RFCS_PYRFU
ID RFCS_PYRFU Reviewed; 852 AA.
AC Q8U4J3; Q9P9H2; Q9P9H3;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Replication factor C small subunit;
DE Short=RFC small subunit;
DE AltName: Full=Clamp loader small subunit;
DE AltName: Full=PfuRFC small subunit;
DE Contains:
DE RecName: Full=Pfu RFC intein;
GN Name=rfcS; OrderedLocusNames=PF0093;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59 AND 585-852, PROTEIN SEQUENCE OF
RP 2-9, FUNCTION, INTEIN SPLICING, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=11274122; DOI=10.1128/jb.183.8.2614-2623.2001;
RA Cann I.K.O., Ishino S., Yuasa M., Daiyasu H., Toh H., Ishino Y.;
RT "Biochemical analysis of replication factor C from the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL J. Bacteriol. 183:2614-2623(2001).
RN [3]
RP ELECTRON MICROSCOPY.
RX PubMed=11469875; DOI=10.1006/jsbi.2001.4357;
RA Mayanagi K., Miyata T., Oyama T., Ishino Y., Morikawa K.;
RT "Three-dimensional electron microscopy of the clamp loader small subunit
RT from Pyrococcus furiosus.";
RL J. Struct. Biol. 134:35-45(2001).
RN [4]
RP FUNCTION.
RX PubMed=12296822; DOI=10.1046/j.1365-2443.2002.00572.x;
RA Matsumiya S., Ishino S., Ishino Y., Morikawa K.;
RT "Physical interaction between proliferating cell nuclear antigen and
RT replication factor C from Pyrococcus furiosus.";
RL Genes Cells 7:911-922(2002).
RN [5]
RP MUTAGENESIS OF GLU-785; GLU-795; ASP-796; GLU-831 AND GLU-835.
RX PubMed=12768447; DOI=10.1007/s00792-002-0308-1;
RA Ishino S., Oyama T., Yuasa M., Morikawa K., Ishino Y.;
RT "Mutational analysis of Pyrococcus furiosus replication factor C based on
RT the three-dimensional structure.";
RL Extremophiles 7:169-175(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=11545747; DOI=10.1016/s1097-2765(01)00328-8;
RA Oyama T., Ishino Y., Cann I.K.O., Ishino S., Morikawa K.;
RT "Atomic structure of the clamp loader small subunit from Pyrococcus
RT furiosus.";
RL Mol. Cell 8:455-463(2001).
CC -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC sliding clamp onto DNA. The complex possesses DNA-dependent ATPase
CC activity which is further stimulated by PCNA.
CC {ECO:0000269|PubMed:11274122, ECO:0000269|PubMed:12296822}.
CC -!- SUBUNIT: Heteromultimer composed of three to four small subunits (RfcS)
CC and one to two large subunits (RfcL). {ECO:0000269|PubMed:11274122}.
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; AE009950; AAL80217.1; -; Genomic_DNA.
DR EMBL; AB037375; BAB03291.1; -; Genomic_DNA.
DR EMBL; AB037375; BAB03292.1; -; Genomic_DNA.
DR RefSeq; WP_011011205.1; NZ_CP023154.1.
DR PDB; 1IQP; X-ray; 2.80 A; A/B/C/D/E/F=1-59, A/B/C/D/E/F=585-852.
DR PDBsum; 1IQP; -.
DR AlphaFoldDB; Q8U4J3; -.
DR SMR; Q8U4J3; -.
DR STRING; 186497.PF0093; -.
DR PRIDE; Q8U4J3; -.
DR EnsemblBacteria; AAL80217; AAL80217; PF0093.
DR GeneID; 41711880; -.
DR KEGG; pfu:PF0093; -.
DR PATRIC; fig|186497.12.peg.97; -.
DR eggNOG; arCOG00469; Archaea.
DR eggNOG; arCOG03154; Archaea.
DR HOGENOM; CLU_015698_0_0_2; -.
DR OMA; QFADNTR; -.
DR OrthoDB; 37207at2157; -.
DR PhylomeDB; Q8U4J3; -.
DR EvolutionaryTrace; Q8U4J3; -.
DR Proteomes; UP000001013; 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 Gene3D; 3.10.28.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003959; ATPase_AAA_core.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR InterPro; IPR008824; RuvB-like_N.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR Pfam; PF05496; RuvB_N; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 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 3D-structure; ATP-binding; Autocatalytic cleavage;
KW Direct protein sequencing; DNA replication; Nucleotide-binding;
KW Protein splicing; Reference proteome.
FT CHAIN 1..59
FT /note="Replication factor C small subunit, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030376"
FT CHAIN 60..584
FT /note="Pfu RFC intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030377"
FT CHAIN 585..852
FT /note="Replication factor C small subunit, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030378"
FT DOMAIN 183..306
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT MUTAGEN 785
FT /note="E->A: Decreases the stability of the PCNA-RFC
FT complex and reduces the clamp-loading activity; when
FT associated with A-795; A-796; A-831 and A-835."
FT /evidence="ECO:0000269|PubMed:12768447"
FT MUTAGEN 795
FT /note="E->A: Decreases the stability of the PCNA-RFC
FT complex and reduces the clamp-loading activity; when
FT associated with A-785; A-796; A-831 and A-835."
FT /evidence="ECO:0000269|PubMed:12768447"
FT MUTAGEN 796
FT /note="D->A: Decreases the stability of the PCNA-RFC
FT complex and reduces the clamp-loading activity; when
FT associated with A-785; A-795; A-831 and A-835."
FT /evidence="ECO:0000269|PubMed:12768447"
FT MUTAGEN 831
FT /note="E->A: Decreases the stability of the PCNA-RFC
FT complex and reduces the clamp-loading activity; when
FT associated with A-785; A-795; A-796 and A-835."
FT /evidence="ECO:0000269|PubMed:12768447"
FT MUTAGEN 835
FT /note="E->A: Decreases the stability of the PCNA-RFC
FT complex and reduces the clamp-loading activity; when
FT associated with A-785; A-795; A-796 and A-831."
FT /evidence="ECO:0000269|PubMed:12768447"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 565..575
FT /evidence="ECO:0007829|PDB:1IQP"
FT STRAND 580..583
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 584..596
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 600..603
FT /evidence="ECO:0007829|PDB:1IQP"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 612..616
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 619..627
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:1IQP"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 649..661
FT /evidence="ECO:0007829|PDB:1IQP"
FT TURN 662..665
FT /evidence="ECO:0007829|PDB:1IQP"
FT STRAND 666..673
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 680..684
FT /evidence="ECO:0007829|PDB:1IQP"
FT STRAND 686..690
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 696..708
FT /evidence="ECO:0007829|PDB:1IQP"
FT TURN 709..711
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 716..726
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 730..741
FT /evidence="ECO:0007829|PDB:1IQP"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 749..755
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 761..773
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 776..790
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 794..804
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 805..807
FT /evidence="ECO:0007829|PDB:1IQP"
FT STRAND 808..810
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 812..830
FT /evidence="ECO:0007829|PDB:1IQP"
FT HELIX 835..850
FT /evidence="ECO:0007829|PDB:1IQP"
SQ SEQUENCE 852 AA; 97793 MW; D4C8B4B945F9946A CRC64;
MSEEIREVKV LEKPWVEKYR PQRLDDIVGQ EHIVKRLKHY VKTGSMPHLL FAGPPGVGKC
LTGDTKVIAN GQLFELGELV EKLSGGRFGP TPVKGLKVLG IDEDGKLREF EVQYVYKDRT
DRLIKIKTQL GRELKVTPYH PLLVNRENGE IKWIKAEELK PGDKLAIPSF LPLITGENPL
AEWLGYFMGS GYAYPSNSVI TFTNEDPLIR QRFMELTEKL FPDAKIRERI HADGTPEVYV
VSRKAWSLVN SISLTLIPRE GWKGIRSFLR AYSDCNGRIE SDAIVLSTDN NDMAQQIAYA
LASFGIIAKM DGEDVIISGS DNIERFLNEI GFSTQSKLKE AQKLIRKTNV RSDGLKINYE
LISYVKDRLR LNVNDKRNLS YRNAKELSWE LMKEIYYRLE ELERLKKVLS EPILIDWNEV
AKKSDEVIEK AKIRAEKLLE YIKGERKPSF KEYIEIAKVL GINVERTIEA MKIFAKRYSS
YAEIGRKLGT WNFNVKTILE SDTVDNVEIL EKIRKIELEL IEEILSDGKL KEGIAYLIFL
FQNELYWDEI TEVKELRGDF IIYDLHVPGY HNFIAGNMPT VVHNTTAALA LARELFGENW
RHNFLELNAS DERGINVIRE KVKEFARTKP IGGASFKIIF LDEADALTQD AQQALRRTME
MFSSNVRFIL SCNYSSKIIE PIQSRCAIFR FRPLRDEDIA KRLRYIAENE GLELTEEGLQ
AILYIAEGDM RRAINILQAA AALDKKITDE NVFMVASRAR PEDIREMMLL ALKGNFLKAR
EKLREILLKQ GLSGEDVLVQ MHKEVFNLPI EEPKKVLLAD KIGEYNFRLV EGANEIIQLE
ALLAQFTLIG KK
