ID A0A1U8K555_GOSHI Unreviewed; 839 AA.
AC A0A1U8K555;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN Name=LOC107913539 {ECO:0000313|RefSeq:XP_016697650.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016697650.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016697650.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016697650.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. The active
CC ATPase sites in the MCM2-7 ring are formed through the interaction
CC surfaces of two neighboring subunits such that a critical structure of
CC a conserved arginine finger motif is provided in trans relative to the
CC ATP-binding site of the Walker A box of the adjacent subunit. The six
CC ATPase active sites, however, are likely to contribute differentially
CC to the complex helicase activity. {ECO:0000256|RuleBase:RU368062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU368062};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368062}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_016697650.1; XM_016842161.1.
DR AlphaFoldDB; A0A1U8K555; -.
DR STRING; 3635.A0A1U8K555; -.
DR PaxDb; 3635-A0A1U8K555; -.
DR GeneID; 107913539; -.
DR KEGG; ghi:107913539; -.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000189702; Chromosome 21.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000347; C:THO complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR CDD; cd17755; MCM4; 1.
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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 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 PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
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 ECO:0000256|RuleBase:RU368062};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000189702}.
FT DOMAIN 429..635
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 92892 MW; E29991608472F2F7 CRC64;
MASESSPANF NNGPSSPDDS FSSPIANTSS PAHRRRRGRR QASTPSSAAA TPPPNPSRFA
NSASTPTPAR STRRGRRPGP ATSPSPAVAA TPSSTDDFSM PSSEGGEDME EATPTFVWGT
NISVQDVKNA IQMFIKHFRD PQELSNDIYG EGKYTRLIHR VLEVEGEWID VDAHDVFNYD
SDLYNKMMRY PLEVLAIFDI VLMDIVSVIN PLFDKHVQVR IHNLKSSTSM RNLNPSDIEK
MVSLKGMVIR CSSIIPEIRE AVFRCIVCGY HSEPVVVDRG RISEPTSCLK QECLAKNSMA
LVHNRCRFAD KQIVRLQETP DEIPEGGTPH TVSLLMHDKL VDAGKPGDRV EVTGIYRAMS
VRVGPTQRTV KSLFKTYIDC LHIKKTDKSR MTAEDPMEVD KGSQRVDDDV QFDEDKVEEL
KELSKQPDIY ERLTRSLAPN IWELDDVKKG LLCQLFGGNA LKLLSGASFR GDVNILLVGD
PGTSKSQLLQ YIHKLAPRGI YTSGRGSSAV GLTAYVAKDP ETGETVLESG ALVLSDRGIC
CIDEFDKMSD NARSMLHEVM EQQTVSIAKA GIIASLNART SVLACANPSG SRYNPRLSVI
DNIHLPPTLL SRFDLIYLIL DKADEQTDRR LAKHIVSLHF EDTEIAEHDV IDLATLTAYV
SYARKNIHPK LSDEAAEELT RGYVEMRKRG NFPGSSKKVI TATPRQIESL IRLSEALARI
RFSETVEMRD VTEAFRLLEV AMQQSATDHS TGTIDMDLIT TGVSASERMR RESVLSATRN
IIMDKLQLGG PSILLLELLD EMKKQNSGTE IHLHDLRTAV ATLASEGFVV LHGDSVKRM
//
