ID H3A418_LATCH Unreviewed; 773 AA.
AC H3A418;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ENSLACP00000004389.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004389.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000004389.1}
RP IDENTIFICATION.
RG Ensembl;
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFYH01197680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01197689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A418; -.
DR STRING; 7897.ENSLACP00000004389; -.
DR Ensembl; ENSLACT00000004427.1; ENSLACP00000004389.1; ENSLACG00000003902.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160405; -.
DR HOGENOM; CLU_015769_1_0_1; -.
DR InParanoid; H3A418; -.
DR OMA; SEMRGAM; -.
DR TreeFam; TF105571; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000003902; Expressed in pectoral fin and 1 other cell type or tissue.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd11928; SH3_SH3RF3_1; 1.
DR CDD; cd11931; SH3_SH3RF3_2; 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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035816; SH3RF1/SH3RF3_SH3_4.
DR InterPro; IPR035612; SH3RF3_SH3_3.
DR PANTHER; PTHR14167:SF62; E3 UBIQUITIN-PROTEIN LIGASE SH3RF3; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 4.
DR SUPFAM; SSF50044; SH3-domain; 4.
DR PROSITE; PS50002; SH3; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..61
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 64..127
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 326..387
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 714..773
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 485..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 82722 MW; E651789DE228B7B4 CRC64;
IPQLPCGKAL YNYEGKEPGD LKFNKGDIII LRRKVDENWY HGELKGNHGF FPASYIQCIK
PLPQPPPQGK ALYDFEVKDK DQDKDCLTFS KDEVLTVIRR VDDNWAEGML GDKIGIFPIL
YVELNETAKQ LIEMDKTSTP ASSGSDTTNP VAMSTGATAT LNSTGAISAI HRRIDGKKNA
KKRHSFTALS MTHKASQALN NRHSMEISAP VLISSSDPRA ATRIGELPHL SSSAPAQPHL
STYILLVTTP AASKLENNES LVLCTEDPIL CSWGEPNGPF SPSSLILFFF FLSSESSSFA
SAAVVGAIGP RIGATGDQGT SPKVQLPLNI YLAMYAYKPQ KNDELELRKG EMYRVIEKCQ
DGWFKGTSLR TGMSGVFPGN YVTPVSRDLL VCSCCRAPFG IGQLRNSLPG TAPPVKGNPA
AAQPGGAGLT NAIAVRPIAP VALTPAQPQL QSCTSPINSC LRLAGQQTVN QARSAMQMVH
PTVPAQDRPT ATVSPLRTQS PPSRVSATVR PHSMVSPQHV HQTAIAGGPG APCARTIIPL
TSAAAAITPP NVSAANLNGE PTWKLLNYIV PASPPGQPGS PSSGGKFCNK EKAIKPKKNQ
KEKKSGLLKL LSGASAKKKS RSPPSVSPTH EPQQQAAAAA EGPVHGAVGP EVLSVSSHGR
AGSCPIESEM QGAMGMEPLH RKTGSLDLNF SISPPARQPC SSMAAVRPEP KLLPHERRYR
VVVPYPPQSE AEIELKEGDI VFVHKKREDG WFKGTLQRNG RTGLFPGSFV ESF
//
