYWE SNGCTGSHFI NIYMHKGVVI
RQLAVLVASE DSSYMPARMV VLGGDDPTNI NTELNTVNVP PSANRIVLLE SITRFWSIVQ
IRIKRCQQGG IDTRVHGFEV LGPKPTFWPV FKEQLCCRTY LFYTTKAHTW CQEILEDKAQ
LLQLFNKLNS ALRHEQMFAD RFLPDAEAAE ALGRTCWEAL ITPIVQSITI SETQVLSPLS
WLLSEYLDNA ESARRCKSRA AIFNSRVRRL THLLVHVDTS RVDTEELKPP IKCSINRSKD
LKNGKEGKNK DVAAVSSSSS SNSVKPKMKN TSSIAGIALC WQGVVQRQVK KFLDSTCSLP
DFVERYRNMY LRLKNAMEEL FGQQTAFVLA LRHGFSAALL QLSILTAMHV SERFAQYIDL
MIQESGVDSG NVETLNQLQQ FLEPMLFLSG LELANTFEHF YRYYLGDRLL GQGKVWLESA
VIMQIGTCFP NRFPQQMLKN LSESEELQQE FHLYRLQQLD KTLQDVDEEM MDDQPSEPEE
ESEVKVLILS PRCWAVSSPC YMDNHSRYFP KQLCTYLAEF TDFYSNSQCM YNLTHSKPRR
LQWTWLGHAE LRYGSCTLYV STLQMYILLQ FNHQADVSVE ALQQATGLSP TMLAHALSPL
TAGKGILTQD SPDNDLVKGV LRLNKKALSQ SLENHSYCYL LPKQTYLNVD EDAARSLERK
RNFIYCIIIQ IMKAEKEMHI DNLVFRVLDT CQKREATRSP GSVRFSCSTT DVLSCVMHVI
SKGYIRRNED SPHIVEFLPE DPSTPQKGQA HFSFSKAELK NNPSSSNADI SLEGIIAAPP
SAEDGVLEAV LLSMGRTMNQ EEVRQLMQRT VQQVSGTLSL DLDQAEHLLV HCKWNVDVLI
QRYTDDPDSL VLAAGLKGLN PQPPPSPVAS CPVCLISQSG EAEPAPTLCC MHYCCRSCWQ
EYLTARIEQN LVMNCNCPIT DCRAQPTSQF FFNILTDKDT IAKYENALLR GYVECCSNLT
WCTNPLGCDQ ILCKENIGSM GTCSKCCWSS CFSCNFPEAH YPASCSHMSQ WMDDGGYYEG
MTMEAQSKHL AKLISKRCPS CQAQIEKNEG CLHMTCAKCN HGFCWRCLKP WKPTHKDYYN
CSAMVSKAAR QEKKFQDYNE RCTFHNQAKD FAINLESKVS SINEALQMKS LTFVIDACKV
LAQARKVLAY SCVYSYYNQD TEKMDVMEQQ MEALELHTNA LQILLEETLL QCTDLASCVR
LLKPEHLNTG LELIRRIQER LVAILQHSTQ DFRVGYNSKT GQEQESAQAS NLSKTTDANK
AAGASESGDS DNNNNNEEEG GDEAEEDDEY DDEEVLEWHE DDEDDIDEDD FFSDDDESEN
LERDFSPFD
//
