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Conserved domains on  [gi|896632252|ref|WP_049513189|]
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MULTISPECIES: M57 family metalloprotease [Streptococcus]

Protein Classification

ZnMc_MMP_like domain-containing protein( domain architecture ID 10136382)

ZnMc_MMP_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 89-229 4.59e-33

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


:

Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 117.21  E-value: 4.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  89 QASARIYLDPQMDSRFQEAYLEAIQNWNQTGAFNFELVTEASKADITATEMNDG--NTPVAGEAESQTNLLTGqflsvTV 166
Cdd:cd04268    1 KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIpyNDGTWSYGPSQVDPLTG-----EI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252 167 RLNHYYLSNPNYGYSYERIVHTAEHELGHAIGLDH-----------------TDEKSVMQPAGS----------FYGIQE 219
Cdd:cd04268   76 LLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHnfaasdrddnvdllaekGDTSSVMDYAPSnfsiqlgdgqKYTIGP 155

                        170
                 ....*....|
gi 896632252 220 EDVERLRKLY 229
Cdd:cd04268  156 YDIAAIKKLY 165
 
Name Accession Description Interval E-value
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 89-229 4.59e-33

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 117.21  E-value: 4.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  89 QASARIYLDPQMDSRFQEAYLEAIQNWNQTGAFNFELVTEASKADITATEMNDG--NTPVAGEAESQTNLLTGqflsvTV 166
Cdd:cd04268    1 KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIpyNDGTWSYGPSQVDPLTG-----EI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252 167 RLNHYYLSNPNYGYSYERIVHTAEHELGHAIGLDH-----------------TDEKSVMQPAGS----------FYGIQE 219
Cdd:cd04268   76 LLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHnfaasdrddnvdllaekGDTSSVMDYAPSnfsiqlgdgqKYTIGP 155

                        170
                 ....*....|
gi 896632252 220 EDVERLRKLY 229
Cdd:cd04268  156 YDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 16-230 1.04e-21

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 89.74  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  16 WRLFWRLVWIVVFLcALAFGFLWYLNGdfQGALKQAERSVKIGQQSI-------DQWEKTGQL-PKLNQTDSHQHSEGRW 87
Cdd:COG5549    3 KSTKLRRLLILLGL-VILTGILVILTS--LPSVSNLNNASSLPPLKVhplpptlAQWQDPTNSgDYFSQIKPTPVGYLVW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  88 PQASARIYLDP---QMDSRFQ---EAYLEAIQNWNQtgAFNFELVTEASKADIT----ATEMNDGNTPVAGEAESQTNL- 156
Cdd:COG5549   80 SQFPVKVYIDRppsAAQQRAQqwvAAVLQAIAEWNA--YLPLEVVENPENADIIivrsNPPLTASPNPETGARSAETTYe 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252 157 --LTGQFLS--VTVRLNHyylsnpnyGYSYERIVHTAEHELGHAIGL-DHTD-EKSVMQPAGS--FYGIQEEDVERLRKL 228
Cdd:COG5549  158 fyDTGNILShrFTILLSP--------NQTGKYLLATARHELGHALGIwGHSPsPTDAMYFSQVrnPPPISPRDINTLKRI 229


                 ..
gi 896632252 229 YE 230
Cdd:COG5549  230 YQ 231
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 39-203 3.64e-07

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 49.05  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252   39 YLNGDFQGALKQAERSVKIGQQSIDQWEKTGQLPKLNQTdshqhsegrwpqasARIYLDPQMD----SRFQEAYLEAIQN 114
Cdd:pfam12388   2 YVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSVTV--------------IKICVNPTSNfnsySRLSTGLDLAIAN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  115 WNQTG-AFNFELV---TEASKADITATemNDGNTP--VAGEAESQTNLLTGQFLSVTVRLNhyylsnpnyGYSYERIVHT 188
Cdd:pfam12388  68 YNRLGlRFTFRLTfgpNTGNSDMVTYD--NTANTPsgTGGSAGFPSGGLPYGTIQIGTGLQ---------SYSTDVNEHV 136

                         170
                  ....*....|....*
gi 896632252  189 AEHELGHAIGLDHTD 203
Cdd:pfam12388 137 ITHELGHSIGFRHSD 151
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 86-206 1.16e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 38.10  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252    86 RWPQA--SARIYlDPQMDSRFQEAYLEAIQNW-NQTGaFNFELVTEASKADITATEMNDGNtpvageaesqtnlltgqFL 162
Cdd:smart00235   4 KWPKGtvPYVID-SSSLSPEEREAIAKALAEWsDVTC-IRFVERTGTADIYISFGSGDSGC-----------------TL 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 896632252   163 SvtvrlnHYYLSNPNYGYSYER---IVHTAEHELGHAIGLDHTDEKS 206
Cdd:smart00235  65 S------HAGRPGGDQHLSLGNgciNTGVAAHELGHALGLYHEQSRS 105
 
Name Accession Description Interval E-value
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 89-229 4.59e-33

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 117.21  E-value: 4.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  89 QASARIYLDPQMDSRFQEAYLEAIQNWNQTGAFNFELVTEASKADITATEMNDG--NTPVAGEAESQTNLLTGqflsvTV 166
Cdd:cd04268    1 KKPITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPADIRYSVIRWIpyNDGTWSYGPSQVDPLTG-----EI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252 167 RLNHYYLSNPNYGYSYERIVHTAEHELGHAIGLDH-----------------TDEKSVMQPAGS----------FYGIQE 219
Cdd:cd04268   76 LLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHnfaasdrddnvdllaekGDTSSVMDYAPSnfsiqlgdgqKYTIGP 155

                        170
                 ....*....|
gi 896632252 220 EDVERLRKLY 229
Cdd:cd04268  156 YDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 16-230 1.04e-21

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 89.74  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  16 WRLFWRLVWIVVFLcALAFGFLWYLNGdfQGALKQAERSVKIGQQSI-------DQWEKTGQL-PKLNQTDSHQHSEGRW 87
Cdd:COG5549    3 KSTKLRRLLILLGL-VILTGILVILTS--LPSVSNLNNASSLPPLKVhplpptlAQWQDPTNSgDYFSQIKPTPVGYLVW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  88 PQASARIYLDP---QMDSRFQ---EAYLEAIQNWNQtgAFNFELVTEASKADIT----ATEMNDGNTPVAGEAESQTNL- 156
Cdd:COG5549   80 SQFPVKVYIDRppsAAQQRAQqwvAAVLQAIAEWNA--YLPLEVVENPENADIIivrsNPPLTASPNPETGARSAETTYe 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252 157 --LTGQFLS--VTVRLNHyylsnpnyGYSYERIVHTAEHELGHAIGL-DHTD-EKSVMQPAGS--FYGIQEEDVERLRKL 228
Cdd:COG5549  158 fyDTGNILShrFTILLSP--------NQTGKYLLATARHELGHALGIwGHSPsPTDAMYFSQVrnPPPISPRDINTLKRI 229


                 ..
gi 896632252 229 YE 230
Cdd:COG5549  230 YQ 231
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 93-230 2.07e-08

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 51.69  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  93 RIYLDPQ--MDSRFQEAYLEAIQN----WNQTGAFNFELVTEASK-ADITATEMNDGNTPVAGEAESQTNLLTGQFLSVT 165
Cdd:cd04279    5 RVYIDPTpaPPDSRAQSWLQAVKQaaaeWENVGPLKFVYNPEEDNdADIVIFFDRPPPVGGAGGGLARAGFPLISDGNRK 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896632252 166 VRLNHYYLSNPNYGYSYERIVHTAEHELGHAIGLDHT--DEKSVMQPAgsfYG--------IQEEDVERLRKLYE 230
Cdd:cd04279   85 LFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHsdRPEDAMYPS---QGqgpdgnptLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 122-216 2.10e-07

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 49.34  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252 122 NFELVTEASKADITATEMNDGNTPVAGEA----ESQTNLLTGQ-FLSVTvrLNHYYLSNPNYGYsyerivHTAEHELGHA 196
Cdd:cd04277   53 DFVEVSDNSGADIRFGNSSDPDGNTAGYAyypgSGSGTAYGGDiWFNSS--YDTNSDSPGSYGY------QTIIHEIGHA 124

                         90       100
                 ....*....|....*....|
gi 896632252 197 IGLDHTDEKSVMQPAGSFYG 216
Cdd:cd04277  125 LGLEHPGDYNGGDPVPPTYA 144
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
 39-203 3.64e-07

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 49.05  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252   39 YLNGDFQGALKQAERSVKIGQQSIDQWEKTGQLPKLNQTdshqhsegrwpqasARIYLDPQMD----SRFQEAYLEAIQN 114
Cdd:pfam12388   2 YVGRDAVVTLEASREMLQTDSDTAEQYRTTNLVGTSVTV--------------IKICVNPTSNfnsySRLSTGLDLAIAN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  115 WNQTG-AFNFELV---TEASKADITATemNDGNTP--VAGEAESQTNLLTGQFLSVTVRLNhyylsnpnyGYSYERIVHT 188
Cdd:pfam12388  68 YNRLGlRFTFRLTfgpNTGNSDMVTYD--NTANTPsgTGGSAGFPSGGLPYGTIQIGTGLQ---------SYSTDVNEHV 136

                         170
                  ....*....|....*
gi 896632252  189 AEHELGHAIGLDHTD 203
Cdd:pfam12388 137 ITHELGHSIGFRHSD 151
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 174-229 8.96e-07

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 47.23  E-value: 8.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896632252  174 SNPNYGYSYErivHTAEHELGHAIGLDHT-DEKSVMQPagsFYG--------IQEEDVERLRKLY 229
Cdd:pfam00413 100 SDPPHGINLF---LVAAHEIGHALGLGHSsDPGAIMYP---TYSpldskkfrLSQDDIKGIQQLY 158
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 187-229 2.36e-06

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 46.04  E-value: 2.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 896632252 187 HTAEHELGHAIGLDH-TDEKSVMQPA----GSFYGIQEEDVERLRKLY 229
Cdd:cd04278  109 SVAAHEIGHALGLGHsSDPDSIMYPYyqgpVPKFKLSQDDIRGIQALY 156
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
165-213 4.50e-06

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 45.33  E-value: 4.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 896632252 165 TVRL-NHYYLSNPNYGYSYERIVHTAEHELGHAIGLDH-TDEKSVMQPAGS 213
Cdd:COG1913  102 TARLrPEFYGLPPDEELFLERVLKEAVHELGHLFGLGHcPNPRCVMHFSNS 152
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 167-228 5.47e-06

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 45.37  E-value: 5.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 896632252 167 RLNHY-YLSNPNYGYSYERIVHTAEHELGHAIGLDH-TDEKSVMQPAGSfygIQEEDVER-------LRKL 228
Cdd:cd11375  104 RLRPEfYGLPPDEGLFLERLLKEAVHELGHLFGLDHcPYYACVMNFSNS---LEETDRKPpylcpvcLRKL 171
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 88-201 6.62e-06

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 45.39  E-value: 6.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252  88 PQASARIYLDPQMDSRFQEAYLEAIQNWNQtgAFN---FELVTEASKADITATEMN---------DGNTPVAGEAESQTN 155
Cdd:cd04276    6 PKEPIVYYLDNTFPEKYRDAIREGVLYWNK--AFEkagFKNAIIVKVLPDDADPGDirynvirwiHSPNGGWAYGPSVVD 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 896632252 156 LLTGQFLSVTVRLNHYYLSNPNYGYSY---ERIVHTAEHELGHAIGLDH 201
Cdd:cd04276   84 PRTGEILKADVILYSGFLRQDQLWYEDllaASLRYLLAHEVGHTLGLRH 132
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 86-206 1.16e-03

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 38.10  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252    86 RWPQA--SARIYlDPQMDSRFQEAYLEAIQNW-NQTGaFNFELVTEASKADITATEMNDGNtpvageaesqtnlltgqFL 162
Cdd:smart00235   4 KWPKGtvPYVID-SSSLSPEEREAIAKALAEWsDVTC-IRFVERTGTADIYISFGSGDSGC-----------------TL 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 896632252   163 SvtvrlnHYYLSNPNYGYSYER---IVHTAEHELGHAIGLDHTDEKS 206
Cdd:smart00235  65 S------HAGRPGGDQHLSLGNgciNTGVAAHELGHALGLYHEQSRS 105
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 105-229 1.37e-03

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 38.27  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896632252 105 QEAYLEAIQNWNQTGAFNFELVT-EASKADIT-ATEMNDGNTPVAGEAE--SQTNLLTGQFLSVTVRLNHYYLSNpnygy 180
Cdd:cd00203   24 QSLILIAMQIWRDYLNIRFVLVGvEIDKADIAiLVTRQDFDGGTGGWAYlgRVCDSLRGVGVLQDNQSGTKEGAQ----- 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896632252 181 syerivhTAEHELGHAIGLDH---------------------TDEKSVMQP-AGSF-----YGIQEEDVERLRKLY 229
Cdd:cd00203   99 -------TIAHELGHALGFYHdhdrkdrddyptiddtlnaedDDYYSVMSYtKGSFsdgqrKDFSQCDIDQINKLY 167
 
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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