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Database: UniProt
Entry: A0A151T9C7_CAJCA
LinkDB: A0A151T9C7_CAJCA
Original site: A0A151T9C7_CAJCA 
ID   A0A151T9C7_CAJCA        Unreviewed;       888 AA.
AC   A0A151T9C7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN   ORFNames=KK1_018227 {ECO:0000313|EMBL:KYP63648.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP63648.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP63648.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC         ECO:0000256|RuleBase:RU364040};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC       ECO:0000256|RuleBase:RU364040};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Microsome
CC       membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR   EMBL; CM003609; KYP63648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151T9C7; -.
DR   STRING; 3821.A0A151T9C7; -.
DR   OMA; LYKCTYV; -.
DR   OrthoDB; 3085317at2759; -.
DR   Proteomes; UP000075243; Chromosome 7.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
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; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF274; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
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|RuleBase:RU364040,
KW   ECO:0000313|EMBL:KYP63648.1};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU364040}; Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075243};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          22..202
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          238..453
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          544..862
FT                   /note="ERAP1-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11838"
FT   ACT_SITE        310
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            394
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   888 AA;  100981 MW;  2D0ABB664724AED4 CRC64;
     MDQKQSIDKF KGKTRLPSFA IPKRYELHLT PDLSSCTFTG TVQISLTINE STNFLVLNAL
     ELVIQNIRFT NSQGQQHTPS DVVVDNDDEI LVLVFDETLS VGGVLRIEFS GILNEQLTGL
     YKCTYVDGGV KKNMAVTQFE AVDARRCFPC WDEPALKATF KVTLTVPSEL TALSNMPVEN
     EKLDGVLKTL YFEKSPLMST YLVAVVVGLF DYNEVTTIDG VKVRVYCAVG KKDQGKLAMD
     IAVKSLDIFT KYFSVPYPLS KLDLVAVPEF SGGAMENYGL IVYRENELLY HDLYSTAAKK
     QRITIVTAHE VAHQWFGNLV TMEWWTHLWL NEGFATWVSY MATDILFPEW NIWSKFLLDA
     ADGLRMDALE KSHPIEVEIH HARSVIEIFD AVSYYKGSAV IRMLQGYLGD VAFQKSLSTY
     IGRYQAQNAK TEDLWNVLSE ISGVPANLMM NTWTKKAGYP VIHVELIDGI LKFKQSQFLL
     FGQHVDGQWI VPITMSIGSY ERQKKFLLET SHGRVDISEL IQSIGDDTNS NEKKYEDDSQ
     ENIWVKVNVD QSGFYRVNYE DKLALRLRKA IQQNCLLPTD KFGILDDGNA LCQACEQSLS
     TLLMLMDVYR KDFDYVIVSK LINVCLDVLK ISMDAIPDSV NELKQYFISL LMFSAEQLGW
     DSKSGEDHSI SLLRGEVFQA LATFDHDKTQ EEALRRFQIL LDDRNTSLLP ANIRKVAYVA
     VMRNTTTENR TGLESLLSFY RSTDVLQERE KILRCIASSA DPNVVIEVLN LLLSDEIPDQ
     DMIYVLAGIS MEGSEAAWRW LKDNWERILA KYGAGLLLTN FIRQIVPLVN SDEKADEIET
     FFASHMNHSI VMNLKLSIEQ IRIKARWIRS VEQEHSLPDL IKQLAQRK
//
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