ID U7Q0S0_SPOS1 Unreviewed; 476 AA.
AC U7Q0S0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=26S protease regulatory subunit 6A {ECO:0000313|EMBL:ERT01428.1};
GN ORFNames=HMPREF1624_02675 {ECO:0000313|EMBL:ERT01428.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT01428.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; KI440843; ERT01428.1; -; Genomic_DNA.
DR AlphaFoldDB; U7Q0S0; -.
DR STRING; 1391915.U7Q0S0; -.
DR eggNOG; KOG0652; Eukaryota.
DR HOGENOM; CLU_000688_2_4_1; -.
DR OrthoDB; 1707207at2759; -.
DR Proteomes; UP000018087; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR041569; AAA_lid_3.
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:SF7; 26S PROTEASOME REGULATORY SUBUNIT 6A; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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 Hydrolase {ECO:0000313|EMBL:ERT01428.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:ERT01428.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT DOMAIN 256..395
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 52513 MW; 7C41357C8EF164AF CRC64;
MSTLEELDDI ERHEREDKDE KKDGGDDQSG KDGKDGAGNG GNKGAAKADG DAEMEDAEPE
EDNVIDEEIL SLSTQEIVTR RRLLENESRI MRSEFQRLAH EKATMVEKIK DNQEKIANNR
QLPYLVGNVV ELLDLDPTAE SSEEGANIDL DATRVGKSAV IKTSTRQTIF LPLIGLVDPE
TLKPGDLIGV NKDSYLILDT LPAEYDSRVK AMEVDEKPTE KYSDVGGLDK QIEELVEAIV
WPMKEAERFK KIGIKAPKGA LMYGPPGTGK TLLARACAAQ TDATFLKLAG PQLVQMFIGD
GAKLVRDCFA LAKEKAPAII FIDELDAVGT KRFDSEKSGD REVQRTMLEL LNQLDGFASD
DRIKVLAATN RVDVLDPALL RSGRLDRKIE FPLPNEEARA QILKIHSRKM KVSSAVNWGE
LARSTDEFGG AMLKAVCVEA GMIALRMGKN QISHEHYVDA IAEVQAKKKD TVNFYA
//