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Database: UniProt
Entry: A0A2H9N8Q6_9ARCH
LinkDB: A0A2H9N8Q6_9ARCH
Original site: A0A2H9N8Q6_9ARCH 
ID   A0A2H9N8Q6_9ARCH        Unreviewed;       363 AA.
AC   A0A2H9N8Q6;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   Flags: Fragment;
GN   ORFNames=COZ60_02595 {ECO:0000313|EMBL:PIX31796.1};
OS   Candidatus Bathyarchaeota archaeon CG_4_8_14_3_um_filter_42_8.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1974384 {ECO:0000313|EMBL:PIX31796.1, ECO:0000313|Proteomes:UP000230737};
RN   [1] {ECO:0000313|EMBL:PIX31796.1, ECO:0000313|Proteomes:UP000230737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG_4_8_14_3_um_filter_42_8 {ECO:0000313|EMBL:PIX31796.1};
RA   Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M.,
RA   Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M.,
RA   Klingl A., Woyke T., Ryan C.M., Banfield J.F.;
RT   "Depth-based differentiation of microbial function through sediment-hosted
RT   aquifers and enrichment of novel symbionts in the deep terrestrial
RT   subsurface.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010}.
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:PIX31796.1}.
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DR   EMBL; PFIN01000144; PIX31796.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H9N8Q6; -.
DR   Proteomes; UP000230737; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR027925; MCM_N.
DR   InterPro; IPR033762; MCM_OB.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR11630:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF14551; MCM_N; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   SMART; SM00350; MCM; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          286..363
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   NON_TER         363
FT                   /evidence="ECO:0000313|EMBL:PIX31796.1"
SQ   SEQUENCE   363 AA;  40750 MW;  F02F9CB7B3015256 CRC64;
     MTEELETIDP QERFQELFKT EKYRQRISQM AVTGKTSLIV DFEDVLIFDQ RLAEELLEKP
     DEYLKRANDA AYAQLQTEDQ EYAEKIADKQ EIVTVRLVRL LEAAQLRKLG SDHIGRLVMV
     EGIVVRSTSM RPMVMRAAFK CKRCGEITPI SQTGQFLKAP FVCSNPSCGA KGLFDFVQEE
     STFIDSQDLR MQERPEDLPP GQLPRTLHIK LIGGEIVDIA RPGDHVSIVG TVCAVSPTLP
     RVGKLRTFIL HVDANSIEVL GKEPEIALPS PEEEEKIHEL AKDPWIHQKI MTSIAPSIYG
     YDHIKESIMY LLFGGVPKYL PDITIRGEMN ALLIGDPGTA KSQLLQYVAR VAPRGLYTSG
     RGT
//
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