RFCS_METJA
ID RFCS_METJA Reviewed; 1847 AA.
AC Q58817;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-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 Contains:
DE RecName: Full=Mja RFC-1 intein;
DE Contains:
DE RecName: Full=Mja RFC-2 intein;
DE Contains:
DE RecName: Full=Mja RFC-3 intein;
GN Name=rfcS; OrderedLocusNames=MJ1422;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC sliding clamp onto DNA. {ECO:0000250}.
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; L77117; AAB99433.1; -; Genomic_DNA.
DR PIR; E64477; E64477.
DR RefSeq; WP_010870940.1; NC_000909.1.
DR AlphaFoldDB; Q58817; -.
DR SMR; Q58817; -.
DR STRING; 243232.MJ_1422; -.
DR MEROPS; N10.007; -.
DR PRIDE; Q58817; -.
DR EnsemblBacteria; AAB99433; AAB99433; MJ_1422.
DR GeneID; 1452326; -.
DR KEGG; mja:MJ_1422; -.
DR eggNOG; arCOG00469; Archaea.
DR eggNOG; arCOG03145; Archaea.
DR eggNOG; arCOG03154; Archaea.
DR eggNOG; arCOG03158; Archaea.
DR HOGENOM; CLU_002046_0_0_2; -.
DR InParanoid; Q58817; -.
DR OMA; VSHNCNY; -.
DR OrthoDB; 37207at2157; -.
DR PhylomeDB; Q58817; -.
DR Proteomes; UP000000805; 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: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; 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; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR Gene3D; 3.10.28.10; -; 3.
DR Gene3D; 3.40.50.300; -; 2.
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 Pfam; PF01381; HTH_3; 1.
DR Pfam; PF14528; LAGLIDADG_3; 3.
DR Pfam; PF08542; Rep_fac_C; 1.
DR Pfam; PF05496; RuvB_N; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 3.
DR SMART; SM00306; HintN; 3.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF51294; SSF51294; 3.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF55608; SSF55608; 3.
DR TIGRFAMs; TIGR01443; intein_Cterm; 3.
DR TIGRFAMs; TIGR01445; intein_Nterm; 3.
DR PROSITE; PS50818; INTEIN_C_TER; 3.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 3.
DR PROSITE; PS50817; INTEIN_N_TER; 3.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; DNA replication; Nucleotide-binding;
KW Protein splicing; Reference proteome; Repeat.
FT CHAIN 1..53
FT /note="Replication factor C small subunit, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030361"
FT CHAIN 54..601
FT /note="Mja RFC-1 intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030362"
FT CHAIN 602..626
FT /note="Replication factor C small subunit, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030363"
FT CHAIN 627..1062
FT /note="Mja RFC-2 intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030364"
FT CHAIN 1063..1124
FT /note="Replication factor C small subunit, 3rd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030365"
FT CHAIN 1125..1667
FT /note="Mja RFC-3 intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030366"
FT CHAIN 1668..1847
FT /note="Replication factor C small subunit, 4th part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000030367"
FT DOMAIN 179..311
FT /note="DOD-type homing endonuclease 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 780..927
FT /note="DOD-type homing endonuclease 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 1348..1508
FT /note="DOD-type homing endonuclease 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
SQ SEQUENCE 1847 AA; 214097 MW; 44EADB5B4D6DE64A CRC64;
MVIIMEKPWV EKYRPKTLDD IVGQDEIVKR LKKYVEKKSM PHLLFSGPPG VGKCLTGDTK
VIVNGEIREI GEVIEEISNG KFGVTLTNNL KVLGIDEDGK IREFDVQYVY KDKTNTLIKI
KTKMGRELKV TTYHPLLINH KNGEIKWEKA ENLKVGDKLA TPRYILFNES DYNEELAEWL
GYFIGDGHAD KESNKITFTN GDEKLRKRFA ELTEKLFKDA KIKERIHKDR TPDIYVNSKE
AVEFIDKLGL RGKKADKVRI PKEIMRSDAL RAFLRAYFDC DGGIEKHSIV LSTASKEMAE
DLVYALLRFG IIAKLREKVN KNNNKVYYHI VISNSSNLRT FLDNIGFSQE RKLKKLLEII
KDENPNLDVI TIDKEKIRYI RDRLKVKLTR DIEKDNWSYN KCRKITQELL KEIYYRLEEL
KEIEKALEEN ILIDWDEVAE RRKEIAEKTG IRSDRILEYI RGKRKPSLKN YIKIANTLGK
NIEKIIDAMR IFAKKYSSYA EIGKMLNMWN SSIKIYLESN TQEIEKLEEI RKTELKLVKE
ILNDEKLIDS IGYVLFLASN EIYWDEIVEI EQLNGEFTIY DLHVPRYHNF IGGNLPTILH
NTTAALCLAR DLFGENWRDN FLELNASVSK DTPILVKIDG KVKRTTFEEL DKIYFETNDE
NEMYKKVDNL EVLTVDENFR VRWRKVSTII RHKVDKILRI KFEGGYIELT GNHSIMMLDE
NGLVAKKASD IKVGDCFLSF VANIEGEKDR LDLKEFEPKD ITSRVKIIND FDIDEDTAWM
LGLYVAEGAV GFKGKTSGQV IYTLGSHEHD LINKLNDIVD KKGFSKYENF TGSGFDRKRL
SAKQIRILNT QLARFVEENF YDGNGRRARN KRIPDIIFEL KENLRVEFLK GLADGDSSGN
WREVVRISSK SDNLLIDTVW LARISGIESS IFENEARLIW KGGMKWKKSN LLPAEPIIKM
IKKLENKING NWRYILRHQL YEGKKRVSKD KIKQILEMVN VEKLSDKEKE VYDLLKKLSK
TELYALVVKE IEIIDYNDFV YDVSVPNNEM FFAGNVPILL HNSDERGIDV IRTKVKDFAR
TKPIGDVPFK IIFLDESDAL TADAQNALRR TMEKYSDVCR FILSCLTGDA KITLPDEREI
KIEDFIKMFE ERKLKHVLNR NGEDLVLAGV KFNSKIVNHK VYRLVLESGR EIEATGDHKF
LTRDGWKEVY ELKEDDEVLV YPALEGVGFE VDERRIIGLN EFYEFLTNYE IKLGYKPLGK
AKSYKELITR DKEKILSRVL ELSDKYSKSE IRRKIEEEFG IKISLTTIKN LINGKIDGFA
LKYVRKIKEL GWDEITYDDE KAGIFARLLG FIIGDGHLSK SKEGRILITA TINELEGIKK
DLEKLGIKAS NIIEKDIEHK LDGREIKGKT SFIYINNKAF YLLLNFWGVE IGNKTINGYN
IPKWIKYGNK FVKREFLRGL FGADGTKPYI KKYNINGIKL GIRVENISKD KTLEFFEEVK
KMLEEFEVES YIKVSKIDNK NLTELIVKAN NKNYLKYLSR ISYAYEKDNF ARLVGEYLRI
KEAYKDIILK EIAENALKEA DGEKSLRELA RKYNVPVDFI INQLKGKDIG LPRNFMTFEE
FLKEKVVDGK YVSERIIKKE CIGYRDVYDI TCHKDPSFIA NGFVSHNCNY PSKIIPPIQS
RCAVFRFSPL KKEDIAKKLK EIAEKEGLNL TESGLEAIIY VSEGDMRKAI NVLQTAAALS
DVIDDEIVYK VSSRARPEEV KKMMELALDG KFMEARDLLY KLMVEWGMSG EDILNQMFRE
INSLDIDERK KVELADAIGE TDFRIVEGAN ERIQLSALLA KMALMGR
