ID H3B2C9_LATCH Unreviewed; 585 AA.
AC H3B2C9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC102348669 {ECO:0000313|Ensembl:ENSLACP00000016050.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016050.1, 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:ENSLACP00000016050.1}
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};
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DR EMBL; AFYH01118332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01118334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B2C9; -.
DR STRING; 7897.ENSLACP00000016050; -.
DR Ensembl; ENSLACT00000016161.1; ENSLACP00000016050.1; ENSLACG00000014135.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000164246; -.
DR HOGENOM; CLU_008645_4_1_1; -.
DR InParanoid; H3B2C9; -.
DR OMA; GRCDTHA; -.
DR TreeFam; TF331018; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR CDD; cd19796; Bbox2_TRIM71_C-VII; 1.
DR CDD; cd14954; NHL_TRIM71_like; 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; 3.
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; IPR000315; Znf_B-box.
DR PANTHER; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR PANTHER; PTHR24104:SF47; E3 UBIQUITIN-PROTEIN LIGASE TRIM71; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}; Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 1..31
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 205..297
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 310..353
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 357..400
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 404..447
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 451..494
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 498..541
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 545..585
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT COILED 60..138
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 585 AA; 64466 MW; 3166AC11366394FE CRC64;
QVMRLYCDTC AVPICRECTL SRHAGHSFGY LQDAVQDSKT LTLQLLANAH QGRQTIKLSI
EKVLSMAEQV ELKAQVIQNE VKTLMSRHRK ALEERECELL SKVEKIRQAK TKTLHLQVEA
LQESLTKLEN TIDCIQKAIL DGGDVEILLA KKQMFLQMQD LKKLGSLFQP HEDTTITLVP
PDAFLIKAIK SLGVISSGAY GPLSTASGEG LKWALRGKAV AFSVFAKDHA GEMRSSGGDA
VVAIVMGPQG SLFGADVFDH HNGTYTVSYC PQLEGEHIIS VTIHSQPIKG SPFRILVKSE
RRYLNISLPI ASFGCEGDED GQLCRPWGVS VSRDGYIIVA DRSNNRVQVF TPSGAFHSKF
GTLGSRPGQF DRPAGVACDQ TDRIVVADKD NHRIQVFTIH GQFLFKFGER GAKNGQFNYP
WDVAVSSEGK ILVSDTRNHR VQLFSPEGTF LNKYGFEGTL WKHFDSPRGV AFSHEGHLVV
TDFNNHRLLV IHSNFQSVKF LGSEGTSSGQ FLRPQGVAVD QGGRIIVADS RNHRIQVFEP
DGSFLCKFGS YGTGFGQMDR PSGLAVTTDG IIVVVDFGNN RVLLF
//
