GenomeNet

Database: UniProt
Entry: Q5RF63
LinkDB: Q5RF63
Original site: Q5RF63 
ID   RECQ1_PONAB             Reviewed;         649 AA.
AC   Q5RF63;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   31-JUL-2019, entry version 80.
DE   RecName: Full=ATP-dependent DNA helicase Q1;
DE            EC=3.6.4.12;
DE   AltName: Full=DNA-dependent ATPase Q1;
DE   AltName: Full=RecQ protein-like 1;
GN   Name=RECQL; Synonyms=RECQL1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA helicase that may play a role in the repair of DNA
CC       that is damaged by ultraviolet light or other mutagens. Exhibits a
CC       magnesium-dependent ATP-dependent DNA-helicase activity that
CC       unwinds single- and double-stranded DNA in a 3'-5' direction (By
CC       similarity). {ECO:0000250}.
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   -!- SUBUNIT: Interacts with EXO1 and MLH1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000305}.
DR   EMBL; CR857298; CAH89594.1; -; mRNA.
DR   RefSeq; NP_001124706.1; NM_001131234.1.
DR   SMR; Q5RF63; -.
DR   STRING; 9601.ENSPPYP00000004971; -.
DR   PRIDE; Q5RF63; -.
DR   GeneID; 100171554; -.
DR   KEGG; pon:100171554; -.
DR   CTD; 5965; -.
DR   eggNOG; KOG0351; Eukaryota.
DR   eggNOG; COG0514; LUCA.
DR   InParanoid; Q5RF63; -.
DR   KO; K10899; -.
DR   OrthoDB; 445763at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00614; recQ_fam; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; DNA-binding; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    649       ATP-dependent DNA helicase Q1.
FT                                /FTId=PRO_0000205051.
FT   DOMAIN      100    275       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      300    451       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     113    120       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       219    222       DEVH box.
FT   MOD_RES     514    514       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P46063}.
FT   MOD_RES     522    522       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P46063}.
FT   MOD_RES     597    597       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P46063}.
FT   MOD_RES     602    602       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6AYJ1}.
FT   MOD_RES     634    634       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P46063}.
SQ   SEQUENCE   649 AA;  73483 MW;  B270A29E121ABA58 CRC64;
     MASVSALTEE LDSITSELHA VEIQIQELTE RQEELIQKKK VLTKKIKQCL EDSDAGASNE
     YDSSPAAWNK EDFPWSGKVK DVLQNVFKLQ KFRPLQLETI NVTMAGKEVF LVMPTGGGKG
     LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK
     NSELKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI
     LKRQFPNASL IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF
     IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLRNLGIH AGAYHANLEP EDKTTVHRKW
     SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDM KADCILYYGF
     GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRLLMAQ HFDEVWNSEA CNKMCDNCCK
     DSAFERKNIT EYCRDLIKIL KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE
     DLEKIIAHFL IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRV
     ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA
//
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