ID A0A1S3LA95_SALSA Unreviewed; 516 AA.
AC A0A1S3LA95;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=ub7i3 {ECO:0000313|RefSeq:XP_013987750.1};
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_013987750.1};
RN [1] {ECO:0000313|RefSeq:XP_013987750.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013987750.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR RefSeq; XP_013987750.1; XM_014132275.1.
DR AlphaFoldDB; A0A1S3LA95; -.
DR STRING; 8030.ENSSSAP00000040385; -.
DR PaxDb; 8030-ENSSSAP00000040385; -.
DR Ensembl; ENSSSAT00000066587; ENSSSAP00000040361; ENSSSAG00000044474.
DR GeneID; 100194956; -.
DR CTD; 10616; -.
DR OrthoDB; 2903477at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa12.
DR Bgee; ENSSSAG00000044474; Expressed in head kidney and 16 other cell types or tissues.
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; cd20345; BRcat_RBR_HOIL1; 1.
DR CDD; cd16633; mRING-HC-C3HC3D_RBR_HOIL1; 1.
DR CDD; cd20358; Rcat_RBR_HOIL1; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR047558; BRcat_RBR_HOIL1.
DR InterPro; IPR047559; HOIL1_RBR_mRING-HC-C3HC3D.
DR InterPro; IPR047557; Rcat_RBR_HOIL1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22770:SF35; RANBP-TYPE AND C3HC4-TYPE ZINC FINGER-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR22770; UBIQUITIN CONJUGATING ENZYME 7 INTERACTING PROTEIN-RELATED; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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:PRU00322}.
FT DOMAIN 198..228
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 284..505
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 288..330
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 174..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 516 AA; 57962 MW; ABBF0464D0CE2653 CRC64;
MGLTMTSPEV FTSNLIEAEE LAQLLSEAIS CGDKEEAKRC SEQLAELCLP VSVMISRKAY
SQDSIRLKVG VGDAQSENYI PVTLLVTLDM TISDLKEKIN SDYGFHPSLQ SWVIGKRLAL
DSTTLYSHGV RKNGDQAYLY IKSAQAANLS RELVNQEEEH RRLDSIIESL SPLLARGATG
PTPPPKTKHP APPPLQPKPQ VGWSCSVCTY ANKPTRPGCE MCGSERPEDY QVPEVYQPDE
QEVQRLQLEE MANLQYQQAL EEERERNFLS LVETDAHSLV PNTEELDCPI CLCSIPPGEG
ATLRECLHVF CRECLKGTIV NSMDPEVTCP YGDEDYSCDR KLQDREIQSL LSQEEHQKLL
ELRLSIAETR SENSYHCKTP DCAGWCIFED EVNEFICELC KETNCLLCKA IHKDMNCKEY
QDDLRIRAEN DVAAKQTTQM LESLLQNGEA MHCPKCKVIV QKKDGCDWIC CLMCKTEICW
VTKQARWGPN GSGDNSGGCG CRFNVARCHP NCQNCH
//
