ID A0A1V4EF21_9ACTN Unreviewed; 464 AA.
AC A0A1V4EF21;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Xaa-Pro aminopeptidase {ECO:0000313|EMBL:OPG11523.1};
GN ORFNames=B1L11_19740 {ECO:0000313|EMBL:OPG11523.1};
OS Microbispora sp. GKU 823.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=1652100 {ECO:0000313|EMBL:OPG11523.1, ECO:0000313|Proteomes:UP000190255};
RN [1] {ECO:0000313|EMBL:OPG11523.1, ECO:0000313|Proteomes:UP000190255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GKU 823 {ECO:0000313|EMBL:OPG11523.1,
RC ECO:0000313|Proteomes:UP000190255};
RA Kruasuwan W.;
RT "Draft genome sequence of sugarcane root-associated plant growth promoting
RT Microbispora sp. GKU 823.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
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:OPG11523.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWJN01000034; OPG11523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4EF21; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000190255; Unassembled WGS sequence.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01087; Prolidase; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:OPG11523.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:OPG11523.1}.
FT DOMAIN 36..172
FT /note="Aminopeptidase P N-terminal"
FT /evidence="ECO:0000259|SMART:SM01011"
SQ SEQUENCE 464 AA; 50931 MW; 67AD739990373F2E CRC64;
MAEKLNTGSH DLPISDALAE FMRGGWADTR EDVAPLPVAA YAAKRRARLA ERLPGERLVI
PSGTLQARSN DDDHRFRTHS AFAYLTGGQQ PDDVLVIEPS GDARLFLHPR PSRAESQEFY
RDRRYGEFWV GRRFDLAEAE AAYQIECAHI DTLPAALSGP ARVLRGVDAS VDGLVSPAGD
DRDAELAAVL SELRLVKDEW EIAELQQAVD ATARGFEDVV RALPAALAHP RGERYVEGVF
GLRSRLEGNA VGYQSIVASG AHACVLHWIR NDGRLDPAEM LLLDAGVEGD NLYTADVTRT
LPLSGRFSPI QRQVYDLVYE AQTAAIAVLR PGVRFREFHE TAMRVISDGL REWGLLTRAQ
ADAGLHRRYT LCSSGHMLGL DVHDCARARA ETYLDGVLEE GQVLTVEPGL YLQPDDLTLP
PELRGIGVRI EDDLVVTADG ARLMSAALPR RADEIESWMA ALAG
//
