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Database: UniProt
Entry: R1EZX4_BOTPV
LinkDB: R1EZX4_BOTPV
Original site: R1EZX4_BOTPV 
ID   R1EZX4_BOTPV            Unreviewed;       397 AA.
AC   R1EZX4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Putative activator 1 41 kDa subunit protein {ECO:0000313|EMBL:EOD53192.1};
GN   ORFNames=UCRNP2_7 {ECO:0000313|EMBL:EOD53192.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD53192.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; KB915640; EOD53192.1; -; Genomic_DNA.
DR   RefSeq; XP_007579334.1; XM_007579272.1.
DR   AlphaFoldDB; R1EZX4; -.
DR   STRING; 1287680.R1EZX4; -.
DR   KEGG; npa:UCRNP2_7; -.
DR   eggNOG; KOG0989; Eukaryota.
DR   HOGENOM; CLU_042324_1_0_1; -.
DR   OMA; GCQSGSF; -.
DR   OrthoDB; 275853at2759; -.
DR   Proteomes; UP000013521; Unassembled WGS sequence.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT   DOMAIN          65..206
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   397 AA;  43269 MW;  AAE6F630C101ADE9 CRC64;
     MANFFDLKAR QAAAAAASSS KAPSTKPETS SLQPWVEKYR PKSLTEVTAQ DHTITVLSRT
     LQSSNLPHML FYGPPGTGKT STILALAKQL YGPDLIKTRV LELNASDERG IGIVRDKVKN
     FARQQLSNPP AGPAGVEYRK RFPCPPFKII ILDEADSMTQ DAQSALRRTM ETYSRITRFC
     LVCNYVTRII DPLASRCSKF RFKSLDTGSA AKRLEGIAAN EGVALGEGAV DALVRVSEGD
     LRKAITFLQS AARLVGAVKA AAPVKKGGKV VDDEDEMDVD DKGGKTVSVT VVEEIAGVIP
     GPTMERLYEA MQPRAKGKVY TEVAKAVEDM VADGWSASQL VQQMYETVLF DEKVEDLKKN
     KITLVFSETD KRLVDGADEH LEILDLCLRI AGILVDG
//
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