ID M7BC57_CHEMY Unreviewed; 932 AA.
AC M7BC57;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=DNA replication licensing factor MCM5 {ECO:0000313|EMBL:EMP33160.1};
GN ORFNames=UY3_09722 {ECO:0000313|EMBL:EMP33160.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP33160.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010}.
CC -!- SIMILARITY: Belongs to the heme oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006134}.
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DR EMBL; KB537019; EMP33160.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BC57; -.
DR STRING; 8469.M7BC57; -.
DR eggNOG; KOG0481; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0004392; F:heme oxygenase (decyclizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006788; P:heme oxidation; IEA:InterPro.
DR CDD; cd19165; HemeO; 1.
DR CDD; cd17756; MCM5; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 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; IPR002051; Haem_Oase.
DR InterPro; IPR016053; Haem_Oase-like.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR018207; Haem_oxygenase_CS.
DR InterPro; IPR031327; MCM.
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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 1.
DR Pfam; PF01126; Heme_oxygenase; 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; PR00088; HAEMOXYGNASE.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00593; HEME_OXYGENASE; 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};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Heme {ECO:0000256|ARBA:ARBA00022617};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 571..776
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 105161 MW; EA2E7F4D1B56247D CRC64;
MEGSKTHSSE SMPGDLSEAL KEATKEVHEQ AESTEFMKNF QRGQVSLQEF KMVMASLYYI
YSALEEEIER NKDHPAYIPV YFPAELHRKT ALQEDLEYFY GPLWREEISC PESTQKYVNR
LHYVGQHEPE LLVAHAYTRY LGDLSGGQVL KKIAQKALHL PSTGEGLEFF TFEGVSNATK
FKQLYRSRMN SIEMDPATKK RVLEEAKRAF LLNIQVFEEL QKFVSQCHEN SHPAQQKSEL
RTRGTSEAHE QGPAPVKEGE KTSMKHTDML PSTPLARWIL VLSFLVTTVA VGLFAMDELK
RHYNLGQYWI EVEMEDLASF DEDLADYLYK QPAEHLQLLE EAAKEVADEV TRPRPAGEET
LQDIQVMLRS DANAANIRSL KSDQMSHLVK IPGIIIAATA VRAKATKIAI QCRTCRNTIS
NITVRPGLEG YALPRKCNTE QAGRPKCPLD PYFIMPDKCK CVDFQTLKLQ ESPDAVPHGE
MPRHMQLYCD RYLCDKVVPG NRVTIMGIYS IKKSGQTKSK GRDNVGVGIR SSYIRVVGIQ
VDTDGSGRSF ASSVTPQEEE EFRHLTSMPN IYETIAKSIA PSIYGSTDIK KAISCLLFGG
SRKRLPDGLT RRGDINLLML GDPGTAKSQL LKFVEKCSPI GVYTSGKGSS AAGLTASVIR
DPSTRSFFME GGAMVLADGG VVCIDEFDKM REDDRVAIHE AMEQQTISIA KAGITTTLNS
RCSVLAAANS VFGRWDETKG EENIDFMPTI LSRFDMIFIV KDEHNEERDV TLAKHVMSLH
VSALTQTQAV EGEIELNKLK KLISYCRMKC GPRLSAEAAE KLKNRYVLMR SGARQHERES
DRRSSIPITV RIVSSLGVEG FTTQEDQEML SRIEKQLKRR FAIGSQVSEH SIVQDFTKQK
YPEHAIYKVL QLMMRRGEIQ HRMQRKVLYR IK
//
