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Database: UniProt
Entry: K7GAL8_PELSI
LinkDB: K7GAL8_PELSI
Original site: K7GAL8_PELSI 
ID   K7GAL8_PELSI            Unreviewed;       577 AA.
AC   K7GAL8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=TRIM45 {ECO:0000313|Ensembl:ENSPSIP00000017329.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000017329.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000017329.1}
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC       {ECO:0000256|ARBA:ARBA00008518}.
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DR   EMBL; AGCU01152279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006132975.1; XM_006132913.2.
DR   AlphaFoldDB; K7GAL8; -.
DR   STRING; 13735.ENSPSIP00000017329; -.
DR   Ensembl; ENSPSIT00000017407.1; ENSPSIP00000017329.1; ENSPSIG00000015385.1.
DR   GeneID; 102445603; -.
DR   KEGG; pss:102445603; -.
DR   CTD; 80263; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000154334; -.
DR   HOGENOM; CLU_013137_14_8_1; -.
DR   OMA; TRCPLCM; -.
DR   OrthoDB; 2916643at2759; -.
DR   TreeFam; TF324196; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR   CDD; cd19809; Bbox1_TRIM45_C-X; 1.
DR   CDD; cd19785; Bbox2_TRIM45_C-X; 1.
DR   Gene3D; 4.10.830.40; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR001298; Filamin/ABP280_rpt.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR047153; TRIM45/56/19.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR   PANTHER; PTHR25462:SF291; TRIPARTITE MOTIF-CONTAINING PROTEIN 45; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00557; IG_FLMN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007267};
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:PRU00024}.
FT   DOMAIN          29..94
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          182..218
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          390..493
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   COILED          281..308
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   577 AA;  63241 MW;  9563C8EA551742AC CRC64;
     MSDLQEQQQQ LGIMAKIPCE VRGLARTRCP LCTKLFSSPK ILPCLHTFCM ACLEQLEPFS
     VLSVQGEDSD STSEGSWLQD HRQPPLSILC PICDTEVGLP PGGTHDLTTD HLAMNEMLQE
     TLQAPGPGIL CDLCVDGEAV KHCPICKANL CHFCCQAHRR QKKTASHAVV GLEDPKGYSQ
     TGKPILCPSH PSEELTLFCE QCDQPVCRDC VVGQHRQHPY DFAANVIHKH GDSMRELLKS
     TQLHVGTLEG ALRHIEGVSS AICSRVEAVA GEIRTFADGY IRAIEEHRNR LLKQLEDLKV
     QKETLLHLQK VQLEQLLMDM QTGVEFTERL LTCGSDLEIL LIKGVVANRL RKLNKVDYNI
     HPGVEDGIQF SPREKAGQCC GYAVFGTLLN RTVDPAKCVL QGEGLHSARQ NQQASFTLLC
     KDTSGEQMGR GGEPVRVTIT HKDKKDCTIK PSVCDKRDGT YHFSYTPEEL GAYTICICVK
     GQHVQGSPFT LTVKNKFRKH QGVFHCCSFC SSGGQKAARC ACGGTMPGGY QGCGHGHKGH
     PGCPHWSCCG RAAENSECPA VPPGENSQRG LLKTVAL
//
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