ID   RFC2_PHANO              Reviewed;         411 AA.
AC   P0C7N7; Q0UV64;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Replication factor C subunit 2;
DE            Short=Replication factor C2;
GN   Name=RFC2; ORFNames=SNOG_04350;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC       delta and epsilon requires the action of the accessory proteins
CC       proliferating cell nuclear antigen (PCNA) and activator 1. Subunit 2
CC       binds ATP and single-stranded DNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5
CC       that forms a complex with PCNA in the presence of ATP. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT88110.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445330; EAT88110.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001794769.1; XM_001794717.1.
DR   AlphaFoldDB; P0C7N7; -.
DR   SMR; P0C7N7; -.
DR   STRING; 321614.P0C7N7; -.
DR   GeneID; 5971637; -.
DR   KEGG; pno:SNOG_04350; -.
DR   InParanoid; P0C7N7; -.
DR   OMA; KIVMVFS; -.
DR   OrthoDB; 1071197at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0090618; P:DNA clamp unloading; IEA:UniProt.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..411
FT                   /note="Replication factor C subunit 2"
FT                   /id="PRO_0000341281"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  45519 MW;  AACD272F14406CCC CRC64;
     MADFFNLKAR QQAAAQASSS KTPTSKQESN RLQPWVEKYR PKTLSEVTAQ DNTIQILSRT
     LQSSNLPHML FYGPPGTGKT STILALAKQL YGPELMKSRV LELNASDERG ISIVRQKVKD
     FARQQLSVAP TYNVMTEDKD GGEAKMVRYR DKYSCPPFKI IVLDEADSMT QDAQSALRRT
     METYSRMTRF CLVCNYVTRI IDPLASRCSK FRFKSLDQGN AVRRVDDIAK LEDVKLDAGV
     SEELVRVADG DLRKAITFLQ SAARLVGATQ TAGRKKKVVV DDEDEMDIDP PSAPSKTTIS
     LEQIAEIAGV IPAPTLASFS DALFPKSAAK SIRYNEIAKV VENMIAEGWS ASQTVSQLYE
     QVMFDERVED IKKVRLAGVF SETDKRLVDG GDEHLAVLDL GVRVAGVLCM G