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Database: UniProt
Entry: A0A421JU56_9ASCO
LinkDB: A0A421JU56_9ASCO
Original site: A0A421JU56_9ASCO 
ID   A0A421JU56_9ASCO        Unreviewed;       417 AA.
AC   A0A421JU56;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=26S protease subunit RPT4 {ECO:0000313|EMBL:RLV95417.1};
GN   ORFNames=JA1_001067 {ECO:0000313|EMBL:RLV95417.1};
OS   Spathaspora sp. JA1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV95417.1, ECO:0000313|Proteomes:UP000285775};
RN   [1] {ECO:0000313|EMBL:RLV95417.1, ECO:0000313|Proteomes:UP000285775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA1 {ECO:0000313|EMBL:RLV95417.1,
RC   ECO:0000313|Proteomes:UP000285775};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV95417.1}.
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DR   EMBL; NSGQ01000005; RLV95417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JU56; -.
DR   STRING; 2028339.A0A421JU56; -.
DR   Proteomes; UP000285775; 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   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010604; P:positive regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0051173; P:positive regulation of nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IEA:UniProt.
DR   GO; GO:0070682; P:proteasome regulatory particle assembly; IEA:UniProt.
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:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:RLV95417.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:RLV95417.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285775}.
FT   DOMAIN          194..333
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          14..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          47..81
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  46615 MW;  0E7E9D5164604395 CRC64;
     MSADENDALL AALNTDDTVG ASSAAATSSD PERDRSLSKF KDKLLEHRKW DSRLKELRLS
     IRDLESDYEK TENDIKALQS VGQIIGEVLK QLDDERFIVK ASSGPRYIVG CRNTIKKSNL
     KNGIRVSLDM TTLTIMRILP REVDPLVYNM TSFEPGEISF NGIGGLNEQI RELREVIELP
     LKNPELFTRV GIKSPKGVLL YGPPGTGKTL LAKAVAATIG ANFIFSPASA IVDKYIGESA
     RLIREMFSYA KEHEPCIIFM DEIDAIGGRR FSEGTSADRE IQRTLMELLN QMDGFDSLGQ
     TKIIMATNRP DTLDPALLRP GRLDRKIEIP LPNESGRLEI FKIHTSKVSK SGEFDFEAMV
     KMSDGFNGAD IRNVVTEAGF FAIREDRDYI LQNDMMKAVR KVADVKKLEG KLDYEKL
//
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