ID M0MEV1_9EURY Unreviewed; 698 AA.
AC M0MEV1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=C449_12550 {ECO:0000313|EMBL:EMA43868.1};
OS Halococcus saccharolyticus DSM 5350.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA43868.1, ECO:0000313|Proteomes:UP000011669};
RN [1] {ECO:0000313|EMBL:EMA43868.1, ECO:0000313|Proteomes:UP000011669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA43868.1,
RC ECO:0000313|Proteomes:UP000011669};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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:EMA43868.1}.
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DR EMBL; AOMD01000027; EMA43868.1; -; Genomic_DNA.
DR RefSeq; WP_006078369.1; NZ_AOMD01000027.1.
DR AlphaFoldDB; M0MEV1; -.
DR STRING; 1227455.C449_12550; -.
DR PATRIC; fig|1227455.4.peg.2572; -.
DR InParanoid; M0MEV1; -.
DR OrthoDB; 6747at2157; -.
DR Proteomes; UP000011669; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR048907; MCM_WH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR Pfam; PF21120; MCM_WH_arc; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 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; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000011669}.
FT DOMAIN 275..483
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 662..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 77929 MW; A2C052DE62B2E65C CRC64;
MARAENTELI DDFEEFYRNY YRNEIGELAR QYPNEQRSLF IDWDDLYRFD SDLADDYRSQ
PGQLQEYAEE ALRLYDLPVD VGLGRAHVRI RGLQETTEIR EIRARHRGQL LSVQGTVQKA
TDVRPKITEA AFECQRCGTL SRIPQTGGDF QEPHECQGCE RQGPFDINFD QSEFVDAQKI
RVQESPEGLR GGETPQDIDV HIEDDITGAV TAGDHVRVTG VLHLDQQESG REATAMFDVY
MDGVSVEIED EQFEDMDIDE ADKRAIVDLS TADDIYDQMI ASIAPSIYGY EQAKLAMTLQ
LFSGVAKHLP DGSRIRGDLH MLLIGDPGTG KSQLLQYIRQ IAPRSVYTSG KGSSSAGLTA
SAVQDDFGEG QQWTLEAGAL VLADQGIAAV DELDKMEAGD RSAMHEALEQ QTISISKAGI
NATLKSRCSL LGAANPKYGR FDQYESIGEQ IDLEPALISR FDLIFTVTDD PDPDRDRELA
EHILRTNYAG ELNTQRTEQT AANVTQSEVD AVTDTVAPAI EPDLLRKYVA YAQRNCFPTM
TEEAKEAISD FYVDLRSKGA DEDAPIPVTA RKLEALVRLA EASARVRLAD TVELEDAERV
IEVVRTQLQD IGVDPETGEF DADIVETGTS KTQRDRIKNV KALIAEIEEE YDAGAPIEEV
LDRAEETGTE RSKAEHELEK LRRQGEVYEP QTDHLRTT
//
