MCM10_DANRE
ID MCM10_DANRE Reviewed; 833 AA.
AC Q5RHY1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein MCM10 homolog;
GN Name=mcm10; ORFNames=si:ch211-206k18.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Acts as a replication initiation factor that brings together
CC the MCM2-7 helicase and the DNA polymerase alpha/primase complex in
CC order to initiate DNA replication. Additionally, plays a role in
CC preventing DNA damage during replication (By similarity).
CC {ECO:0000250|UniProtKB:Q7L590}.
CC -!- SUBUNIT: Self-associates. {ECO:0000250|UniProtKB:Q5EAW4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5EAW4}.
CC -!- DOMAIN: Each zinc finger-like domain binds a zinc ion and is involved
CC in both ssDNA and dsDNA binding, as is the OB-fold domain.
CC {ECO:0000250|UniProtKB:Q5EAW4}.
CC -!- DOMAIN: The N-terminal domain mediates homodimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCM10 family. {ECO:0000305}.
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DR EMBL; BX323869; CAI11761.1; -; Genomic_DNA.
DR RefSeq; NP_001019984.1; NM_001024813.1.
DR AlphaFoldDB; Q5RHY1; -.
DR SMR; Q5RHY1; -.
DR STRING; 7955.ENSDARP00000067338; -.
DR PaxDb; Q5RHY1; -.
DR PRIDE; Q5RHY1; -.
DR Ensembl; ENSDART00000067339; ENSDARP00000067338; ENSDARG00000045815.
DR GeneID; 553396; -.
DR KEGG; dre:553396; -.
DR CTD; 55388; -.
DR ZFIN; ZDB-GENE-041210-42; mcm10.
DR eggNOG; KOG3056; Eukaryota.
DR GeneTree; ENSGT00390000007134; -.
DR HOGENOM; CLU_014680_0_0_1; -.
DR InParanoid; Q5RHY1; -.
DR OMA; VFGLRMI; -.
DR OrthoDB; 758449at2759; -.
DR PhylomeDB; Q5RHY1; -.
DR TreeFam; TF313330; -.
DR Reactome; R-DRE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DRE-68962; Activation of the pre-replicative complex.
DR PRO; PR:Q5RHY1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000045815; Expressed in mature ovarian follicle and 17 other tissues.
DR ExpressionAtlas; Q5RHY1; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR040184; Mcm10.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR015411; Rep_factor_Mcm10_C.
DR InterPro; IPR015408; Znf_Mcm10/DnaG.
DR PANTHER; PTHR13454; PTHR13454; 1.
DR Pfam; PF09332; Mcm10; 1.
DR Pfam; PF09329; zf-primase; 1.
DR SMART; SM01280; Mcm10; 1.
PE 3: Inferred from homology;
KW Coiled coil; DNA damage; DNA replication; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..833
FT /note="Protein MCM10 homolog"
FT /id="PRO_0000278322"
FT REGION 1..122
FT /note="N-terminal domain"
FT /evidence="ECO:0000250"
FT REGION 18..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..360
FT /note="OB-fold domain"
FT /evidence="ECO:0000250"
FT REGION 361..386
FT /note="Zinc finger-like 1"
FT REGION 502..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..760
FT /note="Zinc finger-like 2"
FT /evidence="ECO:0000250"
FT REGION 774..794
FT /note="Zinc finger-like 3"
FT /evidence="ECO:0000250"
FT COILED 70..108
FT /evidence="ECO:0000255"
FT COMPBIAS 22..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 92439 MW; D0E7700B2FE8B2C5 CRC64;
MTEEENLDML LSLFAESEGQ DLESPAAEEG EDNLDDLFDE DDDGEQYIEP EEAEEEKEEE
EEEVSPGKSS SSDLNKSKED LEAELKLMQE KMQKLQQQLE ASQKTTPAQN KPAVQRQSTK
SLTSPQAGVK TTPPTVRDSD GSPSNITAKL KNKQRTAHQP KAASSERQIP IGQSTNQPQP
MRDGAKVNSM LKSPPLIKTP PTVRQPTPRL PVNQEVAVEK FSGLRLRKPR LSSIDIEQKM
ASRKLIRLSQ LPDRLARDNL EDSDWVTFAV IINKITPQSK NNGKTFSIWK LNDLHNLEVN
VSLFLFGSVH TDLWKTDTGT VIGILNPNPM KNKEGSNELS LTVDHPQKVL IIGEAMDFGT
CKAKKKNGDS CTQLVNLYEC QFCQYHVKAQ YKKMSSKRAE LQSSFTGSAP GKGRGRGSLK
ERLCQSDFHY GGMSSLACAP SMSAPQPKKQ PTIQSALASI PTKKLVLNSG QVSGCSDDFR
GLMSMPTPGA LNIKRHLGQS KSSAVAGSSV QSVSASDLLK QQKEQHQQRM MARKKRAEEI
QKRVLQSGGA PVASSRPNVS RGPLLSPKAA SEGPKGSGSS LSGPAVPTLG RGFSEGEDIV
FDMSPPSSKS LSATKLAAVR KLQAKGSVIV KEDPNAVKRK RANSGDITGR VERNIVKAKV
TDENSASEEE EPAMKKRREQ LEYIQSEEFQ RILNAKSSNS WMMGEIEERA MQEYFEPLVQ
KEKMEEKMKS IREMKCRAVT CKTCKYTHFK PADRCVEEKH DYHWHDAVKR FFKCPCGQRK
ICLARMPHGA CSHCGLFKWE RDGMLKEKKG PKIGGELLMP RGEEQPKFLN SLK
