Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171568  28 VSRTLAQGKNVSLTLFSFDKGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARERFKMLLV 107
Cdd:cd02230    1 VSRTLVQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKMLLT 80

                 ...
gi 505171568 108 VVF 110
Cdd:cd02230   81 LIK 83

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171568  28 VSRTLAQGKNVSLTLFSFDKGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARERFKMLLV 107
Cdd:cd02230    1 VSRTLVQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKMLLT 80

                 ...
gi 505171568 108 VVF 110
Cdd:cd02230   81 LIK 83

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171568   42 LFSFDKGEEISSHS-SGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARERFKMLLVVVF 110
Cdd:pfam07883   2 LVTLPPGESSPPHRhPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71

L-ectoine synthase; Reviewed

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505171568  62 VYILDGEAEITI--GGEVFNLKKGETIVMPAGIPHALLARERFKMllVVVFNP 112
Cdd:PRK13290  59 VYCIEGEGEVEDlaTGEVHPIRPGTMYALDKHDRHYLRAGEDMRL--VCVFNP 109

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171568  28 VSRTLAQGKNVSLTLFSFDKGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARERFKMLLV 107
Cdd:cd02230    1 VSRTLVQDDGLRVTLFAFDAGQELSEHTAPGDATVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEEDFKMLLT 80

                 ...
gi 505171568 108 VVF 110
Cdd:cd02230   81 LIK 83

Desulfitobacterium hafniense dsy2733 and related proteins, cupin domain; This family includes bacterial proteins homologous to dsy2733, a Desulfitobacterium hafniense protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505171568  29 SRTLAQGKNVSLTLFSFDKGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARERFKML 105
Cdd:cd06983    1 SMALSNSDNVQISLFAFADGESVSEEEYFGDTLYYVLEGEAEITIGDEKHRLKAGDVLAVPAGVLHAIGGLGAFKLL 77

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505171568  35 GKNVSLTLFSFDKGEEISSHS-SGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARERFKMLLVVVFNP 112
Cdd:COG0662   24 GERLSVKRITVPPGAELSLHVhPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQAP 102

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505171568  13 VLNMENLVSYQEGQVVSRTLAQGKNVSLTLFSFDKGEEISSHS-SGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAG 91
Cdd:cd06122    2 FKDLRDHARFSPEKMQKITLFESERLFCDLYCLEPGQSQKVHAhAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAG 81

                         90       100
                 ....*....|....*....|.
gi 505171568  92 IPHALL--ARERfkmLLVVVF 110
Cdd:cd06122   82 VPHGVRntGAER---LVLLVF 99

uncharacterized Methanocaldococcus jannaschii Moth_1897 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to Moth_1897, a Methanocaldococcus jannaschii protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505171568  29 SRTLAQGKNVSLTLFSFDKGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHAL 96
Cdd:cd06984    2 ARKLYDTEHAQIVHITLKPGESLKKHITPVDVFFYVLEGEGIVEIGEEKQEVEADTLIESPANIPHCL 69

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505171568  35 GKNVSLTLFSFDKGEEISSHSSGGDALVY-ILDGEAEITIGGEVFNLKKGETIVMPAGIPH 94
Cdd:cd02214   16 DPRYSLAHARVPPGESTLPHRLKGSEEVYyILEGEGTMEIDGEPREVGPGDAVLIPPGAVQ 76

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505171568  36 KNVSLTLFSFDKGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLAR--ERFKMLLVV 108
Cdd:cd02222   15 PNFAMRYFEIEPGGHTPLHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTgdEPLGFLCIV 89

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 505171568  63 YILDGEAEITIGGEVFNLKKGETIVMPAGIPHAL 96
Cdd:cd02213   66 VVVSGTAEVTLDGKEKLLKEGESIYIPKGTKHRL 99

Bacillus subtilis YjlB and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to YjlB, a Bacillus subtilis protein of unknown function with a cupin beta barrel fold. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two-domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505171568  54 HSSGGDALVyILDGEAEITIGGE---VFNLKKGETIVMPAGIPHALL-ARERFKML 105
Cdd:cd02219   56 HSTTHEVLG-VASGSATLQLGGPggvEVTVEAGDVVVLPAGVGHKLLeSSDDFQVV 110

AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included is MmsR, a bacterial transcriptional regulator thought to positively regulate the expression of the mmsAB operon. The mmsAB operon contains two structural genes involved in valine metabolism: mmsA which encodes methylmalonate-semialdehyde dehydrogenase, and mmsB which encodes 3-hydroxyisobutyrate dehydrogenase. The cupin domain of members of this subfamily does not contain a metal binding site.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 505171568  63 YILDGEAEITIGGEVFNLKKGETIVMPAGIPH 94
Cdd:cd06986   33 YVLSGKGTFSVNGKTYHLKAGQGFLIPPGEPH 64

gentisate 1,2-dioxygenase, 1-hydroxy-2-naphthoate dioxygenase, and salicylate 1,2-dioxygenase bicupin aromatic ring-cleaving dioxygenases, C-terminal cupin domain; This model represents the C-terminal cupin domains of three closely related bicupin aromatic ring-cleaving dioxygenases: gentisate 1,2-dioxygenase (GDO), salicylate 1,2-dioxygenase (SDO), and 1-hydroxy-2-naphthoate dioxygenase (NDO). GDO catalyzes the cleavage of the gentisate (2,5-dihydroxybenzoate) aromatic ring, a key step in the gentisate degradation pathway allowing soil bacteria to utilize 2,5-xylenol, 3,5-xylenol, and m-cresol as sole carbon and energy sources. NDO catalyzes the cleavage of 1-hydroxy-2-naphthoate as part of the bacterial phenanthrene degradation pathway. SDO is a ring cleavage dioxygenase from Pseudaminobacter salicylatoxidans that oxidizes salicylate to 2-oxohepta-3,5-dienedioic acid via a novel ring fission mechanism. SDO differs from other known GDO's and NDO's in its unique ability to oxidatively cleave many different salicylate, gentisate, and 1-hydroxy-2- naphthoate substrates with high catalytic efficiency. The active site of this enzyme is located in the N-terminal domain but could be influenced by changes in the C-terminal domain, which lacks the strictly conserved metal-binding residues found in other cupin domains and is thought to be an inactive vestigial remnant.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 505171568  47 KGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARER 101
Cdd:cd06992   28 AGFSTRPHRSTASAVYHVVEGSGRTVIGGKTFEWEPGDVFVVPSWAWHSHEADSE 82

uncharacterized protein bxe_c0505, cupin domain; This family includes mostly bacterial proteins homologous to bxe_c0505, a Burkholderia xenovorans protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505171568  61 LVYILDGEAEITI-GGEVFNLKKGETIVMPAGIPHALLAR-ERFKMLLVVV 109
Cdd:cd06980   47 MVYVLKGWVKFEFeGGGEVRLEAGDCVYQPPGIRHNVLDYsDDLELLEITS 97

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 505171568  60 ALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARERFKMLLVVV 109
Cdd:cd02211   49 RFLYVLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRNAGDEPARLLWY 98

Gentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505171568  45 FDKGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARE 100
Cdd:COG3435  235 LPPGFHTRPHRHTGSAVYHVVEGSGRSIVGGERFDWGEGDLFVVPSWAWHSHASAD 290

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 505171568  61 LVYILDGEAEITI-----GGEVFNLKKGETIVMPAGIPHALLAR--ERFKMLLVV 108
Cdd:COG2140   27 WYYVLSGEARMTVqdppgRARTVDVGPGDVVYVPPGYGHYIINTgdEPLVFLAVF 81

Cupriavidus pinatubonensis reut_a1446 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to reut_a1446, a Cupriavidus pinatubonensis protein of unknown function that may be related to mannose-6-phosphate isomerase. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505171568  31 TLAQGKNVSLtlfsfdkgEEISS--HSS--GG------DALVYILDGEAEITI-GGEVFNLKKGETIVMPAGIPH 94
Cdd:cd06981   19 TLLENGGVRI--------ERIVStgQASppGFwydqdeDEWVLLLQGEAELEFeDGEEVELKPGDYLLIPAHCRH 85

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 505171568  48 GEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALL 97
Cdd:cd06988   12 GTTSTPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVK 61

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 505171568  57 GGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLAR 99
Cdd:COG3257   80 GAETFLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNA 122

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 505171568  59 DALVYILDGEAEITIGGEVFNLKKGETIVMPAG--IPHALLAR 99
Cdd:cd02224   40 EEFVYVLSGEGTLRLDGEEVLPRPGDFVGFPAGtgVAHQLINR 82

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505171568  39 SLTLFSFD----KGEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLARER--FKMLLVV 108
Cdd:cd06979   16 RFDLFEFEvspnAGMPPPHYHEDWEETIYGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVHGFVNRSGgpTCRLCVL 91

(S)-ureidoglycine aminohydrolase;

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 505171568  48 GEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHAL 96
Cdd:PRK11171  73 GSDQPEPDEGAETFLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTL 121

AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, similar to Escherichia coli 4-hydroxyphenylacetate catabolism regulatory protein HpaA (also known as 4HPA). HpaA is encoded by the hpaA gene which is located upstream of hpaBC. It is activated by 4-HPA, 3-HPA and phenylacetate, and represents a member of the AraC/XylS family of regulators that recognizes aromatic effectors. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 505171568  61 LVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHA 95
Cdd:cd06999   46 VLYIESGGGEVRLDGRTHPLSAPALVVVPPGVVHG 80

Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.

                          10        20        30
                  ....*....|....*....|....*....|...
gi 505171568   64 ILDGEAEITIGGEVFNLKKGETIVMPAGIPHAL 96
Cdd:pfam01050  90 VVSGTARVTKGGETFLLTENESTYIPLGTIHRL 122

Various environmental stresses-induced protein Ves (function unknown) [Function unknown];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505171568  48 GEEISSHSSGGDALVYILDGEAEITIGGEVFNLKKGETIVMPAGIPHALLA 98
Cdd:COG3758  129 AGTLPLHADAGTGLLYVLAGAWTVALGGEAITLEAGDTLLLEAPAPLLTLT 179