ID U9VZE9_9CYAN Unreviewed; 873 AA.
AC U9VZE9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-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=N836_33540 {ECO:0000313|EMBL:ESA38019.1};
OS Leptolyngbya sp. Heron Island J.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA38019.1, ECO:0000313|Proteomes:UP000017515};
RN [1] {ECO:0000313|EMBL:ESA38019.1, ECO:0000313|Proteomes:UP000017515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Heron Island J {ECO:0000313|EMBL:ESA38019.1,
RC ECO:0000313|Proteomes:UP000017515};
RX PubMed=24503993;
RA Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA Fromme P.;
RT "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL Genome Announc. 2:e01166-e01113(2014).
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:ESA38019.1}.
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DR EMBL; AWNH01000015; ESA38019.1; -; Genomic_DNA.
DR RefSeq; WP_023071131.1; NZ_AWNH01000015.1.
DR AlphaFoldDB; U9VZE9; -.
DR STRING; 1385935.N836_33540; -.
DR PATRIC; fig|1385935.3.peg.1071; -.
DR eggNOG; COG0308; Bacteria.
DR eggNOG; COG1413; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000017515; 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:SF303; AMINOPEPTIDASE N; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000017515};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 25..208
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 244..453
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT COILED 829..870
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 873 AA; 98110 MW; 52335E001D440373 CRC64;
MSVAAYFNAD ENGHKSFELP GASPHYNPDR PGQVEHIALD LDFDIPKKSY RGTCTIRLNP
VRNGVDSLTL DAVSLSIDAI TIGNEQQSFD YDGEQLHIHL SKPTLAGQPI TLAIAYAVKE
PQRGIYFIAP DEHYPDKPYQ VWTQGEDEDS RFWFPCFDYP GQLATSEVRV RVPKKYFALS
NGELVSTEED GKAKIYHWQL DKVHPSYLMT LAIGEYDSIE NEWRGRPVRY YVAKGRKDQI
ELTMGKTPQM MERFSQVFGY DYPFSNYDQA CPADFIFGGM ENTTTTLLTD RCLLDQRAAI
DNLRSETLVA HELAHQWFGD LIVINHWSHA WVKEGMATYS EVLWLEAAYG RDEAMYYHLN
HARAYLAEDA SRYRRPLVTH IYREPIELYD RHIYEKGSCV YHMIRQALGD QLFTKTLKTL
LTDNAHSTVE TVDVLRAIDK ATGKNLRYLF DQYVYRGGHP DYAVSYSWDG DSNLVKLMVT
QTQVADGKSQ VQEGLFDLQI PIGFGYVEND TANVQTVTVR IHERQQAFYF PLQKKPDFMS
FDVGNHTLKT VKLEYPLKEL QAQLKYDPEP ISRLYAAKAI AKKGTLEAVE TLSAALINDS
FWAVRAEVAE ALATIQLDQA VEGLLKGLND KHPKVRRAVV NALAGVKTAA SYKALKSVVE
NGDESYYVEG AAVNALGKVG SSTLDNGKSK EKKTLKLLKM VLEERAGWNE VVRSGAIAGL
SVFKSSEAAL DLLLPYTEIG VPQALRLNAI RSLGKIAAGQ SKVGCDRILD RLEAIAREEF
FLTQVAVVMA LGQMEVSGAV RVLQGLAEQS PDGRVKRRAE EAMGKVRKAI GADKAVDELR
KDLDELKQLN RDLKSRLETL EAKAKAEKKA KEK
//
