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Database: UniProt
Entry: A0A1S3RK85_SALSA
LinkDB: A0A1S3RK85_SALSA
Original site: A0A1S3RK85_SALSA 
ID   A0A1S3RK85_SALSA        Unreviewed;       974 AA.
AC   A0A1S3RK85;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=E3 ubiquitin-protein ligase TRIM37 isoform X1 {ECO:0000313|RefSeq:XP_014052663.1};
GN   Name=trim37 {ECO:0000313|RefSeq:XP_014052663.1};
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_014052663.1};
RN   [1] {ECO:0000313|RefSeq:XP_014052663.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014052663.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_014052663.1; XM_014197188.1.
DR   AlphaFoldDB; A0A1S3RK85; -.
DR   GeneID; 106603466; -.
DR   KEGG; sasa:106603466; -.
DR   OrthoDB; 5487127at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa04.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd19779; Bbox2_TRIM37_C-VIII; 1.
DR   CDD; cd03773; MATH_TRIM37; 1.
DR   CDD; cd16619; mRING-HC-C4C4_TRIM37_C-VIII; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR037299; TRIM37_MATH.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR36754; E3 UBIQUITIN-PROTEIN LIGASE TRIM37; 1.
DR   PANTHER; PTHR36754:SF2; E3 UBIQUITIN-PROTEIN LIGASE TRIM37; 1.
DR   Pfam; PF00917; MATH; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          15..55
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          90..132
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          276..403
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   REGION          447..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          133..167
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        523..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..658
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        796..832
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  107664 MW;  052E013116D6EBCB CRC64;
     MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ CPHCRAPLQL
     RELVNCRWAE EVTQQLDTLQ LCNLSKHEEN DKDKCENHHE KLSVFCWTCK KCICHQCALW
     GGMHGGHTFK PLAEIYEQHV SKVNEEVAKL RRRLMELISL VQEVERNVEA VRGAKDERVR
     EIRNAVEMMI ARLDNQLKNK LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK
     SPEILLMFQQ VHRKPMQSFV TTPVPPDFTS ELVPAYDSST FVLANFSTLR QRADPVYSPP
     LQISGICWRL KVYPDGNGVV RGNYLSVFLE LSAGLPETSK YEYRVEMVHQ ASSDPTKNII
     REFASDFEVG ECWGYNRFFR LDLLASEGYL NMQTDTLVLR YQVRSPTFFQ KCRDQYWYIS
     QLESAQSSYI QQINNLKERL AIELFRRQKS GSSSPPDRRL GPSTSERDSR SGKGPVAEDG
     CQTTATETKE EEEEEEKTQH DDSNELSDGD LEVDCLTGDE EVNPLDGSST SGSSTATSNT
     EENDIDEETM SGENDVEFSG NLEMEEGELP DDVAGAAGGS NHGARCLRRG GGLSSTGSNN
     SLLEIDPVIL IQLLDLKEHS NVESLWGLQP RPPASLLHSQ VQVQSRKERG ERRPQAVRRG
     APDSGVLIRL KAQMAEVRSK MTDVKFQLEA RGEVRAGPSG GATGEQGPSY HADSDLGPSR
     KSTELDLMGK GPGASRHCRS GSWGAIDCSV RCSSSCDAVV CVAGGKKALS PKQECSGLGL
     RRATDGVEKE SRGQSGEELS TPNGSEGALK PHSMQSSPPS LGSSSSCSDS KPCISKHDQE
     QLYGADLYAL GGLNGISTST IARPRTQPMG SGLLTDSSLD CDLEETAEVR QSLLSLAEGP
     SSHPDESHLV HKQTVVLLPG MSSDSEIDCD TENEDEVVAL EAGDCRYDAQ TLPCAGAQLN
     SDDLCFTTGE NTER
//
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