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Database: UniProt
Entry: Q821K9_CHLCV
LinkDB: Q821K9_CHLCV
Original site: Q821K9_CHLCV 
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
//
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