ID L5LKE8_MYODS Unreviewed; 874 AA.
AC L5LKE8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|ARBA:ARBA00019081, ECO:0000256|RuleBase:RU365058};
GN ORFNames=MDA_GLEAN10023974 {ECO:0000313|EMBL:ELK26717.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26717.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent, however specific
CC DNA sequences that define origins of replication have not been
CC identified so far. ORC is required to assemble the pre-replication
CC complex necessary to initiate DNA replication.
CC {ECO:0000256|RuleBase:RU365058}.
CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC dependent manner. It is sequentially assembled at the exit from
CC anaphase of mitosis and disassembled as cells enter S phase. Interacts
CC with CDC6 and KAT7/HBO1. Interacts with LRWD1 predominantly during the
CC G1 phase and with less affinity during mitosis, when phosphorylated.
CC {ECO:0000256|RuleBase:RU365058}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365058}.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000256|ARBA:ARBA00008398,
CC ECO:0000256|RuleBase:RU365058}.
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DR EMBL; KB110890; ELK26717.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LKE8; -.
DR eggNOG; KOG1514; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04719; BAH_Orc1p_animal; 1.
DR CDD; cd08768; Cdc6_C; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR PANTHER; PTHR10763:SF23; ORIGIN RECOGNITION COMPLEX SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF09079; Cdc6_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51038; BAH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365058};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU365058};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365058};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW Nucleus {ECO:0000256|RuleBase:RU365058};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 45..171
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 181..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 98442 MW; 7CA2311E45E2C3EA CRC64;
MAYCSTRLKS RPTYSWVGSP LLDQKLHYQT YKEMSVTSNG CSTEIRIQVG QFVLVEGDDD
ENPYVAKLIE LFEDVSEPYC KKRARVQWFI RFCEISVSKQ HLLGRKPDVQ EIFWYDYPAC
NSNIDAETIS RPVQVVALAP DEVLPTALKN EKTFFVKLSW NEENFKPLSP ELFAELNKLQ
EGSPRGQKPM KTKNSSIDSP SWTSAKHGVK RIELRHSTSK SHQIPTHLVT PRARKRLELG
SFPVTPHTRI SQQTSRVPLE SPRRTKRKVA SEITSPSKRS QPDGLQTSSP ALKAPEKTGE
RRRSCAEQDK ASHERPMILR TRVPALKTTE ISQEITLDPL RGGKRSSVVP SVVLKPQKMK
KREAQTPDAQ DEATSTPHRI RRKSSLLTLN RIRQQLRFLD GSKNDKEEEE FLPAAEIADS
DSEEEEASTP SLPRKTRSCV SRNLHSSTKS SLHTPSKTPK KTPKPRMPRS VTPQIRSRNL
AVRGPASVLE EARLSLHVSA VPDSLPCREK EFQDIYNFVE SKLLDHTGGC MYISGVPGTG
KTATVHEVIH CLQQAAQAND VPPFQYIEVN GMKLTEPHQV YVQILQKMTG QKATANHAAE
LLAKRFRTQG SSQETTVLLV DELDLLWTQK QDVMYNLFDW PTHKEAQLVV LTIANTMDLP
ERIMMNRVSS RLGFTRMSFQ PYTYRQLQQI LMSRLKHLKA FEDDAIQLVA RKVAALSGDA
RRCLDICRRA TEICESSCQK PGSPGQVTVA HLLKAVDEMF SSAYITAIKN SSVMEQSFLR
AILAEFRRSG LEEATFQQVY RQHVELCRME GLPYPTMSET MAVCSHLGSC RLLPVCGSVV
EHPPMNQEVR VEFPIRAHAR VVGSIPSVGC AGGS
//
