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Database: UniProt
Entry: A0A1Y0RFS9_9CYAN
LinkDB: A0A1Y0RFS9_9CYAN
Original site: A0A1Y0RFS9_9CYAN 
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}.
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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
//
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