ID H3B4J9_LATCH Unreviewed; 795 AA.
AC H3B4J9;
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=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=ERCC3 {ECO:0000313|Ensembl:ENSLACP00000016820.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016820.1, 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:ENSLACP00000016820.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
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DR EMBL; AFYH01110417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01110418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01110419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01110420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01110421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01110422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01110423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01110424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B4J9; -.
DR STRING; 7897.ENSLACP00000016820; -.
DR Ensembl; ENSLACT00000016938.1; ENSLACP00000016820.1; ENSLACG00000014815.1.
DR eggNOG; KOG1123; Eukaryota.
DR GeneTree; ENSGT00390000002204; -.
DR HOGENOM; CLU_008213_0_0_1; -.
DR InParanoid; H3B4J9; -.
DR OMA; RCQEIDY; -.
DR TreeFam; TF101233; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000014815; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd18029; DEXHc_XPB; 1.
DR CDD; cd18789; SF2_C_XPB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001161; XPB/Ssl2.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR NCBIfam; TIGR00603; rad25; 1.
DR PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR PRINTS; PR00851; XRODRMPGMNTB.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 328..489
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 90797 MW; 78CCA97F2A809A38 CRC64;
MGKKDKFDKD KKKFKKRHHD EEGEDEDDTP GNESQEAVPS AAGKQVEESG TKQDEYGAKD
YRLQMLLKGD HSSRPLWVAP DGHVFLEAYS PVYKYAQDFL IAIAEPVCRP SHVHEYKLTA
YSLYAAVSVG LQTSDIVEYL QKLSKTSVPD GIIQFIRLCT VSYGKVKLVL KHNRYFVESA
HPDVIQQLLQ DPVVKECRLR TAEGEEMELI TETFSSKSAI SKSSQGNDGP STSQGTDSSQ
TKPDVPADIF DFYEQMDKDE EEEEETQTVS FEVKQEMIEE LQKRCIQLDY PLLAEYDFRN
DTVNPDINID LKPTAVLRPY QEKSLRKMFG NGRARSGVIV LPCGAGKSLV GVTAACTVRK
RCLVLGNSAV SVEQWKAQFK MWSTIDDSQI CRFTSDAKDK PIGCSIAIST YSMLGHTTKR
SWEAERVMEW MKSQEWGLMI LDEVHTIPAK MFRRVLTIVQ AHCKLGLTAT LVREDDKIVD
LNFLIGPKLY EANWMELQNN GYIAKVQCAE VWCPMTPEFY REYVAIKTKK RILMYTMNPN
KFRACQFLIK FHERRNDKII VFADNVFALK EYAIKLNKPY IYGPTSQGER MQILQNFKHN
PKINTIFISK VNVLISQAPL ARQLIGYIKH GVNQLQKAAW NNHVPFFRLG RFSNALHLVG
MVAEEYNAYF YSLVSQDTQE MAYSTKRQRF LVDQGYSFKV ITKLAGMEDE DLAFCTKDEQ
QQLLQKVLAA SDLDAEEEMV PGEFGSKSST QLTRRFGTMS SMSGADDTAY MEYQMPRSKA
ASNKHVHPLF KRFRK
//
