ID A0A0V0VL30_9BILA Unreviewed; 1351 AA.
AC A0A0V0VL30;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Origin recognition complex subunit 1 {ECO:0000313|EMBL:KRX64226.1};
GN ORFNames=T09_5948 {ECO:0000313|EMBL:KRX64226.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX64226.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX64226.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX64226.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ORC1 family.
CC {ECO:0000256|ARBA:ARBA00008398}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX64226.1}.
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DR EMBL; JYDN01000025; KRX64226.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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; PF13855; LRR_8; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00365; LRR_SD22; 3.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681}.
FT DOMAIN 8..124
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 475..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1208..1235
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 483..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..855
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1351 AA; 153697 MW; 03AD1D5628E9FEFB CRC64;
MALFSCMNVE PLHKYCQITK FANKEDYIVY TVRVNVEDVS WTLDRRYSEF DAFDRAHVKF
PGFPSLPPKK VIGNQDVNFL NQRKVQLEKY INSVFIFDCM EQKAKGLASL PRLIASFLHF
NRYEIHSIID EIAIVHVGSD KNSDSFFEFS TLELHAVTER FKMAGSSFGC SPDFRFDFGQ
VAEFIANVKK LKISGNKCTG TSDIRLDKLR FDLMHFKSLE HLWICYCDAS NISGMEFIAA
NLSSLTVHNT LDRISELLSQ CGVDEERCEN LIPWPKVKSV DFSFNNLCHI DASITALRYV
HFLDLACNCL TDICNLQHLP YLRELNLSNN RIEKIDDWHL KLGNVKKIWL VNNRIKQLKG
LAKLYSLEFL DLRDNQLSQI GHIWPLGQLP CLHELLVSGN TAENMVDYRT RILEAFGSRA
NELRLDNEYP TQRELDTVAV RLAIREAKED RRRQLLKVTE QISRELNLAE AEVLNNSKQA
GSEPKRTLKE MRRKEAEERL KMEKIKKAAE DKGPKSKASQ KSPSEKSEKN TKKKSKSRSR
SRSRSRSRDR SLNSSKKMDK SDTKYNSGMI SRELSEHESK SRLKSAAAGQ QRVLDAPLPT
TTVQRRSRAV YGRKPDLDEA DYPLGRIEHT PSSAASSDLF PTNEKKKCPR NYCIPILTFE
IMKLRSSRKI SKCNTSFSYA EEKNSDLCSV TSYDSLPALR RKNPERKCTV ESSSDEEIGN
SACEPSSLNV KMQSASFSKR NLTIGKNISF SADCYEFKTE SSCNDFESDS DFVKKTTLKK
EVDDKFPSCR RSTRIRAGNS GLEKCPTLHH ANSSQVNGKV KNCKKLRSRK QIEEEDDDDY
VEDEVDDDDD DDSVDRADSA AASSCRTSPL KIKMLQFRGK NGRKNAPRAL LNRRSTAQYC
AISDSDLESL ESESDFACKT KRVRKINKKD NKYNKKSQTE EDYTPSNSRL KKGLQGRFHS
AFDELKARLH TSAVPANLPC REKQCLEIEN FVKCCLKSGN NGCLYISGVP GTGKTVAVRQ
AIRALQNDNK LPAFVYCEIN GMQLADPKNI YFKMAGSVFG SSWKSKSADK TQKMLNNFFN
DSNPDKPHLI VLLDEVDYMI AGKQRTLYQV FDWSTLENSK LVLLTVANTL DFPERILCKR
ITSRLGLTRL CFPSYSHAEI QKIIEVRLSG CSAVSADAVQ LVSRKVASVS GDIRRALEIC
RLAADIASSE CENEKAELKR NVTGQKRKQQ QEQKQQLTLE HIGLALKEMA SNLKFAFIKN
TSLHQQLVLR ALVCLYNQTA CDEVSFRMIN IQYKKICHDE DREPLGVREL DRILHIFVSV
GILVLGKQQL GYLDSYFRFA MNAEDISASL Q
//
