ID   RFCS_PYRAB              Reviewed;        1437 AA.
AC   Q9V2G4; G8ZFU5;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Replication factor C small subunit;
DE            Short=RFC small subunit;
DE   AltName: Full=Clamp loader small subunit;
DE   AltName: Full=PabRFC small subunit;
DE   Contains:
DE     RecName: Full=Pab RFC-1 intein;
DE   Contains:
DE     RecName: Full=Pab RFC-2 intein;
GN   Name=rfcS; OrderedLocusNames=PYRAB01100; ORFNames=PAB0068;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, AND SUBUNIT.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12417194; DOI=10.1016/s0022-2836(02)01028-8;
RA   Henneke G., Gueguen Y., Flament D., Azam P., Querellou J., Dietrich J.,
RA   Huebscher U., Raffin J.-P.;
RT   "Replication factor C from the hyperthermophilic archaeon Pyrococcus abyssi
RT   does not need ATP hydrolysis for clamp-loading and contains a functionally
RT   conserved RFC PCNA-binding domain.";
RL   J. Mol. Biol. 323:795-810(2002).
CC   -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC       sliding clamp onto DNA. The complex possesses DNA-independent ATPase
CC       activity. {ECO:0000269|PubMed:12417194}.
CC   -!- SUBUNIT: Heterohexamer composed of four small subunits (RfcS) and two
CC       large subunits (RfcL). {ECO:0000305|PubMed:12417194}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCE69486.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ248283; CAB49034.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69486.1; ALT_INIT; Genomic_DNA.
DR   PIR; C75198; C75198.
DR   AlphaFoldDB; Q9V2G4; -.
DR   SMR; Q9V2G4; -.
DR   IntAct; Q9V2G4; 1.
DR   MINT; Q9V2G4; -.
DR   STRING; 272844.PAB0068; -.
DR   KEGG; pab:PAB0068; -.
DR   PATRIC; fig|272844.11.peg.123; -.
DR   eggNOG; arCOG00469; Archaea.
DR   eggNOG; arCOG03154; Archaea.
DR   eggNOG; arCOG03158; Archaea.
DR   HOGENOM; CLU_002046_0_0_2; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd00081; Hint; 2.
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; 4.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 2.
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   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR01443; intein_Cterm; 2.
DR   NCBIfam; TIGR01445; intein_Nterm; 2.
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; 2.
DR   Pfam; PF14528; LAGLIDADG_3; 2.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 2.
DR   SMART; SM00306; HintN; 2.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR   SUPFAM; SSF55608; Homing endonucleases; 2.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 2.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR   PROSITE; PS50817; INTEIN_N_TER; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Autocatalytic cleavage; Direct protein sequencing;
KW   DNA replication; Nucleotide-binding; Protein splicing; Repeat.
FT   CHAIN           1..61
FT                   /note="Replication factor C small subunit, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030371"
FT   CHAIN           62..560
FT                   /note="Pab RFC-1 intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030372"
FT   CHAIN           561..647
FT                   /note="Replication factor C small subunit, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030373"
FT   CHAIN           648..1255
FT                   /note="Pab RFC-2 intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030374"
FT   CHAIN           1256..1437
FT                   /note="Replication factor C small subunit, 3rd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030375"
FT   DOMAIN          185..301
FT                   /note="DOD-type homing endonuclease 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   DOMAIN          940..1098
FT                   /note="DOD-type homing endonuclease 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
SQ   SEQUENCE   1437 AA;  165246 MW;  9725AC4F4240C985 CRC64;
     MRDMEEVREV KVLEKPWVEK YRPQKLEEIV GQEHIVKRLK HYVKTGSMPH LLFAGPPGVG
     KCLTGDAKVI ANGELTTIGE LVERISNGKL GPTPVRGLTV LGIDEDGKLV ELPVEYVYKD
     KTSELVKIRT RLGRELKVTP YHPLLVNRRN GKIEWVKAEE LKPGDRLAIP SFLPAMLNDN
     PLAEWLGYFF GNGYTDSEER VVFESKSKEL RKRFMELTRK LFQDAEIKED SGKVYVSSSE
     VKRLVKSLNK DSIPEQAWKG LRSFLRAYFD CNAEIKDKII VSTAGKEIAE QISYALAGLG
     IVAEVDDKGS VIISDPENVS RFLDEIGFSV EEKKEEAKAL IKKSTLNLGI YVDKELISYV
     REKLKLSFYE NETMWSPEKA REIAWKLMKE IYYRLDELER FKKALSKSVI IDWSEVEKKK
     EEISEKTGIS VNEILEYAKG KRKPSLEEYV KIAKALGVEL KETLEAIFTF GKKYLGYVIS
     DEIETLEEVR KEELKRLKEL LNDEKLKKGV AYLIFLAQNE LLWDEIIEVE KLKGDFVIYD
     LHVPKYHNFI GGNLPTVLHN TTAALALARE LFGENWRHNF LELNASDERG INVIREKVKE
     FARTKPIGGA SFKIIFLDEA DALTQDAQQA LRRTMEMFSS NVRFILSCVT GDTKVYTPDE
     REVKIRDFMN YFENGLIKEV SNRIGRDTVI AAVSFNSRIV GHPVYRLTLE SGRIIEATGD
     HMFLTPEGWK QTYDIKEGSE VLVKPTLEGT PYEPDPRVII DIKEFYNFLE KIEREHNLKP
     LKEAKTFREL ITKDKEKILR RALELRAEIE NGLTKREAEI LELISADTWI PRAELEKKAR
     ISRTRLNQIL QRLEKKGYIE RRIEGRKQFV RKIRNGKILR NAMDIKRILE EEFGIKISYT
     TVKKLLSGNV DGMAYRILKE VKEKWLVRYD DEKAGILARV VGFILGDGHL ARNGRIWFNS
     SKEELEMLAN DLRKLGLKPS EIIERDSSSE IQGRKVKGRI YMLYVDNAAF HALLRFWKVE
     VGNKTKKGYT VPEWIKKGNL FVKREFLRGL FGADGTKPCG KRYNFNGIKL EIRAKKESLE
     RTVEFLNDVA DLLREFDVDS KITVSPTKEG FIIRLIVTPN DANYLNFLTR VGYAYAKDTY
     ARLVGEYIRI KLAYKNIILP GIAEKAIELA TVTNSTYAAK VLGVSRDFVV NRLKGTQIGI
     TRDFMTFEEF MKERVLNGYV IEKVIKKEKL GYLDVYDVTC ARDHSFISNG LVSHNCNYSS
     KIIEPIQSRC AIFRFRPLND EDIAKRLRYI AENEGLELTE EGLQAILYIA EGDMRRAINI
     LQAAAALDRK ITDENVFLVA SRARPEDIRE MMLLALKGNF LKAREKLREI LLKQGLSGED
     VLVQMHREVF NLPIDEPMKV YLADKIGEYN FRLVEGANEM IQLEALLAQF TLIGKKK
//