ID A0A0V0VLE4_9BILA Unreviewed; 1328 AA.
AC A0A0V0VLE4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Origin recognition complex subunit 1 {ECO:0000313|EMBL:KRX64225.1};
GN ORFNames=T09_5948 {ECO:0000313|EMBL:KRX64225.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX64225.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX64225.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX64225.1};
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:KRX64225.1}.
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DR EMBL; JYDN01000025; KRX64225.1; -; 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; 2.
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; 3.
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 452..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1185..1212
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 460..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..832
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1328 AA; 151075 MW; DED05997D29933E6 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 DASIHLPYLR
ELNLSNNRIE KIDDWHLKLG NVKKIWLVNN RIKQLKGLAK LYSLEFLDLR DNQLSQIGHI
WPLGQLPCLH ELLVSGNTAE NMVDYRTRIL EAFGSRANEL RLDNEYPTQR ELDTVAVRLA
IREAKEDRRR QLLKVTEQIS RELNLAEAEV LNNSKQAGSE PKRTLKEMRR KEAEERLKME
KIKKAAEDKG PKSKASQKSP SEKSEKNTKK KSKSRSRSRS RSRSRDRSLN SSKKMDKSDT
KYNSGMISRE LSEHESKSRL KSAAAGQQRV LDAPLPTTTV QRRSRAVYGR KPDLDEADYP
LGRIEHTPSS AASSDLFPTN EKKKCPRNYC IPILTFEIMK LRSSRKISKC NTSFSYAEEK
NSDLCSVTSY DSLPALRRKN PERKCTVESS SDEEIGNSAC EPSSLNVKMQ SASFSKRNLT
IGKNISFSAD CYEFKTESSC NDFESDSDFV KKTTLKKEVD DKFPSCRRST RIRAGNSGLE
KCPTLHHANS SQVNGKVKNC KKLRSRKQIE EEDDDDYVED EVDDDDDDDS VDRADSAAAS
SCRTSPLKIK MLQFRGKNGR KNAPRALLNR RSTAQYCAIS DSDLESLESE SDFACKTKRV
RKINKKDNKY NKKSQTEEDY TPSNSRLKKG LQGRFHSAFD ELKARLHTSA VPANLPCREK
QCLEIENFVK CCLKSGNNGC LYISGVPGTG KTVAVRQAIR ALQNDNKLPA FVYCEINGMQ
LADPKNIYFK MAGSVFGSSW KSKSADKTQK MLNNFFNDSN PDKPHLIVLL DEVDYMIAGK
QRTLYQVFDW STLENSKLVL LTVANTLDFP ERILCKRITS RLGLTRLCFP SYSHAEIQKI
IEVRLSGCSA VSADAVQLVS RKVASVSGDI RRALEICRLA ADIASSECEN EKAELKRNVT
GQKRKQQQEQ KQQLTLEHIG LALKEMASNL KFAFIKNTSL HQQLVLRALV CLYNQTACDE
VSFRMINIQY KKICHDEDRE PLGVRELDRI LHIFVSVGIL VLGKQQLGYL DSYFRFAMNA
EDISASLQ
//
