ID H3A378_LATCH Unreviewed; 762 AA.
AC H3A378;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=TRIM3 {ECO:0000313|Ensembl:ENSLACP00000004099.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004099.1, 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:ENSLACP00000004099.1}
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 -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; AFYH01155133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01155134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01155135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01155136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01155137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01155138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01155139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3A378; -.
DR STRING; 7897.ENSLACP00000004099; -.
DR Ensembl; ENSLACT00000004135.1; ENSLACP00000004099.1; ENSLACG00000003642.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158173; -.
DR HOGENOM; CLU_008645_5_0_1; -.
DR InParanoid; H3A378; -.
DR OMA; LHQRKNT; -.
DR TreeFam; TF331018; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000003642; Expressed in pelvic fin.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19825; Bbox2_TRIM3_C-VII; 1.
DR CDD; cd14960; NHL_TRIM2_like; 1.
DR CDD; cd16768; RING-HC_TRIM3; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR001258; NHL_repeat.
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; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR PANTHER; PTHR24104:SF21; TRIPARTITE MOTIF-CONTAINING PROTEIN 3; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 5.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
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; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 5.
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 22..63
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 111..152
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 318..419
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 471..514
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 518..561
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 562..603
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 641..669
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 718..761
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 420..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..180
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 762 AA; 84560 MW; A2105AD10ED1ECCC CRC64;
MAKRESSTSP VVRQIDKQFL VCSICLDRYH NPKVLPCLHT FCEKCLQNYI PPQSLTLSCP
VCRQTSILPE KGVAALQNNF FITNLMEVLQ RNPESVREET SMMESVSAVS GKPLSCPNHE
GKGMEFYCES CETAMCRECT EGEHREHVTV PLKDVVEQHK ASLKNQLDAI KNRLPQLAAA
IELVNEISKQ LTERKNDAVS EISSTFEELE RALHQRKNTL INDLEAIASA KQKVLQSQLD
SLRQGQENIK SSCSFTEQAL NHGSETEVLL VKKQMSERLS ELASRRFPER PHENEHLDYI
VETDGLRKSI QNLGVLITTS AIAHETVATG EGLRHAVVGQ QTSVTITTKD KEGELVKSGN
AILNAEIMAP DGSFVEGEVV DNKNGTYELL YTLKCEGEYS LSILLYDQLI KGSPFRVKAV
KPSDVPQSPE DVKRRVKSPS SGHIRQKAVR RPSSMYSTGK KKENPIEDEL IFRVGTRGRE
KGEFTNLQGI SASTSGRIVV ADSNNQCIQV FSNDGQFKLR FGIRGRSPGQ LQRPTGVTVD
MNGDVIVADY DNRWVSIFSS DGKFKNKIGA GRLMGPKGVA VDRNGHIIVV DNKACCVFIF
QSNGKLVTRF GSRGAADRQF AESSDSRLSL MNPTMKMNPF SPHFVAVNNK NEIVVTDFHN
HSVKVRLAEG LFLDYLGAHR NSRTAFDDET EISPERSGTC ECQSWNGSNF NTVFDSAGSF
LSYINTTADP LYGPQGLALT TDGNVIVADS GNHCFKVYRY LQ
//
