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Database: UniProt
Entry: A0A0Q5VNA8_9ACTN
LinkDB: A0A0Q5VNA8_9ACTN
Original site: A0A0Q5VNA8_9ACTN 
ID   A0A0Q5VNA8_9ACTN        Unreviewed;       561 AA.
AC   A0A0Q5VNA8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=ASG36_05695 {ECO:0000313|EMBL:KQS60421.1};
OS   Geodermatophilus sp. Leaf369.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS60421.1, ECO:0000313|Proteomes:UP000051830};
RN   [1] {ECO:0000313|EMBL:KQS60421.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60421.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS60421.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60421.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006637}.
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:KQS60421.1}.
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DR   EMBL; LMQA01000001; KQS60421.1; -; Genomic_DNA.
DR   RefSeq; WP_055760527.1; NZ_LMQA01000001.1.
DR   AlphaFoldDB; A0A0Q5VNA8; -.
DR   STRING; 1736354.ASG36_05695; -.
DR   OrthoDB; 3713880at2; -.
DR   Proteomes; UP000051830; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd18789; SF2_C_XPB; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032830; XPB/Ssl2_N.
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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:KQS60421.1};
KW   Helicase {ECO:0000313|EMBL:KQS60421.1};
KW   Hydrolase {ECO:0000313|EMBL:KQS60421.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:KQS60421.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051830}.
FT   DOMAIN          190..344
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          399..545
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   561 AA;  62462 MW;  CF92F16529D9FB75 CRC64;
     MTDGPLIVQS DKTLLLEVDH PRSKECRAAI APFAELERSP EHVHTYRVTP LALWNARAAG
     HDAEQVVDAL VRFSRYPVPH ALLVDVADTM DRYGRLTLST NPVHGLVLTT TDRAVLTEVS
     RSKKVAPMLS SRIDEDTFVV NPSERGRLKQ ALLKIGWPAE DLAGYVDGQA HPIELDQADW
     HLRDYQQEAV DGFWAGGSGV VVLPCGAGKT LVGAAAMAEA KATTLILVTN TVAGRQWKRE
     LIARTSLTED EIGEYSGERK EIRPVTIATY QVITTRRKGE YRHLDLFDAQ DWGLIVYDEV
     HLLPAPIFRL TADLQSRRRL GLTATLVRED GREDDVFSLI GPKRYDAPWR DIEAQGYIAP
     AECIEVRVSL DDEERMTYAV AEPEERYKIA ATAQSKMPVI RRILERHPDE QKLVIGAYLE
     QLEELGVALD APVIQGSTTN KERERLFAAF RTGEIKTLVV SKVANFSIDL PEAAVAVQVS
     GTFGSRQEEA QRLGRVLRPK ADGRTAHFYT VVSRDTLDSE YSAHRQRFLA EQGYAYTIVD
     AADLAGRGEV NGPDWVDEST D
//
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