ID F2SVY1_TRIRC Unreviewed; 430 AA.
AC F2SVY1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=TERG_06703 {ECO:0000313|EMBL:EGD90475.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD90475.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; GG700655; EGD90475.2; -; Genomic_DNA.
DR AlphaFoldDB; F2SVY1; -.
DR STRING; 559305.F2SVY1; -.
DR VEuPathDB; FungiDB:TERG_06703; -.
DR InParanoid; F2SVY1; -.
DR OMA; QDIGGMD; -.
DR OrthoDB; 5477077at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF8; 26S PROTEASOME REGULATORY SUBUNIT 6B; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT DOMAIN 198..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 58..85
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 430 AA; 47962 MW; 22AAFF4827413689 CRC64;
MAGVLVDTPL GAPSLPKSTL NDAIPDIDPL EGSTNDDEDG YSILKRYQRH LEYIQLQEEY
IKDEQRSLKR ELVRAQEEIK RIQSVPLVIG QFMEAIDQNT GIVQSSTGSN YVVRILSTLD
REKLKPSSSV ALHRHSNSLV DILPPEADSS IAMLGANEKP DVTYADVGGL DMQKQEIREA
VELPLTHFDL YKQIGIDPPR GVLLYGPPGT GKTMLVKAVA NSTTANFIRV VGSEFVQKYL
GEGPRMVRDV FRMARENSPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
QTSNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPSLRDRR ERRLIFTTIA GKMSLSPEVD
LDSLIVRNDP LSGAVIAAIM QEAGLRAVRK NRYNIIQSDL EDAYSSQVKG GQDSDKYVLF
LLHLFPFQPG
//
