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Conserved domains on  [gi|577244852|gb|EUE61760|]
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autolysin [Staphylococcus aureus M0680]

Protein Classification

SH3 domain-containing protein( domain architecture ID 11156870)

Src Homology 3 (SH3) domain-containing protein plays versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3_5 pfam08460
Bacterial SH3 domain;
395-460 1.39e-26

Bacterial SH3 domain;


:

Pssm-ID: 430010 [Multi-domain]  Cd Length: 68  Bit Score: 102.08  E-value: 1.39e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577244852  395 YYMEESARFT-NGNQPITVRKVGPFLSCPVGYQFQPGGYCDYTEVMLQDGHVWVGYTWE-GQRYYLPI 460
Cdd:pfam08460   1 YYPSEQGTFTiGGKTGIVLRKNEPSLSAPVQFVLYKGDKVFYDQVLLADGYVWISYTSYnGVRRYLPV 68
Ami_2 smart00644
Ami_2 domain;
198-322 8.47e-25

Ami_2 domain;


:

Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 98.97  E-value: 8.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852   198 SNPKGIVIHNDAGSkGATAEAYRNGLVNaplSRLEAGIAHSYVSGN-TVWQALDESQVGWHTANQ---IGNKYYYGIEVC 273
Cdd:smart00644   1 PPPRGIVIHHTANS-NASCANEARYMQN---NHMNDIGYHFLVGGDgRVYQGVGWNYVAWHAGGAhtpGYNDISIGIEFI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 577244852   274 QSMGADNATFLKNEQATFQECARLLKKWGLPAN-RNTIRLHNEFTSTSCP 322
Cdd:smart00644  77 GSFDSDDEPFAEALYAALDLLAKLLKGAGLPPDgRYRIVGHRDVAPTEDP 126
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 31-113 3.27e-08

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


:

Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 50.88  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852   31 QCFDYAnagWKALFGLLLKGVGAKDipFANNFDGLATVYQNTPdflaQPGDMVVFGSN-YGAGYGHVAWVIEATLDYIIV 109
Cdd:pfam05257   9 QCTWFV---YWRVAQLGIYLGNAGD--WADAAAGAYKVGSTTP----KVGDIVVFDPGgGGASYGHVAIVEKVNDGSITV 79


                  ....
gi 577244852  110 YEQN 113
Cdd:pfam05257  80 SEQN 83
 
Name Accession Description Interval E-value
SH3_5 pfam08460
Bacterial SH3 domain;
395-460 1.39e-26

Bacterial SH3 domain;


Pssm-ID: 430010 [Multi-domain]  Cd Length: 68  Bit Score: 102.08  E-value: 1.39e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577244852  395 YYMEESARFT-NGNQPITVRKVGPFLSCPVGYQFQPGGYCDYTEVMLQDGHVWVGYTWE-GQRYYLPI 460
Cdd:pfam08460   1 YYPSEQGTFTiGGKTGIVLRKNEPSLSAPVQFVLYKGDKVFYDQVLLADGYVWISYTSYnGVRRYLPV 68
Ami_2 smart00644
Ami_2 domain;
198-322 8.47e-25

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 98.97  E-value: 8.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852   198 SNPKGIVIHNDAGSkGATAEAYRNGLVNaplSRLEAGIAHSYVSGN-TVWQALDESQVGWHTANQ---IGNKYYYGIEVC 273
Cdd:smart00644   1 PPPRGIVIHHTANS-NASCANEARYMQN---NHMNDIGYHFLVGGDgRVYQGVGWNYVAWHAGGAhtpGYNDISIGIEFI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 577244852   274 QSMGADNATFLKNEQATFQECARLLKKWGLPAN-RNTIRLHNEFTSTSCP 322
Cdd:smart00644  77 GSFDSDDEPFAEALYAALDLLAKLLKGAGLPPDgRYRIVGHRDVAPTEDP 126
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
194-376 2.14e-19

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


Pssm-ID: 444359  Cd Length: 177  Bit Score: 85.41  E-value: 2.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852 194 PKRGSNPKGIVIHNDAGsKGATAEAYRNGLVNAplSRlEAGiAHSYVSGNTVWQALDESQVGWH--TANQIGNKYYYGIE 271
Cdd:COG5632   18 PGYKMKPKGIVIHNTAN-PGATAENHANYFNNN--NR-SAS-WHYFVDDKEIIQHIPLNENAWHagDGTGPGNRRSIGIE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852 272 VCQSMGADnatFLKNEQATFQECARLLKKWGLPANRntIRLHNEFTSTSCPHRssvlhtgfdpvtrgLLPEDKRlqLKDY 351
Cdd:COG5632   93 ICENKDGD---FAKAYENAAELIAYLMKKYGIPIDN--VVRHYDWSGKNCPHG--------------LLANGGY--RWDQ 151

                        170       180
                 ....*....|....*....|....*
gi 577244852 352 FIKQIRAYMDGKIPVATVSNESSAS 376
Cdd:COG5632  152 FKADVKSALNGLSTVKPYTKVVKAS 176
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 199-324 1.15e-18

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: 81.95  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852 199 NPKGIVIHNDAGSKGATAEAYRNGLVNaPLSRLEAGI-AHSYVSGN-TVWQALDESQVGWHtANQIGNKYYYGIEVCQSM 276
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAAAVRYLQN-YHMRGWSDIsYHFLVGGDgRIYQGRGWNYVGWH-AGGNYNSYSIGIELIGNF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 577244852 277 GaDNATFLKNEQATFQECARLLKKWGLPaNRNTIRLHNEFT-STSCPHR 324
Cdd:cd06583   79 D-GGPPTAAQLEALAELLAYLVKRYGIP-PDYRIVGHRDVSpGTECPGD 125
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 199-324 1.16e-17

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: 78.94  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852  199 NPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRleAGiAHSYVSGN-TVWQALDESQVGWHTANQIGNKYYYGIEVCQSMG 277
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAACIARGWSD--VS-YHYLIDRDgTIYQLVPENGRAWHAGNGGGNDRSIGIELEGNFG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 577244852  278 ADNATfLKNEQATFQECARLLKKWGLPANRNTIRlHNEFTSTSCPHR 324
Cdd:pfam01510  78 GDPPT-DAQYEALARLLADLCKRYGIPPDRRIVG-HRDVGRKTDPGP 122
SH3b smart00287
Bacterial SH3 domain homologues;
398-464 3.22e-08

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 50.02  E-value: 3.22e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577244852   398 EESARFTNgnQPITVRKvGPFLSCPVGYQFQPGGYCDYTEVmlqDGHVWVGYTW-EGQRYYLPIRTWN 464
Cdd:smart00287   1 SETAVVTG--DGLNVRT-GPGTSSPIIGTLKKGDKVKVLGV---DGQDWAKITYgSGQRGYVPGYVVN 62
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 31-113 3.27e-08

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 50.88  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852   31 QCFDYAnagWKALFGLLLKGVGAKDipFANNFDGLATVYQNTPdflaQPGDMVVFGSN-YGAGYGHVAWVIEATLDYIIV 109
Cdd:pfam05257   9 QCTWFV---YWRVAQLGIYLGNAGD--WADAAAGAYKVGSTTP----KVGDIVVFDPGgGGASYGHVAIVEKVNDGSITV 79


                  ....
gi 577244852  110 YEQN 113
Cdd:pfam05257  80 SEQN 83
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
27-119 3.21e-03

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 37.66  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852  27 WYAF-QCFDYANAGWKALFGLLLKGVG-AKDipFANNFDGLATVYQNTPdflaQPGDMVVFGSNYGAGYGHVAWViEATL 104
Cdd:COG3942   20 GYPYgQCTWYAAWRRAQLGGPIGSGWGnANN--WADNARAAGYTVGSTP----KVGAVAVFTPGVAGPYGHVAVV-ESVN 92

                         90
                 ....*....|....*..
gi 577244852 105 D--YIIVYEQNWLGGGW 119
Cdd:COG3942   93 SdgSILVSEMNWGGPGI 109
 
Name Accession Description Interval E-value
SH3_5 pfam08460
Bacterial SH3 domain;
395-460 1.39e-26

Bacterial SH3 domain;


Pssm-ID: 430010 [Multi-domain]  Cd Length: 68  Bit Score: 102.08  E-value: 1.39e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577244852  395 YYMEESARFT-NGNQPITVRKVGPFLSCPVGYQFQPGGYCDYTEVMLQDGHVWVGYTWE-GQRYYLPI 460
Cdd:pfam08460   1 YYPSEQGTFTiGGKTGIVLRKNEPSLSAPVQFVLYKGDKVFYDQVLLADGYVWISYTSYnGVRRYLPV 68
Ami_2 smart00644
Ami_2 domain;
198-322 8.47e-25

Ami_2 domain;


Pssm-ID: 214760 [Multi-domain]  Cd Length: 126  Bit Score: 98.97  E-value: 8.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852   198 SNPKGIVIHNDAGSkGATAEAYRNGLVNaplSRLEAGIAHSYVSGN-TVWQALDESQVGWHTANQ---IGNKYYYGIEVC 273
Cdd:smart00644   1 PPPRGIVIHHTANS-NASCANEARYMQN---NHMNDIGYHFLVGGDgRVYQGVGWNYVAWHAGGAhtpGYNDISIGIEFI 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 577244852   274 QSMGADNATFLKNEQATFQECARLLKKWGLPAN-RNTIRLHNEFTSTSCP 322
Cdd:smart00644  77 GSFDSDDEPFAEALYAALDLLAKLLKGAGLPPDgRYRIVGHRDVAPTEDP 126
CwlA COG5632
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis];
194-376 2.14e-19

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


Pssm-ID: 444359  Cd Length: 177  Bit Score: 85.41  E-value: 2.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852 194 PKRGSNPKGIVIHNDAGsKGATAEAYRNGLVNAplSRlEAGiAHSYVSGNTVWQALDESQVGWH--TANQIGNKYYYGIE 271
Cdd:COG5632   18 PGYKMKPKGIVIHNTAN-PGATAENHANYFNNN--NR-SAS-WHYFVDDKEIIQHIPLNENAWHagDGTGPGNRRSIGIE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852 272 VCQSMGADnatFLKNEQATFQECARLLKKWGLPANRntIRLHNEFTSTSCPHRssvlhtgfdpvtrgLLPEDKRlqLKDY 351
Cdd:COG5632   93 ICENKDGD---FAKAYENAAELIAYLMKKYGIPIDN--VVRHYDWSGKNCPHG--------------LLANGGY--RWDQ 151

                        170       180
                 ....*....|....*....|....*
gi 577244852 352 FIKQIRAYMDGKIPVATVSNESSAS 376
Cdd:COG5632  152 FKADVKSALNGLSTVKPYTKVVKAS 176
PGRP cd06583
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in ...
 199-324 1.15e-18

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: 81.95  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852 199 NPKGIVIHNDAGSKGATAEAYRNGLVNaPLSRLEAGI-AHSYVSGN-TVWQALDESQVGWHtANQIGNKYYYGIEVCQSM 276
Cdd:cd06583    1 PVKYVVIHHTANPNCYTAAAAVRYLQN-YHMRGWSDIsYHFLVGGDgRIYQGRGWNYVGWH-AGGNYNSYSIGIELIGNF 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 577244852 277 GaDNATFLKNEQATFQECARLLKKWGLPaNRNTIRLHNEFT-STSCPHR 324
Cdd:cd06583   79 D-GGPPTAAQLEALAELLAYLVKRYGIP-PDYRIVGHRDVSpGTECPGD 125
Amidase_2 pfam01510
N-acetylmuramoyl-L-alanine amidase; This family includes zinc amidases that have ...
 199-324 1.16e-17

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: 78.94  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852  199 NPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRleAGiAHSYVSGN-TVWQALDESQVGWHTANQIGNKYYYGIEVCQSMG 277
Cdd:pfam01510   1 PIRYIVIHHTAGPSFAGALLPYAACIARGWSD--VS-YHYLIDRDgTIYQLVPENGRAWHAGNGGGNDRSIGIELEGNFG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 577244852  278 ADNATfLKNEQATFQECARLLKKWGLPANRNTIRlHNEFTSTSCPHR 324
Cdd:pfam01510  78 GDPPT-DAQYEALARLLADLCKRYGIPPDRRIVG-HRDVGRKTDPGP 122
SH3b smart00287
Bacterial SH3 domain homologues;
398-464 3.22e-08

Bacterial SH3 domain homologues;


Pssm-ID: 214600 [Multi-domain]  Cd Length: 63  Bit Score: 50.02  E-value: 3.22e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577244852   398 EESARFTNgnQPITVRKvGPFLSCPVGYQFQPGGYCDYTEVmlqDGHVWVGYTW-EGQRYYLPIRTWN 464
Cdd:smart00287   1 SETAVVTG--DGLNVRT-GPGTSSPIIGTLKKGDKVKVLGV---DGQDWAKITYgSGQRGYVPGYVVN 62
CHAP pfam05257
CHAP domain; This domain corresponds to an amidase function. Many of these proteins are ...
 31-113 3.27e-08

CHAP domain; This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78. This domain is found to be the catalytic domain of PlyCA. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyzes the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine.


Pssm-ID: 461605 [Multi-domain]  Cd Length: 83  Bit Score: 50.88  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852   31 QCFDYAnagWKALFGLLLKGVGAKDipFANNFDGLATVYQNTPdflaQPGDMVVFGSN-YGAGYGHVAWVIEATLDYIIV 109
Cdd:pfam05257   9 QCTWFV---YWRVAQLGIYLGNAGD--WADAAAGAYKVGSTTP----KVGDIVVFDPGgGGASYGHVAIVEKVNDGSITV 79


                  ....
gi 577244852  110 YEQN 113
Cdd:pfam05257  80 SEQN 83
COG3942 COG3942
Surface antigen [Cell wall/membrane/envelope biogenesis];
27-119 3.21e-03

Surface antigen [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443142 [Multi-domain]  Cd Length: 129  Bit Score: 37.66  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577244852  27 WYAF-QCFDYANAGWKALFGLLLKGVG-AKDipFANNFDGLATVYQNTPdflaQPGDMVVFGSNYGAGYGHVAWViEATL 104
Cdd:COG3942   20 GYPYgQCTWYAAWRRAQLGGPIGSGWGnANN--WADNARAAGYTVGSTP----KVGAVAVFTPGVAGPYGHVAVV-ESVN 92

                         90
                 ....*....|....*..
gi 577244852 105 D--YIIVYEQNWLGGGW 119
Cdd:COG3942   93 SdgSILVSEMNWGGPGI 109
 
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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