ID A0A1Y0RFS9_9CYAN Unreviewed; 877 AA.
AC A0A1Y0RFS9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=BZZ01_02545 {ECO:0000313|EMBL:ARV57661.1};
OS Nostocales cyanobacterium HT-58-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV57661.1, ECO:0000313|Proteomes:UP000196302};
RN [1] {ECO:0000313|EMBL:ARV57661.1, ECO:0000313|Proteomes:UP000196302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV57661.1,
RC ECO:0000313|Proteomes:UP000196302};
RA Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT "Genome sequences and microbial community composition of HT-58-2, a
RT tolyporphin-producing cyanobacterium-microbial holobiont.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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 CpcE/RpcE/PecE family.
CC {ECO:0000256|ARBA:ARBA00009299}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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; CP019636; ARV57661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0RFS9; -.
DR KEGG; ncn:BZZ01_02545; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000196302; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase 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; cd09603; M1_APN_like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF13646; HEAT_2; 2.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM00567; EZ_HEAT; 5.
DR SUPFAM; SSF48371; ARM repeat; 1.
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:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:ARV57661.1};
KW Antenna complex {ECO:0000256|ARBA:ARBA00022549};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Phycobilisome {ECO:0000256|ARBA:ARBA00022738};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000196302};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 24..207
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 242..452
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT COILED 836..870
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 877 AA; 100125 MW; 613789E9713C55DF CRC64;
MSQYYFDTEN NRYKSFELPG AKPHYNPDRP GQVEHIFLDL NLDIANRRYH GSCNITLTPI
RNGIDRLNLD AVNLNVESVQ VDGKAQNFDH DGQKLSIQLD PLTQVGKRIV IAIAYSVDKP
QRGIYFIQPD KHYPKKPSQV WTQGEDEDSR FWFPCFDYPG QLSTSEIRIR VPKHLIAISN
GQLIATEEQG EDKIYHWSQQ QVHPTYLMTL AVGDFAEIRD EWNGIPVTYY VEKGREKDAK
RSMGKTPRMI EFLSEKYGYS YPYPKYAQIC VDDFIFGGME NTSATLLTDR CLLDEKAALD
NRNTESLVVH ELAHQWFGDL VVIRHWSHAW IKEGMASYSE VMWTEHEYGA QEAAYYRLLE
ARSYLAEDSD RYRRPMVTHI YREAIELYDR HIYEKGSCVY HMIRAELGDE LFWKAIQTFV
QDNAHKTVET VDLLRAIEKA TGRNLLFLFD QYVYRGGHPD FKVAYTWDGD SNLAKVTVTQ
TQADASNPGN RDLFDLKIPI GFGYVKQEDT KNKENLFASN HFKTFTVRVH EREQSFYFPL
EEKPQFISFD VGNHFLKTVS LEYPVPELKA QLEFDSNPIS RIFAAEALAK KGSLEALKAL
STALKNEPFW GVRVEVAKQL AQINLDQVFD ELVTGLKDQS PYVRRAVAEA LAKIKTHDSY
KALKQLVKEG DPSYYVEAVA TRAIGTIAAG TTEDKPKEEK VIQLLKSVLE EKAGWNEVVR
SGAIAGLAEL KTSEAALNLL LEYTHLGVPQ PLRLAAIRAL GKISTGQSPV NLERILERLT
EISKESFFLT QIAVVTALGQ METPKAIGIL QTLADQTPDG RVHRYAEEEI AKVQNNIGSE
SALRQLRSEL DQLKQQNQEL RSRLENLEAK SQSEPRK
//