ID A0A1S3NNM5_SALSA Unreviewed; 663 AA.
AC A0A1S3NNM5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=E3 ubiquitin-protein ligase CHFR {ECO:0000256|ARBA:ARBA00017908};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=Checkpoint with forkhead and RING finger domains protein {ECO:0000256|ARBA:ARBA00031332};
DE AltName: Full=RING-type E3 ubiquitin transferase CHFR {ECO:0000256|ARBA:ARBA00029800};
GN Name=LOC106580459 {ECO:0000313|RefSeq:XP_014017031.1,
GN ECO:0000313|RefSeq:XP_014017032.1};
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_014017032.1};
RN [1] {ECO:0000313|RefSeq:XP_014017031.1, ECO:0000313|RefSeq:XP_014017032.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017031.1,
RC ECO:0000313|RefSeq:XP_014017032.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body
CC {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the CHFR family.
CC {ECO:0000256|ARBA:ARBA00005797}.
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DR RefSeq; XP_014017031.1; XM_014161556.1.
DR RefSeq; XP_014017032.1; XM_014161557.1.
DR STRING; 8030.ENSSSAP00000072812; -.
DR PaxDb; 8030-ENSSSAP00000072812; -.
DR Ensembl; ENSSSAT00000169751; ENSSSAP00000178144; ENSSSAG00000109055.
DR GeneID; 106580459; -.
DR KEGG; sasa:106580459; -.
DR OMA; ACHIRDS; -.
DR OrthoDB; 450556at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa20.
DR Bgee; ENSSSAG00000063965; Expressed in semen and 14 other cell types or tissues.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd22672; FHA_CHFR; 1.
DR CDD; cd16503; RING-HC_CHFR; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.40.140; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR040909; CHFR_Znf-CRD.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR Pfam; PF10283; zf-CCHH; 1.
DR Pfam; PF17979; zf-CRD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 30..81
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 281..320
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 162..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 73992 MW; 71DE7BAF1A2B8AEC CRC64;
MEKKHGRSQP WGKLVKVDTR SEVLLVNREC TVGRRKGCDL SFPANKLVSG DHCKIVQDKS
SGLVWLEDTS TNGTVINMSK LVKKQIHMLQ HGDVIYFVYR KNEPEQNIAY MYQSIKPERT
FSQDTIGGAT RCSVMQQKAQ TCPVTAAVCV SVEPFLVGPP REQQALDEPQ PSTSSHHLHT
ACSSAASLLH SSALDTRQTE AQNRVTMLYK EEEEKDMEPE RKRRKTDSAD KDYDFGLPHT
SSIAVFGPSP AKVSLIRDLL GKAAVTVEEG KTDKMEESLT CIICQDLLHD CVSLQPCMHT
FCAACYSGWM ERSSLCPTCR CPVERIRKNH ILNNLVEAYL IQHPEKCRSE EDLKSMDSRN
KITRDMLQPK IERSFSDEEG SSDYLFELSD NDSDTSDIGQ PVVICRQCPG YRKEVSQVLW
ATGPAPTALL GPVLPAPLGP APPTPEDRPG KPPGAGESTL STCSDVPTTA PQDYTCPPLG
SHVICTCCLQ PMPDRRAELI GQQLSTQQCV ACLRPFCHMY WGCQRIGCQG CLARFSELNL
TDKCLDGVLN SNNYESEILQ SYLSARGMSW RDMLQEGLQG LQQGTFYLSD YRINSNAILC
FCCGLRAFGE LAYKYRQNIP ASALPAVVTS RPDCYWGRNC RTQVKAHHAT KFNHICEQTR
FKS
//
