ID A0A179FL70_METCM Unreviewed; 555 AA.
AC A0A179FL70;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=26S protease regulatory subunit 4 {ECO:0000313|EMBL:OAQ66332.1};
GN ORFNames=VFPPC_07900 {ECO:0000313|EMBL:OAQ66332.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ66332.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ66332.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ66332.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OAQ66332.1}.
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DR EMBL; LSBJ02000004; OAQ66332.1; -; Genomic_DNA.
DR RefSeq; XP_018143419.1; XM_018286691.1.
DR AlphaFoldDB; A0A179FL70; -.
DR STRING; 1380566.A0A179FL70; -.
DR GeneID; 28850685; -.
DR KEGG; pchm:VFPPC_07900; -.
DR OrthoDB; 1707207at2759; -.
DR Proteomes; UP000078397; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 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:OAQ66332.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:OAQ66332.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000078397}.
FT DOMAIN 333..472
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 120..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 61476 MW; D1D06F3B92CC12AB CRC64;
MTVAAHMVAL ARDLSFQPPR DPALSCRVSL APDGDCPNPL SVIALNLVIN SSINGNHLQP
TVLHSDLAER VIGLPEYSFT GSQSLIRQDG KLISWRLVIY SLLTVDENRV KDNLAWEAKD
KPKYEPPPRP TTRVGRKKRK AGGTSAAAKL PAVYPTSRCK LRLLRMQRIH DHLLLEEEYV
ENQERLRKAK AAKEGAAVGP DADVDRLADE RGRVDDMRGS PMGVGTLEEL IDDDHAIVSS
TTGPEYYVSI MSFVDKDLLE PGASVLLHHK SVSIVGVLTD DTDPIVSVMK LDKAPTESYA
DIGGLESQIQ EVRESVELPL LHPELYEEMG IKPPKGVILY GAPGTGKTLL AKAVANQTSA
TFLRIVGSEL IQKYLGDGPR LVRQLFQVAG ENAPSIVFID EIDAIGTKRY ESTSGGEREV
QRTMLELLNQ LDGFDDRGDV KVIMATNKID TLDPALIRPG RIDRKILFEN PDQNTKRKIF
TLHTSKMNLN DDVDLEEFIS QKDDLSGADI KAICSEAGMM ALRERRMRVQ MADFRSARER
VLRTKQEGEP EGLYL
//