ID A0A072TU77_MEDTR Unreviewed; 975 AA.
AC A0A072TU77;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Peptidase M1 family aminopeptidase N {ECO:0000313|EMBL:KEH21084.1};
GN OrderedLocusNames=MTR_8g098525 {ECO:0000313|EMBL:KEH21084.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH21084.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH21084.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH21084.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH21084,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:KEH21084.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH21084.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH21084,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:KEH21084}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH21084};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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; CM001224; KEH21084.1; -; Genomic_DNA.
DR RefSeq; XP_013447057.1; XM_013591603.1.
DR AlphaFoldDB; A0A072TU77; -.
DR STRING; 3880.A0A072TU77; -.
DR MEROPS; M01.005; -.
DR EnsemblPlants; KEH21084; KEH21084; MTR_8g098525.
DR Gramene; KEH21084; KEH21084; MTR_8g098525.
DR HOGENOM; CLU_007993_2_0_1; -.
DR Proteomes; UP000002051; Chromosome 8.
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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:0000313|EMBL:KEH21084.1};
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:UP000002051};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 115..281
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 322..527
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 535..648
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 652..974
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 975 AA; 109681 MW; 44324FB3159F5C50 CRC64;
MARLVLPSKT LAFSRKSLLG LISPAPLQIN SSVNCFRNIS KSSVRYRHFL ASEVVLRKNC
CPFYSSVPRV KKASRKLICS VATESKQVEE SKMAMPTEIF LKDYKMPDYY FEKVDLKFSL
GEEKTIVSSK ISVFPRVEGS TPPLVLDGQD MTLVSVHVNG KALKEEDYHL DARHLTIQSP
PSGKYDLDIV TEILPQKNTS LEGLYKSSGN FCTQCEAEGF RKITFYQDRP DIMAKYTVRI
EADKSLYPVL LSNGNLVGQG DLEGGKHYAV WEDPFKKPCY LFALVAGQLE SRDDTFTTRS
GRKVSLRIWT PAEDVPKTAH AMYSLKAAMK WDEDVFGLEY DLDLFNIVAV PDFNMGAMEN
KSLNIFNSKL VLASPEAASD ADYAAILGVI GHEYFHNWTG NRVTCRDWFQ LSLKEGLTVF
RDQEFSSDMG SRTVKRVGDV SKLRNYQFPQ DGGPMAHPVR PHSYIKMDNF YTVTGAEVVR
MYKTLLGSQG FRKGMDLYFK RHDGQAVTCE DFYAAMRDAN DADFANFLLW YSQAGTPVVK
VNTSYNPEGH TFSLKISQEI PPTPGQSVKE PMFIPIAVGL LDSTGKDIPL SSIYHDGALQ
SVSSNDQSVS TTILRVTKKE EEFVFTDIFE RPVPSLLRGY SAPIRLESDL TDDDLFFLLA
NDSDEFNRWE AGQILARKLM LSLVDDFQHN KPLVLNSSFV DGFKRILSDS SLDKEFVAKA
ITLPGEGEIM DMMKVADPDA VYTVRSFIRK QLASELRSEF LKTVENNRSS GEYVFDHSNM
ARRALKNIAL AYLASLEDQE FTNLALQEYK TATNMTEQFA ALASVVQNPG KTRDDVLADF
YDKWQNDYLV VNKWFALQAV SDIPGNVGNV RKLLNHPAFD LRNPNKVYSL IGGFCGSPVN
FHAKDGSGYE FLGDIVLQLD KINPQVASRM VSAFSRWRRY DEIRQKLAKA QLEKIMSTNG
LSENVFEIAS KSLAA
//
