ID A0A1Z4V8M3_9CYAN Unreviewed; 857 AA.
AC A0A1Z4V8M3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=NIES806_39640 {ECO:0000313|EMBL:BAZ87733.1};
OS Dolichospermum compactum NIES-806.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Dolichospermum; Dolichospermum compactum.
OX NCBI_TaxID=1973481 {ECO:0000313|EMBL:BAZ87733.1, ECO:0000313|Proteomes:UP000218702};
RN [1] {ECO:0000313|EMBL:BAZ87733.1, ECO:0000313|Proteomes:UP000218702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-806 {ECO:0000313|EMBL:BAZ87733.1,
RC ECO:0000313|Proteomes:UP000218702};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-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; AP018316; BAZ87733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4V8M3; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000218702; 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; 4.
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:BAZ87733.1};
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 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 821..855
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 857 AA; 97620 MW; 9A1649AD35657063 CRC64;
MLQFYFDTEK TGHKRFELPG AKPHYNPDRP GQVEHIFLDL NLDIPNQSCY GSCSIRLLPV
RNGIDRLTLD AVNLKIESVQ VNEVTQKFEY DGEQLCIYLS QPTEIGHRLL IAIAYAAEKP
QRGIYFIQPD KHYPHKPTQV WTQGEDEDSR YWFPCFDYPG QLSTSEIRVR IPQPLVAISN
GELIDSVEEA KYTTYHWSQQ QIHPTYLMTL AVGDFAEIRD EWHGKAVTYY VEKGREADAK
RSMGKTPQMI EFLSEKYGYP YAFPKYAQVC VDDFIFGGME NTSTTLLTDR CLLDERAILD
NRNTESLVVH ELAHQWFGDL VVIKHWSHAW IKEGMASYSE VMWTQREYGD QEAAYYRLSE
ARSYFSEDSS RYRRPMVTHV YREAIELYDR HIYEKGSCVY HMIRAELGDE LFWQAVQTFV
QDNAHQTVET IDLLRAIEKA TGRNLAFLFD QYVYRGGHPD FKVAYAWDGD ANLAKVTVTQ
TQAKADSKDL FNLRIPIGFG YKENPQLTTF TVRVHEKEQS FYFPLTQKPD FISFDVGNNY
LKTVTLEYPI SELKAQLEFD PHPISRIYAA EALAKKGGLE ATLALSSALK NDSFWGVRVE
VAKELAEIQL DQAFDGLVAG LNDPSPFVRR AVISSLSQIK THNSYKAVKS FVQDGDASYY
VEAAACRTIA AIAAAHLEDK PHEDKVINLL KSVLEERAGW NEVVRSGAVA GLSEFKSSET
ALNLLLEYTK SGIPQPLRLS AIRAVGKIST GQTPANIERI LDRLAEIARE TFFLTQVAVL
TALGQMETPK AIGILQSLAN QTADGRVRRY AEEEVSKVQK NIGTDKTLKQ LREELDQIKQ
QNQELKSRLE NLEAKSK
//
