DCR1A_CHICK
ID DCR1A_CHICK Reviewed; 972 AA.
AC Q5QJC4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA cross-link repair 1A protein;
DE AltName: Full=Beta-lactamase MBLAC2;
DE EC=3.5.2.6 {ECO:0000250|UniProtKB:Q6PJP8};
DE AltName: Full=SNM1 homolog A;
DE Short=chSNM1A;
GN Name=DCLRE1A; Synonyms=SNM1A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH PIAS1.
RX PubMed=15572677; DOI=10.1128/mcb.24.24.10733-10741.2004;
RA Ishiai M., Kimura M., Namikoshi K., Yamazoe M., Yamamoto K., Arakawa H.,
RA Agematsu K., Matsushita N., Takeda S., Buerstedde J.-M., Takata M.;
RT "DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus
RT formation.";
RL Mol. Cell. Biol. 24:10733-10741(2004).
CC -!- FUNCTION: May be required for DNA interstrand cross-link repair.
CC {ECO:0000269|PubMed:15572677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000250|UniProtKB:Q6PJP8};
CC -!- SUBUNIT: Binds PIAS1.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; AY376896; AAR27404.1; -; mRNA.
DR RefSeq; NP_001008683.1; NM_001008683.1.
DR AlphaFoldDB; Q5QJC4; -.
DR SMR; Q5QJC4; -.
DR STRING; 9031.ENSGALP00000032457; -.
DR PaxDb; Q5QJC4; -.
DR GeneID; 423902; -.
DR KEGG; gga:423902; -.
DR CTD; 9937; -.
DR VEuPathDB; HostDB:geneid_423902; -.
DR eggNOG; KOG1361; Eukaryota.
DR InParanoid; Q5QJC4; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q5QJC4; -.
DR Reactome; R-GGA-353248; DNA damage recognition in global genomic repair.
DR Reactome; R-GGA-353303; Nucleotide Excision Repair.
DR PRO; PR:Q5QJC4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008800; F:beta-lactamase activity; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..972
FT /note="DNA cross-link repair 1A protein"
FT /id="PRO_0000209118"
FT ZN_FING 105..135
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 14..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 972 AA; 108328 MW; A87696D13B635514 CRC64;
MSEDVLLEED IWEYKSIRKR KPQSNPDSTS VSMQTVTKGK CRPKRKGSGN RKKSVEKNST
PQKSEQRLRP SEDLDPCKDD SSVYAQESVS SLTEQGSPST RPVCDGYCPS CQMPFSLLVV
QTPRWHVAEC LDTPGSVEKE CPDGLLCTST IPSHYKRYSH FLLAASRAGE YLVNSTANTV
ERKMTCSTAA KSSCFPSPVE DSQAEKPSKN LKNVPNNECT SKIKDSEQRK SLNITSESTS
SFADVQKPQQ VFQLTQTTDN SCKFEFYDFT SSQESVSEDL CSQKDTSQPS LLQSKADFSD
WEISYSPLST CEESEGEAEE EKEVKTSQNK LLKVQNFEGP ESNTEVFKFK KQHCEEINTS
SCLYHSEKSA SQSHVDSKCS NSPCVDNQQE MLSAESSFPL NCNQEFQQPG LLSPAINTGN
KESQDKGACV LDSVYSCLTR TQSLLLTEGG RSPLSQKNKV LRAPSVVLTN TDKMTADATE
KGTCQESLQP AVKKEENLDS TGVCFPSPIS KTVSSHSLAS MNAKSSPAKE LKQMDIGVFF
GLKPKVKEES KGEACLSEGK QIPSSVAPSG KRPRQQKRKA EGSVEDLEAV EESSNKDGGD
ANVTSGGQRK WRKRFRESST TDEGARKKQC PFYKKIPGTG FTVDAFQYGE IEGCTAYFLT
HFHSDHYCGL TKNFVFPLYC NKITGNLVKS KLRVKEQYIN VLPMDTECIV NGIKVLLLDA
NHCPGATMIL FYLPSGTAIL HTGDFRADPS MERYPALIGQ KIHTLYLDTT YCSPEYTFPS
QQEVIQFAVN TAFEMVTLNP RTLVVCGTYS IGKEKVFLAI AEVLGSKASM SRDKYKTLQC
LESAAVNSLI TMNWDGTLLH ILPMMQINFK GLQDHLNKFS ENFDQVLAFK PTGWTYSDSC
LSVMDIKPQT RGNITIYGIP YSEHSSYLEM KRFVQWLKPQ KIIPTVNVGD WRARSLMEKH
FRDWMIEGSG HK
