ID A0A0M4QUM9_9PSEU Unreviewed; 765 AA.
AC A0A0M4QUM9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Helicase {ECO:0000313|EMBL:ALE83456.1};
GN ORFNames=XF36_10110 {ECO:0000313|EMBL:ALE83456.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE83456.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE83456.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE83456.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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DR EMBL; CP011868; ALE83456.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4QUM9; -.
DR KEGG; pseh:XF36_10110; -.
DR PATRIC; fig|1641402.3.peg.2159; -.
DR Proteomes; UP000062082; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR InterPro; IPR027785; UvrD-like_helicase_C.
DR PANTHER; PTHR11070:SF45; ATP-DEPENDENT DNA HELICASE UVRD2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:ALE83456.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000062082}.
FT DOMAIN 180..602
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 201..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 765 AA; 83848 MW; 3DD70BEE94F74E17 CRC64;
MAHEQSYVAM LYEQLEDRRR DTARRLADTL REETVGTPQA ITQRDAAAEM LTDRLAGLRA
AEHGLAFGRL DADDGEIRYV GRIGLLDEDN EYEPLLMDWR APAARPFYTA TAANPEGMRR
RRHLRTRLRQ VVAIDDEPLN LAEMSEEERA RSGSGLTSEA ALLAAVSQAR TGRMGDIVAT
IQGEQDRIIR SKPSGVLVVQ GGPGTGKTAV ALHRAAYLLY THRDRLARRG VLVVGPNPTF
LRYIGQVLPS LGETSVVLGT VAQLFPGLDA RRTESPATAE LKGRAEMAPV IAAAVRDREQ
LPRSPVELVV EQQRVVFDRD TVAQARTRAR RSRKPHNEAR RIFRKELLRL LAQQVARRVG
GGESGLLDRR DVGDIRDELA ESTEVAAQLE ELWPTLSPEQ LLTDLFADRR RLNSVARRIP
APERALLERP APGADVPPDL RWTPADVALL DEAAELLGDD GAAQAAAEAA ALREEVEYAQ
GVLDVLDLEE DLDPELLRAT DIIDADRLAE RMQVSRYDST AERAAADREW TYGHIIVDEA
QELSAMAWRM VMRCAPARSM TLVGDIAQTG DRGGAGSWDE VLSPFVARRW RLEQLTVNYR
TPSEIADVAD DVLAEIDASL QPPSSVRSTG VPPWAVALPA GADGDRILVE RVRAERDAVG
DGRTAVLTPQ GRLDRVRAVL DAAGLTTPEP AEGESELDAP VVVLPVAASK GLEFDAVVVV
EPQEMLDESP RGLNDLYVAI TRATQRLGVL HSGELPPVLK RIGRP
//