ID A0A1X4NBM3_9PROT Unreviewed; 1164 AA.
AC A0A1X4NBM3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN ORFNames=THS27_08880 {ECO:0000313|EMBL:OSQ44004.1};
OS Thalassospira sp. MCCC 1A01428.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1470575 {ECO:0000313|EMBL:OSQ44004.1, ECO:0000313|Proteomes:UP000193740};
RN [1] {ECO:0000313|EMBL:OSQ44004.1, ECO:0000313|Proteomes:UP000193740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01428 {ECO:0000313|EMBL:OSQ44004.1,
RC ECO:0000313|Proteomes:UP000193740};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thalassospira sp. MCCC 1A01428.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OSQ44004.1}.
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DR EMBL; JFJZ01000008; OSQ44004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4NBM3; -.
DR STRING; 1470575.THS27_08880; -.
DR Proteomes; UP000193740; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014151; DNA_helicase_AddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02784; addA_alphas; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 9..498
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 528..807
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 973..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1164 AA; 129951 MW; B10E560A999CD7DE CRC64;
MLTGGDGGGD DPNVLQRMAS DPMASVWVSA SAGAGKTKVL SDRVLRQMLS GTEPHRILCL
TFTKAAAAEM ANRVNERLGR WATMDDADLQ RDLAELAGTA PGADETPRAR RLFASVLDAP
GGMKIQTIHA FCQSLLRRFP LEAGLAPHFE IMDDRTAAET MADTQEEVLA YARSGQDPIL
ADALAVVTGQ VREGAFGDVM RDLARERGRL KRMLDFHHGR DRMCEAVYKS LGVAPGQTAD
MMLRAALADG AFDRDGLMMA LAALEAGTKT DKDRVPALVQ FLEKTDIDAR IAVFSDYRTV
FFTASTGAPR AKLITKKAGE NHPSGADALE QECARLVELE KNRKAAMLAE STTALICMGE
AMLARYARKK ALHAWLDYDD LILNSVRLLE QQAGMAGWVL FKLDEGLEHI LIDEAQDTNP
DQWKVVQILA EEFFNDASQH EDKPRTIFAV GDAKQSIYSF QRADPEKFAD MRRHFARRAA
EIEAEWREVP MNISFRSTDA VLGVVDKVFA GPIARQGVGD EGRDVAHQAF RQGHAGRIEL
WPPVAPLARE EQEPWTPPTK IVRLDDPEIR LARVIAGHIR HAIDSREVLP SRGRAVRAGD
FMILVRRRTA FVDEVVKALK ERNVPVAGVD RMEITEQLAV MDLIAFGRFL LMTDDDLNLA
TLLKSPIIGF SEDQLFHLAH NRRRTLWHAL RERAGDDPMF ARAYGFLARW LGRVDYERPF
ELYGELLGGR GEGARGVRAR LVGRLGIEAN DPIDEFLNLA MNYEAEHAPT LQGFLHWLMA
GDAEIKRDLE QSGRDEVRIM TVHGAKGLQA PIVFLPDTMQ VPTQAPNLFW QDKDQLMFWL
PRVALENDRV KLLRDDIALK RDQEYNRLLY VALTRAEDRL YICGWQGQKT PPEHCWYNLC
EAALSDFASP DAMDFSMLSP SGWQGDGFIW ETKQSAEPKL DKIATGMATA GADTSSDDVG
MRKLIRTVAP EEVFPPRPLA PSRPLEDEPS VQSPLGGDQG QSFKRGILIH KLLELLPDLA
PDRRFDAAER FLGQPVHGLE PDQQFEIANE TLAIFDNPDF APIFGPASRA EVPLVGIVGG
DVVSAQIDRL VITGDEVMIV DYKTNRPPPR DVAQTPMAYR RQMAIYRDAL TQMYPDKIIR
CHILWTNGPW MVELPETLMR MQRA
//
