ID A0A498LFS1_LABRO Unreviewed; 1040 AA.
AC A0A498LFS1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA helicase MCM9 {ECO:0000256|ARBA:ARBA00041085};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=ROHU_013048 {ECO:0000313|EMBL:RXN04255.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN04255.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN04255.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN04255.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN04255.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:RXN04255.1}.
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DR EMBL; QBIY01013454; RXN04255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498LFS1; -.
DR STRING; 84645.A0A498LFS1; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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; 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; 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, ECO:0000256|RuleBase:RU004070};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000313|EMBL:RXN04255.1};
KW Hydrolase {ECO:0000313|EMBL:RXN04255.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT DOMAIN 343..469
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 616..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 114990 MW; 0EBF876F87771FED CRC64;
MNMMLSPDQV SFIGLAFETY VMEHHKNDIL QIFQEASEDA HHPVVVNAMT LFEDNMEVGE
CFNAFPSQVL PIFDNALHRA VQTISQSSSL QESFKLKHNL HVRISGLPMC PELTRDHIPK
ARDVGHFLSV TGTVIRTSVT KVLEYERDYM CNKCRHVFSV QASFEQFYSF APPTSCPNED
GCNSFKFTCL SGSDAPPATC KDYQEIKIQE QVQKLSVGSI PRSMLIILED DLVDSCKSGD
DITVYGVVCQ RWKPMFLDCR CDVEIVLKAN YIEVNNEQST TALVLEDIQK EFEDFWDSHK
HDPIAGRNEI LMSLCPQVFG MYVVKLAVAM VLAGGVQRID ASGTKVRGLT VAAVKDSGEW
HLEAGALVLS DGGLCCIDEF NSIKEHDRTS IHEAMEQQTI SVAKAGMVCK LDTRTTILAA
TNPKGQYDPN VSVSVNVALA SPLLSRFDLV LVLLDTKNPE WDKIISSFIL QNKGAPTESS
CLWSMEKMRA YFCLIKTLKP CITQEANTIL SRYYQLQRQS DSRNAARTTI RMLESLSRLA
EAHARLMFRE TVTVEDAVVV VSVMECSMQG GALLGNVNAL HTSFPDDPCE QYKTQCEIVL
ERLGLTDILH KELQRLSRLK NRRPGSPKGT EPRSGHTSEH PAGQNHSNVE VTTDSDPSLD
WFHSLSSPTG TGSVVHTSPV ITSTQNAATT ITTLGTTVLP SNNCSIRRKG SVWEKDEDSS
VVEAVVEKGS KKLRAKRLKE MKASLLLNEE RAVEEMGDDF EMFSHSTPKT GKKPSKRKNT
DQEADFRAES GEDLRSKLTN FTFKPRERMT HTDQPVHEGA KPNAPQVPEK QAERGNLSNS
RPPAEGSRAN KKPRLGTHNK TKEISSEVLN DESTGTSEDT EHQQQLVSRL NSLSPGENNG
NTNKHPPMTD LPKAKVAGST LAMLSRFSFT GSSEEKTGDK TVPVPQVAIN GSTNKVPANS
VSAEQENTRT QAGKNITTDV KTTTMQRGNA RTEQEEVGEN ATKKRRCFEL GSGGPAGLLK
GFSLFSSSVI DDEDLDADWN
//
