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Replication factor C small subunit (RFC small subunit) (Clamp loader small subunit) (PfuRFC small subunit) [Cleaved into: Pfu RFC intein]

 RFCS_PYRFU              Reviewed;         852 AA.
Q8U4J3; Q9P9H2; Q9P9H3;
16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 108.
RecName: Full=Replication factor C small subunit;
Short=RFC small subunit;
AltName: Full=Clamp loader small subunit;
AltName: Full=PfuRFC small subunit;
Contains:
RecName: Full=Pfu RFC intein;
Name=rfcS; OrderedLocusNames=PF0093;
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=186497;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=10430560;
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
DiRuggiero J., Robb F.T.;
"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and
P. horikoshii inferred from complete genomic sequences.";
Genetics 152:1299-1305(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59 AND 585-852, PROTEIN
SEQUENCE OF 2-9, FUNCTION, INTEIN SPLICING, AND SUBUNIT.
STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
PubMed=11274122; DOI=10.1128/JB.183.8.2614-2623.2001;
Cann I.K.O., Ishino S., Yuasa M., Daiyasu H., Toh H., Ishino Y.;
"Biochemical analysis of replication factor C from the
hyperthermophilic archaeon Pyrococcus furiosus.";
J. Bacteriol. 183:2614-2623(2001).
[3]
ELECTRON MICROSCOPY.
PubMed=11469875; DOI=10.1006/jsbi.2001.4357;
Mayanagi K., Miyata T., Oyama T., Ishino Y., Morikawa K.;
"Three-dimensional electron microscopy of the clamp loader small
subunit from Pyrococcus furiosus.";
J. Struct. Biol. 134:35-45(2001).
[4]
FUNCTION.
PubMed=12296822; DOI=10.1046/j.1365-2443.2002.00572.x;
Matsumiya S., Ishino S., Ishino Y., Morikawa K.;
"Physical interaction between proliferating cell nuclear antigen and
replication factor C from Pyrococcus furiosus.";
Genes Cells 7:911-922(2002).
[5]
MUTAGENESIS OF GLU-785; GLU-795; ASP-796; GLU-831 AND GLU-835.
PubMed=12768447; DOI=10.1007/s00792-002-0308-1;
Ishino S., Oyama T., Yuasa M., Morikawa K., Ishino Y.;
"Mutational analysis of Pyrococcus furiosus replication factor C based
on the three-dimensional structure.";
Extremophiles 7:169-175(2003).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=11545747; DOI=10.1016/S1097-2765(01)00328-8;
Oyama T., Ishino Y., Cann I.K.O., Ishino S., Morikawa K.;
"Atomic structure of the clamp loader small subunit from Pyrococcus
furiosus.";
Mol. Cell 8:455-463(2001).
-!- FUNCTION: Part of the RFC clamp loader complex which loads the
PCNA sliding clamp onto DNA. The complex possesses DNA-dependent
ATPase activity which is further stimulated by PCNA.
{ECO:0000269|PubMed:11274122, ECO:0000269|PubMed:12296822}.
-!- SUBUNIT: Heteromultimer composed of three to four small subunits
(RfcS) and one to two large subunits (RfcL).
{ECO:0000269|PubMed:11274122}.
-!- PTM: This protein undergoes a protein self splicing that involves
a post-translational excision of the intervening region (intein)
followed by peptide ligation. {ECO:0000305}.
-!- MISCELLANEOUS: The intein interrupts the potential ATP-binding
site.
-!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS
subfamily. {ECO:0000305}.
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EMBL; AE009950; AAL80217.1; -; Genomic_DNA.
EMBL; AB037375; BAB03291.1; -; Genomic_DNA.
EMBL; AB037375; BAB03292.1; -; Genomic_DNA.
RefSeq; WP_011011205.1; NC_003413.1.
PDB; 1IQP; X-ray; 2.80 A; A/B/C/D/E/F=1-59, A/B/C/D/E/F=585-852.
PDBsum; 1IQP; -.
ProteinModelPortal; Q8U4J3; -.
SMR; Q8U4J3; -.
STRING; 186497.PF0093; -.
PRIDE; Q8U4J3; -.
EnsemblBacteria; AAL80217; AAL80217; PF0093.
GeneID; 1467922; -.
KEGG; pfu:PF0093; -.
PATRIC; fig|186497.12.peg.97; -.
eggNOG; arCOG00469; Archaea.
eggNOG; arCOG03154; Archaea.
eggNOG; COG0470; LUCA.
eggNOG; COG1372; LUCA.
HOGENOM; HOG000154101; -.
KO; K04801; -.
OMA; DGHADSK; -.
OrthoDB; POG093Z05CK; -.
EvolutionaryTrace; Q8U4J3; -.
Proteomes; UP000001013; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro.
GO; GO:0006310; P:DNA recombination; IEA:InterPro.
GO; GO:0006281; P:DNA repair; IEA:InterPro.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
InterPro; IPR003586; Hint_dom_C.
InterPro; IPR003587; Hint_dom_N.
InterPro; IPR036844; Hint_dom_sf.
InterPro; IPR027434; Homing_endonucl.
InterPro; IPR006142; INTEIN.
InterPro; IPR030934; Intein_C.
InterPro; IPR004042; Intein_endonuc.
InterPro; IPR006141; Intein_N.
InterPro; IPR004860; LAGLIDADG_2.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR013748; Rep_factorC_C.
InterPro; IPR008824; RuvB_N.
Pfam; PF14528; LAGLIDADG_3; 1.
Pfam; PF08542; Rep_fac_C; 1.
Pfam; PF05496; RuvB_N; 1.
PRINTS; PR00379; INTEIN.
SMART; SM00305; HintC; 1.
SMART; SM00306; HintN; 1.
SUPFAM; SSF48019; SSF48019; 1.
SUPFAM; SSF51294; SSF51294; 2.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF55608; SSF55608; 1.
TIGRFAMs; TIGR01443; intein_Cterm; 1.
TIGRFAMs; TIGR01445; intein_Nterm; 1.
PROSITE; PS50818; INTEIN_C_TER; 1.
PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
PROSITE; PS50817; INTEIN_N_TER; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Autocatalytic cleavage; Complete proteome;
Direct protein sequencing; DNA replication; Nucleotide-binding;
Protein splicing; Reference proteome.
CHAIN 1 59 Replication factor C small subunit, 1st
part. {ECO:0000255}.
/FTId=PRO_0000030376.
CHAIN 60 584 Pfu RFC intein. {ECO:0000255}.
/FTId=PRO_0000030377.
CHAIN 585 852 Replication factor C small subunit, 2nd
part. {ECO:0000255}.
/FTId=PRO_0000030378.
DOMAIN 183 306 DOD-type homing endonuclease.
{ECO:0000255|PROSITE-ProRule:PRU00273}.
MUTAGEN 785 785 E->A: Decreases the stability of the
PCNA-RFC complex and reduces the clamp-
loading activity; when associated with A-
795; A-796; A-831 and A-835.
{ECO:0000269|PubMed:12768447}.
MUTAGEN 795 795 E->A: Decreases the stability of the
PCNA-RFC complex and reduces the clamp-
loading activity; when associated with A-
785; A-796; A-831 and A-835.
{ECO:0000269|PubMed:12768447}.
MUTAGEN 796 796 D->A: Decreases the stability of the
PCNA-RFC complex and reduces the clamp-
loading activity; when associated with A-
785; A-795; A-831 and A-835.
{ECO:0000269|PubMed:12768447}.
MUTAGEN 831 831 E->A: Decreases the stability of the
PCNA-RFC complex and reduces the clamp-
loading activity; when associated with A-
785; A-795; A-796 and A-835.
{ECO:0000269|PubMed:12768447}.
MUTAGEN 835 835 E->A: Decreases the stability of the
PCNA-RFC complex and reduces the clamp-
loading activity; when associated with A-
785; A-795; A-796 and A-831.
{ECO:0000269|PubMed:12768447}.
HELIX 584 596 {ECO:0000244|PDB:1IQP}.
HELIX 597 599 {ECO:0000244|PDB:1IQP}.
HELIX 600 603 {ECO:0000244|PDB:1IQP}.
STRAND 604 608 {ECO:0000244|PDB:1IQP}.
HELIX 612 616 {ECO:0000244|PDB:1IQP}.
HELIX 619 627 {ECO:0000244|PDB:1IQP}.
HELIX 631 633 {ECO:0000244|PDB:1IQP}.
STRAND 637 642 {ECO:0000244|PDB:1IQP}.
HELIX 644 646 {ECO:0000244|PDB:1IQP}.
HELIX 649 661 {ECO:0000244|PDB:1IQP}.
TURN 662 665 {ECO:0000244|PDB:1IQP}.
STRAND 666 673 {ECO:0000244|PDB:1IQP}.
HELIX 675 677 {ECO:0000244|PDB:1IQP}.
HELIX 680 684 {ECO:0000244|PDB:1IQP}.
STRAND 686 690 {ECO:0000244|PDB:1IQP}.
HELIX 696 708 {ECO:0000244|PDB:1IQP}.
TURN 709 711 {ECO:0000244|PDB:1IQP}.
HELIX 716 726 {ECO:0000244|PDB:1IQP}.
HELIX 730 741 {ECO:0000244|PDB:1IQP}.
STRAND 745 747 {ECO:0000244|PDB:1IQP}.
HELIX 749 755 {ECO:0000244|PDB:1IQP}.
HELIX 761 773 {ECO:0000244|PDB:1IQP}.
HELIX 776 790 {ECO:0000244|PDB:1IQP}.
HELIX 794 804 {ECO:0000244|PDB:1IQP}.
HELIX 805 807 {ECO:0000244|PDB:1IQP}.
STRAND 808 810 {ECO:0000244|PDB:1IQP}.
HELIX 812 830 {ECO:0000244|PDB:1IQP}.
HELIX 835 850 {ECO:0000244|PDB:1IQP}.
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


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