ID A0A011QQP4_9PROT Unreviewed; 524 AA.
AC A0A011QQP4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE SubName: Full=Aminopeptidase N {ECO:0000313|EMBL:EXI91450.1};
DE EC=3.4.11.2 {ECO:0000313|EMBL:EXI91450.1};
GN Name=pepN {ECO:0000313|EMBL:EXI91450.1};
GN ORFNames=AW12_01277 {ECO:0000313|EMBL:EXI91450.1};
OS Candidatus Accumulibacter sp. BA-94.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI91450.1, ECO:0000313|Proteomes:UP000020878};
RN [1] {ECO:0000313|EMBL:EXI91450.1, ECO:0000313|Proteomes:UP000020878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXI91450.1}.
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; JEMZ01000064; EXI91450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011QQP4; -.
DR STRING; 1454005.AW12_01277; -.
DR MEROPS; M01.005; -.
DR PATRIC; fig|1454005.3.peg.1244; -.
DR Proteomes; UP000020878; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 1.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:EXI91450.1};
KW Hydrolase {ECO:0000313|EMBL:EXI91450.1};
KW Protease {ECO:0000313|EMBL:EXI91450.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020878}.
FT DOMAIN 2..124
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 129..233
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 237..523
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 524 AA; 58006 MW; 8D8CD695D239CFDD CRC64;
MSLKEGLTVF RDQEFGADMH GRAVTRIRDV RALRATQFPE DAGPMAHPVR PDSYIEINNF
YTSTVYEKGA EVVRMLQTLI GRQAFRRGMD LYFRRHDGQA VTCDDFVAAM ADAAGVDLRQ
FMRWYDQAGT PHLCANGQHD PASQRYILTL SQSRPASAAE SPFHIPVAIG LVGVDGRDLP
LHLAGEGASV NRGHTTRILS LTAAEQQFVF EGVPTPPVAS LLRDFSAPVI LEHERRDDEL
NFLLAHDSDP FNRWEAGQRL ATRLILAAAA DFAAGRATRW PATFADALRQ SLLHADRDPA
FAAEVLTLPG EATLAEEMAV VDPDALHAAR NGLRRFLAEQ LHDSFLHCYQ SLATAGPYEA
TPAAAGRRAL RNVCLGYLGE LATVAMHQLA MRQFASADNM SDQFAALAVL AQHDCDQRRE
ALAAFHERWQ GEALVIDKWL AVQASSRLPG TLAIVEALLA HASFDLHNPN KVYALLNSFG
NNHVRFHSAD GGGYRFLARR IAEIDRFNPQ VAARLTRRFD RWRA
//
