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Conserved domains on  [gi|700663438|ref|WP_033180965|]
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MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Rhizobium]

Protein Classification

N-acetylmuramoyl-L-alanine amidase( domain architecture ID 18653756)

N-acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides

CATH:  1.10.101.10
EC:  3.5.1.28
Gene Ontology:  GO:0008745|GO:0008270|GO:0071555
PubMed:  20036252
SCOP:  4000784

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
1-167 2.55e-82

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442259  Cd Length: 167  Bit Score: 243.62  E-value: 2.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438   1 MTSFEADcNSARVQPSPNHGERADGRHPDMILLHYTGMPTADGALDWLCRAESQVSSHYFVHENGEVVQLVPETRRAWHA 80
Cdd:COG3023    1 MKGYTID-TGARFVPSPNFDERPAGAEIDLIVIHYTAGPPGGGALDWLTDPALRVSAHYLIDRDGEIYQLVPEDDRAWHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  81 GKSSWHGERDINSLSIGIEIANAGHpgGLPDYPKEQIAAVIELCRDCVKRWSIVPERVLGHSDVAPIRKVDPGEKFPWAE 160
Cdd:COG3023   80 GVSSWRGRTNLNDFSIGIELENPGH--GWAPFTEAQYEALAALLRDLCARYGIPPDHIVGHSDIAPGRKTDPGPAFPWAR 157


                 ....*....
gi 700663438 161 LH--LAGVG 167
Cdd:COG3023  158 LAalLARYG 166
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 186-242 5.32e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 53.67  E-value: 5.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 700663438  186 TGEPVEALQSMLSLYGYGT-EITGEFSEKTAGDVEAFQRHFRPErIDGIADFSTIDTL 242
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPgPVDGYFGPSTEAAVKAFQRAFGLP-VDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
1-167 2.55e-82

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 243.62  E-value: 2.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438   1 MTSFEADcNSARVQPSPNHGERADGRHPDMILLHYTGMPTADGALDWLCRAESQVSSHYFVHENGEVVQLVPETRRAWHA 80
Cdd:COG3023    1 MKGYTID-TGARFVPSPNFDERPAGAEIDLIVIHYTAGPPGGGALDWLTDPALRVSAHYLIDRDGEIYQLVPEDDRAWHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  81 GKSSWHGERDINSLSIGIEIANAGHpgGLPDYPKEQIAAVIELCRDCVKRWSIVPERVLGHSDVAPIRKVDPGEKFPWAE 160
Cdd:COG3023   80 GVSSWRGRTNLNDFSIGIELENPGH--GWAPFTEAQYEALAALLRDLCARYGIPPDHIVGHSDIAPGRKTDPGPAFPWAR 157


                 ....*....
gi 700663438 161 LH--LAGVG 167
Cdd:COG3023  158 LAalLARYG 166
PRK11789 PRK11789
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;
8-162 2.67e-37

1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;


Pssm-ID: 236984  Cd Length: 185  Bit Score: 129.54  E-value: 2.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438   8 CNSARVQPSPNHGERADGRHPDMILLHYTGMPTAD-----------GALDW-----------LcraesQVSSHYFVHENG 65
Cdd:PRK11789  10 LVGARRVPSPNFDARPDGEDISLLVIHNISLPPGEfggpyidalftNRLDPdahpyfaeiagL-----RVSAHFLIRRDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  66 EVVQLVPETRRAWHAGKSSWHGERDINSLSIGIEIANAghpGGLPdYPKEQIAAVIELCRDCVKRWSIVPERVLGHSDVA 145
Cdd:PRK11789  85 EIVQFVSFDDRAWHAGVSSFQGRERCNDFSIGIELEGT---DTLP-FTDAQYQALAALTRALRAAYPIIAERITGHSDIA 160

                        170
                 ....*....|....*..
gi 700663438 146 PIRKVDPGEKFPWAELH 162
Cdd:PRK11789 161 PGRKTDPGPAFDWQRFR 177
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 28-154 3.55e-36

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 124.39  E-value: 3.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438   28 PDMILLHYTGMPTADGALDW----LCRAESQVSSHYFVHENGEVVQLVPETRRAWHAGKSSWhgerdiNSLSIGIEIANa 103
Cdd:pfam01510   2 IRYIVIHHTAGPSFAGALLPyaacIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAGNGGG------NDRSIGIELEG- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 700663438  104 ghPGGLPDYPKEQIAAVIELCRDCVKRWSIVPER-VLGHSDVApiRKVDPGE 154
Cdd:pfam01510  75 --NFGGDPPTDAQYEALARLLADLCKRYGIPPDRrIVGHRDVG--RKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 28-155 2.22e-31

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 112.38  E-value: 2.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  28 PDMILLHYTGMP---TADGALDWLCRA----ESQVSSHYFVHENGEVVQLVPETRRAWHAGKsswhgerDINSLSIGIEI 100
Cdd:cd06583    2 VKYVVIHHTANPncyTAAAAVRYLQNYhmrgWSDISYHFLVGGDGRIYQGRGWNYVGWHAGG-------NYNSYSIGIEL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 700663438 101 ANaghPGGLPDYPKEQIAAVIELCRDCVKRWSI-VPERVLGHSDVAPiRKVDPGEK 155
Cdd:cd06583   75 IG---NFDGGPPTAAQLEALAELLAYLVKRYGIpPDYRIVGHRDVSP-GTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
28-149 2.40e-22

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 88.95  E-value: 2.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438    28 PDMILLHYTGMP--TADGALDWLCRAE-SQVSSHYFVHENGEVVQLVPETRRAWHAGKSSWHGerdINSLSIGIEIANAG 104
Cdd:smart00644   3 PRGIVIHHTANSnaSCANEARYMQNNHmNDIGYHFLVGGDGRVYQGVGWNYVAWHAGGAHTPG---YNDISIGIEFIGSF 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 700663438   105 HPGGLPdyPKEQIAAVIELCRDCVKRWSIVP---ERVLGHSDVAPIRK 149
Cdd:smart00644  80 DSDDEP--FAEALYAALDLLAKLLKGAGLPPdgrYRIVGHRDVAPTED 125
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 186-242 5.32e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 53.67  E-value: 5.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 700663438  186 TGEPVEALQSMLSLYGYGT-EITGEFSEKTAGDVEAFQRHFRPErIDGIADFSTIDTL 242
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPgPVDGYFGPSTEAAVKAFQRAFGLP-VDGIVDPETLAAL 57
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 176-244 4.17e-09

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 51.83  E-value: 4.17e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438 176 TGGRFFQSGDTGEPVEALQSMLSLYGYGT-EITGEFSEKTAGDVEAFQRHFRPErIDGIADFSTIDTLHR 244
Cdd:COG3409    1 ASAPTLRLGDSGEDVRELQQRLNALGYYPgPVDGIFGPATEAAVRAFQRANGLP-VDGIVGPATWAALRA 69
 
Name Accession Description Interval E-value
AmpD COG3023
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];
1-167 2.55e-82

N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442259  Cd Length: 167  Bit Score: 243.62  E-value: 2.55e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438   1 MTSFEADcNSARVQPSPNHGERADGRHPDMILLHYTGMPTADGALDWLCRAESQVSSHYFVHENGEVVQLVPETRRAWHA 80
Cdd:COG3023    1 MKGYTID-TGARFVPSPNFDERPAGAEIDLIVIHYTAGPPGGGALDWLTDPALRVSAHYLIDRDGEIYQLVPEDDRAWHA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  81 GKSSWHGERDINSLSIGIEIANAGHpgGLPDYPKEQIAAVIELCRDCVKRWSIVPERVLGHSDVAPIRKVDPGEKFPWAE 160
Cdd:COG3023   80 GVSSWRGRTNLNDFSIGIELENPGH--GWAPFTEAQYEALAALLRDLCARYGIPPDHIVGHSDIAPGRKTDPGPAFPWAR 157


                 ....*....
gi 700663438 161 LH--LAGVG 167
Cdd:COG3023  158 LAalLARYG 166
PRK11789 PRK11789
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;
8-162 2.67e-37

1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD;


Pssm-ID: 236984  Cd Length: 185  Bit Score: 129.54  E-value: 2.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438   8 CNSARVQPSPNHGERADGRHPDMILLHYTGMPTAD-----------GALDW-----------LcraesQVSSHYFVHENG 65
Cdd:PRK11789  10 LVGARRVPSPNFDARPDGEDISLLVIHNISLPPGEfggpyidalftNRLDPdahpyfaeiagL-----RVSAHFLIRRDG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  66 EVVQLVPETRRAWHAGKSSWHGERDINSLSIGIEIANAghpGGLPdYPKEQIAAVIELCRDCVKRWSIVPERVLGHSDVA 145
Cdd:PRK11789  85 EIVQFVSFDDRAWHAGVSSFQGRERCNDFSIGIELEGT---DTLP-FTDAQYQALAALTRALRAAYPIIAERITGHSDIA 160

                        170
                 ....*....|....*..
gi 700663438 146 PIRKVDPGEKFPWAELH 162
Cdd:PRK11789 161 PGRKTDPGPAFDWQRFR 177
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 28-154 3.55e-36

N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.


Pssm-ID: 460236 [Multi-domain]  Cd Length: 122  Bit Score: 124.39  E-value: 3.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438   28 PDMILLHYTGMPTADGALDW----LCRAESQVSSHYFVHENGEVVQLVPETRRAWHAGKSSWhgerdiNSLSIGIEIANa 103
Cdd:pfam01510   2 IRYIVIHHTAGPSFAGALLPyaacIARGWSDVSYHYLIDRDGTIYQLVPENGRAWHAGNGGG------NDRSIGIELEG- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 700663438  104 ghPGGLPDYPKEQIAAVIELCRDCVKRWSIVPER-VLGHSDVApiRKVDPGE 154
Cdd:pfam01510  75 --NFGGDPPTDAQYEALARLLADLCKRYGIPPDRrIVGHRDVG--RKTDPGP 122
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 28-155 2.22e-31

Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.


Pssm-ID: 133475 [Multi-domain]  Cd Length: 126  Bit Score: 112.38  E-value: 2.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  28 PDMILLHYTGMP---TADGALDWLCRA----ESQVSSHYFVHENGEVVQLVPETRRAWHAGKsswhgerDINSLSIGIEI 100
Cdd:cd06583    2 VKYVVIHHTANPncyTAAAAVRYLQNYhmrgWSDISYHFLVGGDGRIYQGRGWNYVGWHAGG-------NYNSYSIGIEL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 700663438 101 ANaghPGGLPDYPKEQIAAVIELCRDCVKRWSI-VPERVLGHSDVAPiRKVDPGEK 155
Cdd:cd06583   75 IG---NFDGGPPTAAQLEALAELLAYLVKRYGIpPDYRIVGHRDVSP-GTECPGDA 126
Ami_2 smart00644
Ami_2 domain;
28-149 2.40e-22

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 88.95  E-value: 2.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438    28 PDMILLHYTGMP--TADGALDWLCRAE-SQVSSHYFVHENGEVVQLVPETRRAWHAGKSSWHGerdINSLSIGIEIANAG 104
Cdd:smart00644   3 PRGIVIHHTANSnaSCANEARYMQNNHmNDIGYHFLVGGDGRVYQGVGWNYVAWHAGGAHTPG---YNDISIGIEFIGSF 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 700663438   105 HPGGLPdyPKEQIAAVIELCRDCVKRWSIVP---ERVLGHSDVAPIRK 149
Cdd:smart00644  80 DSDDEP--FAEALYAALDLLAKLLKGAGLPPdgrYRIVGHRDVAPTED 125
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
16-153 3.37e-19

N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444359  Cd Length: 177  Bit Score: 81.94  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438  16 SPNHGERA-DGRHPDMILLHYTGMP--TADGALDWLCRAESQVSSHYFVHENgEVVQLVPETRRAWHAGksSWHGERdiN 92
Cdd:COG5632   11 PKNNSYRPgYKMKPKGIVIHNTANPgaTAENHANYFNNNNRSASWHYFVDDK-EIIQHIPLNENAWHAG--DGTGPG--N 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 700663438  93 SLSIGIEIA-NAGHpgglpDYPKEQIAAViELCRDCVKRWSIVPERVLGHSDVApiRKVDPG 153
Cdd:COG5632   86 RRSIGIEICeNKDG-----DFAKAYENAA-ELIAYLMKKYGIPIDNVVRHYDWS--GKNCPH 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 186-242 5.32e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 53.67  E-value: 5.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 700663438  186 TGEPVEALQSMLSLYGYGT-EITGEFSEKTAGDVEAFQRHFRPErIDGIADFSTIDTL 242
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPgPVDGYFGPSTEAAVKAFQRAFGLP-VDGIVDPETLAAL 57
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 176-244 4.17e-09

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 51.83  E-value: 4.17e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 700663438 176 TGGRFFQSGDTGEPVEALQSMLSLYGYGT-EITGEFSEKTAGDVEAFQRHFRPErIDGIADFSTIDTLHR 244
Cdd:COG3409    1 ASAPTLRLGDSGEDVRELQQRLNALGYYPgPVDGIFGPATEAAVRAFQRANGLP-VDGIVGPATWAALRA 69
 
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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