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Database: UniProt
Entry: A0A177CPG4_9PLEO
LinkDB: A0A177CPG4_9PLEO
Original site: A0A177CPG4_9PLEO 
ID   A0A177CPG4_9PLEO        Unreviewed;       415 AA.
AC   A0A177CPG4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Replication factor C subunit 2 {ECO:0000313|EMBL:OAG08818.1};
GN   ORFNames=CC84DRAFT_589564 {ECO:0000313|EMBL:OAG08818.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG08818.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG08818.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG08818.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; KV441550; OAG08818.1; -; Genomic_DNA.
DR   RefSeq; XP_018039183.1; XM_018186798.1.
DR   AlphaFoldDB; A0A177CPG4; -.
DR   STRING; 1460663.A0A177CPG4; -.
DR   GeneID; 28770284; -.
DR   InParanoid; A0A177CPG4; -.
DR   OrthoDB; 275853at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
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:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18140; HLD_clamp_RFC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   InterPro; IPR047854; RFC_lid.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF20; REPLICATION FACTOR C SUBUNIT 4; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT   DOMAIN          65..218
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   415 AA;  45385 MW;  E77431514AB8277F CRC64;
     MADFFNIKAR QQAAAQASSS KAPASKAVTN RLQPWVEKYR PKTLSEVTAQ DNTIQILSRT
     LQSTNLPHML FYGPPGTGKT STILALAKQL YGPELIKTRV LELNASDERG ISIVRAKVKD
     FARQQLSSAP THSITVEDES VEGGFKQVRY RDRYPCPPFK IIVLDEADSM TQDAQSALRR
     TMETYSKMTR FCLVCNYVTR IIDPLASRCS KFRFKSLDQG NAVKRVEDIA KLEGVNLDAG
     VSEELVRVAE GDLRKAITFL QSAARLVGAA QKEAAAGGKR KAHAVMDDDD EMDIDSAAPS
     AAAVSKVHIA EIAGVIPETT LESLTSAIFP GSQSQIQYTK IAKVVEDMIA EGWSAAQTVG
     QLYERVLFDE RVGDLQKMRI TGLFSEVDKR LGDGGDEHLA VLDLGLRISG VLCQG
//
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