NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15830812|ref|NP_309585|]
View 

phage tail assembly protein [Escherichia coli O157:H7 str. Sakai]

Protein Classification

C40 family peptidase( domain architecture ID 10169217)

C40 family peptidase is a cell-wall hydrolase that cleaves peptide cross-bridges between glycan chains and is essential for bacterial growth and viability; typically cleaves the linkage between D-Glu and diaminopimelic acid (or Lys) within peptidoglycan stem peptides; contains a Cys-His-His catalytic triad

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 1-106 2.99e-51

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) found in proteins also containing NlpC/P60 domains; This family contains bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains at the N-terminus of NlpC/P60 phage tail protein domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


:

Pssm-ID: 163704  Cd Length: 108  Bit Score: 162.47  E-value: 2.99e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   1 MLYSNILAHARRCAPAESCGFVVRTPEGERYFPCVNISGEPEDYFRMSPEDWLRAEMQGEIVALVHSHPGGLPWLSEADR 80
Cdd:cd08073   1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                        90       100
                ....*....|....*....|....*...
gi 15830812  81 RLQIKSALSWWLVCR--GEIHKFRCVPH 106
Cdd:cd08073  81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
NLPC_P60 super family cl21534
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 109-222 1.65e-13

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


The actual alignment was detected with superfamily member pfam00877:

Pssm-ID: 473902 [Multi-domain]  Cd Length: 105  Bit Score: 64.61  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   109 GRRFEHG-----VTDCYTLFRDAYHLAGIDMPDFEREddwwrngqnlyldnMAVTGFYRVPLSSAQAGDILLccFG-ASV 182
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--------------QYNAGKKTIPKSEPQRGDLVF--FGtGKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15830812   183 ANHAAIYCGNGELLHHLP-EQLSKRERYSEKWQRRTHSAWR 222
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
 
Name Accession Description Interval E-value
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 1-106 2.99e-51

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) found in proteins also containing NlpC/P60 domains; This family contains bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains at the N-terminus of NlpC/P60 phage tail protein domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163704  Cd Length: 108  Bit Score: 162.47  E-value: 2.99e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   1 MLYSNILAHARRCAPAESCGFVVRTPEGERYFPCVNISGEPEDYFRMSPEDWLRAEMQGEIVALVHSHPGGLPWLSEADR 80
Cdd:cd08073   1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                        90       100
                ....*....|....*....|....*...
gi 15830812  81 RLQIKSALSWWLVCR--GEIHKFRCVPH 106
Cdd:cd08073  81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 2-112 4.55e-26

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 98.45  E-value: 4.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   2 LYSNILAHARRCAPAESCGFVVRTPEGE----RYFPCVNISGEPEDYFRMSPEDWLRA-----EMQGEIVALVHSHPGGL 72
Cdd:COG1310   8 LLDAILAHAEAAYPEECCGLLLGKGGGDkrvtRVYPARNVAESPETRFEIDPEDLLAAerearERGLEIVGIYHSHPDGP 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15830812  73 PWLSEADRRLQIKSALSWWLVC-RGEIHKFRCVpHLTGRRF 112
Cdd:COG1310  88 AYPSETDRAQAAWPGLPYLIVSlPDGGPELRAW-RLRDGRF 127
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 5-83 3.76e-15

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 70.10  E-value: 3.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812      5 NILAHARRCAPAESCGFVVRTPEGERYFPCVNI-----------SGEPEDYFRMSPEDWLRAEMQGEIVALVHSHPGGLP 73
Cdd:smart00232  11 NILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFavpnepqddsvQEYDEDYSHLMDEELKKVNKDLEIVGWYHSHPDESP 90

                           90
                   ....*....|
gi 15830812     74 WLSEADRRLQ 83
Cdd:smart00232  91 FPSEVDVATH 100
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 109-222 1.65e-13

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 64.61  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   109 GRRFEHG-----VTDCYTLFRDAYHLAGIDMPDFEREddwwrngqnlyldnMAVTGFYRVPLSSAQAGDILLccFG-ASV 182
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--------------QYNAGKKTIPKSEPQRGDLVF--FGtGKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15830812   183 ANHAAIYCGNGELLHHLP-EQLSKRERYSEKWQRRTHSAWR 222
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 2-104 3.03e-13

Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism.


Pssm-ID: 464179  Cd Length: 113  Bit Score: 64.06  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812     2 LYSNILAHARRCAPAESCGFVV-RTPEGERYFPCVNISgEPEDYFRMSPEDWLR--AEM---QGEIVALVHSHPGGLPWL 75
Cdd:pfam14464   4 LLDAIVAHARAAHPLECCGILLgNELESQSVRVIPLVN-PMRNRFEIDPGDSLRrvKAArerGLELVGIYHSHPGGPAYP 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15830812    76 SEADRRLQIKSALSWWLVCR--GEIHKFRCV 104
Cdd:pfam14464  83 SETDRRDAAGPLPSYVIGGRapPEIRSWRLV 113
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
118-223 1.71e-08

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 53.16  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812 118 DCYTLFRDAYHLAGIDMPDFERedDWWRNGQnlyldnmavtgfyRVPLSSAQAGDILLccF--GASVANHAAIYCGNGEL 195
Cdd:COG0791 126 DCSGLVQYVYRQAGISLPRTSA--DQAAAGT-------------PVSRSELQPGDLVF--FrtGGGGISHVGIYLGNGKF 188

                        90       100       110
                ....*....|....*....|....*....|
gi 15830812 196 LH-HLPEQLSKRERYSEK-WQRRTHSAWRH 223
Cdd:COG0791 189 IHaSSSGKGVRISSLDSPyWKSRYVGARRV 218
 
Name Accession Description Interval E-value
MPN_NLPC_P60 cd08073
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) ...
 1-106 2.99e-51

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding) found in proteins also containing NlpC/P60 domains; This family contains bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains at the N-terminus of NlpC/P60 phage tail protein domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163704  Cd Length: 108  Bit Score: 162.47  E-value: 2.99e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   1 MLYSNILAHARRCAPAESCGFVVRTPEGERYFPCVNISGEPEDYFRMSPEDWLRAEMQGEIVALVHSHPGGLPWLSEADR 80
Cdd:cd08073   1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                        90       100
                ....*....|....*....|....*...
gi 15830812  81 RLQIKSALSWWLVCR--GEIHKFRCVPH 106
Cdd:cd08073  81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 2-104 7.70e-39

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); prokaryotic; This family contains bacterial and archaeal MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These catalytically active domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163690  Cd Length: 101  Bit Score: 130.37  E-value: 7.70e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   2 LYSNILAHARRCAPAESCGFVVRTPEGeryfPCVNISGEPEDYFRMSPE-DWLRAEMQGEIVALVHSHPGGLPWLSEADR 80
Cdd:cd08059   2 LLKTILVHAKDAHPDEFCGFLSGSKDN----VMDELIFLPFVSGSVSAViDLAALEIGMKVVGLVHSHPSGSCRPSEADL 77

                        90       100
                ....*....|....*....|....
gi 15830812  81 RLQIKSALSWWLVCRGEIHKFRCV 104
Cdd:cd08059  78 SLFTRFGLYHVIVCYPYENSWKCY 101
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 2-112 4.55e-26

Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440921  Cd Length: 127  Bit Score: 98.45  E-value: 4.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   2 LYSNILAHARRCAPAESCGFVVRTPEGE----RYFPCVNISGEPEDYFRMSPEDWLRA-----EMQGEIVALVHSHPGGL 72
Cdd:COG1310   8 LLDAILAHAEAAYPEECCGLLLGKGGGDkrvtRVYPARNVAESPETRFEIDPEDLLAAerearERGLEIVGIYHSHPDGP 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15830812  73 PWLSEADRRLQIKSALSWWLVC-RGEIHKFRCVpHLTGRRF 112
Cdd:COG1310  88 AYPSETDRAQAAWPGLPYLIVSlPDGGPELRAW-RLRDGRF 127
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 2-113 7.40e-21

Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); This family contains archaeal and bacterial MPN (also known as Mov34, PAD-1, JAMM, JAB, MPN+)-like domains. These domains contain the signature JAB1/MPN/Mov34 metalloenzyme (JAMM) motif, EXnHS/THX7SXXD, which is involved in zinc ion coordination and provides the active site for isopeptidase activity for the release of ubiquitin from ubiquitinated proteins (thus having deubiquitinating (DUB) activity) that are tagged for degradation. The JAMM proteins likely hydrolyze ubiquitin conjugates in a manner similar to thermolysin, in which the zinc-polarized aqua ligand serves as the nucleophile, compared with the classical DUBs that do so with a cysteine residue in the active site.


Pssm-ID: 163701  Cd Length: 128  Bit Score: 84.62  E-value: 7.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   2 LYSNILAHARRCAPAESCGFVVRTPEG-----ERYFPCVNISGEPEDYFRMSPEDWLRAEMQG-----EIVALVHSHPGG 71
Cdd:cd08070   3 LLEAILAHAEAEYPEECCGLLLGKGGGvtaivTEVYPVRNVAESPRRRFEIDPAEQLAAQREArerglEVVGIYHSHPDG 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15830812  72 LPWLSEADRRLQIKSALSWWLVC----RGEIHKFRcvphLTGRRFE 113
Cdd:cd08070  83 PARPSETDLRLAWPPGVSYLIVSlaggAPELRAWR----LEGGQFE 124
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 5-83 3.76e-15

JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal subunits. Domain at Mpr1p and Pad1p N-termini. Domain of unknown function.


Pssm-ID: 214573  Cd Length: 135  Bit Score: 70.10  E-value: 3.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812      5 NILAHARRCAPAESCGFVVRTPEGERYFPCVNI-----------SGEPEDYFRMSPEDWLRAEMQGEIVALVHSHPGGLP 73
Cdd:smart00232  11 NILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFavpnepqddsvQEYDEDYSHLMDEELKKVNKDLEIVGWYHSHPDESP 90

                           90
                   ....*....|
gi 15830812     74 WLSEADRRLQ 83
Cdd:smart00232  91 FPSEVDVATH 100
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 109-222 1.65e-13

NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.


Pssm-ID: 395705 [Multi-domain]  Cd Length: 105  Bit Score: 64.61  E-value: 1.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812   109 GRRFEHG-----VTDCYTLFRDAYHLAGIDMPDFEREddwwrngqnlyldnMAVTGFYRVPLSSAQAGDILLccFG-ASV 182
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--------------QYNAGKKTIPKSEPQRGDLVF--FGtGKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 15830812   183 ANHAAIYCGNGELLHHLP-EQLSKRERYSEKWQRRTHSAWR 222
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 2-104 3.03e-13

Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ubiquitin isopeptidase/ deubiquitinase in the ubiquitin-based signaling and protein turnover pathways in eukaryotes. Prokaryotic JAB domains are predicted to have a similar role in their cognates of the ubiquitin modification pathway. The domain is widely found in bacteria, archaea and phages where they are present in several gene contexts in addition to those that correspond to the prokaryotic cognates of the eukaryotic Ub pathway. Other contexts in which JAB domains are present include gene neighbor associations with ubiquitin fold domains in cysteine and siderophore biosynthesis, and phage tail morphogenesis, where they are shown or predicted to process the associated ubiquitin. A distinct family, the RadC-like JAB domains are widespread in bacteria and are predicted to function as nucleases. In halophilic archaea the JAB domain shows strong gene-neighborhood associations with a nucleotidyltransferase suggesting a role in nucleotide metabolism.


Pssm-ID: 464179  Cd Length: 113  Bit Score: 64.06  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812     2 LYSNILAHARRCAPAESCGFVV-RTPEGERYFPCVNISgEPEDYFRMSPEDWLR--AEM---QGEIVALVHSHPGGLPWL 75
Cdd:pfam14464   4 LLDAIVAHARAAHPLECCGILLgNELESQSVRVIPLVN-PMRNRFEIDPGDSLRrvKAArerGLELVGIYHSHPGGPAYP 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15830812    76 SEADRRLQIKSALSWWLVCR--GEIHKFRCV 104
Cdd:pfam14464  83 SETDRRDAAGPLPSYVIGGRapPEIRSWRLV 113
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
118-223 1.71e-08

Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440554 [Multi-domain]  Cd Length: 218  Bit Score: 53.16  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830812 118 DCYTLFRDAYHLAGIDMPDFERedDWWRNGQnlyldnmavtgfyRVPLSSAQAGDILLccF--GASVANHAAIYCGNGEL 195
Cdd:COG0791 126 DCSGLVQYVYRQAGISLPRTSA--DQAAAGT-------------PVSRSELQPGDLVF--FrtGGGGISHVGIYLGNGKF 188

                        90       100       110
                ....*....|....*....|....*....|
gi 15830812 196 LH-HLPEQLSKRERYSEK-WQRRTHSAWRH 223
Cdd:COG0791 189 IHaSSSGKGVRISSLDSPyWKSRYVGARRV 218
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH