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Conserved domains on  [gi|1447699609|ref|NP_310749|]
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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

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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) ...
 3-108 7.49e-49

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: 156.30  E-value: 7.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609   3 QTESAILVHARRCAPAESCGFVIGTPEGERYQPCVNISAEPEAYFRIAPEDWLQAEMQGEIVALVHSHPGGLPWLSEADR 82
Cdd:cd08073     1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                          90       100
                  ....*....|....*....|....*...
gi 1447699609  83 RLQIKSALPWWLVCR--GEIHKFRCVPH 108
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.
 111-224 1.21e-15

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: 70.39  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609 111 GRRFEHG-----VTDCYTLFRDAYHLAGITLPDFEREddwwrngqnlyldnMAATGFYRVPLSSAQAGDILLccFG-ASV 184
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--------------QYNAGKKTIPKSEPQRGDLVF--FGtGKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1447699609 185 ANHAAIYCGNGELLHHLP-EQLSKRERYSEKWQRRTHSVWR 224
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) ...
 3-108 7.49e-49

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: 156.30  E-value: 7.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609   3 QTESAILVHARRCAPAESCGFVIGTPEGERYQPCVNISAEPEAYFRIAPEDWLQAEMQGEIVALVHSHPGGLPWLSEADR 82
Cdd:cd08073     1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                          90       100
                  ....*....|....*....|....*...
gi 1447699609  83 RLQIKSALPWWLVCR--GEIHKFRCVPH 108
Cdd:cd08073    81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 7-114 8.15e-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: 97.68  E-value: 8.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609   7 AILVHARRCAPAESCGFVIGTPEGE----RYQPCVNISAEPEAYFRIAPEDWLQA-----EMQGEIVALVHSHPGGLPWL 77
Cdd:COG1310    11 AILAHAEAAYPEECCGLLLGKGGGDkrvtRVYPARNVAESPETRFEIDPEDLLAAerearERGLEIVGIYHSHPDGPAYP 90

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1447699609  78 SEADRRLQIKSALPWWLVC-RGEIHKFRCVpHLTGRRF 114
Cdd:COG1310    91 SETDRAQAAWPGLPYLIVSlPDGGPELRAW-RLRDGRF 127
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 111-224 1.21e-15

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: 70.39  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609 111 GRRFEHG-----VTDCYTLFRDAYHLAGITLPDFEREddwwrngqnlyldnMAATGFYRVPLSSAQAGDILLccFG-ASV 184
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--------------QYNAGKKTIPKSEPQRGDLVF--FGtGKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1447699609 185 ANHAAIYCGNGELLHHLP-EQLSKRERYSEKWQRRTHSVWR 224
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 7-92 2.85e-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: 2.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609    7 AILVHARRCAPAESCGFVIGTPEGERYQPCVNI-----------SAEPEAYFRIAPEDWLQAEMQGEIVALVHSHPGGLP 75
Cdd:smart00232  11 NILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFavpnepqddsvQEYDEDYSHLMDEELKKVNKDLEIVGWYHSHPDESP 90

                           90
                   ....*....|....*..
gi 1447699609   76 WLSEADRRLQIKSALPW 92
Cdd:smart00232  91 FPSEVDVATHESYQAPW 107
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 3-106 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 1447699609   3 QTESAILVHARRCAPAESCGFVIGTP-EGERYQPCVNIsAEPEAYFRIAPEDWLQ--AEM---QGEIVALVHSHPGGLPW 76
Cdd:pfam14464   3 PLLDAIVAHARAAHPLECCGILLGNElESQSVRVIPLV-NPMRNRFEIDPGDSLRrvKAArerGLELVGIYHSHPGGPAY 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1447699609  77 LSEADRRLqIKSALPWWLVCRGEIHKFRCV 106
Cdd:pfam14464  82 PSETDRRD-AAGPLPSYVIGGRAPPEIRSW 110
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
120-225 1.91e-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: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609 120 DCYTLFRDAYHLAGITLPDFERedDWWRNGQnlyldnmaatgfyRVPLSSAQAGDILLccF--GASVANHAAIYCGNGEL 197
Cdd:COG0791   126 DCSGLVQYVYRQAGISLPRTSA--DQAAAGT-------------PVSRSELQPGDLVF--FrtGGGGISHVGIYLGNGKF 188

                          90       100       110
                  ....*....|....*....|....*....|
gi 1447699609 198 LH-HLPEQLSKRERYSEK-WQRRTHSVWRH 225
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) ...
 3-108 7.49e-49

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: 156.30  E-value: 7.49e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609   3 QTESAILVHARRCAPAESCGFVIGTPEGERYQPCVNISAEPEAYFRIAPEDWLQAEMQGEIVALVHSHPGGLPWLSEADR 82
Cdd:cd08073     1 KLEDAILAHAKAEYPREACGLVVRKGRKLRYIPCRNIAADPEEHFEISPEDYAAAEDEGEIVAVVHSHPDGSPAPSEADR 80

                          90       100
                  ....*....|....*....|....*...
gi 1447699609  83 RLQIKSALPWWLVCR--GEIHKFRCVPH 108
Cdd:cd08073    81 AQQEATGLPWIIVSWpeGDLRVFRPVGY 108
MPN_prok_mb cd08059
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 3-106 1.20e-45

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: 148.09  E-value: 1.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609   3 QTESAILVHARRCAPAESCGFVIGTPEGeryqPCVNISAEPEAYFRIAPE-DWLQAEMQGEIVALVHSHPGGLPWLSEAD 81
Cdd:cd08059     1 DLLKTILVHAKDAHPDEFCGFLSGSKDN----VMDELIFLPFVSGSVSAViDLAALEIGMKVVGLVHSHPSGSCRPSEAD 76

                          90       100
                  ....*....|....*....|....*
gi 1447699609  82 RRLQIKSALPWWLVCRGEIHKFRCV 106
Cdd:cd08059    77 LSLFTRFGLYHVIVCYPYENSWKCY 101
Rri1 COG1310
Proteasome lid subunit RPN8/RPN11, contains Jab1/MPN domain metalloenzyme (JAMM) motif ...
 7-114 8.15e-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: 97.68  E-value: 8.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609   7 AILVHARRCAPAESCGFVIGTPEGE----RYQPCVNISAEPEAYFRIAPEDWLQA-----EMQGEIVALVHSHPGGLPWL 77
Cdd:COG1310    11 AILAHAEAAYPEECCGLLLGKGGGDkrvtRVYPARNVAESPETRFEIDPEDLLAAerearERGLEIVGIYHSHPDGPAYP 90

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1447699609  78 SEADRRLQIKSALPWWLVC-RGEIHKFRCVpHLTGRRF 114
Cdd:COG1310    91 SETDRAQAAWPGLPYLIVSlPDGGPELRAW-RLRDGRF 127
MPN_like cd08070
Mpr1p, Pad1p N-terminal (MPN) domains with catalytic isopeptidase activity (metal-binding); ...
 7-115 9.68e-20

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: 81.92  E-value: 9.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609   7 AILVHARRCAPAESCGFVIGTPEG-----ERYQPCVNISAEPEAYFRIAPEDWLQAEMQG-----EIVALVHSHPGGLPW 76
Cdd:cd08070     6 AILAHAEAEYPEECCGLLLGKGGGvtaivTEVYPVRNVAESPRRRFEIDPAEQLAAQREArerglEVVGIYHSHPDGPAR 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1447699609  77 LSEADRRLQIKSALPWWLVC----RGEIHKFRcvphLTGRRFE 115
Cdd:cd08070    86 PSETDLRLAWPPGVSYLIVSlaggAPELRAWR----LEGGQFE 124
NLPC_P60 pfam00877
NlpC/P60 family; The function of this domain is unknown. It is found in several lipoproteins.
 111-224 1.21e-15

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: 70.39  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609 111 GRRFEHG-----VTDCYTLFRDAYHLAGITLPDFEREddwwrngqnlyldnMAATGFYRVPLSSAQAGDILLccFG-ASV 184
Cdd:pfam00877   1 GVPYRWGggspsGFDCSGLVRYAFAKVGIELPRSSGQ--------------QYNAGKKTIPKSEPQRGDLVF--FGtGKG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1447699609 185 ANHAAIYCGNGELLHHLP-EQLSKRERYSEKWQRRTHSVWR 224
Cdd:pfam00877  65 ISHVGIYLGNGQMLHASTgGGVSISSLNGGYWQKRLVGVRR 105
JAB_MPN smart00232
JAB/MPN domain; Domain in Jun kinase activation domain binding protein and proteasomal ...
 7-92 2.85e-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: 2.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609    7 AILVHARRCAPAESCGFVIGTPEGERYQPCVNI-----------SAEPEAYFRIAPEDWLQAEMQGEIVALVHSHPGGLP 75
Cdd:smart00232  11 NILKHAIRDGPEEVCGVLLGKSNKDRPEVKEVFavpnepqddsvQEYDEDYSHLMDEELKKVNKDLEIVGWYHSHPDESP 90

                           90
                   ....*....|....*..
gi 1447699609   76 WLSEADRRLQIKSALPW 92
Cdd:smart00232  91 FPSEVDVATHESYQAPW 107
Prok-JAB pfam14464
Prokaryotic homologs of the JAB domain; These are metalloenzymes that function as the ...
 3-106 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 1447699609   3 QTESAILVHARRCAPAESCGFVIGTP-EGERYQPCVNIsAEPEAYFRIAPEDWLQ--AEM---QGEIVALVHSHPGGLPW 76
Cdd:pfam14464   3 PLLDAIVAHARAAHPLECCGILLGNElESQSVRVIPLV-NPMRNRFEIDPGDSLRrvKAArerGLELVGIYHSHPGGPAY 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1447699609  77 LSEADRRLqIKSALPWWLVCRGEIHKFRCV 106
Cdd:pfam14464  82 PSETDRRD-AAGPLPSYVIGGRAPPEIRSW 110
NlpC COG0791
Cell wall-associated hydrolase, NlpC_P60 family [Cell wall/membrane/envelope biogenesis];
120-225 1.91e-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: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699609 120 DCYTLFRDAYHLAGITLPDFERedDWWRNGQnlyldnmaatgfyRVPLSSAQAGDILLccF--GASVANHAAIYCGNGEL 197
Cdd:COG0791   126 DCSGLVQYVYRQAGISLPRTSA--DQAAAGT-------------PVSRSELQPGDLVF--FrtGGGGISHVGIYLGNGKF 188

                          90       100       110
                  ....*....|....*....|....*....|
gi 1447699609 198 LH-HLPEQLSKRERYSEK-WQRRTHSVWRH 225
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.
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