ID K9QFC1_9NOSO Unreviewed; 859 AA.
AC K9QFC1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=Nos7107_2916 {ECO:0000313|EMBL:AFY43512.1};
OS Nostoc sp. PCC 7107.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=317936 {ECO:0000313|EMBL:AFY43512.1, ECO:0000313|Proteomes:UP000010381};
RN [1] {ECO:0000313|EMBL:AFY43512.1, ECO:0000313|Proteomes:UP000010381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7107 {ECO:0000313|EMBL:AFY43512.1,
RC ECO:0000313|Proteomes:UP000010381};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Nostoc sp. PCC 7107.";
RL Submitted (AUG-2012) 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; CP003548; AFY43512.1; -; Genomic_DNA.
DR RefSeq; WP_015113723.1; NC_019676.1.
DR AlphaFoldDB; K9QFC1; -.
DR STRING; 317936.Nos7107_2916; -.
DR KEGG; nos:Nos7107_2916; -.
DR PATRIC; fig|317936.3.peg.3172; -.
DR eggNOG; COG0308; Bacteria.
DR eggNOG; COG1413; Bacteria.
DR HOGENOM; CLU_014298_0_1_3; -.
DR InParanoid; K9QFC1; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000010381; 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: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; 7.
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:0000313|EMBL:AFY43512.1};
KW Antenna complex {ECO:0000256|ARBA:ARBA00022549};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AFY43512.1};
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:UP000010381};
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 REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 830..857
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 859 AA; 97390 MW; E82651FB597A6171 CRC64;
MTHSYFDTDN NGHKSFELPG ARPHYNPDRP GQVEHIFLDL HLDIPKQSYH GSCSIRLSPI
RSGIDRLLLD AVNLNIQSVQ VDEVAQKFDY DGERLAIKLD QPTELGKRIL IAIAYSAEKP
QRGIYFIQPD KHYPHKPTQV WTQGEDEDSR FWFPCFDYPG QLSTSEIRVR VPKSLVAISN
GELIDTSEEG SEKIYHWSQQ QVHPTYLMTL AVGDFAEIRD EWKGKPVTYY VEKGREADAK
RSMGKTPRMI EFLSEKYGYA YAFPKYAQVC VDDFIFGGME NTSTTLLTDR CLLDERAALD
NRNTESLVVH ELAHQWFGDL LVIKHWSHAW IKEGMASYSE VMWMEQEYSA AEAAYYRLLE
ARSYLSEDSS RYRRPMVTHV YREAIELYDR HIYEKGSCVY HMIRAELGEE LFWHAIQTFV
QDNAHKTVET VDLLRAIDKA TGRNLAFLFD QYVYRGGHPD FKVAYAWDGD ANLAKVTVTQ
TQADNNSSKN LFDLKIPIGF GYSTQHSPFT TFTVRVHEPE QTFYFPLSAK PDFISFDVGN
HFLKTVTLEY PVPELKAQLE FDPDPISRVY AAAALAKKGG LEATKALSTS LKNDPFWGVR
VEVAKQLAEV KLDQAFDGLV TGLKDKSPYV RRAVVNALAT IKTYDSYKAV KEVIQEGDRS
YYVEAAAALA IGAIAAANLD EKPKEEKVIK LLKSVLEEKA GWNEVVRSGA VNGLAELKTS
EAALNLLLEY TKQGVPQALR LAAIRALGKI SVGQTPVNLE RILDRLTELA KETFFLTQVA
VVTALGKMET PKAIGILRSL AEQTPDGRVR RYADEEIANV QKHIGPETAL RQLREELDQL
KQQNQELKSR LENLEAKSK
//
