ID A0A3P9BVH9_9CICH Unreviewed; 838 AA.
AC A0A3P9BVH9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSMZEP00005013958.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005013958.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005013958.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005013958.1}
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 RefSeq; XP_004555600.1; XM_004555543.1.
DR AlphaFoldDB; A0A3P9BVH9; -.
DR STRING; 106582.ENSMZEP00005013958; -.
DR Ensembl; ENSMZET00005014429.1; ENSMZEP00005013958.1; ENSMZEG00005010524.1.
DR GeneID; 101484065; -.
DR KEGG; mze:101484065; -.
DR CTD; 344558; -.
DR GeneTree; ENSGT00940000160405; -.
DR OrthoDB; 5407056at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265160; LG16.
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 Reference proteome {ECO:0000313|Proteomes:UP000265160};
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 143..202
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 205..268
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 402..463
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 779..838
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 277..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 88332 MW; 8EAD326CBDEEE1F2 CRC64;
MLTLSADMDE SSSLLDLLEC SVCLERLDTT AKVLPCQHTF CRRCLENIVS SRNELRCPEC
RILVDCGVDD LPANILLVRL LDGIKQRPQR GSGGGGGVGA GGRQSLAGGS LQGYAAGISA
SPPGTAIREL PVATRSSPVK NIPALPCGKA LYSYEGKEPG DLQFSKGDII ILRRKVDDNW
YHGELNGCHG FLPASYIQLL RPLSQTPPQG KALYDFEVKD KDQDKDCLAF SKDEVLTVIR
RVDENWAEGM LGDKIGIFPI LYVELNETAK QLMEIDKPIP ANAPGPSSEP APLGPCSSGP
SPSASPSNGN GFGHRRGEGK KNAKKRHSFT ALSVSQRAAQ LNNRHSMEIS HPVLISSSDP
RAAARIQDAS PPGPSPSSAG VLVPPKVASI TSELLAHAKV QLPLNIYLAL YAYKPQKADE
LELRKGEMYR VTEKCQDGWF KGTSLRTAAS GVFPGNYVTP VSRAPFGVGA TRSSCLSSPG
GGSGCSQVAS KILDPSSPGS PGPSSSRPGT PLVNSANAVN SISPASSPQT AAAQLKNCLR
SSQHTNQART SMQLVHSPSA ASPERPTVAI SPLRSQSSSP SRCPGQSGRP LSMVSPGPSL
GPSPLSSPAS RPILPLSSPL SCLTPPNVSA VLLNGESASP LQPPSPGPSH TTAQGVLAPK
AEKKERKAGG LLKLLSGAAA KKKPRSPPSS PPTHDPTGQG AVATDPVHHH HHHARSGSCP
MASQGRAGSC PIESDMAGAI GLEPLHRKSG SLDTNFPMSP PATRAGNALM VLRPEPKPLS
RERYRVVVPY PPQSEAEIEL REGDVVFVHK KRDDGWYKGT LQRTGQTGLF PGSFVESF
//
