ID A0A0V1A1X8_9BILA Unreviewed; 446 AA.
AC A0A0V1A1X8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Proteasome subunit alpha type-7 {ECO:0000313|EMBL:KRY18508.1};
GN Name=psma7 {ECO:0000313|EMBL:KRY18508.1};
GN ORFNames=T12_13880 {ECO:0000313|EMBL:KRY18508.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18508.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY18508.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18508.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KRY18508.1}.
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DR EMBL; JYDQ01000046; KRY18508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A1X8; -.
DR STRING; 990121.A0A0V1A1X8; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03755; proteasome_alpha_type_7; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.50.10420; NagB/RpiA/CoA transferase-like; 1.
DR InterPro; IPR002698; FTHF_cligase.
DR InterPro; IPR024185; FTHF_cligase-like_sf.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR NCBIfam; TIGR02727; MTHFS_bact; 1.
DR PANTHER; PTHR11599:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 1.
DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR Pfam; PF01812; 5-FTHF_cyc-lig; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000054783}.
FT DOMAIN 4..26
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
SQ SEQUENCE 446 AA; 50987 MW; C6F5B223EF104CF1 CRC64;
MERYDRAITI FSPDGHLFQV EYAQEAVKKG SVAVGIKGKD CVVIAAEKKL VAKLQDDRTI
RKINKVDHHI AMTFAGLNAD ARILVNMARL ECQSWNLSMS VPVTVEYLAR YIANVKQKYT
QSNGRRPFGV SAIIGGFDSD GTAHLYQTEP SGTYYEWNAN CTGRNSHTVR SFLEKRYCPE
AVEDVKSCVK LALRALYEVV QAGVQNIEVG VMTFEKERPE PKARFRIIEW PELQSIIKEV
TSEKEQEGVY RKPKLLKQNL RKKLKQTLQN LGEEEKARQS RAVFRKLLNF PVYCMSKRIS
TFVSMRNEID TKPIIEHIFT SGKECFVPCF ESGNNRMEMV RLRDMEDFFN MQETCWGIKQ
PCNPDGRENC FNSDGLDLII VPGVAFTVDG KRLGHGKGYY DNYLARYFAK FSHRPHTIGI
AFAEQIVSDL PVESHDHVLE KVLFPN
//
