ID   A0A0K1E5F3_CHOCO        Unreviewed;       912 AA.
AC   A0A0K1E5F3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=CMC5_001770 {ECO:0000313|EMBL:AKT36064.1};
OS   Chondromyces crocatus.
OC   Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae;
OC   Chondromyces.
OX   NCBI_TaxID=52 {ECO:0000313|EMBL:AKT36064.1, ECO:0000313|Proteomes:UP000067626};
RN   [1] {ECO:0000313|EMBL:AKT36064.1, ECO:0000313|Proteomes:UP000067626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cm c5 {ECO:0000313|EMBL:AKT36064.1,
RC   ECO:0000313|Proteomes:UP000067626};
RA   Zaburannyi N., Bunk B., Maier J., Overmann J., Mueller R.;
RT   "Genome analysis of myxobacterium Chondromyces crocatus Cm c5 reveals a
RT   high potential for natural compound synthesis and the genetic basis for the
RT   loss of fruiting body formation.";
RL   Submitted (JUL-2015) 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 peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   EMBL; CP012159; AKT36064.1; -; Genomic_DNA.
DR   RefSeq; WP_050428640.1; NZ_CP012159.1.
DR   AlphaFoldDB; A0A0K1E5F3; -.
DR   STRING; 52.CMC5_001770; -.
DR   KEGG; ccro:CMC5_001770; -.
DR   PATRIC; fig|52.7.peg.190; -.
DR   OrthoDB; 9816201at2; -.
DR   Proteomes; UP000067626; Chromosome.
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; 3.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067626};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          49..262
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          300..506
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          102..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   912 AA;  101384 MW;  FCE7AEB3489F806C CRC64;
     MAESRLHERC ACGSSLSSSS SFAASRPFTL AGTKRVYERP RPFTVRHIAL DLALDIDAKS
     IEGSARLDVV RLDPAATKIT LDALGFEIAA VEIAVSQAEG EASSVKRASK APPAKASAKG
     AKGKGAKAQA SAKGKASDGA GFSAADYSYD GEALRVTVPE GAAEASIRVQ YRAVPRRGMY
     FLAPDEHVPE RPRQVWTQCQ DEDARHIFPC VDKPHIKQTT ELRVKIPAGW TCLSNGELLS
     PAKDQKQGIF HFRLDEPHPS YLFTLVAGEF TRIEEEVNGV PLAYLVPRGR EEDGKRTFAR
     TPEMIRHFGE KLGVPYPWKR YSQVVVSDFI FGGMENTTAT TMYEHILLDE RAAIDISSDD
     LIAHELAHQW FGDLVTCRDW SHGWLNEGFA TFMEHVDREH HLGRDEYEHG LVGDMDAYLG
     EAKGRYRRPV VCLDYDVPID LFDRHLYEKG GLVLHLLRRE LGDELFWRAV NTYLTRHARG
     VVETRDLQRA FEDTSGRSLE RFFEQWVFRS GHAEVEVKIE FDDTLCTVTV KQSHGPGGSR
     DARDHGPSTD AAPSAFAFDL VLDFGFGEVQ REVRRVEQAT HTFAIPLPRR PKFVVVDPDL
     RVLGELSVEA PVDLLRGQLA HAPTARGRAL AAHLLGKKDD PVTVKALSRT LGDEKEFWGV
     RAEAAEALGR IRSDEALSIL IGRVDLKHAK VRRAVVRALG RFRSNKAAEA LQKLALRDAS
     YLVEAESARA LGATRQTAAF DTLVEILDRP SWGDVIRSGA LDGLAHLRDD RALPHVLART
     RYGVPARGRR AAILALPRIG ADRKIREALE DLLDTADPHV RVDVIRALAE LGDPKARGAM
     QRALDRELDG RVRRRLREVL RDLAGAGRRE ADRLRDELET LRREHHELKA RVSKLEGVSS
     AQKGAKKGES KP
//