ID R7YS87_CONA1 Unreviewed; 546 AA.
AC R7YS87;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=W97_03936 {ECO:0000313|EMBL:EON64703.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON64703.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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DR EMBL; JH767569; EON64703.1; -; Genomic_DNA.
DR RefSeq; XP_007780020.1; XM_007781830.1.
DR AlphaFoldDB; R7YS87; -.
DR STRING; 1168221.R7YS87; -.
DR GeneID; 19901247; -.
DR eggNOG; KOG2028; Eukaryota.
DR HOGENOM; CLU_017985_0_1_1; -.
DR OMA; RIILSQC; -.
DR OrthoDB; 206891at2759; -.
DR Proteomes; UP000016924; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18139; HLD_clamp_RarA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006642; Rad18_UBZ4.
DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00734; ZnF_Rad18; 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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016924};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..25
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|SMART:SM00734"
FT DOMAIN 167..284
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 39..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 59213 MW; 7A4482B0F076E052 CRC64;
MIACPICDKQ VKERDINAHI DSGCQALVVD QSEDASKASP VSSFFQPQAA KRALSSTATP
KAAPGGRELA RPRDGTSNGE GRQDGAHING KKRSIEPENE VELSPHEATP AQSHALATPA
PKRTKLNALR KVAPLAERMR PRTLDEVCGQ GLVGSNGVIR GLIEQDRVPS MILWGAPGTG
KTTIARLIAN TAGTRFVEIN STSSGVGECK KLFAEARSEL QLTGRKTIIF CDEIHRFSKS
QQDVFLGPVE AGEVTLIGAT TENPSFKIVD SLLSRCRTFT LAKLTNENII TILQRALQAE
DTSSQSTLVD DGMIRYLAAF ADGDARTALN LLELAMDLAK GPGMTQDEIK KSLTQTLVYD
RAGDQHYDTI SAFHKSIRGS DPDASLYYLA RMLQSGEDPL YIARRLIIVA SEDIGLADNS
MLGLATAAYT ACEKIGMPEC RINLSHATVA MALSPKSTRV YRSLGNAMKA LQEPGIAGLP
VPVHLRNAPT KLMKEMGYGK EYKYNPDYVG GKIAQDYLPE RLLGRTFLDE RDLGEKVDMD
LSAPER
//
