ID   G3TQP1_LOXAF            Unreviewed;       615 AA.
AC   G3TQP1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
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:ENSLAFP00000017886.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017886.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000017886.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017886.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000017886.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017886.2};
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}.
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DR   AlphaFoldDB; G3TQP1; -.
DR   Ensembl; ENSLAFT00000022115.2; ENSLAFP00000017886.2; ENSLAFG00000023013.2.
DR   GeneTree; ENSGT00940000160405; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd11925; SH3_SH3RF3_3; 1.
DR   CDD; cd11785; SH3_SH3RF_C; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 3.
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; 1.
DR   Pfam; PF14604; SH3_9; 2.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SH3-domain; 3.
DR   PROSITE; PS50002; SH3; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..51
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          196..257
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          556..615
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          156..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  64620 MW;  374DFC0957D52C06 CRC64;
     IKDKDQDKDC LTFTKDEILT VIRRVDDNWA EGMLGDKIGI FPLLYVELND SAKQLIEMDK
     TCLAAASGCD ASLPSDPSAA ATLAPSSTLS STGAVSAFQR RIDGKKNAKK RHSFTALSVT
     HKSSQAVSNR HSMEISAPVL ISSSDPRAAA RIGELAQLSS SAPTQDSSSS AGSATMAVPR
     AGAAAGEQGT SPKVQLPLNV YLALYAYKPQ KNDELELRKG EMYRVTEKCQ DGWFKGTSLR
     TGVSGVFPGN YVTPVSRVPV GGAGPPRNNV VGGSPLAKGM TTTIHPGGGS LSSPATATRP
     ALPLTTPQAH AQHQAGSPPV GSCLRHSAQP AASQARSTIP TAAHSSAQAQ DRPTATVSPL
     RTQNSPSRLP AAGLRPHSVV SPQHVHQPPI QMCPRPVIPL TSAASAITPP NVSAANLNGE
     VGGGPIGGLL TSSPTNTGCK PDEKKNEKKE KKSGLLKLLA GASTKKKSRS PPSISPTHDP
     QVAVDTSLQG AMGPEVSSLS SHGRAGSCPI ESEMQGAMGM EPLHRKTGSL DLNFSLSPSR
     QVPLSMAAIR PEPKPLPRER YRVVVSYPPQ SEAEIELKEG DIVFVHKKRE DGWYKGTLQR
     NGRTGLFPGS FVESF
//