RFCS_PYRAB
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 25-MAY-2022, entry version 124.
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 PRIDE; Q9V2G4; -.
DR EnsemblBacteria; CAB49034; CAB49034; 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 OMA; VSHNCNY; -.
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:0009378; F:four-way junction helicase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; 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; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR Gene3D; 3.10.28.10; -; 2.
DR Gene3D; 3.40.50.300; -; 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; IPR008824; RuvB-like_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR Pfam; PF08542; Rep_fac_C; 1.
DR Pfam; PF05496; RuvB_N; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF51294; SSF51294; 2.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF55608; SSF55608; 2.
DR TIGRFAMs; TIGR01443; intein_Cterm; 2.
DR TIGRFAMs; TIGR01445; intein_Nterm; 2.
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