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Conserved domains on  [gi|1403757721|emb|SQE44939|]
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putative allophanate hydrolase subunit 2 [Escherichia coli]

Protein Classification

5-oxoprolinase/urea amidolyase family protein( domain architecture ID 10015763)

5-oxoprolinase/urea amidolyase family protein similar to Escherichia coli YbgK

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
urea_amlyse_rel TIGR00724
biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces ...
1-310 0e+00

biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This model models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins. [Unknown function, General]


:

Pssm-ID: 129807  Cd Length: 314  Bit Score: 522.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721   1 MLKIIRAGMYTTVQDGGRHGFRQSGISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEAR 80
Cdd:TIGR00724   1 MIEILRAGSHTLIQDLGRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHCDVIFAVTGADTDLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  81 LDDNAVWTGWR-LPMKAGQRLTLKRPQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKHDF 159
Cdd:TIGR00724  81 LNDGQVIPQWRpYEVKRGQILSLGRLKSGMRGYLAVRGGIDVPPVLGSCSTDLRANIGGYEGRPLKAGDVLPLGSNELDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 160 MEAQGVKQLL--WGNRIRALPGPEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTT-DRELLSHGLLPGVVQV 236
Cdd:TIGR00724 161 NEPQGLIPQIpeWRIEIRVLPGPEYDFFKRESIEAFWRSEWKVSSNSDRMGYRLQGPKLKHARpNRELLTHGIVYGSIQV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403757721 237 PHNGQPIVLMNDAQTTGGYPRIACIIEADMYHLAQIPLGQPIHFVQCSLEEALKARQDQQRYFEQLAWRLHNEN 310
Cdd:TIGR00724 241 PPNGQPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQSIKFVPLSLEEALKLRESQERYIKQLRGTLLREN 314
 
Name Accession Description Interval E-value
urea_amlyse_rel TIGR00724
biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces ...
1-310 0e+00

biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This model models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins. [Unknown function, General]


Pssm-ID: 129807  Cd Length: 314  Bit Score: 522.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721   1 MLKIIRAGMYTTVQDGGRHGFRQSGISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEAR 80
Cdd:TIGR00724   1 MIEILRAGSHTLIQDLGRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHCDVIFAVTGADTDLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  81 LDDNAVWTGWR-LPMKAGQRLTLKRPQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKHDF 159
Cdd:TIGR00724  81 LNDGQVIPQWRpYEVKRGQILSLGRLKSGMRGYLAVRGGIDVPPVLGSCSTDLRANIGGYEGRPLKAGDVLPLGSNELDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 160 MEAQGVKQLL--WGNRIRALPGPEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTT-DRELLSHGLLPGVVQV 236
Cdd:TIGR00724 161 NEPQGLIPQIpeWRIEIRVLPGPEYDFFKRESIEAFWRSEWKVSSNSDRMGYRLQGPKLKHARpNRELLTHGIVYGSIQV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403757721 237 PHNGQPIVLMNDAQTTGGYPRIACIIEADMYHLAQIPLGQPIHFVQCSLEEALKARQDQQRYFEQLAWRLHNEN 310
Cdd:TIGR00724 241 PPNGQPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQSIKFVPLSLEEALKLRESQERYIKQLRGTLLREN 314
PxpC COG1984
5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism]; ...
1-281 3.68e-159

5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism];


Pssm-ID: 441587  Cd Length: 285  Bit Score: 445.31  E-value: 3.68e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721   1 MLKIIRAGMYTTVQDGGRHGFRQSGISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEAR 80
Cdd:COG1984     2 MLEVLKPGLLTTVQDLGRPGYQHLGVPPSGAMDRLALRLANRLVGNPEGAAALEITLGGPTLRFEEDTVIALTGADMPAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  81 LDDNAVWTGWRLPMKAGQRLTLKRPQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKHDFm 160
Cdd:COG1984    82 LDGRPVPPWRPVAVKAGDVLTLGAPRAGARAYLAVAGGIDVPPVLGSRSTDLRAGLGGLEGRALQAGDVLPLGAPAAAA- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 161 EAQGVKQLL---WGNRIRALPGPEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTTDRELLSHGLLPGVVQVP 237
Cdd:COG1984   161 PGRGLPAELlpgEEVTLRVVPGPQDDWFTEEAIERFFSSEWTVTPQSDRMGYRLEGPPLERAHPSEILSEGIVPGAIQVP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1403757721 238 HNGQPIVLMNDAQTTGGYPRIACIIEADMYHLAQIPLGQPIHFV 281
Cdd:COG1984   241 PDGQPIVLLADRQTTGGYPKIATVISADLPRLAQLRPGDTVRFV 284
AHS2 smart00797
Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase ...
25-297 2.77e-141

Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase (AHS2).


Pssm-ID: 214821  Cd Length: 280  Bit Score: 399.55  E-value: 2.77e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721   25 GISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEARLDDNAVWTGWRLPMKAGQRLTLKR 104
Cdd:smart00797   3 GVPPSGAMDQLALRLANRLVGNPENAAALEITLGGPTLRFTADAVIALTGADFPATLDGQPVPPWKPFAVRAGQVLSLGA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  105 PQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKH-----DFMEAQGVKQLLWGNRIRALPG 179
Cdd:smart00797  83 PKAGARAYLAVRGGIDVPPVLGSRSTDTRGGFGGFEGRALKAGDVLPLGAAPAaapagAALPAALIPDYGKEWVIRVIPG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  180 PEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTTDRELLSHGLLPGVVQVPHNGQPIVLMNDAQTTGGYPRIA 259
Cdd:smart00797 163 PHPDFFTEESIERFFSSEWKVTPNSDRMGYRLEGPKLEWLHPSNIISEGVAIGAIQVPPDGQPIILLADRQTTGGYPKIA 242
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1403757721  260 CIIEADMYHLAQIPLGQPIHFVQCSLEEALKARQDQQR 297
Cdd:smart00797 243 TVISADLWKLAQLRPGDKVRFVPVSLEEAQALLREQER 280
CT_A_B pfam02626
Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ...
25-281 7.18e-133

Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 460627  Cd Length: 264  Bit Score: 377.91  E-value: 7.18e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  25 GISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEARLDDNAVWTGWRLPMKAGQRLTLKR 104
Cdd:pfam02626   2 GVPPSGAMDPLALRLANRLVGNPEGAAALEITLGGPTLRFHADAVIAVTGADMPATLDGKPVPMWTPVAVKAGDVLSFGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 105 PQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKHDFMEAQGVKQLLW-----GNRIRALPG 179
Cdd:pfam02626  82 PRGGLRAYLAVAGGFDVPPVLGSRSTDLLGGLGGHEGRPLRAGDVLPLGPPAAPAPALAPLPPAPPppdtpEWVIRVVPG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 180 PEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTTDRELLSHGLLPGVVQVPHNGQPIVLMNDAQTTGGYPRIA 259
Cdd:pfam02626 162 PQDDWFTPEALETFFSTEWTVSPNSDRMGYRLDGEALHPARGSNILSEGYVPGAIQVPPGGQPIILLADGQTTGGYPKIA 241
                         250       260
                  ....*....|....*....|..
gi 1403757721 260 CIIEADMYHLAQIPLGQPIHFV 281
Cdd:pfam02626 242 TVISADLWKLAQLRPGDKVRFV 263
 
Name Accession Description Interval E-value
urea_amlyse_rel TIGR00724
biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces ...
1-310 0e+00

biotin-dependent carboxylase uncharacterized domain; Urea amidolyase of Saccharomyces cerevisiae is a 1835 amino acid protein with an amidase domain, a biotin/lipoyl cofactor attachment domain, a carbamoyl-phosphate synthase L chain-like domain, and uncharacterized regions. It has both urea carboxylase and allophanate hydrolase activities. This model models a domain that represents uncharacterized prokaryotic proteins of about 300 amino acids, regions of prokaryotic urea carboxylase and of the urea carboxylase region of yeast urea amidolyase, and regions of other biotin-containing proteins. [Unknown function, General]


Pssm-ID: 129807  Cd Length: 314  Bit Score: 522.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721   1 MLKIIRAGMYTTVQDGGRHGFRQSGISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEAR 80
Cdd:TIGR00724   1 MIEILRAGSHTLIQDLGRVGYRRIGVPHSGAMDAYSLRLANRLVGNPDDTPAIEVTLGGPTIRFHCDVIFAVTGADTDLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  81 LDDNAVWTGWR-LPMKAGQRLTLKRPQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKHDF 159
Cdd:TIGR00724  81 LNDGQVIPQWRpYEVKRGQILSLGRLKSGMRGYLAVRGGIDVPPVLGSCSTDLRANIGGYEGRPLKAGDVLPLGSNELDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 160 MEAQGVKQLL--WGNRIRALPGPEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTT-DRELLSHGLLPGVVQV 236
Cdd:TIGR00724 161 NEPQGLIPQIpeWRIEIRVLPGPEYDFFKRESIEAFWRSEWKVSSNSDRMGYRLQGPKLKHARpNRELLTHGIVYGSIQV 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403757721 237 PHNGQPIVLMNDAQTTGGYPRIACIIEADMYHLAQIPLGQPIHFVQCSLEEALKARQDQQRYFEQLAWRLHNEN 310
Cdd:TIGR00724 241 PPNGQPIILMADAQTTGGYPKIAVVIEADLWKVAQVRPGQSIKFVPLSLEEALKLRESQERYIKQLRGTLLREN 314
PxpC COG1984
5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism]; ...
1-281 3.68e-159

5-oxoprolinase subunit C/Allophanate hydrolase subunit 2 [Amino acid transport and metabolism];


Pssm-ID: 441587  Cd Length: 285  Bit Score: 445.31  E-value: 3.68e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721   1 MLKIIRAGMYTTVQDGGRHGFRQSGISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEAR 80
Cdd:COG1984     2 MLEVLKPGLLTTVQDLGRPGYQHLGVPPSGAMDRLALRLANRLVGNPEGAAALEITLGGPTLRFEEDTVIALTGADMPAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  81 LDDNAVWTGWRLPMKAGQRLTLKRPQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKHDFm 160
Cdd:COG1984    82 LDGRPVPPWRPVAVKAGDVLTLGAPRAGARAYLAVAGGIDVPPVLGSRSTDLRAGLGGLEGRALQAGDVLPLGAPAAAA- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 161 EAQGVKQLL---WGNRIRALPGPEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTTDRELLSHGLLPGVVQVP 237
Cdd:COG1984   161 PGRGLPAELlpgEEVTLRVVPGPQDDWFTEEAIERFFSSEWTVTPQSDRMGYRLEGPPLERAHPSEILSEGIVPGAIQVP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1403757721 238 HNGQPIVLMNDAQTTGGYPRIACIIEADMYHLAQIPLGQPIHFV 281
Cdd:COG1984   241 PDGQPIVLLADRQTTGGYPKIATVISADLPRLAQLRPGDTVRFV 284
AHS2 smart00797
Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase ...
25-297 2.77e-141

Allophanate hydrolase subunit 2; This domain represents subunit 2 of allophanate hydrolase (AHS2).


Pssm-ID: 214821  Cd Length: 280  Bit Score: 399.55  E-value: 2.77e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721   25 GISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEARLDDNAVWTGWRLPMKAGQRLTLKR 104
Cdd:smart00797   3 GVPPSGAMDQLALRLANRLVGNPENAAALEITLGGPTLRFTADAVIALTGADFPATLDGQPVPPWKPFAVRAGQVLSLGA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  105 PQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKH-----DFMEAQGVKQLLWGNRIRALPG 179
Cdd:smart00797  83 PKAGARAYLAVRGGIDVPPVLGSRSTDTRGGFGGFEGRALKAGDVLPLGAAPAaapagAALPAALIPDYGKEWVIRVIPG 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  180 PEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTTDRELLSHGLLPGVVQVPHNGQPIVLMNDAQTTGGYPRIA 259
Cdd:smart00797 163 PHPDFFTEESIERFFSSEWKVTPNSDRMGYRLEGPKLEWLHPSNIISEGVAIGAIQVPPDGQPIILLADRQTTGGYPKIA 242
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1403757721  260 CIIEADMYHLAQIPLGQPIHFVQCSLEEALKARQDQQR 297
Cdd:smart00797 243 TVISADLWKLAQLRPGDKVRFVPVSLEEAQALLREQER 280
CT_A_B pfam02626
Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ...
25-281 7.18e-133

Carboxyltransferase domain, subdomain A and B; Urea carboxylase (UC) catalyzes a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A and B subdomains of the CT domain. This domain covers the whole length of KipA (kinase A) from Bacillus subtilis. It can also be found in S. cerevisiae urea amidolyase Dur1,2, which is a multifunctional biotin-dependent enzyme with domains for urea carboxylase and allophanate (urea carboxylate) hydrolase activity.


Pssm-ID: 460627  Cd Length: 264  Bit Score: 377.91  E-value: 7.18e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721  25 GISHCGTLDMPALRIANLLVGNDANAPALEITLGQLTVEFETDGWFALTGAGCEARLDDNAVWTGWRLPMKAGQRLTLKR 104
Cdd:pfam02626   2 GVPPSGAMDPLALRLANRLVGNPEGAAALEITLGGPTLRFHADAVIAVTGADMPATLDGKPVPMWTPVAVKAGDVLSFGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 105 PQHGMRSYLAVAGGIDVPPVMGSCSTDLNVGIGGLEGRLLKDGDRLPIGKSKHDFMEAQGVKQLLW-----GNRIRALPG 179
Cdd:pfam02626  82 PRGGLRAYLAVAGGFDVPPVLGSRSTDLLGGLGGHEGRPLRAGDVLPLGPPAAPAPALAPLPPAPPppdtpEWVIRVVPG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403757721 180 PEYHEFDRASQDAFWRSPWQLSPQSNRMGYRLQGQILKRTTDRELLSHGLLPGVVQVPHNGQPIVLMNDAQTTGGYPRIA 259
Cdd:pfam02626 162 PQDDWFTPEALETFFSTEWTVSPNSDRMGYRLDGEALHPARGSNILSEGYVPGAIQVPPGGQPIILLADGQTTGGYPKIA 241
                         250       260
                  ....*....|....*....|..
gi 1403757721 260 CIIEADMYHLAQIPLGQPIHFV 281
Cdd:pfam02626 242 TVISADLWKLAQLRPGDKVRFV 263
 
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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