ID A0A0V0RQ71_9BILA Unreviewed; 1421 AA.
AC A0A0V0RQ71;
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:KRX16594.1};
GN Name=NISCH {ECO:0000313|EMBL:KRX16594.1};
GN ORFNames=T07_2866 {ECO:0000313|EMBL:KRX16594.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX16594.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX16594.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX16594.1};
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:KRX16594.1}.
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DR EMBL; JYDL01000103; KRX16594.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0RQ71; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 533..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..124
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 508..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1278..1305
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 508..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..925
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 161806 MW; 4C777D6BF25BC925 CRC64;
MALFSCMNVE PLHKYCQITK FANKEDYIVY TVRVNVEDVS WTLDRRYSEF DAFDRAHVKF
PGFPSLPPKK VIGNQDVNFL NQRKVQLEKY INSVFIFDCM EQKAKGLASL PRLIASFLHF
NRYEIHSIID EIAIVHVGSD KNSDSFFEFS TLELHAVTER FKMAGSSFGC SPDFRFDFGQ
VAEFIANVKK LKISGNKCTG TSDIRLDSLR FDLMHFKSLE HLWICYCDAS NISGMEYIAA
NLSSLTVHNT LDRISELLSQ CGVDEERCEN LIPWPKVKSV DFSFNNLCHI DASITALRYV
HFLDLACNCL TDICNLQHLP YLRELNLSNN RIEKIDDWHL KLGNVKKIWL VNNRIKQLKG
LAKLYSLEFL DLRDNQLSQI GHIWPLGQLP CLHELLVSGN TAENMVDYRT RILEAFGSRA
NELRLDNEYP TQRELDTVAV RLAIREAKED RRRQLLKVTE QISRELNLAE AEVLNISKQA
GSSAYSEPKR TLKEMRRKEA EERLKMEKIK KAAEDKSPKS KASSKNTSEK SGSDNSICFV
FIASYSFFIH SFQEKNTKRK SKSRSRSRSR SRSRDRSQNS SKKIDKSDTK YNSGMISREL
SEHESKSPLK SAAGQQRVSD APLPTTTVQR RSRAVYGRKP DLDEADYPLG RIEHTPSSAV
LSDLLPTNDR KKFSRTYCMY ALFFIICCIV ASVLTFEIMK LRSSRKISKY STSCSYAEEK
NSDLCSDTSD DSLPALRRKN PERKRIYESS SDEEIGNNAC ELSSLNVKMR SASFSKRNLT
IGKNISFSAG CYEFKNELSC SDFESDSDFV KKTTLKKEVD DKFPSCRRST RIRAGHSGLE
KCPTSHHANS SQVNGKVKNC KNLRSRKQIE EDDDDDYVED EVDDDDDDYV EDEVDDDDDY
VEDEVDDDDD DYVEDEVDDD DDSVDRADSA AASSCRTSPL KIHMMQLRGK NGRKNAPRAS
LNRCSTAQYC AVSDSDLESL ESESDFACKT KRVRKINKKD NKYNKKSQTE EDYTPSNSRL
KKGFQGRFHS AFDELKARLH TSAVPANLPC REKQCLEIEN FVKCCLKSGN NGCLYISGVP
GTGKTVAVRQ AIRALQNDNK LPEFVYCEIN GMQLADPKNI YFKMAGSVFG SSWKSKSADK
TQKMLNNFFN DSNPDKPHLI ALLDEVDYMI AGKQRTLYQV FDWSTLENSK LILLTVANTL
DFPERILCKR ITSRLGLTRL CFPSYSHAEI QKIIEVRLSG CSAVSADAVQ LVSRKVASVS
GDIRRALEIC RLAADIASSE CENEKAELKR NVSGQKRKQQ QEQKQQLTLE HIGLALKEMA
SNLKFAFVKN TSLHQQLVLR ALVCLYNQTA CDEVSFRMIN IQYKKICHDE DKEPLGVREL
DRILHIFVSV GILVLGKQQL GYLDSYFRFA MNAEDISASL Q
//
