ID A0A1Q9P8P5_9ARCH Unreviewed; 1643 AA.
AC A0A1Q9P8P5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=mcm {ECO:0000313|EMBL:OLS30750.1};
GN ORFNames=HeimAB125_18230 {ECO:0000313|EMBL:OLS30750.1};
OS Candidatus Heimdallarchaeota archaeon AB_125.
OC Archaea; Asgard group; Candidatus Heimdallarchaeota.
OX NCBI_TaxID=1841596 {ECO:0000313|EMBL:OLS30750.1, ECO:0000313|Proteomes:UP000186239};
RN [1] {ECO:0000313|EMBL:OLS30750.1, ECO:0000313|Proteomes:UP000186239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB_125 {ECO:0000313|EMBL:OLS30750.1};
RX PubMed=28077874; DOI=10.1038/nature21031;
RA Zaremba-Niedzwiedzka K., Caceres E.F., Saw J.H., Backstrom D.,
RA Juzokaite L., Vancaester E., Seitz K.W., Anantharaman K., Starnawski P.,
RA Kjeldsen K.U., Scott M.B., Nunoura T., Banfield J.F., Schramm A.,
RA Baker B.J., Spang A., Ettema T.J.G.;
RT "Asgard archaea illuminate the origin of eukaryotic cellular complexity.";
RL Nature 541:353-358(2017).
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:OLS30750.1}.
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DR EMBL; MEHH01000139; OLS30750.1; -; Genomic_DNA.
DR Proteomes; UP000186239; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 2.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 3.
DR Gene3D; 3.10.28.10; Homing endonucleases; 2.
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; 3.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR01443; intein_Cterm; 2.
DR NCBIfam; TIGR01445; intein_Nterm; 2.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR Pfam; PF14890; Intein_splicing; 2.
DR Pfam; PF14528; LAGLIDADG_3; 3.
DR Pfam; PF00493; MCM; 3.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR00379; INTEIN.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR SUPFAM; SSF55608; Homing endonucleases; 3.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50818; INTEIN_C_TER; 2.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR PROSITE; PS50817; INTEIN_N_TER; 2.
DR PROSITE; PS50051; MCM_2; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OLS30750.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000}.
FT DOMAIN 289..423
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT DOMAIN 523..662
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 811..833
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 833..857
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT DOMAIN 1011..1144
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 1356..1378
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 1371..1449
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 1643 AA; 186563 MW; 553846227389895E CRC64;
MVVDMPSSTN ERFREFFQAY QDENGRHFYV EQVQKMSLEG LLSLFVNYDD LLRFDPELAR
LLREEPEETI KIADDALIEV LKIEDPIYAA SEETKGLFHV RFSNLPDLID LRRLRSVHLG
NLIAVEGIVI RQSVVKPLLI EGVFQCVRCS QVHYIQQEGG YYAEPPKCIN PNCGKNGPFN
LITEQSTYTD YQKITVQEKP ESLPPGQIPR NVPARLIGDL VDTVRAGDRA VVSGILRMKV
KGIQRGKMAT FDPWLDVNFV SSREMEFEDI DIDPDTEQEI LDLSTDINIH RRIVRSIAPS
IYGMETIKEA LATVLFGGVS RVAPDGMKQR GESNLLMIGD PGVAKSQLLQ YVHRLAPRGL
LTSGKASSAA GLTAAVIRDA ETGEFGLEAG ALVLADRGVC LTADTEILLS SGKISTIEEI
VEEDHKGEVI SFNPDSFSLN SNKIINTSKR ISNDVYQLEF SSGDILKATK EHPLPTWDNG
LVWKEVEELK SGDIIIDFRN YPFPESVDNS ETEYPLSEEL AEILGLIVTD GNLSKEKYKI
SFYSKSEELL QRYKFLVEQI FGLRTGNYVD KRNMVTRLYF DNKQVHTFLR NLGIPNINKS
KTPCILPNII DAPATIIHAF LSGVVNGDGS VSNRKYGGII DIVVGNKETA VFYQKLLRKI
GIAARLNKLK QKGGGVVADG DYTTYKVSIT GVSNIKKFNP DKLISYKKKA YQKIVRRQDK
SDKIYKIDRI IQSLSSLIPH GSKSILYKNS IRKSQLKSLG INKENIRNAL EKLSKFKEVK
QSSEYILLSK IIENDVHFII LKDKTKIESQ TVYNLEIDND NTFFGNFIPV HNCLIDEFDK
MNPVDRSSIH EAMEQQSYHP SFEISFLNGY KRQIGSFVND LFSENEKSKI KGKDCEILSV
ENMAYEVLTT DFKKIYPTNV NRISRHLAPD HFIKITYSNG RDIIVTPEHP VFTIVNGEIQ
TVDADKVTEN MFIPGVQKLS FKNSSSLVTD YSRGIKEVSL PDEITDDLAK FLGYYTAEGY
SYKGSSLEVG LCNTDPVIID DMIDCINSTF NIEPIDYTQQ NRTVRIISTD IYNYLTENFP
TTFQKSYKKR IDKKIFCTER SMRIEFLSAA FAGDGSVEST SIAYSTASKG LAQDYQDLLL
TLGISSRITS EIYSYGKNKE HQRTRYKVYI RGDSLTKFAY QVIRNPETNP KLMKLIFNSN
NRNRKHNVLP PDAANLIISS LHDLGLSYNG YFYQHLKNSY GITVETIDKY YIDLSNRLQL
LQSKTDYFKT SQELRIYLGY SVSKMAKFVG ISRGTLAKYE RENKPDLLPK YKHVLEDQLE
KVRNSLQELD YLREFRWLRI KKLEKIKNEG EFATKWVYDV TIEPTENFIS HGLILHNTVS
IAKAGIVAQL NARTSVIAAA NPRFGRYEET RPPIENINLP ATILSRFDLI YVIRDEPDAD
TDRRMARHIL ELRRGHVIED TEPTIDIDLL RKYVSYAKQH IQPSLTDDAM ERIEQFYLGL
RKETDETSAI AITPRYLEAI IRLSEAQARM ALKEDVTIDH VEAAINLLVA SLEKVGKDPV
TGRVDIDYLL SGTTKTSRSK MQIIIDIMKE ESRVGSSDVV SIRRIKELAK EQNIDDEFVD
RVITQLRSNG EIYSPSDGFV KLA
//
