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Database: UniProt
Entry: M2T2N5_COCSN
LinkDB: M2T2N5_COCSN
Original site: M2T2N5_COCSN 
ID   M2T2N5_COCSN            Unreviewed;       416 AA.
AC   M2T2N5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=COCSADRAFT_38154 {ECO:0000313|EMBL:EMD63292.1};
OS   Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS   spot blotch fungus) (Bipolaris sorokiniana).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD63292.1, ECO:0000313|Proteomes:UP000016934};
RN   [1] {ECO:0000313|EMBL:EMD63292.1, ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; KB445645; EMD63292.1; -; Genomic_DNA.
DR   RefSeq; XP_007701091.1; XM_007702901.1.
DR   AlphaFoldDB; M2T2N5; -.
DR   STRING; 665912.M2T2N5; -.
DR   GeneID; 19139185; -.
DR   KEGG; bsc:COCSADRAFT_38154; -.
DR   eggNOG; KOG0989; Eukaryota.
DR   HOGENOM; CLU_042324_1_0_1; -.
DR   OMA; GCQSGSF; -.
DR   OrthoDB; 275853at2759; -.
DR   Proteomes; UP000016934; 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:UP000016934}.
FT   DOMAIN          65..218
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          271..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  45859 MW;  375E9F1B40B8E7CB CRC64;
     MADFFNIKAR QQAAAQASSS KTPTTKQEPN RLQPWVEKYR PKTLSEVTAQ DNTIQVLSRT
     MQSSNLPHML FYGPPGTGKT STILALAKEL YGPELMKSRV LELNASDERG ISIVRQKVKD
     FARQQLSVAP TYNVMVEDKS GTGEGGMVRY RDKYPCPPFK IIVLDEADSM TQDAQSALRR
     TMETYSRMTR FCLVCNYVTR IIDPLASRCS KFRFKSLDQG NAVKRVSDIA ALENVRLDDG
     VAEELVRVAD GDLRKAITFL QSAARLVGAL QSQGGSNKKG KKRTAVPEDD EMDIDSSNTA
     TPSVSLPTIA EIAGVLPPDT LSTFTSALFP KSSAQKSIRY NEIAKVVENM VAEGWSAAQT
     VGQLYEQIMF DERVEDVKKV RLAAVFSETD KRLVDGSDEH LAVLDLGVRV AGVLCL
//
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