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Database: UniProt
Entry: G3ST10_LOXAF
LinkDB: G3ST10_LOXAF
Original site: G3ST10_LOXAF 
ID   G3ST10_LOXAF            Unreviewed;       855 AA.
AC   G3ST10;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|ARBA:ARBA00019081, ECO:0000256|RuleBase:RU365058};
GN   Name=ORC1 {ECO:0000313|Ensembl:ENSLAFP00000003139.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003139.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000003139.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003139.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000003139.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003139.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; G3ST10; -.
DR   STRING; 9785.ENSLAFP00000003139; -.
DR   Ensembl; ENSLAFT00000003759.3; ENSLAFP00000003139.3; ENSLAFG00000003758.3.
DR   eggNOG; KOG1514; Eukaryota.
DR   GeneTree; ENSGT00530000063498; -.
DR   HOGENOM; CLU_012774_0_1_1; -.
DR   InParanoid; G3ST10; -.
DR   OMA; CKQHLLG; -.
DR   TreeFam; TF313743; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0005664; C:nuclear origin of replication recognition complex; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0006270; P:DNA replication initiation; IEA:Ensembl.
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   SMART; SM01074; Cdc6_C; 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:UP000007646}.
FT   DOMAIN          45..171
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          213..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..425
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..452
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   855 AA;  96558 MW;  7C799DF3CA4F1F7D CRC64;
     MASYTTRLKT RQTYSWVGRP LLDRKLHYQT YNEMCVKIEG CSTQIHIQVG QFVLIAGDCE
     QYPYVAKLIE LFEDDSEPYS KKRARVQWCV RFCEVPVRKQ HLLGRKPAAQ EIFWYDYPAC
     DGNINAEAII GPVRVVALAP DEAIPVDLKN EKTLFMKLSW NEKKFRPLSP ELLANLDKLR
     ESSPRCQKPV GTKTRSIESL PWTTAEQVVR SIESRHSASK SCQTPTHSVT PRARKRLELN
     SLGLPRTPDS STSRQNACAS LGSPGRTKRK VAFSEVTSPC KRPQPDELQT SSPALKSPCT
     KDNKKCSPEC HMTLRTRVPV LKATEITEHK TLSPISGGRK SLVVSDVVLK PENIKKRKVE
     EPEAQNEATS TPHRVNRKSS TLALNRIRQQ LQFLGNNKNE QEEEEFLPAA EISDSSREEE
     EVSTPPFSRA HSSVPRSRCS SMKSSFQTPS KTPKKTPKRR TPCQVTPQIR SRSLAAQEPA
     SALEEARLRL HVSAVPESLP CREREFQDIY NFVESKLLDR TGGCMYISGV PGTGKTATVH
     EVTRCLQQAA QANDVPPFQY VEVNGMKLTE PHQVYVQILQ KLTGQKATAN HAAQLLAKRF
     CTRGSPQETT VLLVDELDLL WTQKQDVMYN LFDWPTHKEA RLVVLTIANT MDLPERIMMN
     RVASRLGLTR MSFQPYTHSQ LQQILMSRLK HVKVFEDDAI QLVARKVAAL SGDARRCLDI
     CRRATEICEL SPQKPDSPGL VTVAHLMEAV DEMFSSSYIT AIKNSSVLEQ GFLRAILAEF
     RRTGLEEATF QQVYSQHVVL CRMEGLPYPT MSETMVCSRL GSCRLLLVEP SRNDLLLRVR
     LNVSQDDVLY ALKEE
//
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