ID A0A2A2L7I9_9BILA Unreviewed; 778 AA.
AC A0A2A2L7I9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Proteasome subunit alpha type-4 {ECO:0000256|ARBA:ARBA00021341};
GN ORFNames=WR25_27000 {ECO:0000313|EMBL:PAV82088.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV82088.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV82088.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV82088.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity.
CC {ECO:0000256|ARBA:ARBA00002000}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC ProRule:PRU00808}.
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:PAV82088.1}.
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DR EMBL; LIAE01007081; PAV82088.1; -; Genomic_DNA.
DR EMBL; LIAE01007081; PAV82089.1; -; Genomic_DNA.
DR EMBL; LIAE01007081; PAV82090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2L7I9; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd18997; LGIC_ECD_nAChR; 1.
DR CDD; cd03752; proteasome_alpha_type_4; 1.
DR CDD; cd15860; SNARE_USE1; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR019150; Vesicle_transport_protein_Use1.
DR PANTHER; PTHR11599:SF13; PROTEASOME SUBUNIT ALPHA TYPE-4; 1.
DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR Pfam; PF09753; Use1; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 469..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..27
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 283..321
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 778 AA; 90005 MW; 6954A3F5838347AA CRC64;
MARRYDSKTT IFSPEGRLYQ VEYAMEAISH AGTCLGIMAE DGVLLAAEKR NVHKLLDDSV
LNEKIYRLSN NISCTVAGIT SDANVLINHL RWWAANYRLR FGEEMPVEQL VQELCNEKQR
FTQRGGKRPF GVSLLYAGWD KHYGYQLYQS DPSGNYTGWK ATCIGNNHAA AVSLLKQEYK
EQSLEDAKKL AIKVLWKTLD VKLASEKIEM AVLKRKDGKT VLEELTDKEL ETLIAEHEKK
EKEAETMAEK MPTPSDQTEL AFLRLLERTK KLCDNVETNA HKIQAAAGQL EALLNKMHEL
NKAESNELVQ YTRELNQLRI ISQVAMQKSA ENKLQQIERI PKLFPLLNGG GKETEEKEEE
IGEQLQSSNE IKLKNKTIYE QELRDELFHR IHQDKKEIKH DEMQEQMANE LLSLTRSLKE
NMKVAGNVIK DDNQRLVRMQ QQVDSNEERL SAESVRLARH AYKCGFDCML VFIVFFIFIS
FIWMVLVMKI FPKVSDWRKS TCQQSLRPQY RCLTHIHMGM RTGNYNVFFE FTVVIPVIKN
LCLEDNLSNI NALSPFVLML AVLYSVILEL ATSPTSQVLH ERNHFKDRYT EEQKLLDYIL
FNYEKAVRPV KNSSSTVVVK LGMTLTNLFD MDERNQVLTI NVWLDQWNPA DFNNIKSIRI
PCDLIWLPDI VLYNSADDYT TGYMKSRAML DFDGTVFWPP PTQLRSTCKV DVTLFPFDYQ
KCSLKFGSWT YHGFQLDITN RSNNIDLSMF VQSGEFDLVK VYQKRKVTRY TCCPGKCI
//
