ID A0A0C1KAC8_9BACT Unreviewed; 1161 AA.
AC A0A0C1KAC8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative ATP-dependent helicase {ECO:0000313|EMBL:KIC76067.1};
DE EC=3.6.4.- {ECO:0000313|EMBL:KIC76067.1};
GN ORFNames=DB42_EC00130 {ECO:0000313|EMBL:KIC76067.1};
OS Neochlamydia sp. EPS4.
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Neochlamydia.
OX NCBI_TaxID=1478175 {ECO:0000313|EMBL:KIC76067.1, ECO:0000313|Proteomes:UP000031344};
RN [1] {ECO:0000313|EMBL:KIC76067.1, ECO:0000313|Proteomes:UP000031344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPS4 {ECO:0000313|EMBL:KIC76067.1,
RC ECO:0000313|Proteomes:UP000031344};
RX PubMed=25069652; DOI=10.1093/molbev/msu227;
RA Domman D., Collingro A., Lagkouvardos I., Gehre L., Weinmaier T.,
RA Rattei T., Subtil A., Horn M.;
RT "Massive expansion of Ubiquitination-related gene families within the
RT Chlamydiae.";
RL Mol. Biol. Evol. 31:2890-2904(2014).
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:KIC76067.1}.
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DR EMBL; JSDQ01000008; KIC76067.1; -; Genomic_DNA.
DR RefSeq; WP_039386911.1; NZ_JSDQ01000008.1.
DR AlphaFoldDB; A0A0C1KAC8; -.
DR STRING; 1478175.DB42_EC00130; -.
DR PATRIC; fig|1478175.3.peg.229; -.
DR Proteomes; UP000031344; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18012; DEXQc_arch_SWI2_SNF2; 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; IPR013663; Helicase_SWF/SNF/SWI_bac.
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; PF08455; SNF2_assoc; 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:KIC76067.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIC76067.1};
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 55..92
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
FT DOMAIN 711..872
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1001..1147
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1161 AA; 133503 MW; F5653F859B6A6802 CRC64;
MLNFRKLKQD YSSALLKDGK ALYEKGTVSS AKIVTLDAQR VRLSCKVQGA FEKTYNCEIE
IDRRESTTMD SDCDCPHQYD CQHLSAVLFY LEAHLDETIV KYSKETDLGK NPAIDESEKE
TLRETFKEAE TKETVRRNKK QQKELLIEYV GASDVLGKSP FFLPEEELIQ DKAELAIIFS
NIAPTSPQSY VEVQLALRLP FRSKPLNIAN AREFLDSLCY QEPFYIGNKR YYFTLQSFDE
DSAQTLKMLM NFARFPEVKE DRNLRLIHID LEAFGNLLAQ AYEGAIARPK ALNTSYETEA
EHPLLPCFYC GTMEEPLRYS GQLGKLRFEL EYIKADSPKI LVNPTLMIDE DQRVTLPEVR
LFECAKPGLL YQNNYYRFQP RIRRKHLRNL PAIRDVTIPE ALFGTFVENS LPELMRYADI
YNREIIDRFV TLPFVGKLRA ICDINYLNGE LEAALQFIYD DIVVPAAPSQ INPNHILPFV
TTEGILARNL TEEQKILREL FQDFIYDPST GFFIAKTDKK IIEFMTDIIP HNQDRIKFNC
PENLLDQFIY EETKFKIHLK ETDRIDQYEV HIKVNGYLNG FTLDMLWECL STKRAFVELA
RKKSTKKKDS ASKSHKILVL ELDKLAPIIQ LLDDIGVKQL ADHVQVCPLW SLSSIDVKAY
QGLPLDITMS PKLKLIQEQM LGMAVPCTSV IPKNIQASLR SYQNEGVSWL NRLRDMHLNG
ILADDMGLGK TLQSIIAITQ HKLEHPKAIS LVVCPTSLVY NWKEEIGKFN PQLKVLAVDG
TPTQRKKLLT SIRDFDVIIT SYSLLQKDVD FYITIKFGYC ILDEAQHIKN RGTRNAKSVK
MIQAAHRLIL TGTPIENSLD ELWSLFDFLM PGLLSSYERF VEKYIRHPSQ PAGSQLEILR
QKVSPFILRR MKQDVLSELP PVSEIVYHCH LSETQRELYH SYAASAREEL SKLVKREGFE
KIQIHVLATL TRLKQICCHP AIFAKDKAEV GDSSKYDMLM ELLQTLIEGK HKTVIFSQYT
RMLNIMREDL QRQGIPFEYL DGASKNRLNI VKKFNEDQNI PVFLVSLKAG GTGLNLVGAD
TVIHYDMWWN PAVENQATDR VHRIGQKNAV SAYKLVTLNT IEEKIMELQN RKKGLVKKVV
SSDDEAISKL TWEEVLELLQ T
//
