UVRD_MYCPN
ID UVRD_MYCPN Reviewed; 715 AA.
AC P75437;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable DNA helicase II homolog;
DE EC=3.6.4.12;
GN Name=uvrD; OrderedLocusNames=MPN_341; ORFNames=MP495;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: Has both ATPase and helicase activities. Unwinds DNA duplexes
CC with 3' to 5' polarity with respect to the bound strand and initiates
CC unwinding most effectively when a single-stranded region is present.
CC Involved in the post-incision events of nucleotide excision repair and
CC methyl-directed mismatch repair (By 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 -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; U00089; AAB96143.1; -; Genomic_DNA.
DR PIR; S73821; S73821.
DR RefSeq; NP_110029.1; NC_000912.1.
DR RefSeq; WP_010874697.1; NC_000912.1.
DR AlphaFoldDB; P75437; -.
DR SMR; P75437; -.
DR IntAct; P75437; 2.
DR STRING; 272634.MPN_341; -.
DR EnsemblBacteria; AAB96143; AAB96143; MPN_341.
DR GeneID; 66609003; -.
DR KEGG; mpn:MPN_341; -.
DR PATRIC; fig|272634.6.peg.365; -.
DR HOGENOM; CLU_004585_6_1_14; -.
DR OMA; HCANILI; -.
DR BioCyc; MPNE272634:G1GJ3-538-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..715
FT /note="Probable DNA helicase II homolog"
FT /id="PRO_0000102077"
FT DOMAIN 7..295
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 296..554
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 31..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 83497 MW; D68896507E933181 CRC64;
MAFNISTQLN KEQRAAVTCG KGVNIVYSGA GTGKTTIISQ RFAYLFNQKR INPSNILALT
YTRKAASEMK QRILELLPEK YHKDVNIYTF HSFCSRFLRE EGQKNFVIDD DLSNFLKDFL
KESELKSQKV LQIIDGFKNA YFDFDTNSLK DDERLVELCE FHLDPQERNF QLFKETAIAA
FVEYEKGKQQ NNKIDFADLL IKTCTLLSKD HKLLRKWSKK FQYILGDEFQ DTNQIQYELI
KMLASHHQNL FLVGDNNQMI YRWRGAVSDI IDSLKSDFKV RPENEFYITQ NYRCDQNILT
VANSILGTIY AKENQPDSTK GFLFSAIKSN RLPVYFQASS VEGQHSWIIN KIKNLHKNHG
IQYKDMAILF RTNRNMDSMT EALEADGSIP LKQNKGFFKQ LETFKKVLVA LITRSNYDIK
LALKSLRVWP NVLNKSLTVN EQVNLDKILQ NLEQAIFLDE HTRGELTEAA KVFTRLIKFV
EEQQFEALLA FTFEALNTDQ FVCNFIFRTL QKLQTENKNF TITDFINELR FQQDELKQSK
DNVINLITVH SAKGLEFEAV FIYGINQDNF PLKSKNQIID LQRELDELRL FYVALTRAKK
YLFLLSVYQM SGEIIYPSKF IRFINKEDRL EIATINHKVH QDDEFFDSSK TEDYQKKYLT
ENTDFVNGDS VSHRTYGKGV VVEVREDAVC VAFKNSKYGQ RWIVKNHRDL VKAVY