| Tag | Content |
|---|
| CPLM ID | CPLM-023375 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA replication licensing factor Mcm5 |
Protein Synonyms/Alias | Minichromosome maintenance 5 protein; DmMCM5 |
Gene Name | Mcm5 |
Gene Synonyms/Alias | CG4082 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 142 | LKSDCVSKLVKIAGI | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Acts as component of the Mcm2-7 complex (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. |
Sequence Annotation | DOMAIN 328 534 MCM.
NP_BIND 378 385 ATP (Potential).
MOTIF 509 512 Arginine finger. |
Keyword | ATP-binding; Cell cycle; Complete proteome; DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 733 AA |
Protein Sequence | MEGFDDAGVF FSDNFGGDNQ QDAQINLQAV KKKYKEFIRT FNEENFFYKY RDTLKRNYLN 60
GRYFLEIEME DLVGFDETLA DKLNKQPTEH LEIFEEAARE VADEITAPRP EHEEHMHDIQ 120
ILLSSNANPT NIRQLKSDCV SKLVKIAGII VAASGISAKA TRMSIQCLSC STVIPNLKVN 180
PGLEGYALPR KCNTEQAGRP KCPLDPFFIM PDKCKCVDFQ TLKLQELPDF VPQGEIPRHL 240
QLFCDRSLCE RVVPGNRVLI QGIYSIRKVG KPSRRDGREK AVVGVRAPYM RVVGITVDSE 300
GAGAISRYSN ITSDEEEHFR RMAASGDIYE RLSQSLAPSI FGSRDIKKAI TCMLFGGSRK 360
RLPDGLCRRG DINVLLLGDP GTAKSQLLKF VEKVAPIAVY TSGKGSSAAG LTASVMKDPQ 420
TRNFVMEGGA MVLADGGVVC IDEFDKMRED DRVAIHEAME QQTISIAKAG ITTTLNSRCS 480
VLAAANSIFG RWDDTKGEEN IDFMPTILSR FDMIFIVKDI HDESRDITLA KHIINVHLSS 540
NKSAPSEPAE GEISLSTFKK YIHYCRTHCG PRLSEAAGEK LKSRYVLMRS GAGQQEKASD 600
KRLSIPITVR QLEAVIRISE SLAKIRLQPF ATDEHVNEAL RLFQVSTLDA AMTGSLAGAE 660
GFTTEEDQET LNRIEKQLKR RFAIGSQVSE QNILQDFLRQ KYEERTVMKV IHTMIRRGEL 720
QHRMQRKMLY RIC 733 |
Gene Ontology | GO:0042555; C:MCM complex; IEA:InterPro. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0003678; F:DNA helicase activity; IEA:InterPro. GO:0030261; P:chromosome condensation; IMP:FlyBase. GO:0032508; P:DNA duplex unwinding; IEA:GOC. GO:0042023; P:DNA endoreduplication; IMP:FlyBase. GO:0006270; P:DNA replication initiation; IEA:InterPro. GO:0000712; P:resolution of meiotic recombination intermediates; IMP:FlyBase. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |