ID Q821K9_CHLCV Unreviewed; 1205 AA.
AC Q821K9;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Helicase, Snf2/Rad54 family {ECO:0000313|EMBL:AAP05670.1};
GN OrderedLocusNames=CCA_00931 {ECO:0000313|EMBL:AAP05670.1};
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941 {ECO:0000313|EMBL:AAP05670.1, ECO:0000313|Proteomes:UP000002193};
RN [1] {ECO:0000313|EMBL:AAP05670.1, ECO:0000313|Proteomes:UP000002193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / GPIC
RC {ECO:0000313|Proteomes:UP000002193};
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
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DR EMBL; AE015925; AAP05670.1; -; Genomic_DNA.
DR RefSeq; WP_011006883.1; NC_003361.3.
DR AlphaFoldDB; Q821K9; -.
DR STRING; 227941.CCA_00931; -.
DR KEGG; cca:CCA_00931; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_271671_0_0_0; -.
DR OrthoDB; 18878at2; -.
DR Proteomes; UP000002193; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF04434; SWIM; 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.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:AAP05670.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 49..83
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 728..887
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1020..1169
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1205 AA; 137371 MW; ED099AB8AA3331BE CRC64;
MVLNALAGFR QTAIDYLATN RQDIALDFSG DCYNIRIPDE DSPDGNWLST LRFSDIDNLT
FASCSCPDGD CCVHLMTAFF SAYDAHGWLP LHHKFDISFW HALFLKLFLE EAQLHADGDR
QYSITSPHIT LEISALSSEA FTEWLPIIHQ TPEPKTYTKK TFPQSVLYRV AKQFFFFSEA
GARLDLIENS QGFPTQFAMQ WEGISLKGEI LDFSTLENLF PKINFSQTSL PGNYSDFSIT
KVRVAPEESK IYFTVEPIAH DHANQPITEI GSIGYIAGSQ QVILPSKETF VSIYLISLLP
ETLKKQILAL LHYDSEERPI RYSIHFLRDS SISFSAYLDT PGDLENGKLI YPDFCYVPEK
GLFTVVGLLS PQISFVIKAD QVEEFLNNEG MLIREPGFEV FTDRIPEGQL TYNITQQGVL
LFHYNTGNPA AIDIHYGPWT YYSGQGFFLQ RKADLEIQDG LIVEADHIPN FIMKHEVVLR
TIPNFFAPTP PLKNLFFEVH KETKGSGLYL KPVFQGLEEE NCRLFGVFLY RENLGFNLLP
TPLQPLCSLP RKIPAEQVPD FINQNSQNDK LVFTDPQLCP PVTFELVILS ITRPHPSSPL
HLHLELKTNI GSIPLGIVLQ ALKNKKAFVF TKAGFLSFQH CLFQFLKQFI SAQKCLIPEN
TVIATVTDIF KLDALAPLST HEHISASASD LAFFSQLKAA CLPPIPQSLF STDHKLRPYQ
NSGLLWLWFL YNHRLSGLLC DEMGLGKTHQ ATALLDIVFQ SAEPTERPKF LIVCPTSVLP
HWEHTLATHL PTVSIFAFHG PNKPENLPPT DVIITSYGTL RQNYAKFYKV SFTVTVFDEI
HMAKNKNSQI HKILCRLDSQ MKLGLTGTPI ENNLLEFKGL LDIILPNYLP SDALFKKLFT
KKTPAEIDDE IIPSQDLLLK LTRPFILRRT KKLVLPELPE KVESIIPCTL SPEQKKLYQS
TLKREKAQIQ QLESPEEQTV NYLHVFALLN HLKQICNHPA IFFKNPDKYR EHESGKWNAF
VRLLHESLSS GYKVVVFSQY IHMIRIIMLY LEEIGVKYAS IQGKSLNRKE EIEYFTTDPE
CRVFVGSLLA AGTGINLTAG NVVIMYDRWW NPAKENQALD RVHRIGQKNT VFIYKLMTED
TLEERIHYLI EKKIRLLDKV ISTQNSNILH MLNREDLITI LSYKDERNGV DDTANIPNDE
ENSIF
//