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Database: UniProt
Entry: A0A0P4UT85_9CYAN
LinkDB: A0A0P4UT85_9CYAN
Original site: A0A0P4UT85_9CYAN 
ID   A0A0P4UT85_9CYAN        Unreviewed;       854 AA.
AC   A0A0P4UT85;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=NIES2104_12910 {ECO:0000313|EMBL:GAP94774.1};
OS   Leptolyngbya sp. NIES-2104.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP94774.1, ECO:0000313|Proteomes:UP000052243};
RN   [1] {ECO:0000313|EMBL:GAP94774.1, ECO:0000313|Proteomes:UP000052243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP94774.1,
RC   ECO:0000313|Proteomes:UP000052243};
RX   PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA   Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA   Kawachi M.;
RT   "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT   and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL   DNA Res. 22:403-412(2015).
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:GAP94774.1}.
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DR   EMBL; BBWW01000001; GAP94774.1; -; Genomic_DNA.
DR   RefSeq; WP_058996627.1; NZ_BBWW01000001.1.
DR   AlphaFoldDB; A0A0P4UT85; -.
DR   STRING; 1552121.NIES2104_12910; -.
DR   InParanoid; A0A0P4UT85; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000052243; Unassembled WGS sequence.
DR   GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
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; 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; 6.
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:GAP94774.1};
KW   Antenna complex {ECO:0000256|ARBA:ARBA00022549};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          24..207
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          243..452
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          817..851
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   854 AA;  97113 MW;  99D8C3601F17097B CRC64;
     MLHQFSLDTD NGHRSFELPG ARPHYNPDRP GQVEHIFLDL ILDIPNQSYQ GTCTIRLNPI
     RNGIDRLTLD AVNLNIESVK IDDISQQFDY DGEQLQIQLK QPTRIGEKIE LAIAYHVEKP
     QRGLYFIAPT QDYPNKPTQV WTQGEDEDSR FWFPCFDYPG QLTTSEIRVA VPKQMIAVSN
     GELIATEDRG DARIFHWYQR EIHPAYLMTL AIGDFAELRD EWQGKPVTYY VEKGREEQAR
     LSMGKTPQMI EFFSQKYGYP YAFPKYAQVC VDDFIFGGME NTSTTLLTDR CLLDGRAAID
     NRSTESLVAH ELAHQWFGDL IVIKHWSHAW VKEGMASYAE VMWFEEEYGR EEALYYLLGQ
     ARQYLDEDAS RYRRSLVTHV YREAIELYDR HIYEKGSCVY HMIRAELGDE LFYSAIATFL
     NDNAHRTVET IDLLRAIEKS TGRNLTFLFD QYVYRGGHPD FKVNYAWDSD SNLAKVTVSQ
     SQSELFDLRI PIGINFVNAG KVDQKTFTVR IHEKEQSFYF PLEKKPDFIS FDVDNYHLKT
     VELEYPMPEL KAQLQYDSDP VSRLYAAQAI AKKGGLEAVR VLSEALKRDH FWGVRAEIAE
     SLATIKLDQA VEAVIAGLND PEARVRRTIA GCLAQIATPE SYAALGSIVE KGDASYYVEA
     TALRSFGKVA ASGLSESSEE ETLKLIERVL KERQGWNEVV RAGAIGALSQ LKTSEAALNL
     ILEYTQPGVP QPLRLSAIRA LGPISTGQDK INVERILERL KTLSRETFFL TQVAVAVSLG
     QMETTKAIGI LQSLADQTPD GRVRRIAEES VQKVQKNAGS DKAVKQLREE LDQLKKENQD
     LKSRLENLEA KTKG
//
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