ID A0A1Y1JDX5_PLAGO Unreviewed; 914 AA.
AC A0A1Y1JDX5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=PGO_040170 {ECO:0000313|EMBL:GAW79417.1};
OS Plasmodium gonderi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW79417.1, ECO:0000313|Proteomes:UP000195521};
RN [1] {ECO:0000313|Proteomes:UP000195521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521};
RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.;
RT "Plasmodium gonderi genome.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036578}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116, ECO:0000256|PIRNR:PIRNR036578}.
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:GAW79417.1}.
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DR EMBL; BDQF01000004; GAW79417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1JDX5; -.
DR EnsemblProtists; GAW79417; GAW79417; PGO_040170.
DR OMA; LICNERN; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000195521; Unassembled WGS sequence.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd17748; BRCT_DNA_ligase_like; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF6; REPLICATION FACTOR C SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036578}; Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000195521}.
FT DOMAIN 192..281
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 104296 MW; 5F36B898113B3B58 CRC64;
MSSAEKKLFD DDSSSDGGRK RKRLKKVTTN LFDDSEDDND LFNKEEVSHT SQTHSVVEIK
DGTDEDDSYN SPKIMNNNPL SSKSTGKSMY HDITSYFKPN SKKMEDQTNS NGITNRNLKR
EREEDEDELM NQITYKKKHT LAGKKEKTKM EQDFNNSDNR SAEKKYSTTW STSSRNNNKG
GDLANNFDYL PFHNLKFVLT GVFKNFSRDE LQSKIKENGG SVMSAVSSRT HYLIHGEYLE
DGRLYNEGKK YQKAFELQQS SKSIIKILNE EQLLQMIPQE KNENLNGADN FDNAGGDASG
YNASFSKTEH YDSTKFKSEN DNNSSSSKSF HNYSTNAHEQ IGSTHQKKHL PNEQNNPGEE
KKILNQLWVE KYRPKNLNEL VGNNQNVLKL KNWLASWDDV CIKGLKKQVT KTFRGVFENV
NARCALLSGS AGIGKTTTAK IVAESSGYNV IEFNASDERN KAAVEKISEM ATGGYSIASI
KSRKLTKTCI IMDEVDGMSS GDKGGSAAIL KLIEKTKCPI ICICNDRQNN KMRTLANKCY
DLKFTTPNKN SVVKRLLEIC KKENVMMEPN ALELLWESTN GDMRQMLNAL QLLSKTYKKI
QFLDLKKELN NSNKNIQSLA NPFEITLKLL NFHESSKLKI RDIMDLFFVD YELIPFFISE
NYTNVFNDND KSANSITKWN AYSQISCDLV LAEKIKYNMK TNMDFSLLPH FSILSCVCPV
MRIKMLKSFM SGRINFPSAF GKISTFNKNK RLLNELCFNI SYKLNVCPKH MITSGFLNYI
YSKIIEPLAT NNIPKAIQMM EDYNITKEMI TENIPSLRLP TQENLYDKLD SKTKASFTRL
YNASHVIKND PNMLRKGFKT AEKKGLYKLN EYESDDDMDE LSESKEEKDD DDILVKTKVD
KKSAAKAKPK GKKR
//
