Catalytic domain of bacterial PuuE allantoinases, Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins; Allantoinase (EC 3.5.2.5) can hydrolyze allantoin((2,5-dioxoimidazolidin-4-yl)urea), one of the most important nitrogen carrier for some plants, soil animals, and microorganisms, to allantoate. DAL1 gene from Saccharomyces cerevisiae encodes an allantoinase. However, some organisms possess allantoinase activity but lack DAL1 allantoinase. In those organisms, a defective allantoinase gene, named puuE (purine utilization E), encodes an allantoinase that specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. PuuE allantoinase is related to polysaccharide deacetylase (DCA), one member of the carbohydrate esterase 4 (CE4) superfamily, that removes N-linked or O-linked acetyl groups of cell wall polysaccharides, and lacks sequence similarity with the known DAL1 allantoinase that belongs to the amidohydrolase superfamily. PuuE allantoinase functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCAs. It appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common features of DCAs that are normally metal ion dependent and recognize multimeric substrates. This family also includes a chitin deacetylase 1 (SpCDA1) encoded by the Schizosaccharomyces pombe cda1 gene. Although the general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall, the actual function of SpCDA1 might involve allantoin hydrolysis. It is likely orthologous to PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  32 WPGEARIAVQFVLNYEEGAENNVLHGDAGSEQFLSDIIGAASYPDRHMSMDSLYEYGSRAGFWRIHNEFQKRGLPLTVFG 111
Cdd:cd10977     1 WPGGARVAVSFVLNYEEGGERSILHGDGASESFLSEIVGAPLPGVRDLSMESLYEYGSRAGVWRILRLFDRRDVPLTVFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 112 VAMALARHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMDLFGKAPTGWYTGRDSPNTRRLVVEQGG 191
Cdd:cd10977    81 VAMALERNPAVARAMVAAGHEIASHGWRWIDYQGMDEAEEREHIRRAIAIIERLTGERPLGWYTGRASPNTRRLVVEEGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 192 FSYDSDYYGDDLPFWTqvtcqDGTVRPHLIIPYTLETNDMRFATPQGFNTAEQFYTYLKDSFDVLYEEGESAPKMLSVGM 271
Cdd:cd10977   161 FLYDSDSYDDDLPYWV-----DVEGKPHLVVPYTLDTNDMRFATAQGFNTADDFFTYLKDAFDVLYEEGAEAPKMMSIGL 235

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1338958651 272 HCRLLGRPGRFRALTRFLDYIQQHEKVWICTRQQIADH 309
Cdd:cd10977   236 HCRLIGRPGRFAGLERFLEHVKSHDGVWVARREDIARH 273

Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyses glucosidic bonds in xylan.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  85 YEYGSRAGFWRIHNEFQKRGLPLTVFGVAMALARHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMD 164
Cdd:pfam01522  13 FDDGPSENTPAILDVLKKYGVKATFFVIGGNVERYPDLVKRMVEAGHEIGNHTWSHPNLTGLSPEEIRKEIERAQDALEK 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1338958651 165 LFGKAPTGW-YTGRDSPNTRRLVVEQGGFSY 194
Cdd:pfam01522  93 ATGKRPRLFrPPYGSYNDTVLEVAKKLGYTA 123

Catalytic domain of bacterial PuuE allantoinases, Schizosaccharomyces pombe chitin deacetylase 1 (SpCDA1), and similar proteins; Allantoinase (EC 3.5.2.5) can hydrolyze allantoin((2,5-dioxoimidazolidin-4-yl)urea), one of the most important nitrogen carrier for some plants, soil animals, and microorganisms, to allantoate. DAL1 gene from Saccharomyces cerevisiae encodes an allantoinase. However, some organisms possess allantoinase activity but lack DAL1 allantoinase. In those organisms, a defective allantoinase gene, named puuE (purine utilization E), encodes an allantoinase that specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. PuuE allantoinase is related to polysaccharide deacetylase (DCA), one member of the carbohydrate esterase 4 (CE4) superfamily, that removes N-linked or O-linked acetyl groups of cell wall polysaccharides, and lacks sequence similarity with the known DAL1 allantoinase that belongs to the amidohydrolase superfamily. PuuE allantoinase functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCAs. It appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common features of DCAs that are normally metal ion dependent and recognize multimeric substrates. This family also includes a chitin deacetylase 1 (SpCDA1) encoded by the Schizosaccharomyces pombe cda1 gene. Although the general function of chitin deacetylase (CDA) is the synthesis of chitosan from chitin, a polymer of N-acetyl glucosamine, to build up the proper ascospore wall, the actual function of SpCDA1 might involve allantoin hydrolysis. It is likely orthologous to PuuE allantoinase, whereas it is more distantly related to the CDAs found in other fungi, such as Saccharomyces cerevisiae and Mucor rouxii. Those CDAs are similar with rizobial NodB protein and are not included in this family.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  32 WPGEARIAVQFVLNYEEGAENNVLHGDAGSEQFLSDIIGAASYPDRHMSMDSLYEYGSRAGFWRIHNEFQKRGLPLTVFG 111
Cdd:cd10977     1 WPGGARVAVSFVLNYEEGGERSILHGDGASESFLSEIVGAPLPGVRDLSMESLYEYGSRAGVWRILRLFDRRDVPLTVFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 112 VAMALARHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMDLFGKAPTGWYTGRDSPNTRRLVVEQGG 191
Cdd:cd10977    81 VAMALERNPAVARAMVAAGHEIASHGWRWIDYQGMDEAEEREHIRRAIAIIERLTGERPLGWYTGRASPNTRRLVVEEGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 192 FSYDSDYYGDDLPFWTqvtcqDGTVRPHLIIPYTLETNDMRFATPQGFNTAEQFYTYLKDSFDVLYEEGESAPKMLSVGM 271
Cdd:cd10977   161 FLYDSDSYDDDLPYWV-----DVEGKPHLVVPYTLDTNDMRFATAQGFNTADDFFTYLKDAFDVLYEEGAEAPKMMSIGL 235

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1338958651 272 HCRLLGRPGRFRALTRFLDYIQQHEKVWICTRQQIADH 309
Cdd:cd10977   236 HCRLIGRPGRFAGLERFLEHVKSHDGVWVARREDIARH 273

Catalytic domain of bacterial PuuE allantoinases, Helicobacter pylori peptidoglycan deacetylase (HpPgdA), and similar proteins; This family is a member of the very large and functionally diverse carbohydrate esterase 4 (CE4) superfamily. It contains bacterial PuuE (purine utilization E) allantoinases, a peptidoglycan deacetylase from Helicobacter pylori (HpPgdA), Escherichia coli ArnD, and many uncharacterized homologs from all three kingdoms of life. PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. However, in contrast with the typical DCAs, PuuE allantoinase and HpPgdA might not exhibit a solvent-accessible polysaccharide binding groove and only recognize a small substrate molecule. ArnD catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  39 AVQFVLNYEEGAENNVLHGDAGSeqflsdiigaasypdrhMSMDSLYEYGSRAGFWRIHNEFQKRGLPLTVFGVAMALAR 118
Cdd:cd10916     1 AVSVTVDVEGWAGGAASHGAPMA-----------------PAAYSWGRYGLRVGIPRLLDLLDRHGVRATFFVPGRVAER 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 119 HPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMDLFGKAPTGWYTGR--DSPNTRRLVVEQgGFSYDS 196
Cdd:cd10916    64 FPDAVRAIVAAGHEIAAHGYAHEDVLALSREQEREVLLRSLELLEELTGQRPTGWRSPGltFSPDTLELLAEL-GYLYDG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 197 DYYGDDLPFWTQvtcQDGTVRPHLIIPYTLETNDMRFATPQGFnTAEQFYTYLKDSFDVLYEEGesapKMLSVGMHCRLL 276
Cdd:cd10916   143 DTYDDDLPYYWR---DATGGGPILELPYTTVLNDLRFFMGGGG-LPRAFYENWKEQFDVLYARG----RYLSLTLHPRVI 214

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1338958651 277 GRPGRFRALTRFLDYIQQHEKVWICTRQQIADH 309
Cdd:cd10916   215 GRPARAAALDRFLRYVKSHPDVWFATHDEIARH 247

Putative catalytic domain of Synechocystis sp. Sll1306 protein and other bacterial homologs; The family contains Synechocystis sp. Sll1306 protein and uncharacterized bacterial polysaccharide deacetylases. Although their biological function remains unknown, they show very high sequence homology to the catalytic domain of bacterial PuuE (purine utilization E) allantoinases. PuuE allantoinase specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. It functions as a homotetramer. Its monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. PuuE allantoinase appears to be metal-independent and acts on a small substrate molecule, which is distinct from the common feature of polysaccharide deacetylases that are normally metal ion dependent and recognize multimeric substrates.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  32 WPGEARIAVQFVLNYEEGAENNVLHGDAGSEQFLSDiigaasYPDrhMSMDSLYEYGSRAGFWRIHNEFQKRGLPLTVFG 111
Cdd:cd10978     2 WPNGARLVISISMQFEAGGQPIKGEGPFPPEDPPKG------YPD--LPTNTWYQYGYKEGIPRMLDLWDKHGIKVTSHM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 112 VAMALARHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMDLFGKAPTGW--YTGRDSPNTRRLVVEQ 189
Cdd:cd10978    74 VGRAVEKHPDLAKEIVQRGHEAAAHGRDWQNQFSMSREQERAFIQDGVDSIQKVTGQRPVGYnaFWLRGSPNTLDILQEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 190 GgFSYDSDYYGDDLPFWTQVTCQDGTVrphliIPYTLETNDMRFATPQGFnTAEQFYTYLKDSFDVLYEEGESAPKMLSV 269
Cdd:cd10978   154 G-FVYHIDDVSRDEPFIIPVNGKDFVV-----VPYTLRNNDIVRFEGRAY-SSDAYLQELKDEFDQLYEEAAHRRRMMSI 226

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1338958651 270 GMHCRLLGRPGRFRALTRFLDYIQQHEKVWICTRQQIA 307
Cdd:cd10978   227 SLHDRISGTPQRVRVLDEFLTYAKSHPGVTFMRKDDIA 264

Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  87 YGSRAGFWRIHNEFQKRGLPLTVFGVAMALARHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMDLF 166
Cdd:COG0726    28 DGPREGTPRLLDLLKKYGVKATFFVVGSAVERHPELVREIAAAGHEIGNHTYTHPDLTKLSEEEERAEIARAKEALEELT 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1338958651 167 GKAPTGWYT--GRDSPNTRRLVVEQgGFSY--DSDYYGDDLPFWTQVTCQD---GTVRPHLIIPYTLE 227
Cdd:COG0726   108 GKRPRGFRPpyGRYSPETLDLLAEL-GYRYilWDSVDSDDWPYPSADAIVDrvlKYLKPGSIRPGTVE 174

Catalytic domain of Escherichia coli 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD and other bacterial homologs; This family is represented by Escherichia coli 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD (EC 3.5.1.n3). ArnD plays an important role in the biosynthesis of undecaprenyl phosphate alpha-4-amino-4-deoxy-L-arabinose (alpha-L-Ara4N). It catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. The ArnD-dependent deformylation likely occurs on the inner leaflet of the inner membrane. This family also includes many uncharacterized bacterial polysaccharide deacetylases. All family members show high sequence homology to the catalytic domain of bacterial PuuE (purine utilization E) allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA), and are classified within the larger carbohydrate esterase 4 (CE4) superfamily.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651 118 RHPEIVQAISEANYDVVSHGWRWIHYQS----MDAKTERQHIQQAVDVLMDLFGKAPT-----GWYTgrdspNTRRL-VV 187
Cdd:cd10939    87 RLADIIRQVAKAGHEVGIHAWDHVKWQDrldaMSAAEIKREFDKGVALFEKIFGRPPStsaapGWQA-----NDRSLeIK 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1338958651 188 EQGGFSYDSDYYGDDlPFWTQVtcqDGTVRPHLIIPYTLETND 230
Cdd:cd10939   162 DEFGFRYASDCRGGH-PFYPLL---AGKPLGTLQIPTTLPTLD 200

Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA); This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  85 YEYGSRAGFWRIHNEFQKRGLPLTVFGVAMALARHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMD 164
Cdd:cd10941    26 QERRLEEGLDRLLDLLDKHGVKATFFVLGEVAERYPDLIRRIAEAGHEIASHGYAHERVDRLTPEEFREDLRRSKKILED 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1338958651 165 LFGKAPTGWYTGRDSPNTRRL-VVEQGGFSYDS 196
Cdd:cd10941   106 ITGQKVVGFRAPNFSITPWALdILAEAGYLYDS 138

Putative catalytic domain of chitin deacetylase-like proteins with additional chitin-binding peritrophin-A domain (ChBD) and/or a low-density lipoprotein receptor class A domain (LDLa); Chitin deacetylases (CDAs, EC 3.5.1.41) are secreted metalloproteins belonging to a family of extracellular chitin-modifying enzymes that catalyze the N-deacetylation of chitin, a beta-1,4-linked N-acetylglucosamine polymer, to form chitosan, a polymer of beta-(1,4)-linked d-glucosamine residues. CDAs have been isolated and characterized from various bacterial and fungal species and belong to the larger carbohydrate esterase 4 (CE4) superfamily. This family includes many CDA-like proteins mainly from insects, which contain a putative CDA-like catalytic domain similar to the catalytic NodB homology domain of CE4 esterases. In addition to the CDA-like domain, family members contain two additional domains, a chitin-binding peritrophin-A domain (ChBD) and a low-density lipoprotein receptor class A domain (LDLa), or have the ChBD domain but do not have the LDLa domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1338958651 239 FNTAEQFYTYLKDSFDVLYEeGESAPKMLSvgMHCRLLG-RPGRFRALTRFLDYIQQHEKVWICTRQQIADhWIKH 313
Cdd:cd10974   197 ILSGDQVYEWLQHNFERHYL-TNRAPYGLY--FHTNWLKtKNELLRALQKFLDEILQLPDVYFVTMTQAIQ-WMQN 268

Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338958651  95 RIHNEFQKRGLPLTVFGVAMALARHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMDLFGKAPTgWY 174
Cdd:cd10917    18 KILDILAEYGVKATFFVVGENVEKHPDLVRRIVAEGHEIGNHTYSHPDLTKLSPEEIRAEIERTQDAIEEATGVRPR-LF 96

                          90
                  ....*....|....*....
gi 1338958651 175 ---TGRDSPNTRRLVVEQG 190
Cdd:cd10917    97 rppYGAYNPEVLAAAAELG 115

Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis and its bacterial homologs; The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1338958651 118 RHPEIVQAISEANYDVVSHGWRWIHYQSMDAKTERQHIQQAVDVLMDLFGKAPTgWY 174
Cdd:cd10950    46 KNPDLVRKIAKDGHEIGNHGYSHPDPSQLSYEQNREEIRKTNEIIEEITGEKPK-LF 101