ID A0A0V1L6A9_9BILA Unreviewed; 1347 AA.
AC A0A0V1L6A9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Origin recognition complex subunit 1 {ECO:0000313|EMBL:KRZ55081.1};
GN Name=ORC1 {ECO:0000313|EMBL:KRZ55081.1};
GN ORFNames=T02_4521 {ECO:0000313|EMBL:KRZ55081.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ55081.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ55081.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ55081.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ55081.1}.
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DR EMBL; JYDW01000123; KRZ55081.1; -; Genomic_DNA.
DR Proteomes; UP000054721; 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; 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; 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:UP000054721}.
FT DOMAIN 8..124
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 504..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1204..1231
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 504..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 837..856
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1347 AA; 153432 MW; 38026DD46EC213F4 CRC64;
MALFSCMNVE PLHKYCQITK FANKEDYIVY TVRVNVEDVS WTLDRRYSEF DAFDRAHVKF
PGFPSLPPKK VIGNQDVNFL NQRKVQLEKY INSVFIFDCM EQKAKGLASL PRLIASFLHF
NRYEIHSIID EIAIVHVGSD KNSDSFFEFS TLELHAVTER FKMAGSSFGC SPDFRFDFGQ
VAEFIANVKK LKISGNKCTG TSDIRLDSLR 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 AEVLNISKQA
GSEPKRTLKE MRRKEAEERL KMEKIEKAAE DKGPKSKASQ KKTSEKSEKN TKKKSKSRSR
SRSRSRSRDR SVNSSEKMHK SDTKYNSGMI SRELSEHESK SRLKSAPAGQ QRVLDAPLPT
TTVQRRSRAV YGRKPDLDEA DYPLGRTEHT PSNAASSDLF PTNEKKKCPR NYCIPILTFE
IMKLRSRRII SKCNTSFSYA EEKNSDLCSV TSDDSLPALR RKNLARKCTV VSSSDEEIEN
SACEPSSLNI KMRSALFSKR NLTIEKNISF SADCYEFKTE SSCSDFESDS DFVKKTTLKK
EVDDKFPSCR RSTRIRAGNS GLEKCPTLHH ANSSHINGKV KNCKKLRSRK QIKEEDDDDY
VEDEVDDDDD DDSVDSADSA AASSCRTSPF KIKMLQFRGK NAPRASLNRR STAQYCATSD
SDLESLESES DFACKTKRVR KINKKDNKYN KKSQTEEDYT PSNSRLKKGF QGRFHSAFDE
LKARLHTSAV PANLPCREKQ CLEIENFVKC CLKSGNNGCL YISGVPGTGK TVAVRQAIRA
LQNDNKLPEF VYCEINGMQL ADPKNIYFKM AGSVFGSSWK SKSADKTQKM LNNFFNDSNP
DKPHLIALLD EVDYMIAGKQ RTLYQVFDWS TLENSKLVLL AVANTLDFPE RILCKRITSR
FGLTRICFPS YSHAEIQKII EVRLSGCSAV SADAVQLVSR KVASVSGDIR RALEICRLAA
DIASSECENE KAELKRNVTG QKRKQQQEQK QQLTLEHIGL ALKEMASNLK FAFIKNTSLH
QQLVLRALVC LYNQTACDEV SFRMINIQYK KICHDEDREP LGVRELDRIL HIFVSVGILV
LGKQQLGYLD SYFRFAMNAE DISASLQ
//
