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Database: UniProt
Entry: A0A0D2Q459_GOSRA
LinkDB: A0A0D2Q459_GOSRA
Original site: A0A0D2Q459_GOSRA 
ID   A0A0D2Q459_GOSRA        Unreviewed;      1261 AA.
AC   A0A0D2Q459;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Peptidase M16 N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B456_002G111600 {ECO:0000313|EMBL:KJB14134.1};
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:KJB14134.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB14134.1, 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   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CM001741; KJB14134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2Q459; -.
DR   MEROPS; M16.004; -.
DR   EnsemblPlants; KJB14134; KJB14134; B456_002G111600.
DR   Gramene; KJB14134; KJB14134; B456_002G111600.
DR   Proteomes; UP000032304; Chromosome 2.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF33; STROMAL PROCESSING PEPTIDASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          213..339
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          358..595
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          926..1152
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1261 AA;  141149 MW;  83C33BE11B88D4BB CRC64;
     MATSSSSSVM SAILVPHNRW DSSISRGRRS LVRVNIPVPA ASVPLARFHP TAAAARMRQM
     KLKKKKKSDA PKAWKWSTSV SHSQQLKKWI PCCSSLSRNC YGETTPFPLP KSAQPFFLHK
     SRFPLATHTF SSSGKRFCSP CATVGPDEPH AASTTCPDGL LENQNFDSLY PQLQTSELEE
     FLSTELPSNP KLHRGQLKNG LRYLILPNKV PPNRFEAHME VHVGSIDEED DEQGIAHMIE
     HVAFLGSKKR EKLLGTGARS NAYTDFHHTV FHIHSPTCTK DADEDLLPLV LDALNEIAFH
     PKFLSSRVEK ERRAILSELQ MMNTIEYRVD CQLLQHLHSE NKLSKRFPIG LEEQIKKWDA
     DKIRKFHERW YFPANATLYI VGDIDNISKT INQIEAVFEQ TGLENETASP PTSSAFGAMA
     NFLVPKLSAG FAGSSSHERS SNSSDQSKIL KKERLAVRPP IKHNWSLPGH NTDMKPPQIF
     QHELLQNFSI NMFCKIPVSK VRTFRDLRNV LMKRIFLSAL HFRINTRYKS SNPPFTSVEL
     DHSDSGREGC TVTTLTITAE PKNWQNAIKV AVQEVRRLKE FGVTKGELTR YMDALLKDSE
     QLSAMIDNVS SVDNLDFIME SDALGHIVMD QRQGHESLMA VAGTVTLDEV NSIGALVLEF
     ISDFGKPTAP LPAAVVACVP KKVHIDGLGE TEFKITASEI ISSIESGLKE PIEAEPELEV
     PKELLSPQQL QELRMQQKPS FIPLSPEINV TKLHDKETGI TQCRLSNGIP VNYKISKNET
     RGGVMRLIVG GGRAAETSGS KGAVVVGVRT LSEGGRVGNF SREQVELFCV NHLINCSLES
     TEEFISMEFR FTLRDNGMHA AFQLLHMVLE HSVWLEDAFD RARQLYLSYY RSIPKSLERS
     TAHKLMLAMM DGDERFVEPT PKSLQNLTLK SVKDAVMNQF VADNMEVSIV GDFSQEEIES
     CILDYLGTVR ASRDSEREPE FSPILFRTSP SDLQFQQVFL KDTDERACAY IAGPAPNRWG
     FTIDGKDLLE SVADIPITDE AQLHSEEGNN VQKDLRRKLR EHPLFFGITM GLLAEVINSR
     LFTTVRDSLG LTYDVSFELN LFDRLKLGWY VISVTSTPSK VYKAVDACKN VLRGLHSNKV
     APRELERAKR TLLMRHEAEI KSNAYWLGLL AHLQASSVPR KDISCVKELT SLYEAATIED
     IYLAYDQLKV DEDSLYSCIG IAGVNAGEGA MASLEEEESN EGFQGVIPVG RGLSTMTRPT
     T
//
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