ID A0A073AYT9_9PSEU Unreviewed; 664 AA.
AC A0A073AYT9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminopeptidase {ECO:0000313|EMBL:KEI44953.1};
GN ORFNames=GU90_06965 {ECO:0000313|EMBL:KEI44953.1};
OS Saccharopolyspora rectivirgula.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=28042 {ECO:0000313|EMBL:KEI44953.1, ECO:0000313|Proteomes:UP000031419};
RN [1] {ECO:0000313|EMBL:KEI44953.1, ECO:0000313|Proteomes:UP000031419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43113 {ECO:0000313|EMBL:KEI44953.1,
RC ECO:0000313|Proteomes:UP000031419};
RA Barrera C., Millon L., Rognon B., Zaugg C., Monod M.;
RT "Saccharopolyspora rectivirgula DSM-43113 Genome sequencing.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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:KEI44953.1}.
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DR EMBL; JNVU01000017; KEI44953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A073AYT9; -.
DR STRING; 28042.GU90_06965; -.
DR eggNOG; COG2234; Bacteria.
DR Proteomes; UP000031419; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:KEI44953.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:KEI44953.1};
KW Protease {ECO:0000313|EMBL:KEI44953.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031419}.
FT DOMAIN 124..212
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 305..490
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 552..657
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 220..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 560..587
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 664 AA; 72392 MW; 09629DC1462CED27 CRC64;
MQPSPATAQS SAGELRMWER ALQEEVDAGS AAQLSEAMST YPGRVGTEGA ERRAQYSVEK
LTEWGLNPKV ESYQVYASRP SNISVTMTGP QHRELEVKEP PYPWHENFED VVVGYNAYSP
PGNVTADVVY VNYGLPDDYA RLAEMGVDVR GKIVLARYGQ SFRGVKSKVA EEHGAAGVIL
YSDPADDGFT RGEVYPDGPW RNADGIQRGS VQYIFQYPGD PLTPGEPSTP GTPRIDPSEA
DNLPGVPTTP ISYGQAQHLL AALEGPPAPP EWQGGLDLTY RVGPGPTRVN LDLDIDYRQI
PVNDVIVEIP GSKHPEQKVV LGAHYDSWTY GTKDDVAGWT TLMETARAMA ELRQRGWQPE
RTIVLAGWDG EEYGLLGATE WVEQHRADLL DNALVYLNMD GAGGGKNFSA SSVPALDDVL
ADIAKEIEDP EHGTLYRNWQ QASGEQTPVP ERLGSGSDYT PFLDHLGIAS ADFGTSTPSG
EYHSAYDDLH MMRNHLDPGY RYHEVAAAFA GTFALRMAGS DIAPMVYSDY ATAVEGHLAN
LDAKQADSRV VDLAPAYEAA REWRAAAAEL ERAARAARGE RAEAINDALI AQERALTQPE
GLPGRSWYKH MVYAPGLYTG YAVQPLSAID DAISAGDAET AREYRDLLVD SLREATEEAR
EALS
//
