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Conserved domains on  [gi|15596399|ref|NP_249893|]
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hydrolase [Pseudomonas aeruginosa PAO1]

Protein Classification

hydrolase( domain architecture ID 10099061)

putative YcaC-like hydrolase with unknown specificity

CATH:  3.40.50.850
Gene Ontology:  GO:0016787
PubMed:  9782055
SCOP:  4000591

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-204 1.35e-169

isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of unknown function, found in both Pseudomonas aeruginosa and Escherichia coli K-12, with an isochorismate family crystal structure.


:

Pssm-ID: 469349  Cd Length: 201  Bit Score: 463.71  E-value: 1.35e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    4 TYKRLDKNDAAVLFVDHQAGLLSLVRDFSPDEFKNNVLALADIARFFNLPTILTTSFEDGPNGPLVPELKEMFPQAPYIA 83
Cdd:NF041461   1 PYKRLDKDDAAVLLVDHQTGLLSLVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399   84 RPGNINAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLM 163
Cdd:NF041461  81 RPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQLM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15596399  164 NWFSVGCELHRDWRNDIEGFGAILGGHLPAYANLIQSFGTK 204
Cdd:NF041461 161 NWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
 
Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-204 1.35e-169

isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of unknown function, found in both Pseudomonas aeruginosa and Escherichia coli K-12, with an isochorismate family crystal structure.


Pssm-ID: 469349  Cd Length: 201  Bit Score: 463.71  E-value: 1.35e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    4 TYKRLDKNDAAVLFVDHQAGLLSLVRDFSPDEFKNNVLALADIARFFNLPTILTTSFEDGPNGPLVPELKEMFPQAPYIA 83
Cdd:NF041461   1 PYKRLDKDDAAVLLVDHQTGLLSLVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399   84 RPGNINAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLM 163
Cdd:NF041461  81 RPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQLM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15596399  164 NWFSVGCELHRDWRNDIEGFGAILGGHLPAYANLIQSFGTK 204
Cdd:NF041461 161 NWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 14-174 1.93e-68

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 206.29  E-value: 1.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  14 AVLFVDHQAGLLSLVRDFspDEFKNNVLALADIARFFNLPTILTTSFEdGPNGPLVPELKEMFPQAPYIARPGnINAWDN 93
Cdd:cd01012   1 ALLLVDVQEKLAPAIKSF--DELINNTVKLAKAAKLLDVPVILTEQYP-KGLGPTVPELREVFPDAPVIEKTS-FSCWED 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  94 EDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLMNWFSVGCELH 173
Cdd:cd01012  77 EAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQ 156


                .
gi 15596399 174 R 174
Cdd:cd01012 157 R 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 14-163 2.18e-32

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 114.62  E-value: 2.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  14 AVLFVDHQAGLLSLVRDFSP--DEFKNNVLALADIARFFNLPTILTT--------SF-----------EDGPNGPLVPEL 72
Cdd:COG1335   1 ALLVIDVQNDFVPPGALAVPgaDAVVANIARLLAAARAAGVPVIHTRdwhppdgsEFaefdlwpphcvPGTPGAELVPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  73 KEmFPQAPYIARPGNiNAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAW 152
Cdd:COG1335  81 AP-LPGDPVVDKTRY-SAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                       170
                ....*....|.
gi 15596399 153 ARMTAAGAQLM 163
Cdd:COG1335 159 ARLRAAGATVV 169
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 13-165 9.03e-25

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 95.16  E-value: 9.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    13 AAVLFVDHQAGLLSLVRDFSPD--EFKNNVLALADIARFFNLPTILTT------------------SFEDGPNGP-LVPE 71
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGiaAILENINRLLKAARKAGIPVIFTRqvpepddadfalkdrpspAFPPGTTGAeLVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    72 LKEMfPQAPYIARPGnINAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAA 151
Cdd:pfam00857  81 LAPL-PGDLVVDKTR-FSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAA 158

                         170
                  ....*....|....
gi 15596399   152 WARMTAAGAQLMNW 165
Cdd:pfam00857 159 LERLAQRGAEVTTT 172
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 101-164 9.78e-10

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 55.84  E-value: 9.78e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596399  101 KATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLMN 164
Cdd:PTZ00331 142 KAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLEAGVILLT 205
 
Name Accession Description Interval E-value
C_hydro_YcaC NF041461
isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of ...
 4-204 1.35e-169

isochorismate family cysteine hydrolase YcaC; YcaC is a well-conserved cysteine hydrolase of unknown function, found in both Pseudomonas aeruginosa and Escherichia coli K-12, with an isochorismate family crystal structure.


Pssm-ID: 469349  Cd Length: 201  Bit Score: 463.71  E-value: 1.35e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    4 TYKRLDKNDAAVLFVDHQAGLLSLVRDFSPDEFKNNVLALADIARFFNLPTILTTSFEDGPNGPLVPELKEMFPQAPYIA 83
Cdd:NF041461   1 PYKRLDKDDAAVLLVDHQTGLLSLVRDFSPDEFKNNVLALADIAKYFNLPTILTTSFEDGPNGPLVPELKEMFPDAPYIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399   84 RPGNINAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLM 163
Cdd:NF041461  81 RPGQINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVAFPALSALEEGYEVFVVTDASGTFNEVTRDAAWDRMSQAGAQLM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15596399  164 NWFSVGCELHRDWRNDIEGFGAILGGHLPAYANLIQSFGTK 204
Cdd:NF041461 161 NWFAVACELHRDWRNDVEGLGTLFSNHIPDYRNLMTSYAAV 201
YcaC_related cd01012
YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown ...
 14-174 1.93e-68

YcaC related amidohydrolases; E.coli YcaC is an homooctameric hydrolase with unknown specificity. Despite its weak sequence similarity, it is structurally related to other amidohydrolases and shares conserved active site residues with them. Multimerisation interface seems not to be conserved in all members.


Pssm-ID: 238494 [Multi-domain]  Cd Length: 157  Bit Score: 206.29  E-value: 1.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  14 AVLFVDHQAGLLSLVRDFspDEFKNNVLALADIARFFNLPTILTTSFEdGPNGPLVPELKEMFPQAPYIARPGnINAWDN 93
Cdd:cd01012   1 ALLLVDVQEKLAPAIKSF--DELINNTVKLAKAAKLLDVPVILTEQYP-KGLGPTVPELREVFPDAPVIEKTS-FSCWED 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  94 EDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLMNWFSVGCELH 173
Cdd:cd01012  77 EAFRKALKATGRKQVVLAGLETHVCVLQTALDLLEEGYEVFVVADACGSRSKEDHELALARMRQAGAVLTTSESVLFELQ 156


                .
gi 15596399 174 R 174
Cdd:cd01012 157 R 157
PncA COG1335
Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction ...
 14-163 2.18e-32

Nicotinamidase-related amidase [Coenzyme transport and metabolism, General function prediction only]; Nicotinamidase-related amidase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440946 [Multi-domain]  Cd Length: 169  Bit Score: 114.62  E-value: 2.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  14 AVLFVDHQAGLLSLVRDFSP--DEFKNNVLALADIARFFNLPTILTT--------SF-----------EDGPNGPLVPEL 72
Cdd:COG1335   1 ALLVIDVQNDFVPPGALAVPgaDAVVANIARLLAAARAAGVPVIHTRdwhppdgsEFaefdlwpphcvPGTPGAELVPEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  73 KEmFPQAPYIARPGNiNAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAW 152
Cdd:COG1335  81 AP-LPGDPVVDKTRY-SAFYGTDLDELLRERGIDTLVVAGLATDVCVLSTARDALDLGYEVTVVEDACASRDPEAHEAAL 158

                       170
                ....*....|.
gi 15596399 153 ARMTAAGAQLM 163
Cdd:COG1335 159 ARLRAAGATVV 169
cysteine_hydrolases cd00431
Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine ...
 14-155 1.41e-29

Cysteine hydrolases; This family contains amidohydrolases, like CSHase (N-carbamoylsarcosine amidohydrolase), involved in creatine metabolism and nicotinamidase, converting nicotinamide to nicotinic acid and ammonia in the pyridine nucleotide cycle. It also contains isochorismatase, an enzyme that catalyzes the conversion of isochorismate to 2,3-dihydroxybenzoate and pyruvate, via the hydrolysis of the vinyl ether bond, and other related enzymes with unknown function.


Pssm-ID: 238245 [Multi-domain]  Cd Length: 161  Bit Score: 107.35  E-value: 1.41e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  14 AVLFVDHQAGLLSLVRDFSP--DEFKNNVLALADIARFFNLPTILTTSF------------------EDGPNGPLVPELK 73
Cdd:cd00431   1 ALLVVDMQNDFVPGGGLLLPgaDELVPNINRLLAAARAAGIPVIFTRDWhppddpefaellwpphcvKGTEGAELVPELA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  74 eMFPQAPYIARpGNINAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWA 153
Cdd:cd00431  81 -PLPDDLVIEK-TRYSAFYGTDLDELLRERGIDTLVVCGIATDICVLATARDALDLGYRVIVVEDACATRDEEDHEAALE 158


                ..
gi 15596399 154 RM 155
Cdd:cd00431 159 RL 160
Isochorismatase pfam00857
Isochorismatase family; This family are hydrolase enzymes.
 13-165 9.03e-25

Isochorismatase family; This family are hydrolase enzymes.


Pssm-ID: 376404 [Multi-domain]  Cd Length: 173  Bit Score: 95.16  E-value: 9.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    13 AAVLFVDHQAGLLSLVRDFSPD--EFKNNVLALADIARFFNLPTILTT------------------SFEDGPNGP-LVPE 71
Cdd:pfam00857   1 TALLVIDMQNDFVDSGGPKVEGiaAILENINRLLKAARKAGIPVIFTRqvpepddadfalkdrpspAFPPGTTGAeLVPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    72 LKEMfPQAPYIARPGnINAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAA 151
Cdd:pfam00857  81 LAPL-PGDLVVDKTR-FSAFAGTDLDEILRELGIDTLVLAGVATDVCVLSTARDALDRGYEVVVVSDACASLSPEAHDAA 158

                         170
                  ....*....|....
gi 15596399   152 WARMTAAGAQLMNW 165
Cdd:pfam00857 159 LERLAQRGAEVTTT 172
nicotinamidase_related cd01014
Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share ...
 14-152 7.77e-11

Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.


Pssm-ID: 238496 [Multi-domain]  Cd Length: 155  Bit Score: 57.99  E-value: 7.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  14 AVLFVDHQAGLLSLVR-DFSPDEFKNNVLALADIARFFNLPTILTTSFEDGPnGPLVP--ELKEMFPQApyIARPGNI-- 88
Cdd:cd01014   1 ALLVIDVQNGYFDGGLpPLNNEAALENIAALIAAARAAGIPVIHVRHIDDEG-GSFAPgsEGWEIHPEL--APLEGETvi 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596399  89 -----NAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAW 152
Cdd:cd01014  78 ektvpNAFYGTDLEEWLREAGIDHLVICGAMTEMCVDTTVRSAFDLGYDVTVVADACATFDLPDHGGVL 146
nicotinamidase cd01011
Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, ...
 101-163 1.22e-10

Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA).


Pssm-ID: 238493  Cd Length: 196  Bit Score: 58.04  E-value: 1.22e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596399 101 KATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLM 163
Cdd:cd01011 134 RERGIDRVDVVGLATDYCVKATALDALKAGFEVRVLEDACRAVDPETIERAIEEMKEAGVVLV 196
PTZ00331 PTZ00331
alpha/beta hydrolase; Provisional
 101-164 9.78e-10

alpha/beta hydrolase; Provisional


Pssm-ID: 240363  Cd Length: 212  Bit Score: 55.84  E-value: 9.78e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596399  101 KATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWARMTAAGAQLMN 164
Cdd:PTZ00331 142 KAHGVRRVFICGLAFDFCVLFTALDAVKLGFKVVVLEDATRAVDPDAISKQRAELLEAGVILLT 205
PLN02621 PLN02621
nicotinamidase
 9-164 1.28e-09

nicotinamidase


Pssm-ID: 178229  Cd Length: 197  Bit Score: 55.56  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399    9 DKNDAAVLFVDHQAGLLSLVRDFSPdefknNVLALADIARFFNLPTILTTSFEDGP----------NGPLV----PElKE 74
Cdd:PLN02621  17 DPKQAALLVIDMQNYFSSMAEPILP-----ALLTTIDLCRRASIPVFFTRHSHKSPsdygmlgewwDGDLIldgtTE-AE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399   75 MFPQAPYIARPGNI------NAWDNEDFVKAVKATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVR 148
Cdd:PLN02621  91 LMPEIGRVTGPDEVvekstySAFYNTRLEERLRKIGVKEVIVTGVMTNLCCETTAREAFVRGFRVFFSTDATATANEELH 170

                        170
                 ....*....|....*.
gi 15596399  149 DAAWARMTAAGAQLMN 164
Cdd:PLN02621 171 EATLKNLAYGFAYLVD 186
PRK11609 PRK11609
bifunctional nicotinamidase/pyrazinamidase;
101-163 7.02e-06

bifunctional nicotinamidase/pyrazinamidase;


Pssm-ID: 183228  Cd Length: 212  Bit Score: 44.98  E-value: 7.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596399  101 KATGKKQLIIAGVVTDVCVAFPTLSALEEGFDVFVVTDASGTFNPVVRDAAWA--RMTAAGAQLM 163
Cdd:PRK11609 138 REHGITELIVMGLATDYCVKFTVLDALALGYQVNVITDGCRGVNLQPQDSAHAfmEMSAAGATLY 202
EntB1 COG1535
Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
7-144 3.60e-04

Isochorismate hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441144 [Multi-domain]  Cd Length: 204  Bit Score: 39.83  E-value: 3.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399   7 RLDKNDAAVLFVDHQAgllSLVRDFSPD-----EFKNNVLALADIARFFNLPTILT------TSFEDG----------PN 65
Cdd:COG1535  14 TLDPARAALLIHDMQN---YFLRPYDPDeppirELVANIARLRDACRAAGIPVVYTaqpgdqTPEDRGllndfwgpglTA 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596399  66 GP----LVPELkemfpqAPyiaRPGNI-------NAWDNEDFVKAVKATGKKQLIIAGVVTDVCVafpTLSALE---EGF 131
Cdd:COG1535  91 GPegqeIVDEL------AP---APGDTvltkwrySAFQRTDLEERLRELGRDQLIITGVYAHIGC---LATAVDafmRDI 158

                       170
                ....*....|...
gi 15596399 132 DVFVVTDASGTFN 144
Cdd:COG1535 159 QPFVVADAVADFS 171
 
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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