ID A0A0D2PSB7_GOSRA Unreviewed; 504 AA.
AC A0A0D2PSB7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|PROSITE:PS00631};
DE Flags: Fragment;
GN ORFNames=B456_001G0323001 {ECO:0000313|EMBL:KJB06906.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB06906.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB06906.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
CC -!- SUBUNIT: Homohexamer (dimer of homotrimers).
CC {ECO:0000256|ARBA:ARBA00011867}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; CM001740; KJB06906.1; -; Genomic_DNA.
DR EMBL; CM001740; KJB06907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2PSB7; -.
DR STRING; 29730.A0A0D2PSB7; -.
DR EnsemblPlants; KJB06906; KJB06906; B456_001G0323001.
DR EnsemblPlants; KJB06907; KJB06907; B456_001G0323001.
DR Gramene; KJB06906; KJB06906; B456_001G0323001.
DR Gramene; KJB06907; KJB06907; B456_001G0323001.
DR eggNOG; KOG2597; Eukaryota.
DR OMA; PLCELMP; -.
DR Proteomes; UP000032304; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304}.
FT DOMAIN 356..363
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KJB06906.1"
SQ SEQUENCE 504 AA; 52660 MW; A5212439C271B4DB CRC64;
ISFAAKEIDV AEWKGDILAV GVTEKDMSKD ENYKFQNSIL KKLDGLLGGM LAEASSEEDF
TGKAGKSMVL RLPSCGSKRV GLIGLGKTAS SPASFQRLGE AVAAAAKTAQ ANSVAIVLAS
SEGLSNESKL STASAIASGT VLGIYEDSRY KSEPRKPKLN SVDIIGLGTG PELEKMLKYA
ENVSSAIIFG RELVNSPANV LTPAALAAEA SNIASLYSDV LSANILSAEQ CKELKMGSYL
GVAAASANPP HFIHLCYKPS SGPIKTKLAL VGKGLTFDSG GYNIKTGAGC SIDIMKTDMG
GSAAVLGAAK ALGQIKPPGV EVHFIVASCE NMISGTGMRP GDIITASNGK TIEVNNTDAE
GRLTLADALV YACKQGVDKI VDLATLTGAC IVALGPSIAG VFTPSDDLAK EVFEASEVSG
EKFWRMPLEE SYWESMKSGV ADMVNTGGRQ GGAITAALFL KQFVDEKVQW MHIDLAGPVW
NDKKRVATGF GIATLVEWVL KNSS
//
