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Conserved domains on  [gi|2008374040|emb|CAE6402786|]
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unnamed protein product [Rhizoctonia solani]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
393-649 6.16e-160

Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


:

Pssm-ID: 350142 [Multi-domain]  Cd Length: 262  Bit Score: 464.79  E-value: 6.16e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIGENKLNGSA-FQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNPTTKQYVM 471
Cdd:cd18821     1 IQAHGGGILKVGDTYYWFGEDKTDGSNlFQGVSCYSSTDLVNWTFEGLALPPQESGDLGPNRVVERPKVIYNPSTGKYVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 472 YMHIDSSNYGEAKVGVATGSSVCGTYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRANGLRIDKLSDDYLSVVSNVY 551
Cdd:cd18821    81 WMHIDSSNYGDARVGVATSDTVTGPYTYVGSFRPLGYESRDIGVFQDDDGTAYLLFEDRDNGLRIYRLSDDYLSVVELVY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 552 K-WAEKYEAPAVIKSSaGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFAPAGSRTWDSQTTFVLPIG----NNFM 626
Cdd:cd18821   161 TfIAAGLEAPAMFKVD-GTYYLLGSHLTGWRPNDNVYFTATSLSGPWSEPGLIAPEGTNTYNSQSTFVLPVGgskkTTYI 239
                         250       260
                  ....*....|....*....|...
gi 2008374040 627 YMGDRWFSSNLMRSTYVWLPLTI 649
Cdd:cd18821   240 YMGDRWDSPDLSASTYVWLPLTI 262
SURF6 pfam04935
Surfeit locus protein 6; The surfeit locus protein SURF-6 is shown to be a component of the ...
173-367 2.31e-55

Surfeit locus protein 6; The surfeit locus protein SURF-6 is shown to be a component of the nucleolar matrix and has a strong binding capacity for nucleic acids.


:

Pssm-ID: 461491 [Multi-domain]  Cd Length: 197  Bit Score: 188.98  E-value: 2.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 173 DELLEeQRRKRGILREKRRQATRERKRNEEAGKQKKPAAQERAKVHqtntqliVPDPVPGESSSGMANVTFSAIASSGGP 252
Cdd:pfam04935   1 EELLE-ERRKKKEERKAKKKERKEKAKKEEARKREEAEASEDSEAK-------ASPKSPPKGTEASGNLVFGKIDFDDGS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 253 ----------SKAKKYATATDPRAALSQLASRNEKLSSLPAEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTAKRKE 322
Cdd:pfam04935  73 qltsdlskkkKSKKKGPTGKDPKQALKKLEAKKAKLEELDEEKRKEIEEKEKWLKALARAEGEKVKDDEKLLKKALKRKE 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2008374040 323 KEKLKSKAEWNKRKEALSANMAAKQKKRTDNIAQRNERRNDARKG 367
Cdd:pfam04935 153 KQKKKSKKEWKERKEGVEKSKAARQKKREENLKKRKEEKKKKKKK 197
CBM35_galactosidase-like cd04081
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind ...
681-803 4.86e-34

Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43; This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.


:

Pssm-ID: 271147  Cd Length: 125  Bit Score: 126.64  E-value: 4.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 681 YEAESASRSG-AAVIASCSGCSGSSAVGYIGGSGNGVLTFNNVASNASTRTTLRIKHMNGDTTQRYGTVTVNGV-AQTVA 758
Cdd:cd04081     3 YEAEAATLTGsAAAVSCSCGCSGGGAVGVGGGGNGGTVTFNNVTASAAGTYTLTIDYINGDVNDRNATVSVNGGaAQRVA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2008374040 759 FLPTADGATPGSSVVHVNLNSGsSNTVSIAAYNgGYVADVDRLMV 803
Cdd:cd04081    83 FPPTGGWNTPGSVTVLVDLKAG-SNTITFSNSG-GWAPDIDRITV 125
RRP14 pfam15459
60S ribosome biogenesis protein Rrp14; RRP14 is a family of nucleolar 60S ribosomal biogenesis ...
12-75 5.43e-25

60S ribosome biogenesis protein Rrp14; RRP14 is a family of nucleolar 60S ribosomal biogenesis proteins from eukaryotes. RRP14 functions in ribosome synthesis as it is required for the maturation of both small and large subunit rRNAs and it helps to prevent premature cleavage of the pre-rRNA at site C2. It also plays a role in cell polarity and/or spindle positioning 2],


:

Pssm-ID: 464729 [Multi-domain]  Cd Length: 62  Bit Score: 98.47  E-value: 5.43e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2008374040  12 SLEKHNKAFETLLQLIPARYYLPQERDDENNSSKYQKNKKKqSAPKQAvKEATKKARREKLDPA 75
Cdd:pfam15459   1 RLEAHNDFFDSLLSLIPAKFYLPPDETDESNSKKYSKNKKK-KAKKQA-KEASKKAKRAKLDPD 62
 
Name Accession Description Interval E-value
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
393-649 6.16e-160

Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350142 [Multi-domain]  Cd Length: 262  Bit Score: 464.79  E-value: 6.16e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIGENKLNGSA-FQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNPTTKQYVM 471
Cdd:cd18821     1 IQAHGGGILKVGDTYYWFGEDKTDGSNlFQGVSCYSSTDLVNWTFEGLALPPQESGDLGPNRVVERPKVIYNPSTGKYVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 472 YMHIDSSNYGEAKVGVATGSSVCGTYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRANGLRIDKLSDDYLSVVSNVY 551
Cdd:cd18821    81 WMHIDSSNYGDARVGVATSDTVTGPYTYVGSFRPLGYESRDIGVFQDDDGTAYLLFEDRDNGLRIYRLSDDYLSVVELVY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 552 K-WAEKYEAPAVIKSSaGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFAPAGSRTWDSQTTFVLPIG----NNFM 626
Cdd:cd18821   161 TfIAAGLEAPAMFKVD-GTYYLLGSHLTGWRPNDNVYFTATSLSGPWSEPGLIAPEGTNTYNSQSTFVLPVGgskkTTYI 239
                         250       260
                  ....*....|....*....|...
gi 2008374040 627 YMGDRWFSSNLMRSTYVWLPLTI 649
Cdd:cd18821   240 YMGDRWDSPDLSASTYVWLPLTI 262
SURF6 pfam04935
Surfeit locus protein 6; The surfeit locus protein SURF-6 is shown to be a component of the ...
173-367 2.31e-55

Surfeit locus protein 6; The surfeit locus protein SURF-6 is shown to be a component of the nucleolar matrix and has a strong binding capacity for nucleic acids.


Pssm-ID: 461491 [Multi-domain]  Cd Length: 197  Bit Score: 188.98  E-value: 2.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 173 DELLEeQRRKRGILREKRRQATRERKRNEEAGKQKKPAAQERAKVHqtntqliVPDPVPGESSSGMANVTFSAIASSGGP 252
Cdd:pfam04935   1 EELLE-ERRKKKEERKAKKKERKEKAKKEEARKREEAEASEDSEAK-------ASPKSPPKGTEASGNLVFGKIDFDDGS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 253 ----------SKAKKYATATDPRAALSQLASRNEKLSSLPAEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTAKRKE 322
Cdd:pfam04935  73 qltsdlskkkKSKKKGPTGKDPKQALKKLEAKKAKLEELDEEKRKEIEEKEKWLKALARAEGEKVKDDEKLLKKALKRKE 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2008374040 323 KEKLKSKAEWNKRKEALSANMAAKQKKRTDNIAQRNERRNDARKG 367
Cdd:pfam04935 153 KQKKKSKKEWKERKEGVEKSKAARQKKREENLKKRKEEKKKKKKK 197
CBM35_galactosidase-like cd04081
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind ...
681-803 4.86e-34

Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43; This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.


Pssm-ID: 271147  Cd Length: 125  Bit Score: 126.64  E-value: 4.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 681 YEAESASRSG-AAVIASCSGCSGSSAVGYIGGSGNGVLTFNNVASNASTRTTLRIKHMNGDTTQRYGTVTVNGV-AQTVA 758
Cdd:cd04081     3 YEAEAATLTGsAAAVSCSCGCSGGGAVGVGGGGNGGTVTFNNVTASAAGTYTLTIDYINGDVNDRNATVSVNGGaAQRVA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2008374040 759 FLPTADGATPGSSVVHVNLNSGsSNTVSIAAYNgGYVADVDRLMV 803
Cdd:cd04081    83 FPPTGGWNTPGSVTVLVDLKAG-SNTITFSNSG-GWAPDIDRITV 125
RRP14 pfam15459
60S ribosome biogenesis protein Rrp14; RRP14 is a family of nucleolar 60S ribosomal biogenesis ...
12-75 5.43e-25

60S ribosome biogenesis protein Rrp14; RRP14 is a family of nucleolar 60S ribosomal biogenesis proteins from eukaryotes. RRP14 functions in ribosome synthesis as it is required for the maturation of both small and large subunit rRNAs and it helps to prevent premature cleavage of the pre-rRNA at site C2. It also plays a role in cell polarity and/or spindle positioning 2],


Pssm-ID: 464729 [Multi-domain]  Cd Length: 62  Bit Score: 98.47  E-value: 5.43e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2008374040  12 SLEKHNKAFETLLQLIPARYYLPQERDDENNSSKYQKNKKKqSAPKQAvKEATKKARREKLDPA 75
Cdd:pfam15459   1 RLEAHNDFFDSLLSLIPAKFYLPPDETDESNSKKYSKNKKK-KAKKQA-KEASKKAKRAKLDPD 62
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
400-597 2.21e-19

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 90.39  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 400 MIKEGSTYYWIGENklnGSAFQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNptTKQYVMYMHIDSSN 479
Cdd:COG3507    36 IIRVGDTYYLYGTS---FEYFPGLPIFHSKDLVNWELVGHALDRLPQWADPYSGGIWAPDIRYH--NGKYYLYYTAVDGG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 480 YGEAKVGVATGSSVCGTYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRANGLRIDKLSDDYLSVVSNVYK----WAE 555
Cdd:COG3507   111 KNRSGIGVATADDPEGPWSDPGPLVCPGGNGIDPSVFVDDDGKAYLVYGSGGGGIYVAELDPDTGKLLGEPKTlapgGEG 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2008374040 556 KY-EAPAVIKsSAGVYFMFASqlTGWNTNDN---MYSTSTSLSGPW 597
Cdd:COG3507   191 GWiEGPHIYK-RNGYYYLFYS--EGGTCNSGyavRVARSKSPTGPY 233
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
400-601 7.95e-13

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 69.66  E-value: 7.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 400 MIKEGSTYYWIGENklnGSAFQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNpTTKQYVMYMHIDSSN 479
Cdd:pfam04616  15 ILRVGDDYYLTTSS---FEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNASWAPDISYH-DGKYYLYYTAVAHGI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 480 YgeakvgVATGSSVCGTYSYRGSFQPLGFeSRDMGLYKDTDGTAYLL-----TEDRANGLRIDKLSDDYLSVVSNVYK-- 552
Cdd:pfam04616  91 F------VATADSPDGPWSDPGKLKSGGG-GIDPSLFHDDDGKKYLVwggwdPRHGHGGIYLQELDNDGLKLVGPVTKli 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2008374040 553 WAEK-------YEAPAVIKSSAGVYFMFASQLTGWnTNDNMYSTSTSLSGPWLSWK 601
Cdd:pfam04616 164 YPGTrwvggkvTEGPHLYKRNGYYYLTYAAGGTGG-PYAVGVARSRSPLGPYEWHP 218
PTZ00121 PTZ00121
MAEBL; Provisional
177-374 5.55e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 5.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  177 EEQRRKRGILREKRRQATRERKRNEEAgKQKKPAAQERAKVHQTNTQLIVPDPVPGESSSGMANVTFSAIASSGGPSKAK 256
Cdd:PTZ00121  1209 EEERKAEEARKAEDAKKAEAVKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  257 KYATATDPRAA-----LSQLASRNEKLSSLPAEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTAKRKEKEKLKSKAE 331
Cdd:PTZ00121  1288 EKKKADEAKKAeekkkADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2008374040  332 WNK------RKEALSANMAAKQKKRTDNIAQRNERRNDARKGIKPKAAA 374
Cdd:PTZ00121  1368 AAEkkkeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
136-407 8.42e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 136 QPMPSYESISTV---RAKLHARINGLKQERGGLTGEPGSRDELLE---EQRRKRGILREKRRQATRERKRNEEAGKQKKP 209
Cdd:TIGR02794  30 EPGGGAEIIQAVlvdPGAVAQQANRIQQQKKPAAKKEQERQKKLEqqaEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 210 AAQERAKVHQTntqlivpdpvpgesssgmanvtfsaiassggpSKAKKYATATDPRAALSQLASRNEKlsslPAEKRKAI 289
Cdd:TIGR02794 110 AAKQAEEKQKQ--------------------------------AEEAKAKQAAEAKAKAEAEAERKAK----EEAAKQAE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 290 EERSRWEKAEIRAEGgkvhdDATRLKKTAKRKEKE--KLKSKAEWNKRK-EALSANMAAKQKKRTDNIAQRNERRNDARK 366
Cdd:TIGR02794 154 EEAKAKAAAEAKKKA-----EEAKKKAEAEAKAKAeaEAKAKAEEAKAKaEAAKAKAAAEAAAKAEAEAAAAAAAEAERK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2008374040 367 GikpkAAATLQIVPAATwTASGTNQHIQAHGGGMIKEGSTY 407
Cdd:TIGR02794 229 A----DEAELGDIFGLA-SGSNAEKQGGARGAAAGSEVDKY 264
 
Name Accession Description Interval E-value
GH43_Pc3Gal43A-like cd18821
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ...
393-649 6.16e-160

Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350142 [Multi-domain]  Cd Length: 262  Bit Score: 464.79  E-value: 6.16e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIGENKLNGSA-FQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNPTTKQYVM 471
Cdd:cd18821     1 IQAHGGGILKVGDTYYWFGEDKTDGSNlFQGVSCYSSTDLVNWTFEGLALPPQESGDLGPNRVVERPKVIYNPSTGKYVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 472 YMHIDSSNYGEAKVGVATGSSVCGTYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRANGLRIDKLSDDYLSVVSNVY 551
Cdd:cd18821    81 WMHIDSSNYGDARVGVATSDTVTGPYTYVGSFRPLGYESRDIGVFQDDDGTAYLLFEDRDNGLRIYRLSDDYLSVVELVY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 552 K-WAEKYEAPAVIKSSaGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFAPAGSRTWDSQTTFVLPIG----NNFM 626
Cdd:cd18821   161 TfIAAGLEAPAMFKVD-GTYYLLGSHLTGWRPNDNVYFTATSLSGPWSEPGLIAPEGTNTYNSQSTFVLPVGgskkTTYI 239
                         250       260
                  ....*....|....*....|...
gi 2008374040 627 YMGDRWFSSNLMRSTYVWLPLTI 649
Cdd:cd18821   240 YMGDRWDSPDLSASTYVWLPLTI 262
GH43_CtGH43-like cd18822
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
393-649 6.66e-104

Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350143  Cd Length: 266  Bit Score: 320.72  E-value: 6.66e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIGENKLNGSAFQSVNCYSSTNLVEWKYVGALLTLQS-SGDLGPSRVVERPKVIYNPTTKQYVM 471
Cdd:cd18822     1 IQAHGGGILKVGGTYYWYGENRDNNNGFNGVSLYSSTDLVNWEFRNTVLTRDTcSASELASCKIERPKVIYNPKTGKFVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 472 YMHI-DSSNYGEAKVGVATGSSVCGTYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRANG-LRIDKLSDDYLSVVSN 549
Cdd:cd18822    81 WAHWeNGKDYGLARAAVATSDTPDGDYTFHGSFRPLGYDSRDMTLFVDDDGTAYLISAANDNAdLNIYRLTPDYLSVDSL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 550 VYK-WAEKY-EAPAVIKsSAGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFapAGSRTWDSQTTFVLPIGN---- 623
Cdd:cd18822   161 VATlFKGQHrEAPALVK-RNGYYYLFTSGASGWYPNQGQYASATSLAGPWSSLRNI--GNNTTFGSQSTFILPVGGsggt 237
                         250       260
                  ....*....|....*....|....*....
gi 2008374040 624 NFMYMGDRW---FSSNLMRSTYVWLPLTI 649
Cdd:cd18822   238 SYLYMGDRWnspWGGDLGDSRYVWLPLSF 266
GH43_CtGH43-like cd08985
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ...
393-649 6.03e-97

Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350099 [Multi-domain]  Cd Length: 273  Bit Score: 302.71  E-value: 6.03e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIGENK---LNGSAFQSVNCYSSTNLVEWKYVGALLTLQSSG---DLGPSRVVERPKVIYNPTT 466
Cdd:cd08985     1 IHAHGGGILQEGDTYYWYGESRkglDNDNLSHGINCYSSTDLYNWRFEGLVLPASGVEvvrDISPGYVIERPKVLYNART 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 467 KQYVMYMHIDSSNYGEAKVGVATGSSVCGTYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRAN-GLRIDKLSDDYLS 545
Cdd:cd08985    81 RKYVMWFHLDNPNYGFAAVGVATSDTPTGPFTFVRSFRPDGYPSRDMTLFQDPDGTAYLVRSTDHNtDIGISRLSDDYLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 546 VVSNVYKW-AEKYEAPAVIKsSAGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFAPAG---SRTWDSQTTFVLPI 621
Cdd:cd08985   161 TTGASSTFkGPKREAPALFK-RGGTYYLITSGLTGWNPNPSRLARADSPLGPWSTWGNLPVGGpgaDTTYDSQPAFVFPV 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2008374040 622 ----GNNFMYMGDRW--FSSNLMRSTYVWLPLTI 649
Cdd:cd08985   240 egqgGELFIYMGDRWnpGGGGVGNATYVWLPLLF 273
GH43_CtGH43-like cd18825
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
393-649 2.54e-92

Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350146 [Multi-domain]  Cd Length: 285  Bit Score: 291.04  E-value: 2.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIGENKLNGS----AFQSVNCYSSTNLVEWKYVGALLTLQSS---GDLGPSRVVERPKVIYNPT 465
Cdd:cd18825     1 IQAHGGGILKHNGTYYWYGEDKTGGTyrrvDVIGVSCYSSKDLYNWKDEGIVLDAVDDapaSDLYPNNVVERPKVIYNKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 466 TKQYVMYMHID--SSNYGEAKVGVATGSSVCGTYSYRGSFQP----------LGFESRDMGLYKDTDGTAYLLTEDRANG 533
Cdd:cd18825    81 TKKYVMWFHLDgpGADYSRARAGVAVSDSPTGPFKYLGSFRPnageknrdfsNGQMSRDMTLFVDDDGKAYLIYSSEENK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 534 -LRIDKLSDDYLSvVSNVYKWA---EKYEAPAVIKsSAGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFA---PA 606
Cdd:cd18825   161 tLYIAKLTDDYTG-VTGDYARIligQSREAPAVFK-HDGKYYMITSGCTGWAPNAARYAVADSIFGPWKEIGNPCrgpND 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2008374040 607 GSR-TWDSQTTFVLPIG---NNFMYMGDRWFSSNLMRSTYVWLPLTI 649
Cdd:cd18825   239 DADtTFGSQSTFVLPVDgenGKFIYMGDRWNPKDLADSRYVWLPITF 285
GH43_CtGH43-like cd18826
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
393-648 1.57e-58

Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350147 [Multi-domain]  Cd Length: 269  Bit Score: 200.17  E-value: 1.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIGENKLNGS-----AFQSVNCYSSTNLVEWKYVGALLTL---QSSGDLGPSRVVERPKVIYNP 464
Cdd:cd18826     1 IQAHGGSVIYVDGVYYWYGENKEHTDgesgiWHWGVRCYSSTDLYNWEDEGLIIPPdpdDPSSPLHPTRIMDRPHIIYNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 465 TTKQYVMYMHIdSSNYGEAKVGVATGSSVCGTYSYRGSF-QPLGFESRDMGLYKDTDGTAYLLTEDRANGLRIDKLSDDY 543
Cdd:cd18826    81 KTGKYVCWLKL-YPGGDVQYFGVLTADSPTGPYTYVHKFlGPLGMGAGDFDLVVDPDGKAYLYFERVHKEVVCADLTDDY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 544 LSVvsnvykwAEKY-------------EAPAVIKSSaGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFAPA-GSR 609
Cdd:cd18826   160 TDV-------TGEYsthfpglgppfarEAPAVFKRG-GKHYLLTSGTTGYFPNPSEVAVADSYHGPWTVLGNPHVGdGSE 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2008374040 610 -TWDSQTTFVLPI-GNNFMY--MGDRWfssnlmRSTYVWLPLT 648
Cdd:cd18826   232 tSFNSQISSVFKVpGKKDLYiaMADRW------ISRYVWLPIR 268
SURF6 pfam04935
Surfeit locus protein 6; The surfeit locus protein SURF-6 is shown to be a component of the ...
173-367 2.31e-55

Surfeit locus protein 6; The surfeit locus protein SURF-6 is shown to be a component of the nucleolar matrix and has a strong binding capacity for nucleic acids.


Pssm-ID: 461491 [Multi-domain]  Cd Length: 197  Bit Score: 188.98  E-value: 2.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 173 DELLEeQRRKRGILREKRRQATRERKRNEEAGKQKKPAAQERAKVHqtntqliVPDPVPGESSSGMANVTFSAIASSGGP 252
Cdd:pfam04935   1 EELLE-ERRKKKEERKAKKKERKEKAKKEEARKREEAEASEDSEAK-------ASPKSPPKGTEASGNLVFGKIDFDDGS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 253 ----------SKAKKYATATDPRAALSQLASRNEKLSSLPAEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTAKRKE 322
Cdd:pfam04935  73 qltsdlskkkKSKKKGPTGKDPKQALKKLEAKKAKLEELDEEKRKEIEEKEKWLKALARAEGEKVKDDEKLLKKALKRKE 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2008374040 323 KEKLKSKAEWNKRKEALSANMAAKQKKRTDNIAQRNERRNDARKG 367
Cdd:pfam04935 153 KQKKKSKKEWKERKEGVEKSKAARQKKREENLKKRKEEKKKKKKK 197
GH43_RcAra43A-like cd18823
Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This ...
393-648 6.59e-54

Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis arabinanase Ara43A and Fibrobacter succinogenes subsp. succinogenes S85 Fisuc_1994 / FSU_2517. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350144 [Multi-domain]  Cd Length: 289  Bit Score: 188.33  E-value: 6.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYWIG------------ENKLNGSAFQSVNCYSSTNLVEWKYVGALLT----LQSSGDLGPSRVVE 456
Cdd:cd18823     1 IYSQGGGVFKVGDTYYWYGvkysgavtyaanTKKNSDTSFKSVTLYSSTDLVNWTFEGNVLTasgaVDTAGDFAGAGWVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 457 RPKVIYNPTTKQYVMYMHIDSSNYGEAKVGVATGSSVCGTYSYrGSFQPL-----GFESRDMGLYKDTDGTAYLL-TEDR 530
Cdd:cd18823    81 RPGVAYNSATGKYVLLIQWGSTGNGRNGVLFATSDSPTGPFTY-QRVQPMidnvgTNNTGDQTSFFDDDGKAYLVySNDR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 531 ANG-LRIDKLSDDYLSVVSNVYKWAEKY---EAPAVIKSsAGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWK---TF 603
Cdd:cd18823   160 GRGsLYIAKLRSDYLGIEPAVRIDNYVGpgrEGNALFKY-GGTYYLCASDLHGWNASQTYYMVATSLTGPYSPSNvleTT 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2008374040 604 APAGSRTWDSQTTFVLPI----GNNFMYMGDRW--FSSN-LMRStyVWLPLT 648
Cdd:cd18823   239 GPESDNSHVTQTGFFIPVhgskGTTYVYCGDRWsdFAGNgIGYN--QWYPLT 288
CBM35_galactosidase-like cd04081
Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind ...
681-803 4.86e-34

Carbohydrate Binding Module family 35 (CBM35); appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43; This family includes carbohydrate binding module family 35 (CBM35); these are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind alpha-D-galactose (CBM35-Gal), including glycoside hydrolase (GH) families GH27 and GH43. Examples of proteins which contain CBM35s belonging to this family includes the CBM35 of an exo-beta-1,3-galactanase from Phanerochaete chrysosporium 9 (Pc1,3Gal43A) which is appended to a GH43 domain, and the CBM35 domain of two bifunctional proteins with beta-L-arabinopyranosidase/alpha-D-galactopyranosidase activities from Fusarium oxysporum 12S, Foap1 and Foap2 (Fo/AP1 and Fo/AP2), that are appended to GH27 domains. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). Some CBM35s bind their ligands in a calcium-dependent manner. In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. GH43 includes beta-xylosidases and beta-xylanases, using aryl-glycosides as substrates, while family GH27 includes alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases.


Pssm-ID: 271147  Cd Length: 125  Bit Score: 126.64  E-value: 4.86e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 681 YEAESASRSG-AAVIASCSGCSGSSAVGYIGGSGNGVLTFNNVASNASTRTTLRIKHMNGDTTQRYGTVTVNGV-AQTVA 758
Cdd:cd04081     3 YEAEAATLTGsAAAVSCSCGCSGGGAVGVGGGGNGGTVTFNNVTASAAGTYTLTIDYINGDVNDRNATVSVNGGaAQRVA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2008374040 759 FLPTADGATPGSSVVHVNLNSGsSNTVSIAAYNgGYVADVDRLMV 803
Cdd:cd04081    83 FPPTGGWNTPGSVTVLVDLKAG-SNTITFSNSG-GWAPDIDRITV 125
GH43_CtGH43-like cd18824
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ...
393-648 2.29e-32

Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350145 [Multi-domain]  Cd Length: 282  Bit Score: 127.15  E-value: 2.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 393 IQAHGGGMIKEGSTYYW------IGENKLNGSAFQSVNCYSSTNLVEWKYVGALLtLQSSGDlGPSRVVERPKVIYNPTT 466
Cdd:cd18824     1 IDAHDGKIYFFGGAYYWygtpygCGCGSCGFTLFCGFVVYSSVDLVNWTYRGVLF-DPNTCA-GSPGVCFRPHVVYNART 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 467 KQYVMYmhIDSSNyGEAKVGVATGSSVCGTYSYRGS--FQPLGFESRDMGLYKDTDGTAYLL--TEDRANGLRIDKLSDD 542
Cdd:cd18824    79 GRYVLW--YNAYD-GSSGYAVATSSTPTGPFVTVPDpvLAPAGLQAGDFSLFVDDDGTGYLAytTIDFPQSIVVEQLTDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 543 YLSVVSN-----VYKWAekyEAPAVIKsSAGVYFMFASqltgwNTN-------DNMYSTSTSLSGPW----------LSW 600
Cdd:cd18824   156 YLNTTGEyvrdlIDQEA---EAPSIFK-RNGIYYILAS-----NTCcgccqgtGARVYRATSPLGPWtrqidinscaGAL 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2008374040 601 KTFAPAGSrTWDSQTTFVLPIGNN-----FMYMGDRWFSSNLMR---STYVWLPLT 648
Cdd:cd18824   227 FPPSDSAY-TCGGQPTAVLPLPSPggetlYLYMGDRWRTAPDGRkghDGHYWQPLS 281
RRP14 pfam15459
60S ribosome biogenesis protein Rrp14; RRP14 is a family of nucleolar 60S ribosomal biogenesis ...
12-75 5.43e-25

60S ribosome biogenesis protein Rrp14; RRP14 is a family of nucleolar 60S ribosomal biogenesis proteins from eukaryotes. RRP14 functions in ribosome synthesis as it is required for the maturation of both small and large subunit rRNAs and it helps to prevent premature cleavage of the pre-rRNA at site C2. It also plays a role in cell polarity and/or spindle positioning 2],


Pssm-ID: 464729 [Multi-domain]  Cd Length: 62  Bit Score: 98.47  E-value: 5.43e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2008374040  12 SLEKHNKAFETLLQLIPARYYLPQERDDENNSSKYQKNKKKqSAPKQAvKEATKKARREKLDPA 75
Cdd:pfam15459   1 RLEAHNDFFDSLLSLIPAKFYLPPDETDESNSKKYSKNKKK-KAKKQA-KEASKKAKRAKLDPD 62
GH_F cd08978
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ...
396-633 4.10e-24

Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350092 [Multi-domain]  Cd Length: 251  Bit Score: 102.13  E-value: 4.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 396 HGGGMIKEGSTYYWIGENkLNGSAFQSVNCYSSTNLVEWKYVGALLTLQSSGDLGpSRVVERPKVIYNPTtKQYVMYMHI 475
Cdd:cd08978     1 ADPSILKDNGRYYIYATT-DDTGTGTGIVVWKSKDLVNWKEEGTVLSRGKSKSWG-TGNLWAPEVYYFNS-GKWYLYYSA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 476 dSSNYGEAKVGVATGSSVCG--TYSYRGSFQPLGFESRDMGLYKDTDGTAYLL--TEDRANGLRIDKLSDDYLSVVSNV- 550
Cdd:cd08978    78 -VPNGGGGRIYVATSDSPEGpfTPIVSGKLGDRGSGSIDPTVFVDDDGKLYLYygDEDDSGDIYVAELDPDLLTIKGDVt 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 551 -----YKWAEKY----EAPAVIKSSaGVYFMFASQLTGWNTNDNMYSTSTSLSGPWLSWKTFAP----AGSRTWDSQTTF 617
Cdd:cd08978   157 lligeVVGSGFRgnyfEGPAVFKRN-GYYYLIYSAGGTDGGYAIGYATSDSPLGPWEKASHNPGlqtsGATGIYGPGHGS 235
                         250
                  ....*....|....*.
gi 2008374040 618 VLPIGnnfmymGDRWF 633
Cdd:cd08978   236 IFQDE------GDRWY 245
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
400-597 2.21e-19

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 90.39  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 400 MIKEGSTYYWIGENklnGSAFQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNptTKQYVMYMHIDSSN 479
Cdd:COG3507    36 IIRVGDTYYLYGTS---FEYFPGLPIFHSKDLVNWELVGHALDRLPQWADPYSGGIWAPDIRYH--NGKYYLYYTAVDGG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 480 YGEAKVGVATGSSVCGTYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRANGLRIDKLSDDYLSVVSNVYK----WAE 555
Cdd:COG3507   111 KNRSGIGVATADDPEGPWSDPGPLVCPGGNGIDPSVFVDDDGKAYLVYGSGGGGIYVAELDPDTGKLLGEPKTlapgGEG 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2008374040 556 KY-EAPAVIKsSAGVYFMFASqlTGWNTNDN---MYSTSTSLSGPW 597
Cdd:COG3507   191 GWiEGPHIYK-RNGYYYLFYS--EGGTCNSGyavRVARSKSPTGPY 233
GH43_bXyl-like cd09004
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
408-597 3.32e-14

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350118 [Multi-domain]  Cd Length: 266  Bit Score: 73.41  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 408 YWI--GENKLNGSAFQSVNCYSSTNLVEWKYVGALLTLQ---SSGDLG---PSrVVERpkviynptTKQYVMYMHIDSsn 479
Cdd:cd09004    12 YYIypTTDGPPGWSSTSFHVFSSTDLVNWTDHGIILDLAndvWWANKGawaPA-VAER--------NGKYYFYFSAGS-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 480 ygeaKVGVATGSSVCGtySYRGSFQPL------GFESRDMGLYKDTDGTAYLLTedrANG-LRIDKLSDDYLS-----VV 547
Cdd:cd09004    81 ----QIGVAVSDSPTG--PFTDLGRPLvtggdyGGQAIDPMVFVDDDGQAYLYW---GNGtAYVARLNDDMVSfdgevVV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2008374040 548 SNVykwAEKY-EAPAVIKsSAGVYFMFASQlTGWNTNDN--MYSTSTSLSGPW 597
Cdd:cd09004   152 SIT---PPNFrEGPFVHK-RNGIYYLSWSE-NDTRDPDYrvRYATSDSPLGPW 199
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
400-601 7.95e-13

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 69.66  E-value: 7.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 400 MIKEGSTYYWIGENklnGSAFQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNpTTKQYVMYMHIDSSN 479
Cdd:pfam04616  15 ILRVGDDYYLTTSS---FEWFPGIPIFHSKDLVNWKLVGPVLVRRSQLSGRGSNASWAPDISYH-DGKYYLYYTAVAHGI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 480 YgeakvgVATGSSVCGTYSYRGSFQPLGFeSRDMGLYKDTDGTAYLL-----TEDRANGLRIDKLSDDYLSVVSNVYK-- 552
Cdd:pfam04616  91 F------VATADSPDGPWSDPGKLKSGGG-GIDPSLFHDDDGKKYLVwggwdPRHGHGGIYLQELDNDGLKLVGPVTKli 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2008374040 553 WAEK-------YEAPAVIKSSAGVYFMFASQLTGWnTNDNMYSTSTSLSGPWLSWK 601
Cdd:pfam04616 164 YPGTrwvggkvTEGPHLYKRNGYYYLTYAAGGTGG-PYAVGVARSRSPLGPYEWHP 218
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
400-597 2.94e-12

Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580); This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350105 [Multi-domain]  Cd Length: 283  Bit Score: 67.97  E-value: 2.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 400 MIKEGSTYYWIGENKLNGSAFqsvNCYSSTNLVEWKYVGALLTlqssgdlGPSRVVER----PKVIYNPTTkqYVMY--- 472
Cdd:cd08991     5 VLKHNGTYYLYGTGGDDGRGF---KVYVSDDLVNWEYPGGALE-------EPGLWGTKgfwaPEVFYYNGK--FYMYysa 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 473 MHIDSSNygeaKVGVATGSSVCGTYSYRG-SFQPLGFESRDMGLYKDTDGTAYL------LTEDRANGLRIDKLSDDYLS 545
Cdd:cd08991    73 NGGDHGE----HIAVAVSDSPLGPFRDKGkLLIPAGGFSIDAHVFIDDDGKWYLyyvrddLGGEPGNRIYVAELEDDLSL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2008374040 546 VVSNV------YKWAEKY---------EAPAVIKsSAGVYFMFASqltgwnTNDNM-------YSTSTSLSGPW 597
Cdd:cd08991   149 IGEPTlvlcptADERWEYgegrdwhttEGPTVLK-HNGTYYLTYS------ANHFRspdyavgYATADSPLGPW 215
GH43_ABN cd08988
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ...
396-598 5.96e-12

Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350102 [Multi-domain]  Cd Length: 277  Bit Score: 67.16  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 396 HGGGMIKEGSTYYWIGenklNGSAFQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVER----PKVIYNptTKQYVM 471
Cdd:cd08988     1 HDPSIIKEGGTYYAFG----TGTDGFGIPIAKSKDLGNWTIVGEAFATLPSWKGGSPPSADGnlwaPDISQH--KGKYYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 472 YMHIDSSNYGEAKVGVATGSSVCGTYSYRGSFQPlGFESRDMG------LYKDTDGTAYLLTEDRANGLRIDKLSDDYLS 545
Cdd:cd08988    75 YYSVSDNGSNTSAIGLATANNPQGPFKDEGPAKP-VVTSDNAGnaidpdLFQDEDGQNWLLYGSFWGGIWLQKLDKNGLV 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2008374040 546 VVSNVYKWAE------KYEAPAVIKSSaGVYFMFASQ---LTGWNTNDNM-YSTSTSLSGPWL 598
Cdd:cd08988   154 VNPPGNGKSIavlyyvSIEAPYITYAG-GYYYLFVSAgscCDGGNSTYHTrVGRSKKVTGPYL 215
GH43_AXH_like cd08990
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ...
425-597 1.05e-11

Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase; This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350104 [Multi-domain]  Cd Length: 269  Bit Score: 66.08  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 425 CYSSTNLVEWKYVGALLtlqssgdlgPSRVVER--------PKVIYNPTTkqYVMY--MHIDSSNYGeakVGVATGSSVC 494
Cdd:cd08990    34 VFSSTDLVNWTDHGEIL---------PPDDVFWwasgnawaPDAVYKNGK--YYFYfpVGQASDGFG---IGVAVSDSPA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 495 G-----TYSYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDRaNGLRIDKLSDDYLSVVSNVYKWAEK-----YEAPAVIK 564
Cdd:cd08990   100 GpfkdaLGKPLIPEGLNGIEGIDPAVFVDDDGRAYLYFGGG-GGYYVAKLKDDMISLAGEPQKIKNGglkgfFEAPWVFK 178
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2008374040 565 sSAGVYFMFASqlTGWNTNDNM-YSTSTSLSGPW 597
Cdd:cd08990   179 -RNGTYYLSYA--GGWAYPAEIaYSTADSPLGPY 209
GH43_ABN-like cd08999
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ...
401-597 3.62e-11

Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350113 [Multi-domain]  Cd Length: 284  Bit Score: 64.86  E-value: 3.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 401 IKEGSTYYWIGENklngSAFQSVNCYSSTNLVEWKYVG--ALltlqssGDLGPSRVVER----PKVIYNPTTKqYVMYmh 474
Cdd:cd08999    14 IRVGGTYYAFATN----SGGKNVQVATSTDLVTWTLLGgdAL------PDLPAWAAAGGntwaPDVVRRPDGK-YVMY-- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 475 idssnY-GEAK------VGVATGSSVCGTYSYRGS--FQPL-GFESRDMGLYKDTDGTAYLL--TEDRANG----LRIDK 538
Cdd:cd08999    81 -----YsARLKssgkhcIGVATSDSPLGPFTPVGEppLCPLdQGGAIDPSGFVDPDGKRYLVykVDGNSIGvptpIMLQE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 539 LSDDYLSVV-------SNVYKWAEKY-EAPAVIKsSAGVYFMFASqlTGWNTNDN---MYSTSTSLSGPW 597
Cdd:cd08999   156 LSADGLTLVgepvellLNDGPWDGPLvEAPSLVK-RDGTYYLFYS--SNCYCSPSyavGYATSKSITGPY 222
CBM35_pectate_lyase-like cd04082
Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes ...
681-803 4.25e-08

Carbohydrate Binding Module family 35 (CBM35), pectate lyase-like; appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans; This family includes carbohydrate binding module family 35 (CBM35) domains that are non-catalytic carbohydrate binding domains that are appended mainly to enzymes that bind mannan (Man), xylan, glucuronic acid (GlcA) and possibly glucans. Included in this family are CBM35s of pectate lyases, including pectate lyase 10A from Cellvibrio japonicas, these enzymes release delta-4,5-anhydrogalaturonic acid (delta4,5-GalA) from pectin, thus identifying a signature molecule for plant cell wall degradation. CBM35s are unique in that they display conserved specificity through extensive sequence similarity but divergent function through their appended catalytic modules. They are known to bind alpha-D-galactose (Gal), mannan (Man), xylan, glucuronic acid (GlcA), a beta-polymer of mannose, and possibly glucans, forming four subfamilies based on general ligand specificities (galacto, urono, manno, and gluco configurations). In contrast to most CBMs that are generally rigid proteins, CBM35 undergoes significant conformational change upon ligand binding. Some CBM35s bind their ligands in a calcium-dependent manner, especially those binding uronic acids.


Pssm-ID: 271148  Cd Length: 124  Bit Score: 52.18  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 681 YEAESASRSGAAVIASCSgcsgssavGYiggSGNGVLTFNNVA-------SNAST--RTTLRIKHMNGDTTQRYGTVTVN 751
Cdd:cd04082     3 YQAEDASVDQGVIESNHA--------GY---TGSGFVNTDNAVgsyiewtVNAPTagTYTLTFRYANGSTSNRPADISVN 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2008374040 752 G--VAQTVAFLPTADGATPGSSVVHVNLNSGsSNTVSIAAYNGGYVADVDRLMV 803
Cdd:cd04082    72 GntVAATLSFPSTGAWTTWATSSVTVPLNAG-TNTIRLTATTAEGLPNIDYLTV 124
CBM35_Lmo2446-like cd04083
Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446; This family includes ...
681-803 2.46e-07

Carbohydrate Binding Module 35 (CBM35) domains similar to Lmo2446; This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes. Some CBM35 domains belonging to this family are appended to glycoside hydrolase (GH) family domains, including glycoside hydrolase family 31 (GH31), for example the CBM35 domain of Lmo2446, an uncharacterized protein from Listeria monocytogenes EGD-e. These CBM35s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. GH31 has a wide range of hydrolytic activities such as alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, or alpha-1,4-glucan lyase, cleaving a terminal carbohydrate moiety from a substrate that may be a starch or a glycoprotein. Most characterized GH31 enzymes are alpha-glucosidases.


Pssm-ID: 271149  Cd Length: 125  Bit Score: 50.33  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 681 YEAESASRSGAAVIASCSGcsgssavGYIG-------GSGNGVLTFNNVASNASTrTTLRIKHMNGDTTQRYGTVTVNGV 753
Cdd:cd04083     3 YEAENAALSGGAVVNTDHA-------GYSGtgfvdgfATAGASVTFTVNVPAAGT-YTLTLRYANGTGSAKTLSLYVNGT 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2008374040 754 -AQTVAFLPTADGATPGSSVVHVNLNSGsSNTVSIaAYNGGYVADV--DRLMV 803
Cdd:cd04083    75 kVKQVSLPSTGSWDTWGTATETVTLRAG-TNTIEL-RYDAGDSGNVnlDNITV 125
GH43_Xsa43E-like cd18618
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ...
425-597 2.66e-07

Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350130 [Multi-domain]  Cd Length: 275  Bit Score: 52.99  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 425 CYSSTNLVEWKYVGALLTLQS----SGDLGPSRVVERpkviynpTTKQYvMYMHIDSSNYGEAKVGVATGSSVCGTY--- 497
Cdd:cd18618    37 VFSTTDMVNWTDHGAVLSLKDfswaKGDAWAGQVIER-------NGKFY-WYVPVHHKTNGGFAIGVAVSDSPTGPFkda 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 498 -------SYRGSFQPLGFESRDMGLYKDTDGTAYLLTEDraNGLRIDKLSDDYLSVVSNVYKWAEK-----YEAPAVIKS 565
Cdd:cd18618   109 lgkplitNDMTGTTNHSWDDIDPTVFIDDDGQAYLYWGN--PELYYVKLKEDMISLDGEIGTIDISglpdfTEAPWVHKR 186
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2008374040 566 SAGVYFMFASqltGWNTNDNmYSTSTSLSGPW 597
Cdd:cd18618   187 NGLYYLSYAA---GFPEKIA-YATSDSPTGPW 214
GH43_ABN-like cd18616
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ...
400-598 2.95e-07

Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350128 [Multi-domain]  Cd Length: 291  Bit Score: 52.96  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 400 MIKEGSTYYWI---GENKLNGSAFQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIY-NpttKQYVMYMHI 475
Cdd:cd18616    13 VIRGDDGYFYAyatEDPWGDGGGFRLVPILRSKDLVNWEYVGDAFTSKPRWKWDPGGGLWAPDIRYiD---GKYVLYYSL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 476 -DSSNYGEAKVGVAT-----------GSSVCGT-YSYRGSFQPLGFEsrdmglykdTDGTAYLLTEDRaNGLRIDKLSDD 542
Cdd:cd18616    90 sDWGADPNPGIGVATadspagpftdqGKLFDSNeIGVRNSIDPFVFE---------DDGKKYLFWGSF-YGIYAVELTAD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2008374040 543 YLSVVSNVYKW--AEKYEAPAVIKSSaGVYFMFASQLTGWNTNDNMYST----STSLSGPWL 598
Cdd:cd18616   160 GLALKPGEKVQiaGDRYEGPYIVKRD-GYYYLFGSAGSCCEGPNSTYRVvvgrSESLLGPYV 220
PTZ00121 PTZ00121
MAEBL; Provisional
177-374 5.55e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 5.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  177 EEQRRKRGILREKRRQATRERKRNEEAgKQKKPAAQERAKVHQTNTQLIVPDPVPGESSSGMANVTFSAIASSGGPSKAK 256
Cdd:PTZ00121  1209 EEERKAEEARKAEDAKKAEAVKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  257 KYATATDPRAA-----LSQLASRNEKLSSLPAEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTAKRKEKEKLKSKAE 331
Cdd:PTZ00121  1288 EKKKADEAKKAeekkkADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2008374040  332 WNK------RKEALSANMAAKQKKRTDNIAQRNERRNDARKGIKPKAAA 374
Cdd:PTZ00121  1368 AAEkkkeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
PTZ00121 PTZ00121
MAEBL; Provisional
147-369 1.51e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  147 VRAKLHARINGLKQERGGLTGEPGSRDELLE--EQRRKRGILR--EKRRQATRERKRNEEAGKQ---KKPAAQERAKVHQ 219
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKADELKkaEEKKKADEAKkaEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADA 1333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  220 TNTQlivpdpvpGESSSGMANVtfsaiaSSGGPSKAKKYATATDPRAALSQLASRNEKLSSlPAEKRKAiEERSRWEKAE 299
Cdd:PTZ00121  1334 AKKK--------AEEAKKAAEA------AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKA-EEKKKADEAK 1397
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  300 IRAEGGKVHDDATRLKKTAKRKEKEkLKSKAEwnKRKEALSANMAAKQKKRTDNIAQRNERRNDARKGIK 369
Cdd:PTZ00121  1398 KKAEEDKKKADELKKAAAAKKKADE-AKKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
PTZ00121 PTZ00121
MAEBL; Provisional
177-377 2.13e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  177 EEQRRKRGILR---EKRRQATRERKRNEEAGKQKKPAAQERAKVHQTNTQlivPDPVPGESSSGMANVTFSAIASSGGPS 253
Cdd:PTZ00121  1325 EEAKKKADAAKkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE---EAKKKADAAKKKAEEKKKADEAKKKAE 1401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  254 KAKKYATATDPRAALSQLAS----------RNEKLSSLPAEKRKAIEERSRWEKAEiRAEGGKVHDDATRLKKTAKRKEK 323
Cdd:PTZ00121  1402 EDKKKADELKKAAAAKKKADeakkkaeekkKADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAE 1480
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2008374040  324 EK-----LKSKAEWNKRKeALSANMAAKQKKRTDNIAQRNERR--NDARKGIKPKAAATLQ 377
Cdd:PTZ00121  1481 EAkkadeAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKkaDEAKKAEEAKKADEAK 1540
PTZ00121 PTZ00121
MAEBL; Provisional
40-372 3.58e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040   40 ENNSSKYQKNKKKQSAPKQAvKEATKKAR-REKLDPANNKSilDIQREAAGVQSLA-----SSNAKQKGKQRATSEDGDS 113
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKA-DEAKKKAEeKKKADEAKKKA--EEAKKADEAKKKAeeakkAEEAKKKAEEAKKADEAKK 1477
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  114 DDPDVEMADLSDTPDASVPAAAQPMPSYESISTVRAKLHARINGLKQERGGLTGEPGSRDEL--LEEQRRKRGILREKRR 191
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkkAEEKKKADELKKAEEL 1557
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  192 QATRERKRNEEAGK--QKKPAAQERAKV-HQTNTQLIVPDPVPGESSSGMAnvTFSAIASSGGPSKAKKYATATDPRAAL 268
Cdd:PTZ00121  1558 KKAEEKKKAEEAKKaeEDKNMALRKAEEaKKAEEARIEEVMKLYEEEKKMK--AEEAKKAEEAKIKAEELKKAEEEKKKV 1635
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  269 SQLASRNEKlsslpaEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTAKRKEKEKLKSKAEWNKRKEALSANM----- 343
Cdd:PTZ00121  1636 EQLKKKEAE------EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeelkk 1709
                          330       340       350
                   ....*....|....*....|....*....|
gi 2008374040  344 -AAKQKKRTDNIAQRNERRNDARKGIKPKA 372
Cdd:PTZ00121  1710 kEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
GH43_FsAxh1-like cd09001
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ...
400-603 1.16e-05

Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase; This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350115 [Multi-domain]  Cd Length: 270  Bit Score: 47.89  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 400 MIKEGSTYYWIGenklngsafqSVNCYS-------STNLVEWKYVG-ALLTLqssgDLGPSRVVERPKVIYN-----PTT 466
Cdd:cd09001    16 VIRVGDTYYMVS----------STMHFSpgapilhSKDLVNWEIVGyVVDRL----DDGDAYYLEDGKNAYGkgiwaPSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 467 KQ-----YVMYmhidSSNYGeaKVGVATGSSVCGTYSYRgSFQPLGFEsrDMGLYKDTDGTAYLLTedrANG-LRIDKLS 540
Cdd:cd09001    82 RYhngkfYVYF----CTNTG--GTYVYTADDPAGPWSRP-ALIGKGYH--DPSLLFDDDGKAYLVY---GNGeIRLTELS 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2008374040 541 DDYLSVVSN---VYKWAEK---YEAPAVIKSSaGVYFMFASQLTGWnTNDNMYSTSTSLSGPWLSWKTF 603
Cdd:cd09001   150 PDGTGVGGEgrvIIDGTEEglgAEGSHLYKIN-GYYYIFNIEWGGG-GRTQVVLRSKSLYGPYEGRVVL 216
GH43_BT3675-like cd18828
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
424-597 1.24e-05

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675); This glycosyl hydrolase family 43 (GH43) subgroup includes the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the GH43_bXyl subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl subgroup also includes enzymes annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350149 [Multi-domain]  Cd Length: 283  Bit Score: 47.66  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 424 NCYSSTNLVEWKYVGALLTLQSSGDL--------GPSrVVERpkviynptTKQYVMYMHIDSSNyGEAKVGVATGSSVCG 495
Cdd:cd18828    30 HVFSSDDLVTWKDEGVILDLKNDQVVpwatgnawAPT-IEER--------DGKYYFYFCGKNPD-GRSQIGVAVADSPTG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 496 TYSYRGsfQPLGFESRD---MG-------LYKDTDGTAYLLTedrANG-LRIDKLSDDYLSVVSNVYKWAEK----YEAP 560
Cdd:cd18828   100 PFTAQG--SPLITHEMArvtMGqaidpsvFTDPVDGKYYLYW---GNGyAAIAELNDDMISIKPGTLVNLDGltdfREAV 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2008374040 561 AVIKSSAGVYFMFASQLTG---WNTNdnmYSTSTSLSGPW 597
Cdd:cd18828   175 TVLYRDGLYHFTWSCDDTGsenYHVN---YGTSDSPYGPI 211
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
403-609 2.20e-05

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655; This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350097  Cd Length: 262  Bit Score: 46.84  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 403 EGSTYY------WIGEN-KLNGSafQSVNCYSSTNLVEWKYVgALLTLQSSGDLGpsrvveR---PKVIYNPTTKQYVMY 472
Cdd:cd08983    28 EDGKFYlvatdlWIAGGaQWNGS--RGIGVWESTDLVNWSEQ-RLVKMVSPPNAG------NawaPEAIYDPETGQYVVY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 473 MHidSSNYGEAKvgvaTGSSVCgTYSYRGSFQ----PLGFESRDMGlYKDT-----DGTAYLLTEDRANGLRI-----DK 538
Cdd:cd08983    99 WS--SSLYGDGG----GGNHRI-YYATTKDFKtfsePKVLFDPGFN-VIDTtivkdGGTYYRFYKDETTGKGIrlatsDS 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2008374040 539 LSDDYLSVVSNVYK-WAEKYEAPAVIKS-SAGVYFMFASQLTGWNtndNMYSTSTSLSGPWLSWKT---FAPAGSR 609
Cdd:cd08983   171 LTGPWTTVTTGGGAgTGGGVEGPTVFKLnDGGKWYLYYDQYGGGG---YGPFETTDLASGTWTPASedySLPGGPR 243
GH43_XynD-like cd09003
Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan ...
388-597 6.08e-05

Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as AXH activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350117 [Multi-domain]  Cd Length: 315  Bit Score: 45.72  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 388 GTNQHIQAHGGGMIKEgSTYYWIgenklngsafQSVNCYSSTNLVEWKYVGALLTLQSSGDLGPSRVVERPKVIYNPTTK 467
Cdd:cd09003    25 GTNDDQQYNANGKKKD-NSYYNI----------NSLTVISSDDMVNWTDHGEIPVAGPNGIAKWAGNSWAPSVAYKNING 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 468 QYVMYMHIDSSNYGeakVGVATGSSVCGTYS--------YRGSFQPLG----FesrDMGLYKDTDGTAYL--------LT 527
Cdd:cd09003    94 KDKFYLYFANGGGG---IGVLTADSPTGPWTdplgkpliTRSTPGCAGvvwlF---DPAVFIDDDGQGYLyfgggvpgGS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 528 EDRANGLRIDKLSDDYLSVVSNvykwAEKYEAPavikssagvYFMFASQL------------TGWNTNDNM--------- 586
Cdd:cd09003   168 EANPKTARVIKLGDDMISVDGS----AVTIDAP---------YFFEASGInkingkyyysycTNFSGRDDPaypgagsia 234
                         250
                  ....*....|.
gi 2008374040 587 YSTSTSLSGPW 597
Cdd:cd09003   235 YMTSDNPMGPF 245
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
104-365 7.28e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 46.10  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 104 QRATSEDGDSDDPDVEmadlsdTPDASVPAAAQPMPsyESISTVRAKLHARINGLKQERGGLTGE-PGS----RDELLEE 178
Cdd:pfam15709 107 EADTVQNGDGEDYDVH------HLHRGLPRHRPESP--EKLTAVDTSLLPRAREGKTEPRLFNQEtPASishaERELIDK 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 179 QRRKRGILREKRRQATRER--KRNEEA-------------------GKQKKPAAQ----ERAKVHQTNTQLIVPDPVPGE 233
Cdd:pfam15709 179 AKRRKGTKTDKTKTPKRERegKVHGEAeaavgksreskaekkseliSKGKKTGAKrkrtQKERNLEVAAELSGPDVINSK 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 234 SSSGMANV-TFSAIASSGGPSKAKKYAT-----ATDPRAALSQLA-------SRNEKLSSLPA-------EKRKAIEERS 293
Cdd:pfam15709 259 ETEDASERgAFSSDSVVEDPWLSSKYDAeesqvSIDGRSSPTQTFvvtgnmeSEEERSEEDPSkallekrEQEKASRDRL 338
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2008374040 294 RWEKAEIRaeggkvhddatRLKKTAKRKEKEKLKS-KAEWNKRKEALSANMAAKQKKRTDNIAQRNERRNDAR 365
Cdd:pfam15709 339 RAERAEMR-----------RLEVERKRREQEEQRRlQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEER 400
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
136-407 8.42e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 136 QPMPSYESISTV---RAKLHARINGLKQERGGLTGEPGSRDELLE---EQRRKRGILREKRRQATRERKRNEEAGKQKKP 209
Cdd:TIGR02794  30 EPGGGAEIIQAVlvdPGAVAQQANRIQQQKKPAAKKEQERQKKLEqqaEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 210 AAQERAKVHQTntqlivpdpvpgesssgmanvtfsaiassggpSKAKKYATATDPRAALSQLASRNEKlsslPAEKRKAI 289
Cdd:TIGR02794 110 AAKQAEEKQKQ--------------------------------AEEAKAKQAAEAKAKAEAEAERKAK----EEAAKQAE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 290 EERSRWEKAEIRAEGgkvhdDATRLKKTAKRKEKE--KLKSKAEWNKRK-EALSANMAAKQKKRTDNIAQRNERRNDARK 366
Cdd:TIGR02794 154 EEAKAKAAAEAKKKA-----EEAKKKAEAEAKAKAeaEAKAKAEEAKAKaEAAKAKAAAEAAAKAEAEAAAAAAAEAERK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2008374040 367 GikpkAAATLQIVPAATwTASGTNQHIQAHGGGMIKEGSTY 407
Cdd:TIGR02794 229 A----DEAELGDIFGLA-SGSNAEKQGGARGAAAGSEVDKY 264
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
149-375 9.99e-05

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 45.74  E-value: 9.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 149 AKLHARINGLKQER--GGLTGEPGSRDELLEEQRR-------KRGILREKRRQATRERKRNEEAGKQKKPAAQERAKVHQ 219
Cdd:PRK07735   28 AKHGAEISKLEEENreKEKALPKNDDMTIEEAKRRaaaaakaKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 220 TNTQL-IVPDPVPGESSSgmanvtfSAIASSGGPSKAKKYATATDPRAALSQLASRNEKLSSLPAEKRKAieersrwEKA 298
Cdd:PRK07735  108 LAKQKrEGTEEVTEEEKA-------AAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAA-------AAA 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2008374040 299 EIRAEGGKVHDDATRLKKTAKRKEKEKLKSKAEWNKRKEALSANMAAKQKKRTDNIAQRNERRNDARKGIKPKAAAT 375
Cdd:PRK07735  174 KAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAA 250
GH43-like cd08986
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ...
426-597 1.06e-04

Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350100 [Multi-domain]  Cd Length: 257  Bit Score: 44.91  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 426 YSSTNLVEWKYVGALLTLQSSG--DLGPSRVVERPKV---IYNPTTkQYV--MYMHIDSSNYGEAKVGVATGSSVCGTYS 498
Cdd:cd08986    36 WRSKDLKDWEYLGLVWDLEKDGwwQWEPQWWTPDSKNkraLWAPEI-HYIngTWYITHSMNGGGTGLLKSTTGKPEGPYV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 499 YRGSFqplGFESR-DMGLYKDTDGTAYLLTedrANGLrIDKLSDDYLSVVSNVYK-----WAEKYEAPAVIKSSAGVYFM 572
Cdd:cd08986   115 DPMGG---PLGKGiDPSLFEDDDGTVYLVW---GNGQ-IARLKKDMSGFAEEPRKidpsgNREIGHEGAFIFKIGGKYVL 187
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2008374040 573 FAsqlTGWNTN-------DNMYSTSTSLSGPW 597
Cdd:cd08986   188 FG---AAWSTDkmrkgtyDLYYATSDSIYGPY 216
GH43_XlnD-like cd18827
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ...
425-596 2.34e-04

Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350148 [Multi-domain]  Cd Length: 277  Bit Score: 43.81  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 425 CYSSTNLVEWKYVGALLTLQSSgdlgPS--RVVERPKVIYNPtTKQYVMYMHIDSSNYGEAK-VGVATGSSVCGTYS-YR 500
Cdd:cd18827    30 AFSSPDLVHWTKHERILDMADV----PWanRAVWAPSVIEKN-GKYYLYFAANDIQSDDEGGgIGVAVADRPEGPFKdAL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 501 GsfQPL------GFESRDMGLYKDTDGTAYLLTEDR--ANglrIDKLSDDYLSVV----SNVYKW--AEKY-EAPAVIKS 565
Cdd:cd18827   105 G--KPLigefhnGAQPIDQHVFKDDDGQAYLYYGGWghCN---VAKLNDDMTSLVpfddGETFKEitPEGYvEGPFMFKR 179
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2008374040 566 SAGVYFMFASqlTGWNTNDNM--YSTSTSLSGP 596
Cdd:cd18827   180 NGKYYFMWSE--GGWTGPDYSvaYAVADSPLGP 210
GH43_XYL-like cd08989
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ...
401-643 2.82e-04

Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350103 [Multi-domain]  Cd Length: 272  Bit Score: 43.50  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 401 IKEGSTYYwigenkLNGSAFQSVNC---YSSTNLVEWKYVGALLTLQSSGDLGP---SRVVERPKVIYNpTTKQYVMYMH 474
Cdd:cd08989    14 VRVGDDYY------MVNSTFQYFPGipiSHSKDLVHWTPIGHALTRPEQLDLTGgpdGGGIWAPDISYH-DGKFYIYYTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 475 IdsSNYGEAKVG---VATGSSVCGTYSYRGSFQPLGFesrDMGLYKDTDGTAYLLTEDRanGLRIDKLSDD---YLSVVS 548
Cdd:cd08989    87 V--LNVGSWKGRrnyLVTSEDPEGPWSEPVWLDEGGI---DPSLFVDDDGKHYMLLNPG--GIRLAELNPDctkQIGEPK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 549 NVYKWAEKY--EAPAVIKSSAGVYFMFASQLTGwnTNDNMYST-STSLSGPW--------LSWKT-FAPAGSRtwdSQTT 616
Cdd:cd08989   160 RIWEGTGGRapEGPHLYKKDGYYYLLTAEGGTG--YGHAITIArSKTIYGPYepcpynpiLRQQDpQAPLQRC---GHGK 234
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2008374040 617 FV-LPIGNNFM-YMGDRWF---SSNLMRSTYV 643
Cdd:cd08989   235 LVeTPDGEWWMvYLCGRPLpggYCPLGRETAL 266
CBM35_mannanase-like cd04086
Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, ...
681-803 4.03e-04

Carbohydrate Binding Module 35 (CBM35); appended to several carbohydrate binding enzymes, including several glycoside hydrolase (GH) family 26 mannanase domains; This family includes carbohydrate binding module 35 (CBM35) domains that are appended to several carbohydrate binding enzymes, including periplasmic component of ABC-type sugar transport system involved in carbohydrate transport and metabolism, and several glycoside hydrolase (GH) domains, including GH26. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the strong binding of the GH catalytic modules with their dedicated, insoluble substrates. Examples of proteins having CMB35s belonging to this family are mannanase A from Clostridium thermocellum (GH26), Man26B from Paenibacillus sp. BME-14 (GH26), and the multifunctional Cel44C-Man26A from Paenibacillus polymyxa GS01 (which has two GH domains, GH44 and GH26). GH26 mainly includes mannan endo-1,4-beta-mannosidase which hydrolyzes 1,4-beta-D-linkages in mannans, galacto-mannans, glucomannans, and galactoglucomannans, but displays little activity towards other plant cell wall polysaccharides. A few proteins belonging to this family have additional CBM3 domains; these CBM3s are not found in the CBM6-CBM35-CBM36_like superfamily.


Pssm-ID: 271152  Cd Length: 119  Bit Score: 40.66  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 681 YEAESASRSGAAVIASCSGCSGSsavGYIGG--SGNGVLTFN-NVASNAstRTTLRIKHMnGDTTQRYGTVTVNGVAQTV 757
Cdd:cd04086     3 YEAEDGTLTGVTVATSRSGYSGT---GYVTGfdDDGDSLTFTvNVPEAG--LYDLVIRYA-APYGDKENNLYVNGTSVGE 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2008374040 758 AFLPTADGATPgSSVVHVNLNSGsSNTVSIAAYNGGYvaDVDRLMV 803
Cdd:cd04086    77 ISFPATTKFTE-VSAGKVLLNAG-ENTITIENSWGWY--DIDYITV 118
PTZ00121 PTZ00121
MAEBL; Provisional
8-371 4.25e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040    8 ELRASLEKHNKAFEtllqlipARYYLPQERDDENNSSKYQKNKKKQSAPKQAvkEATKKARREKLDPANNKSILDIQREA 87
Cdd:PTZ00121  1435 EAKKKAEEAKKADE-------AKKKAEEAKKAEEAKKKAEEAKKADEAKKKA--EEAKKADEAKKKAEEAKKKADEAKKA 1505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040   88 AGVQSLASSNAKQKGKQRAtsedgDSDDPDVEMADLSDTPDASVPAAAQPMPSYESISTVRAKLHARINGLKQERGGLTG 167
Cdd:PTZ00121  1506 AEAKKKADEAKKAEEAKKA-----DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  168 EPGSRDELLEEQRRKRGIL---REKRRQATRERKRNEEAGK--QKKPAAQERAKVHQTNTQLIVPDPVPGESSSGMANVT 242
Cdd:PTZ00121  1581 RKAEEAKKAEEARIEEVMKlyeEEKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  243 FSAIASSGGPSKAKKyaTATDPRAALSQLASRNEKLSSLPAEKRKaIEERSRWEKAEIR-AEGGKVHDDATRLKKTAKRK 321
Cdd:PTZ00121  1661 IKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEEAKK-AEELKKKEAEEKKkAEELKKAEEENKIKAEEAKK 1737
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2008374040  322 EKEKLKSKAEwNKRKEALSANMAAKQKKRTDNIAQ--RNERRNDARKGIKPK 371
Cdd:PTZ00121  1738 EAEEDKKKAE-EAKKDEEEKKKIAHLKKEEEKKAEeiRKEKEAVIEEELDEE 1788
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
241-366 5.19e-04

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 41.60  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 241 VTFSAIASSGGPSKAKKYATATDPRAALSQLASRNEKLSSlpAEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTAKR 320
Cdd:pfam11600   2 RSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERL--KEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2008374040 321 KEK-EKLKSKAewNKRK---EALSANMAAKQKKRTDNIAQRNERRNDARK 366
Cdd:pfam11600  80 KEKaEKLRLKE--EKRKekqEALEAKLEEKRKKEEEKRLKEEEKRIKAEK 127
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
177-374 5.93e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 43.40  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 177 EEQRRKRGILREKRRQATRERKRNEEAGKQKKPAAQERAKvhqtntqliVPDPVPG---ESSSGMANVTFSAIASSGGPS 253
Cdd:PRK05035  444 EKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAK---------DKDAVAAalaRVKAKKAAATQPIVIKAGARP 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 254 KAKKYATATDPRAALSQLASRNEKLSSLPAEKRKAIE---ERSRWEKAEiRAEGGKVHDDATRLKKTAKRKEKEKLKSK- 329
Cdd:PRK05035  515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAaaiARAKAKKAA-QQAANAEAEEEVDPKKAAVAAAIARAKAKk 593
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 330 --------------AEWNKRKEALSANMA-AKQKKRTDNIAQRNERRNDARKGIKPKAAA 374
Cdd:PRK05035  594 aaqqaasaepeeqvAEVDPKKAAVAAAIArAKAKKAEQQANAEPEEPVDPRKAAVAAAIA 653
PTZ00121 PTZ00121
MAEBL; Provisional
10-366 9.99e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 9.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040   10 RASLEKHNKAFETLLQLIPARYYLPQERDDENNSSKYQKNKKKQSapKQAVKEATKKARREKLDPANNKSildiqREAAG 89
Cdd:PTZ00121  1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE--KKKADEAKKAEEKKKADEAKKKA-----EEAKK 1316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040   90 VQSLASSNAKQKGKQRATSEDGDSDDPDVEMADLSDTPDASVPAAAQPMPSYESISTVRAKLHARINGLKQErggltgEP 169
Cdd:PTZ00121  1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE------EK 1390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  170 GSRDEL---LEEQRRKRGILREK---RRQATRERKRNEEAGK--QKKPAAQERAKVHQTNTQlivpdpvpGESSSGMANV 241
Cdd:PTZ00121  1391 KKADEAkkkAEEDKKKADELKKAaaaKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKK--------AEEAKKAEEA 1462
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  242 TFSAiassggpsKAKKYATATDPRAalsQLASRNEKLSSLPAEKRKAIEERSRWEKAEIRAEGGKVHDDATR---LKKTA 318
Cdd:PTZ00121  1463 KKKA--------EEAKKADEAKKKA---EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeAKKAE 1531
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 2008374040  319 KRKEKEKLKSKAEWNKRKEALSAN--MAAKQKKRTDNIAQRNERRNDARK 366
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEelKKAEEKKKAEEAKKAEEDKNMALR 1581
CBM6-CBM35-CBM36_like cd02795
Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module ...
681-801 1.09e-03

Carbohydrate Binding Module 6 (CBM6) and CBM35_like superfamily; Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules. This alignment model also contains the C-terminal domains of bacterial insecticidal toxins, where they may be involved in determining insect specificity through carbohydrate binding functionality.


Pssm-ID: 271143  Cd Length: 124  Bit Score: 39.86  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 681 YEAESASRSGAAVIASCSGCSGSSAVGYIGGSGnGVLTFNNVASNASTRtTLRIKHMNGDT-TQRYGTVTVNGVAQTVAF 759
Cdd:cd02795     2 IEAEDATLTGGTAVSTAAGASGGGYVIGFSSGG-DSVTFTVTVPKAGTY-RLAVRYASPNGnGSRSVSLDGNGKLVGTIT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2008374040 760 LPTADGATPGSSVVH-VNLNSGSSNTVSIAAYNGGYVADVDRL 801
Cdd:cd02795    80 VPSTGGWDTWGTASVsVNLPDAGGHTLKIVGTGDNGGANIDYV 122
GH43_GsAbnA-like cd18832
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1, ...
401-598 3.07e-03

Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 350153 [Multi-domain]  Cd Length: 332  Bit Score: 40.70  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 401 IKEGSTYYWIGENklngsafqsVNCYSSTNLVEWKYVGALLTLQSS--GDLGPSRVVER--------------PKVIYNP 464
Cdd:cd18832     7 VKDDGTYYVFGSH---------LAAAKSTDLMNWTQFTNGVTTDNPllFNLFDSTAWELaedfnwagggnlwaPDVIYNK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 465 TTKQYVMYMHIdSSNYGEAKVGVATGSSVCGTYSYRGS-----FQPLGFESRDMGLYK------------------DTDG 521
Cdd:cd18832    78 AMGKYCMYYSV-SGDDSPSAIGLATADNIEGPYTYKGTvlksgFTGSTSADADVYLTGgkynnnyhpnaidpcvfyDKDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 522 T-----------AYLLTEDRANGLRI------DKLSDDYLSVvsnvyKWAEKY----EAPAVIKS-SAGVYFMFASqlTG 579
Cdd:cd18832   157 KlwmvygswsggIFLLELDPKTGLRDysvetdGNLPDQYYGK-----KIAGGYhasgEGPYILYDkDTGYYYLFVS--YG 229
                         250       260
                  ....*....|....*....|...
gi 2008374040 580 WNTNDNMYST----STSLSGPWL 598
Cdd:cd18832   230 GLDANGGYNIrvfrSKNPDGPYV 252
PTZ00121 PTZ00121
MAEBL; Provisional
159-372 3.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  159 KQERGGLTGEPGSRDELLEEQRRKRGILREKRRQATRERKRNEEAGKQKKPAAQERAKVHQTNTQlivpdpvpGESSSGM 238
Cdd:PTZ00121  1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK--------AEEAKKA 1317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  239 ANVTFSAIASSGGPSKAKKYATATDPRAalsQLASRNEKLSSLPAEKRKAIEERSRWEKAEIRAEGGKVHDDATRLKKTA 318
Cdd:PTZ00121  1318 DEAKKKAEEAKKKADAAKKKAEEAKKAA---EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040  319 KRKEK-EKLKSKAEWNKRKE-----ALSANMAAKQKKRTDNIAQRNERRNDARKgIKPKA 372
Cdd:PTZ00121  1395 EAKKKaEEDKKKADELKKAAaakkkADEAKKKAEEKKKADEAKKKAEEAKKADE-AKKKA 1453
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
256-396 3.85e-03

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 40.60  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2008374040 256 KKYATATDPRA-ALSQLASRNEKLSSLPAEKRKAIEERSR-----WEKAEIRAEGgkvhddaTRLKKTAK-RKEKEKLKS 328
Cdd:PRK00247  275 RKYPLTDEFKEhHAEQRAQYREKQKEKKAFLWTLRRNRLRmiitpWRAPELHAEN-------AEIKKTRTaEKNEAKARK 347
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2008374040 329 KAEWNKRKEALSANMAAKQKKRTDNIAQRNERRNDARKGIKP-KAAATLQIVPAATWTASGTNQHIQAH 396
Cdd:PRK00247  348 KEIAQKRRAAEREINREARQERAAAMARARARRAAVKAKKKGlIDASPNEDTPSENEESKGSPPQVEAT 416
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
158-219 6.40e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 6.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2008374040 158 LKQERggLTGEPGSRDEL-LEEQRRKRGI-LREKRRQATRERKRNEEAGKQ-KKPAAQERAKVHQ 219
Cdd:pfam15709 363 LQQEQ--LERAEKMREELeLEQQRRFEEIrLRKQRLEEERQRQEEEERKQRlQLQAAQERARQQQ 425
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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