GenomeNet

Database: UniProt
Entry: S9VX56_9TRYP
LinkDB: S9VX56_9TRYP
Original site: S9VX56_9TRYP 
ID   S9VX56_9TRYP            Unreviewed;       754 AA.
AC   S9VX56;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN   ORFNames=STCU_05271 {ECO:0000313|EMBL:EPY28160.1};
OS   Strigomonas culicis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY28160.1, ECO:0000313|Proteomes:UP000015354};
RN   [1] {ECO:0000313|EMBL:EPY28160.1, ECO:0000313|Proteomes:UP000015354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA   Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA   Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA   Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA   Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT   Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT   Family.";
RL   PLoS ONE 8:E60209-E60209(2013).
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:RU368061}.
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|RuleBase:RU368061};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368061}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368061}.
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:EPY28160.1}.
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   EMBL; ATMH01005271; EPY28160.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9VX56; -.
DR   EnsemblProtists; EPY28160; EPY28160; STCU_05271.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000015354; Unassembled WGS sequence.
DR   GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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; IPR031327; MCM.
DR   InterPro; IPR008046; Mcm3.
DR   InterPro; IPR018525; MCM_CS.
DR   InterPro; IPR001208; MCM_dom.
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:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   PRINTS; PR01659; MCMPROTEIN3.
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|RuleBase:RU368061};
KW   DNA-binding {ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368061};
KW   Hydrolase {ECO:0000256|RuleBase:RU368061};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU368061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015354}.
FT   DOMAIN          326..531
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          554..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          687..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..656
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  81904 MW;  D217AB9CC3A316CA CRC64;
     MLSNRTLTEE QTLIRRHFTD FFESERYEEK YHRRIQAMIV ADKARLVMDI GDLLDFHLDV
     ASLEAAGGVG GDGGATNPNT PTSLGMGIIR EPGKYLPLLE LALHDVVLRQ QPEYLKVDYR
     SRAVHIGFEG PVGTVLSPRE LYARHLNTMV ALEGIVTRQS TNRPRVLETV HYCPETNKFT
     KKEFRDQLTP MLDSSHLPTV NVMPKTDMEG HALRTELGLS TFMDSQCAIL QEAPERAPTG
     QLPRNVEVRF DDDLVDAVKP GDRVVVVGVF MPYTTADSKS FQSIVLVNHV APTQAAAYLS
     RYISSVEDRL VAFAKKSIHR EGPSGVLQVL AKAVAPTLYG ITHEKRAVLL LMVGGVERQA
     HNTHIRGDIN VLLVGEPSTA KSQLLRFVLG VAPLALSTTG KGSSGVGLTA AVAVDAYTGE
     RSLSAGAMVL ADRGILCIDE FDKMGASDRV AMHEAMEQQT VTIAKAGVHA SLNARCSVLA
     AANPIYGFYS VHHRLAFNVG LPESLLSRFD LTFIILDQHS SAHNRRIATH ILRNHMTSTP
     VTLDPVVTKT IVDGGVDAGP RGGRRERGWG DAARPGLSHD REQYGREHRE RGLPAGVHPV
     LQGRQPAPHG GLAAARQPAL RAVARGAAGR HPRRLLRHRA NAGVDHPPRH RPREAAAVAD
     GGGGRRGGCD GAAAVVRARR VGCDAAARRR QPHLARGGGA RRRSRGGDRG GAQARHRCRR
     RRAQPRGGRA AAHAAGGHHA PRACRQRRQR AVPP
//
DBGET integrated database retrieval system