ID U4T1A2_9GAMM Unreviewed; 880 AA.
AC U4T1A2;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=M917_2600 {ECO:0000313|EMBL:ERL54452.1};
OS Psychrobacter aquaticus CMS 56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1354303 {ECO:0000313|EMBL:ERL54452.1, ECO:0000313|Proteomes:UP000016761};
RN [1] {ECO:0000313|EMBL:ERL54452.1, ECO:0000313|Proteomes:UP000016761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 56 {ECO:0000313|EMBL:ERL54452.1,
RC ECO:0000313|Proteomes:UP000016761};
RX PubMed=24201199;
RA Reddy G.S., Ara S., Singh A., Kumar Pinnaka A., Shivaji S.;
RT "Draft Genome Sequence of Psychrobacter aquaticus Strain CMS 56T, Isolated
RT from a Cyanobacterial Mat Sample Collected from Water Bodies in the McMurdo
RT Dry Valley Region of Antarctica.";
RL Genome Announc. 1:e00918-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:ERL54452.1}.
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DR EMBL; AUSW01000035; ERL54452.1; -; Genomic_DNA.
DR AlphaFoldDB; U4T1A2; -.
DR STRING; 1354303.M917_2600; -.
DR MEROPS; M01.005; -.
DR PATRIC; fig|1354303.4.peg.2558; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000016761; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 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 Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
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 NCBIfam; TIGR02414; pepN_proteo; 1.
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 Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:ERL54452.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ERL54452.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 47..209
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 250..460
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 466..560
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 563..875
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 880 AA; 98978 MW; CA3EBBE451A47755 CRC64;
MSTAETDAQI INPDMPDVPP HAPSKINLKD YKKPSFDVET IDLDIKLFET YAQIDSVLKM
VRQTTGDLVL FGEDLELLMV KMNGSQLGTE DYQQQAGKLT ISDAPNEVTL EIQVRICPQT
NTALEGFYMA GSGDDTMFVT QCEPEGFRKI TFYPDRPDVL AIFTTRLEAD KRYPTLLANG
NLVEAGEVTD EPNRHYAIWH DPTNKPSYLF ACVVADLDVL TDSYKTSEGR NVLLEIYAKS
ADIDKCDVGM QALKDAMKWD EVNYGRAYDL DRYMIVAVSQ FNMGAMENKG LNIFNTACVL
SSPETTTDAR SFSVKAIIAH EYFHNWTGNR ITCRDWFQLC LKEGFTVYRD QSFSADQQSS
AVQRIDDVAT LRAHQFSEDA GPLAHPVRPE SFVEINNFYT TTVYEKGAEI VRMIANTLGQ
EDFRKGTDEY FRRYDGQAVT VEDFLSALSI TDNKIEDFID WYRQPGTPVV SGHQNYDSAT
QTLTITLSQQ TRHVSGFDAP KPLPIPVATA LFDKDSGNII AERMLLLDQA TQTFACEDVA
SEPVVSLLRD FSAPVQLNYD YQDEDLAFLL THETNGFNRW QVTQMLVNRI LLQGQGSKSS
PDVYLQALAQ TLPRLAADDA MLAARLLDIP SAQELASAIN KNYDPELIKA QREALYQQVA
EALKDQWAGL YEQLPMQSYE DSADARGTRA LRNVVLDMAL TANVNGAVEW AEQQYNNASC
MTERFGALKA MVNHQVTNAD EYLADFYERF QENDLVIDLW FSVQASADTV STDVIQSLLE
HQDFDWNTPN RVRSVISAFS SQPTVLWTQE GLEIYTGVIK KLDDANPVLA SRLLQTLARW
NTLVEPRRQM AHNKLLDLQK HAASKHVIES LESVLKAENG
//
