ID J9J692_9SPIT Unreviewed; 1096 AA.
AC J9J692;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=Minichromosome maintenance 9 {ECO:0000256|ARBA:ARBA00042301};
GN ORFNames=OXYTRI_20770 {ECO:0000313|EMBL:EJY81715.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY81715.1};
RN [1] {ECO:0000313|EMBL:EJY81715.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY81715.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {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:EJY81715.1}.
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DR EMBL; AMCR01006568; EJY81715.1; -; Genomic_DNA.
DR AlphaFoldDB; J9J692; -.
DR EnsemblProtists; EJY81715; EJY81715; OXYTRI_20770.
DR OrthoDB; 206676at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630:SF48; DNA HELICASE MCM9; 1.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}.
FT DOMAIN 346..552
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 762..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 897..924
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1096 AA; 125471 MW; 22041CFD12763C13 CRC64;
MASNANEIME YFMKESYDQL VPILMGEDTI IYYDITVDLL DFIYNFPFLG GKFHEHPFEF
LEFLKDTLVA CQQKIVEKDE DKLPVNVVVK KNLDVKLLNI PPTKEVVAES IRAVNTEYQN
KFIILTGTVV RTGHVNSREL FKQFKCRQCE KEFTCESDIT EYNNFKLPQR CDGKVQTKEN
PFFKIAKTLI NNIKNKNMKG QLDENQNFDN PKREANTGFQ TSACKSKSFQ PVDGTSEFSD
YQEIKLQELF KTLKPGLIPR SMMVILQNTL VEICKPGDDV MITGVLIQRW KNMPPAPGTR
PFIELALLAN NVEVLNKREF SKSNSINMDT LNEFKRFWRK HDPIIGRQIL IKSVCPNIYE
RYDVKLGLLL SLIGGVAQHQ EETKFKVRGQ VHLLMVGEPG TGKSQMLQAA THLSQRSVQT
TGIGTTSAGL TVSCFKDGAE YVLEAGALVL ADCGVCCIDE FSLIKNDDRA SIHEAMEQQT
ISIAKGGIVC KINTRTTIIA ATNPGRTQKW DPNYDLQQNT GIMSSLLSRF DLIFIMLDEH
QVEDDIQKAD FVLNRSCLNR SEVKQEFQLW PQEKLANYIN FVQKVFEPVV TEEAEIMLKA
YFAYLRMNPK VNKDRKTVRM LESIIRMTEA HARLLMKSQA TVFDAICVII LMEHTLMTNL
FGSEILPSII MRSAIEYKQI RDDLTYRLGL DGICFGEQDE SIELYKQCQT PSPVKRLEDS
MFINNAESNF DFSFVGGSEF SFQSQDEQSH FFRQNSQING FKHNSSNLMR SNNGSQMPNF
KIHNSGSQSL NSLSSQSLAR NLGQQLQHSS TLQKSNSQLL DLNISKTTEK YLENQIVIPE
ENSSELILND DLFNGMSELS DTSNNFQDLL SDLSQITSCD RYANQELKEN PIIEIQQPSL
QEEAKVLESQ INQLQAHIQA NLEEESNHDQ QVTVSDFMEN EILYETKSQH INQGLIQVQQ
SQQINKEWDQ FQTQINQKQI DKPEDQTLTK KNLLLTKFKL CTDQNAKILS QVDDQIQNLQ
CDIFNQSKNQ DQQENIQRIN ATSKGVTILD DLEEYDEQSL IQQSQQEIDQ QINQGNDQII
ENNEDDDDND NDFLFD
//
