ID   RFCS_THEKO              Reviewed;         866 AA.
AC   Q5JHP2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Replication factor C small subunit;
DE            Short=RFC small subunit;
DE   AltName: Full=Clamp loader small subunit;
DE   Contains:
DE     RecName: Full=Pko RFC intein;
GN   Name=rfcS; OrderedLocusNames=TK2218;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-6, AND FUNCTION.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=14646196; DOI=10.1271/bbb.67.2373;
RA   Kitabayashi M., Nishiya Y., Esaka M., Itakura M., Imanaka T.;
RT   "Gene cloning and function analysis of replication factor C from
RT   Thermococcus kodakaraensis KOD1.";
RL   Biosci. Biotechnol. Biochem. 67:2373-2380(2003).
CC   -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC       sliding clamp onto DNA. {ECO:0000305|PubMed:14646196}.
CC   -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and large
CC       subunits (RfcL). {ECO:0000250}.
CC   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The intein interrupts the potential ATP-binding site.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP006878; BAD86407.1; -; Genomic_DNA.
DR   RefSeq; WP_011251168.1; NC_006624.1.
DR   AlphaFoldDB; Q5JHP2; -.
DR   SMR; Q5JHP2; -.
DR   STRING; 69014.TK2218; -.
DR   EnsemblBacteria; BAD86407; BAD86407; TK2218.
DR   GeneID; 78448758; -.
DR   KEGG; tko:TK2218; -.
DR   PATRIC; fig|69014.16.peg.2174; -.
DR   eggNOG; arCOG00469; Archaea.
DR   eggNOG; arCOG03154; Archaea.
DR   HOGENOM; CLU_015698_0_0_2; -.
DR   InParanoid; Q5JHP2; -.
DR   OrthoDB; 7928at2157; -.
DR   PhylomeDB; Q5JHP2; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd00081; Hint; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   InterPro; IPR047854; RFC_lid.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF5; REPLICATION FACTOR C SUBUNIT 2; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   Pfam; PF14890; Intein_splicing; 1.
DR   Pfam; PF14528; LAGLIDADG_3; 2.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF55608; Homing endonucleases; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Autocatalytic cleavage; Direct protein sequencing;
KW   DNA replication; Nucleotide-binding; Protein splicing; Reference proteome.
FT   CHAIN           1..59
FT                   /note="Replication factor C small subunit, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030382"
FT   CHAIN           60..599
FT                   /note="Pko RFC intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030383"
FT   CHAIN           600..866
FT                   /note="Replication factor C small subunit, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030384"
FT   DOMAIN          183..313
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
SQ   SEQUENCE   866 AA;  99691 MW;  0E9386BB07638F0D CRC64;
     MSEEVKEVKI LEKPWVEKYR PQRLEDIVGQ DHIVKRLKHY VKTGSMPHLL FAGPPGVGKC
     LTGDAKVIAN GRLFELGELV EKVSKGRFGP TPVEGLKVLG IDEDGKLREF EVQYVYKDRA
     ERLIKVRTRL GRELKVTPYH PLLVNRKNGE IMWVKAEELR PGDRLAVPRF LPAIAEEDPL
     AEWLGYFIGD GHADSKNKVI TFTNTDPSLR QRFMELTERL FPDAKIRERI HKNRAPDVYV
     NSRRAWELVS SLGLAGRKAD KVYIPEKGWE GIRSFLRAYF DCDAGVDKNA VVLATASREM
     AEQVTYALAG FGITSKIREK KVRGKTYYHV TISGSENLER FLSEIGFSHR EKLERTLKLV
     KKPNPNLDSL NVNYELISYV RDRLKLNFSD DKRSWSHRKA RKISWELMKE IYYRLDELER
     LKESLSRSIL IDWNEMAERR KEIAEKTGIR ADRLLEYIKG KRKPSLRNYI KIAKALGIDL
     EPTINAMRVF ARKYSSYAEI GRKLGTWNSS VRIILESNTE KIKELEEIRK IELELIGEIL
     SDEKLKEGVA YLIFLSQNEL YWDEITEVKE LKGDFVIYDL HVPGYHNFIA GNMPTVVHNT
     TAALALAREL FGENWRHNFL ELNASDERGI NVIREKVKEF ARTKPIGGAS FKIIFLDEAD
     ALTQDAQQAL RRTMEMFSNN VRFILSCNYS SKIIEPIQSR CAIFRFRPLR DEDIAKRIRY
     IAENEGLELT EEGLQAILYV AEGDLRRAIN VLQAAAALDT KITDENVFLV ASRARPEDVR
     EMMTLALEGN FLKAREKLRD ILLRQGLSGE DVLIQMHKEV FNLPIPEDKK VALADKIGEY
     NFRLVEGANE MIQLEALLAQ FTIMGK
//