ID C2M4T6_CAPGI Unreviewed; 1087 AA.
AC C2M4T6;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Helicase C-terminal domain protein {ECO:0000313|EMBL:EEK14697.1};
DE EC=3.1.21.3 {ECO:0000313|EMBL:EEK14697.1};
GN ORFNames=CAPGI0001_1307 {ECO:0000313|EMBL:EEK14697.1};
OS Capnocytophaga gingivalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=553178 {ECO:0000313|EMBL:EEK14697.1, ECO:0000313|Proteomes:UP000003622};
RN [1] {ECO:0000313|EMBL:EEK14697.1, ECO:0000313|Proteomes:UP000003622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 /
RC 27 {ECO:0000313|Proteomes:UP000003622};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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:EEK14697.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACLQ01000016; EEK14697.1; -; Genomic_DNA.
DR RefSeq; WP_002667326.1; NZ_ACLQ01000016.1.
DR AlphaFoldDB; C2M4T6; -.
DR STRING; 553178.CAPGI0001_1307; -.
DR eggNOG; COG4096; Bacteria.
DR Proteomes; UP000003622; 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:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006304; P:DNA modification; IEA:InterPro.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR025285; DUF4145.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF13643; DUF4145; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF00271; Helicase_C; 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; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000313|EMBL:EEK14697.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:EEK14697.1};
KW Hydrolase {ECO:0000313|EMBL:EEK14697.1};
KW Nucleotide-binding {ECO:0000313|EMBL:EEK14697.1}.
FT DOMAIN 397..581
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 658..851
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 143..170
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1087 AA; 124512 MW; 137BB15874DE1BDA CRC64;
MRSNFEFLKE IEPHILYRIA HLAEMYLYTD PNGCLMKLRQ FAEVMVNEVF QIEHIALPYD
NNQANRISVL KREGIIEHQL GRILNELRQR GNEAVHAGFD SLTSAKTLLQ MAYHLAQWYA
LSYGEGTGGH TFVMPQEEDI PNAAELQAEK EAQDQQIKAL TEQLLGLQKQ QSYWEAAQTK
EFINAQKERA RRTQQYTKNL QLSEAETRQL IDAQLCEAGW QADTEHLRYS KGTRPEKGKN
LAIAEWPTDK GFADYALFVG LQLVGIVEAK AKHKDISSIL SNQCKDYATH IKKEHACYLI
GQWGDYQVPF LFATNGRKYL KQLDTKAGIW FLDVRDNGNI SKALQGWKSP QGLLEDLAQD
IAKATQDLAQ TPYDLLRDPN GLNLRPYQIR AVEASEKALT EGRRSVLLSM ATGTGKTRTL
LAMIYRFLAA KRFKRILFLV DRNVLGRQAL DVFKDVKLED LQTLYNIYPI NELGEKTIAK
ETKIQLSTVQ AMVRRILYNE AEDMPSVSDY DLVIVDEAHR GYILDKEMSE DEFDFRNQED
FISKYTMVID YFDAVKIAVT ATPALHTTQL FGKPVFEYSY REAVLDGFLV DYNLPHHIFT
QQRIEGIHYA KGDTVQAYDP EKNEVIDLSE IPDELNFEVE QFNRNIIVEG FNRAVLEEIA
QSLDPTGEGK TLIFAVDDAH ADLVVKILKE IYAEQGVDND AIQKITGSIG DKKRVEDAIK
RFRNEINPNI VVTVDLLTTG VDVPEITTLV FLRLVKSRIL FEQMMGRATR LCPKINKESF
EVYDPVGVFD FFAEVSEMVP IVVNPNTTLE DIINGFEHTE DPELIAKYTQ QLLARLQRRV
KNISQQDFDY FCSLSQGVSP KDFLTTLKNI PSTEVKSFVR ENIKAIACLF HSQAKTVKYK
YISDKPDEVR EHYVGYGKTQ QRPGDYIEQF SAYIAENRNK LAALNLLCTR PSELTRSELK
HLYLEMAQEG YTLKELNKAW NNAKNVEITA DLIGMIRTLA LGNALVDYKV RLDNAFEKLK
QTHSFNAMET KWLDRIKTFL EKEQYIEKAD FDTGAFQNAG GYEKINKVFK NHLGEIVDEL
KEYLFMG
//
