UniProt: A0A072TQI6

Database: UniProt
Entry: A0A072TQI6_MEDTR

LinkDB:  A0A072TQI6_MEDTR 
Original site:  A0A072TQI6_MEDTR

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
Literature (2)   
   PubMed (2)   
All databases (18)   

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ID   A0A072TQI6_MEDTR        Unreviewed;       594 AA.
AC   A0A072TQI6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN   OrderedLocusNames=MTR_8g038785 {ECO:0000313|EMBL:KEH19113.1};
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:KEH19113.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:KEH19113.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH19113.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH19113,
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:KEH19113.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:KEH19113.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:KEH19113,
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:KEH19113}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH19113};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
CC   -!- SIMILARITY: Belongs to the NifU family.
CC       {ECO:0000256|ARBA:ARBA00006420}.
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DR   EMBL; CM001224; KEH19113.1; -; Genomic_DNA.
DR   RefSeq; XP_013445087.1; XM_013589633.1.
DR   AlphaFoldDB; A0A072TQI6; -.
DR   STRING; 3880.A0A072TQI6; -.
DR   EnsemblPlants; KEH19113; KEH19113; MTR_8g038785.
DR   Gramene; KEH19113; KEH19113; MTR_8g038785.
DR   HOGENOM; CLU_459586_0_0_1; -.
DR   Proteomes; UP000002051; Chromosome 8.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 3.
DR   Gene3D; 3.30.300.130; Fe-S cluster assembly (FSCA); 1.
DR   InterPro; IPR034904; FSCA_dom_sf.
DR   InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR10516:SF466; FK506-BINDING PROTEIN 59; 1.
DR   PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   Pfam; PF00254; FKBP_C; 3.
DR   Pfam; PF01106; NifU; 1.
DR   SUPFAM; SSF117916; Fe-S cluster assembly (FSCA) domain-like; 1.
DR   SUPFAM; SSF54534; FKBP-like; 3.
DR   PROSITE; PS50059; FKBP_PPIASE; 3.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          188..278
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          309..398
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          426..514
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   594 AA;  65611 MW;  52FB5264D8E078AF CRC64;
     MATLTPICSI PAELNLSIQQ KQHNFNFALF NLKNPKQNSR TSTTIIHLSF TANQNQSSMG
     LYSAKKFDLT APNVDLVLED VRPYLISDGG NVDVVSVENG VVSLKLQGVC ESCPSSTTTM
     KMGMKRVLKE KFEEVKVLKK KNHVTYATLG GEVSRSWKLR THSILSITHL RMHSLMDEDG
     DNPIPNLDDE VHVHFTGTLL LDGKKFDSSS DRGTSTFSFT LGRGQVIKGW GEGMRTMRKG
     EKALFTIPPE LAYGKSGLPP NIPPNATLQY DVELLSSTSS KDICDICMDG GLFKEILDEG
     EKWENPKDLD EVLVKYEAHL DDGTLVAKSD GVEFTVKEGF FCLALSKAVK TMKKGENVAL
     TVKPQYGFGV KGKPAHGDEI AVPPNATLKI NLELVSWKTV FEVTDDKKVI KKILKEGEGY
     KCPKDGAAVK LKLIGKLQDD TVFLKKGHGD EFTTDEEQVI DGLDKAVMTM KKGEVALLTI
     APEYAFGSSE SQQELAVVPP NSTLYYEVEL VSFIKCFQDI LSGDIGFTVH TTEESQNGNF
     DSILMSSTTV HPRYSHLNLE EKGMHYNGDA SHVLTLATTF RLVLFCRLIV HVII
//

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