ID A0A0R3QSJ7_9BILA Unreviewed; 687 AA.
AC A0A0R3QSJ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Origin recognition complex subunit 1 {ECO:0000256|RuleBase:RU365058};
GN ORFNames=BTMF_LOCUS8731 {ECO:0000313|EMBL:VDO29239.1};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001069901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0001069901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO29239.1, ECO:0000313|Proteomes:UP000280834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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: ORC is composed of six subunits.
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; UZAG01016568; VDO29239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3QSJ7; -.
DR STRING; 42155.A0A0R3QSJ7; -.
DR WBParaSite; BTMF_0001069901-mRNA-1; BTMF_0001069901-mRNA-1; BTMF_0001069901.
DR Proteomes; UP000050602; Unplaced.
DR Proteomes; UP000280834; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 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; 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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365058};
KW DNA replication {ECO:0000256|RuleBase:RU365058};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU365058};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365058};
KW Nucleus {ECO:0000256|RuleBase:RU365058};
KW Reference proteome {ECO:0000313|Proteomes:UP000280834}.
FT DOMAIN 353..503
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 687 AA; 77769 MW; 59B7A3E50EBE69F1 CRC64;
MFINKNVLWD EKSENAISDS LMAKDEGNEN ISNKRILPKR KAKLMGRRYF EDLFVLNPPP
NKRSRSSLVL QQAKLVPVFN YDDNLNRFGL EKEDSDEDSE NIKSKDLDAS RISLPSTLPS
TVIDVSRTCK RRVSVASKIC KSKKSSIWKQ KIGTSDDGFS LHKSFKLSDK VDLVDGEVQK
SKSEKVDENL EKPFKRIDGL YSNHCKKPFI IVKRTKVFAG AKFINDKHSS LGQGSEDNDG
GKDFEFSGIL ENLTELDSHS GTNSNIHSEK NLKIRRQYNS VCKSRRLIAE KKSTDQYATC
GIISNVCAIR VETLEAVYRR LHTSEIPERL PCREAEFDRI CAFIKGCVTN DAISQAMYVS
GVPGTGKTAT VLQAVRYLKA SENFSGFNFV AVNAMELSDP KQIFVKIYQD LFSLKKKIAP
KTARKKLNHI FQYHDKKRLP IIVLVDELDL LNTKRQEIIY DIFNWSANEE SLVSVIAIAN
TLDLPERLFS QRVSSRLGAN RLCFQPYDHD EVAYIIRDRL RNSTAVEAEA IELASRKVAA
ISGDLRKALD ILRSATELAI NANQKQLTMK NVQEAIRQAS TSVRVELIRA LPRHSILLLR
AALAEQLSSG LDEFQFHLLF KQYRLQCNVA NINPMSTSST YRNAMEMCSE RLLIAASGTG
SMSRRFRLGM TTHDIQFAFK QVDESVF
//