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Database: UniProt
Entry: A0A1C7NV91_9FUNG
LinkDB: A0A1C7NV91_9FUNG
Original site: A0A1C7NV91_9FUNG 
ID   A0A1C7NV91_9FUNG        Unreviewed;       429 AA.
AC   A0A1C7NV91;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=26S protease regulatory subunit 6A {ECO:0000313|EMBL:OBZ91394.1};
GN   Name=Psmc3 {ECO:0000313|EMBL:OBZ91394.1};
GN   ORFNames=A0J61_00558 {ECO:0000313|EMBL:OBZ91394.1};
OS   Choanephora cucurbitarum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC   Choanephora.
OX   NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ91394.1, ECO:0000313|Proteomes:UP000093000};
RN   [1] {ECO:0000313|EMBL:OBZ91394.1, ECO:0000313|Proteomes:UP000093000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ91394.1,
RC   ECO:0000313|Proteomes:UP000093000};
RA   Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT   "Choanephora cucurbitarum.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBZ91394.1}.
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DR   EMBL; LUGH01000013; OBZ91394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7NV91; -.
DR   STRING; 101091.A0A1C7NV91; -.
DR   InParanoid; A0A1C7NV91; -.
DR   OrthoDB; 1707207at2759; -.
DR   Proteomes; UP000093000; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:OBZ91394.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:OBZ91394.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093000}.
FT   DOMAIN          209..348
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          35..69
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   429 AA;  48160 MW;  EB4D209D28F94A3B CRC64;
     MTTLEDKSLW ESQNNDDDIG QDILRLAPDE ITNRTRLLEN DIKVMKSEIV RLQHEQAAMK
     ERIKDNKEKI KMNKQLPYLV GNVVELLDVE PDEEDSEGAN VDLDGQIKGK CAVIKTSTRQ
     TIFLPLIGLV DANELKPGDL IGVNKDSYLV LDKLPSEYDS RVKAMEVDEK PTEDYNDIGG
     LNKQIEELVE AVVLPMTHAD RFKNLGIKPP KGVLMYGPPG TGKTLLARAC AAQTNSTYLK
     LAGPQLVQMF IGDGAKLVRD AFELAKEKSP AIIFIDELDA IGTKRFDSEK SGDREVQRTM
     LELLNQLDGF SSDDRIKVIA ATNRIDILDP ALLRSGRLDR KIEFPLPNEE ARARIIQIHS
     RKMNVNKDVN FDELARCCDE FNGAQCKAIC VESGMLALRR GAVEITHEDF MEAIQEVQAK
     KKMTLQYYA
//
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