ID A0A074VY63_9PEZI Unreviewed; 438 AA.
AC A0A074VY63;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=26S proteasome subunit P45 {ECO:0000313|EMBL:KEQ64194.1};
GN ORFNames=M437DRAFT_74033 {ECO:0000313|EMBL:KEQ64194.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ64194.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ64194.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ64194.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; KL584829; KEQ64194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VY63; -.
DR STRING; 1043003.A0A074VY63; -.
DR HOGENOM; CLU_000688_2_4_1; -.
DR OrthoDB; 5488626at2759; -.
DR Proteomes; UP000030672; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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; IPR048723; PRS7-like_OB.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF13; 26S PROTEASOME REGULATORY SUBUNIT 7; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF21236; PRS7_OB; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:KEQ64194.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030672}.
FT DOMAIN 213..352
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 438 AA; 48853 MW; 828F0F041F45D3C9 CRC64;
MPSATGQNWE KYQKKFADDE VEEKKITPLT DEDIQVLKTY GAAPYAAALK KLEKEIKDRQ
TSVNEKIGVK ESDTGLAPPH LWDIAADRQR MSEEQPLQVA RCTKIIADEN EEKSKYVINV
KQIAKFVVNL GERVSPTDIE EGMRVGVDRN KYQIMLPLPP KIDPSVTMMT VEDKPDVTYG
DVGGCKEQIE KLREVVEMPL LSPERFVHLG IDPPKGALLY GPPGTGKTLC ARAVANRTDA
TFIRVIGSEL VQKYVGEGAR MVRELFEMAR TKKACIIFFD EIDAVGGARF DDGAGGDNEV
QRTMLELITQ LDGFDARGNI KVMFATNRPS TLDPALMRPG RIDRKIEFAL PDMEGRANIL
RIHAKSMSVE RDIRWELISR LCPNATGAEL RSVATEAGMF AIRARRKVAT EKDFLSAVEK
VIRGGLKFNS TAAYAQYN
//
