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}.
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; 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
//