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Database: UniProt
Entry: R9ABX5_WALI9
LinkDB: R9ABX5_WALI9
Original site: R9ABX5_WALI9 
ID   R9ABX5_WALI9            Unreviewed;       765 AA.
AC   R9ABX5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401};
GN   ORFNames=J056_001669 {ECO:0000313|EMBL:EOQ99584.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ99584.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
CC   -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC       {ECO:0000256|ARBA:ARBA00006116}.
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DR   EMBL; KE007240; EOQ99584.1; -; Genomic_DNA.
DR   RefSeq; XP_009269572.1; XM_009271297.1.
DR   AlphaFoldDB; R9ABX5; -.
DR   STRING; 1299270.R9ABX5; -.
DR   GeneID; 20374621; -.
DR   KEGG; wic:J056_001669; -.
DR   eggNOG; KOG1968; Eukaryota.
DR   HOGENOM; CLU_003574_1_0_1; -.
DR   OMA; LICNERN; -.
DR   OrthoDB; 6297at2759; -.
DR   Proteomes; UP000014064; Unassembled WGS sequence.
DR   GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR   CDD; cd00009; AAA; 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:SF37; 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};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014064}.
FT   DOMAIN          65..155
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..735
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  84542 MW;  CE90BB5056DEF547 CRC64;
     MAPKRKTVVI SDSDEDVPPP KQKNSPQKKS KSSASSSAPA SSFSYKDYLQ RPGPESLGSK
     SIPEGAPGCL SGLTLVFTGE LDNVGRDSAV EAAKRYGAKV TAAPSGKTSY VILGREPGPK
     KLQTIQDKGL KTLDEDGFCN LIATTSPSQD PSYLNKVKKD EAKVKKDAEE MEAIEKEQKA
     KDKRSSKASS FESTSPNSQL WTVKYAPTQL KDICGNKGQV EKILNWLQNW QHQLQAGFPS
     DNSKNDIKSK RALLVHGAPG IGKTTAAHLA AKIAGFSPLE LNASDVRSKK LIENTTNIDN
     TSIDSFFGSN SETHPLNHST CLIFDECDGM SSGDRGGVGA MNTLIRKTRI PIICICNDKA
     NPKMRPFQST CGDIVFRRPE ATQVRSRIMS ILHREKMKLD PVVVDQLVSG SQSDIRQVIN
     MISTWKLLSS SMNFDQGKEL VQQNQKFTIQ TPWTVMSNLF SPHMFGATST STLGSKADYY
     FHDHSLIPLF VQENYVKCNP AKARDSNNEK AEFKRMKYAS KAADAISDGD LVDSMIHGSQ
     QQWGLMPLHA MNSTVRPASF MYGGFKSFGR DTISFPMWLG QYSKTNKNIR ALGEIQAKMR
     VKVSGDRDEI RQYYYPTLWP RMFNPLTESV PDIDSVINLL DNYMLSKDDF DVMSELGVGD
     LALEKTVKCI PTKNKTAFTR NYNNRDHPIA FSRGQVIKPS AAQIKAEVPD HEDVLDDEDD
     NVVDVKEEED DENDDVTADK LVKQPKKPAA SKRGKASASR GKGSK
//
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