ID A0A3B4YTB8_SERLL Unreviewed; 843 AA.
AC A0A3B4YTB8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=SH3RF3 {ECO:0000313|Ensembl:ENSSLDP00000031481.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000031481.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000031481.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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DR AlphaFoldDB; A0A3B4YTB8; -.
DR Ensembl; ENSSLDT00000032378.1; ENSSLDP00000031481.1; ENSSLDG00000024178.1.
DR GeneTree; ENSGT00940000160405; -.
DR OrthoDB; 5407056at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261360; Unplaced.
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; cd16750; RING-HC_SH3RF3; 1.
DR CDD; cd11928; SH3_SH3RF3_1; 1.
DR CDD; cd11925; SH3_SH3RF3_3; 1.
DR CDD; cd11785; SH3_SH3RF_C; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 4.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR InterPro; IPR028502; SH3RF3_RING-HC_Zfn.
DR InterPro; IPR035612; SH3RF3_SH3_3.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14167:SF62; E3 UBIQUITIN-PROTEIN LIGASE SH3RF3; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 3.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR00499; P67PHOX.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50044; SH3-domain; 4.
DR PROSITE; PS50002; SH3; 4.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 20..61
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 141..200
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 203..266
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 400..461
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 784..843
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 276..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 88980 MW; 610F43DF65F19FFA CRC64;
MLTLSADMDE SSSLLDLLEC SVCLERLDTT AKVLPCQHTF CRRCLENIVS SRNELRCPEC
RILVDCGVDD LPANILLVRL LDGIKQRPQR GSGGGVGAGG RQSLAGGSLQ GYAAGISASP
PGSAIRELPV ATRSSPVKNI PALPCGKALY SYEGKEPGDL QFSKGDIIIL RRKVDDNWYH
GELNGCHGFL PASYIQLLRP LSQTPPQGKA LYDFEVKDKD QDKDCLAFSK DEVLTVIRRV
DENWAEGMLG DKIGIFPILY VELNETAKQL MEIDKPTQTN VPGPSSEPAP LGPCSPGPSP
SASPSNGNGS GHRRGEGKKN AKKRHSFTAL SVSQRAAQLN NRHSMEISHP VLISSSDPRA
AARIQDASPP GPSPSSAGVL VPPKVASITS ELLAHAKVQL PLNIYLALYA YKPQKADELE
LRKGEMYRVT EKCQDGWFKG TSLRTAASGV FPGNYVTPVS RAPFGVGATR GSCLSSPVGG
SGGGGGGGSG CSQVGSKISD PSSPASPGPS SSRPSTPLVN SANSIHAISP ASSPQTAAAQ
LKNCLRSSQH TVNQARTSMQ LVHSPPAGSP ERPTVAISPL RPQSSSPSRC HGQSGRPLSM
VSPGPSLGPS PLSSPASRPL LPLSSPLSCL TPPNVSAVLL NGEPASPLQP PSPGPSHAPT
QGALAPKPEK KERKAGGLLK LLSGAAAKKK PRSPPSSPPT HNPSLADPTH HSHHHHHHAR
SGSCPMASQG RAGSCPIESE MAGAIGLEPL HRKSGSLDTN FPMSPPATRV GNPLMVLRPE
PKPLSRERYR VVVPYPPQSE AEIELREGDV VFVHKKREDG WYKGTLQRTG QTGLFPSSFV
ESF
//
