Sequence of CATB_MEDTR
EC Number:3.4.22.16
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-/- bonds) as well as an endopeptidase
Other sequences found for EC No. 3.4.22.16
General information:
Sequence
0 MAQWTLLIVF FCVATAAAGL SFHDSNPIRM VSDMEEQLLQ VIGESRHAVS FARFANRYGK
60 RYDTVDEMKR RFKIFSENLQ LIKSTNKKRL GYTLGVNHFA DWTWEEFRSH RLGAAQNCSA
120 TLKGNHRITD VVLPAEKDWR KEGIVSEVKD QGHCGSCWTF STTGALESAY AQAFGKNISL
180 SEQQLVDCAG AYNNFGCNGG LPSQAFEYIK YNGGLETEEA YPYTGQNGLC KFTSENVAVQ
240 VLGSVNITLG AEDELKHAVA FARPVSVAFQ VVDDFRLYKK GVYTSTTCGS TPMDVNHAVL
300 AVGYGIEDGV PYWLIKNSWG GEWGDHGYFK MEMGKNMCGV ATCSSYPVVA
Download this sequence
Download all sequences for 3.4.22.16
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
523318
Young N.D.,Debelle F.,Oldroyd G.E.D.,Geurts R.,Cannon S.B.,Udvardi M.K.,Benedito V.A.,Mayer K.F.X.,Gouzy J.,Schoof H.,Van de Peer Y.,Proost S.,Cook D.R.,Meyers B.C.,Spannagl M.,Cheung F.,De Mita S.,Krishnakumar V.,Gundlach H.,Zhou S.,Mudge J.,Bharti A.K.,Murray J.D.,Naoumkina M.A.,Rosen B.,Silverstein K.A.T.,Tang H.,Rombauts S.,Zhao P.X.,Zhou P.,Barbe V.,Bardou P.,Bechner M.,Bellec A.,Berger A.,Berges H.,Bidwell S.,Bisseling T.,Choisne N.,Couloux A.,Denny R.,Deshpande S.,Dai X.,Doyle J.J.,Dudez A.-M.,Farmer A.D.,Fouteau S.,Franken C.,Gibelin C.,Gish J.,Goldstein S.,Gonzalez A.J.,Green P.J.,Hallab A.,Hartog M.,Hua A.,Humphray S.J.,Jeong D.-H.,Jing Y.,Jocker A.,Kenton S.M.,Kim D.-J.,Klee K.,Lai H.,Lang C.,Lin S.,Macmil S.L.,Magdelenat G.,Matthews L.,McCorrison J.,Monaghan E.L.,Mun J.-H.,Najar F.Z.,Nicholson C.,Noirot C.,O'Bleness M.,Paule C.R.,Poulain J.,Prion F.,Qin B.,Qu C.,Retzel E.F.,Riddle C.,Sallet E.,Samain S.,Samson N.,Sanders I.,Saurat O.,Scarpelli C.,Schiex T.,Segurens B.,Severin A.J.,Sherrier D.J.,Shi R.,Sims S.,Singer S.R.,Sinharoy S.,Sterck L.,Viollet A.,Wang B.-B.,Wang K.,Wang M.,Wang X.,Warfsmann J.,Weissenbach J.,White D.D.,White J.D.,Wiley G.B.,Wincker P.,Xing Y.,Yang L.,Yao Z.,Ying F.,Zhai J.,Zhou L.,Zuber A.,Denarie J.,Dixon R.A.,May G.D.,Schwartz D.C.,Rogers J.,Quetier F.,Town C.D.,Roe B.A.
The Medicago genome provides insight into the evolution of rhizobial symbioses.
Nature
480
520-524
2011
523319
Tang H.,Krishnakumar V.,Bidwell S.,Rosen B.,Chan A.,Zhou S.,Gentzbittel L.,Childs K.L.,Yandell M.,Gundlach H.,Mayer K.F.,Schwartz D.C.,Town C.D.
An improved genome release (version Mt4.0) for the model legume Medicago truncatula.
BMC Genomics
15
312-312
2014
523320
Pecrix Y.,Staton S.E.,Sallet E.,Lelandais-Briere C.,Moreau S.,Carrere S.,Blein T.,Jardinaud M.F.,Latrasse D.,Zouine M.,Zahm M.,Kreplak J.,Mayjonade B.,Satge C.,Perez M.,Cauet S.,Marande W.,Chantry-Darmon C.,Lopez-Roques C.,Bouchez O.,Berard A.,Debelle F.,Munos S.,Bendahmane A.,Berges H.,Niebel A.,Buitink J.,Frugier F.,Benhamed M.,Crespi M.,Gouzy J.,Gamas P.
Whole-genome landscape of Medicago truncatula symbiotic genes.
Nat. Plants
4
1017-1025
2018
523321
Rech S.S.,Heidt S.,Requena N.
A tandem Kunitz protease inhibitor (KPI106)-serine carboxypeptidase (SCP1) controls mycorrhiza establishment and arbuscule development in Medicago truncatula.
Plant J.
75
711-725
2013