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Conserved domains on  [gi|2793893884|ref|WP_372070317|]
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MULTISPECIES: biosynthetic peptidoglycan transglycosylase, partial [unclassified Vibrio]

Protein Classification

biosynthetic peptidoglycan transglycosylase( domain architecture ID 10468720)

biosynthetic peptidoglycan transglycosylase is involved in the final stages of peptidoglycan synthesis

CATH:  1.10.3810.10
Gene Ontology:  GO:0071555|GO:0008955|GO:0009252|GO:0008360
PubMed:  8830253
SCOP:  4002510

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 66-213 1.95e-33

Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.


:

Pssm-ID: 459993 [Multi-domain]  Cd Length: 177  Bit Score: 119.55  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  66 YEADRHKVSL----KNLIQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRK 140
Cdd:pfam00912   9 GEENREYVPLddipPALKNAVLAIEDRRFYEHGGVDPKGIARALLSnLRSGRIVQGGSTITQQLAKNLF-LTPERTLTRK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884 141 FVEILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGE---------------IIPNPSKAEAFFLVERVSN 205
Cdd:pfam00912  88 LKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKdasdltlaeaallagLPQAPSRYNPLRNPERAKR 167


                  ....*...
gi 2793893884 206 IRRSLLAN 213
Cdd:pfam00912 168 RRNLVLDR 175
 
Name Accession Description Interval E-value
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 66-213 1.95e-33

Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.


Pssm-ID: 459993 [Multi-domain]  Cd Length: 177  Bit Score: 119.55  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  66 YEADRHKVSL----KNLIQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRK 140
Cdd:pfam00912   9 GEENREYVPLddipPALKNAVLAIEDRRFYEHGGVDPKGIARALLSnLRSGRIVQGGSTITQQLAKNLF-LTPERTLTRK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884 141 FVEILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGE---------------IIPNPSKAEAFFLVERVSN 205
Cdd:pfam00912  88 LKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKdasdltlaeaallagLPQAPSRYNPLRNPERAKR 167


                  ....*...
gi 2793893884 206 IRRSLLAN 213
Cdd:pfam00912 168 RRNLVLDR 175
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 7-193 4.35e-32

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 123.88  E-value: 4.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884   7 LVGLLTSLWIAILTLVFRTSLLDTHESLRLILTQQIsklirlpvtpnveyLIYRAN---LAT-YEADRHKVSL----KNL 78
Cdd:COG0744    21 LLAVLVLAALAGLVALYVADLPDPEELEDLALPQTS--------------TIYDRDgtlIATlGDENREWVPLdqipPHL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  79 IQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRKFVEILLAPWLNKVLEKR 157
Cdd:COG0744    87 KDAVVAIEDRRFYEHGGVDPKGIARALVAnLTAGGVVQGGSTITQQLVKNLF-LSNERTLSRKLKEALLALKLERKYSKD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2793893884 158 RILEIYICSVRYENRCFGVLSAMQHFFG---------E------IIPNPSK 193
Cdd:COG0744   166 EILELYLNTVYFGRGAYGIEAAAQYYFGksasdltlaEaallagLVKAPSY 216
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 69-200 1.66e-28

penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273955 [Multi-domain]  Cd Length: 531  Bit Score: 113.12  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  69 DRHKVSL----KNLIQLLIFIEDRDFYKHSGISYKAIGRGILSLFKLKRRS-GGSTIQQQLVRTLFiLDLSKTKRRKFVE 143
Cdd:TIGR02074   1 RREYVPIddipENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLeGGSTITQQLAKNLY-LTNERTITRKIQE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2793893884 144 ILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGEIIPNPSKAEAFFLV 200
Cdd:TIGR02074  80 ALLALKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLA 136
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 78-167 9.13e-15

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 73.65  E-value: 9.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  78 LIQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRKFVEILLAPWLNKVLEK 156
Cdd:PRK09506  223 LVDTLLATEDRHFYEHDGISLYSIGRAVLAnLTAGRTVQGGSTLTQQLVKNLF-LSNERSLWRKANEAYMALIMDARYSK 301

                          90
                  ....*....|.
gi 2793893884 157 RRILEIYICSV 167
Cdd:PRK09506  302 DRILELYLNEV 312
 
Name Accession Description Interval E-value
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 66-213 1.95e-33

Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.


Pssm-ID: 459993 [Multi-domain]  Cd Length: 177  Bit Score: 119.55  E-value: 1.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  66 YEADRHKVSL----KNLIQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRK 140
Cdd:pfam00912   9 GEENREYVPLddipPALKNAVLAIEDRRFYEHGGVDPKGIARALLSnLRSGRIVQGGSTITQQLAKNLF-LTPERTLTRK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884 141 FVEILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGE---------------IIPNPSKAEAFFLVERVSN 205
Cdd:pfam00912  88 LKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKdasdltlaeaallagLPQAPSRYNPLRNPERAKR 167


                  ....*...
gi 2793893884 206 IRRSLLAN 213
Cdd:pfam00912 168 RRNLVLDR 175
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 7-193 4.35e-32

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 123.88  E-value: 4.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884   7 LVGLLTSLWIAILTLVFRTSLLDTHESLRLILTQQIsklirlpvtpnveyLIYRAN---LAT-YEADRHKVSL----KNL 78
Cdd:COG0744    21 LLAVLVLAALAGLVALYVADLPDPEELEDLALPQTS--------------TIYDRDgtlIATlGDENREWVPLdqipPHL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  79 IQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRKFVEILLAPWLNKVLEKR 157
Cdd:COG0744    87 KDAVVAIEDRRFYEHGGVDPKGIARALVAnLTAGGVVQGGSTITQQLVKNLF-LSNERTLSRKLKEALLALKLERKYSKD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2793893884 158 RILEIYICSVRYENRCFGVLSAMQHFFG---------E------IIPNPSK 193
Cdd:COG0744   166 EILELYLNTVYFGRGAYGIEAAAQYYFGksasdltlaEaallagLVKAPSY 216
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 69-200 1.66e-28

penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273955 [Multi-domain]  Cd Length: 531  Bit Score: 113.12  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  69 DRHKVSL----KNLIQLLIFIEDRDFYKHSGISYKAIGRGILSLFKLKRRS-GGSTIQQQLVRTLFiLDLSKTKRRKFVE 143
Cdd:TIGR02074   1 RREYVPIddipENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLeGGSTITQQLAKNLY-LTNERTITRKIQE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2793893884 144 ILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGEIIPNPSKAEAFFLV 200
Cdd:TIGR02074  80 ALLALKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLA 136
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
76-185 4.67e-24

Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 101.00  E-value: 4.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  76 KNLIQLLIFIEDRDFYKHSGISYKAIGRGILSLFKL-KRRSGGSTIQQQLVRTLFiLDLSKTKRRKFVEILLAPWLNKVL 154
Cdd:COG5009    76 PLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTgRRVQGGSTITQQVAKNFL-LSPERTLTRKIKEAILALRIEQEL 154

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2793893884 155 EKRRILEIYICSVRYENRCFGVLSAMQHFFG 185
Cdd:COG5009   155 SKDEILELYLNKIYLGHRAYGVAAAAQTYFG 185
PBP_1b TIGR02071
penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) ...
 78-185 7.57e-18

penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273952 [Multi-domain]  Cd Length: 730  Bit Score: 82.85  E-value: 7.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  78 LIQLLIFIEDRDFYKHSGISYKAIGRGILSLFKLKR-RSGGSTIQQQLVRTLFiLDLSKTKRRKFVEILLAPWLNKVLEK 156
Cdd:TIGR02071 159 LVDTLLATEDRDFYEHDGISLYSIGRAVWVNLTAGRtVQGGSTLTQQLVKNLF-LSNERSLWRKANEAYMALILDARYSK 237

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2793893884 157 RRILEIYICSV----RYENRCFGVLSAMQHFFG 185
Cdd:TIGR02071 238 DRILELYLNEVylgqSGDDAIHGFPLASQYYFG 270
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 61-199 8.43e-17

monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain described by pfam00912 for transglycosylases. Species with this protein will have several other transglycosylases as well. All species with this protein are Proteobacteria that produce murein (peptidoglycan). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273951 [Multi-domain]  Cd Length: 224  Bit Score: 76.73  E-value: 8.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  61 ANLATYEADRHKVSL----KNLIQLLIFIEDRDFYKHSGISYKAIGRgilSLFKLKRR----SGGSTIQQQLVRTLFiLD 132
Cdd:TIGR02070  46 QGDPTCGIQHRWRPYdqisPNLKRAVIASEDAKFVEHHGFDWEAIQD---ALEKNEKSgkvvRGGSTISQQLAKNLF-LW 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2793893884 133 LSKTKRRKFVEILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGEIIPNPSKAEAFFL 199
Cdd:TIGR02070 122 SGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSASNLTRGQAARL 188
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
 70-164 1.10e-15

Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 76.41  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  70 RHKVSLKN----LIQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFilDLSKTKRRKFVEI 144
Cdd:COG4953    65 RLPVPLDEvsprYLQALLAYEDRRFYYHPGVNPLALLRAAWQnLRSGRIVSGGSTLTMQVARLLE--PRPRTLSGKLRQI 142

                          90       100
                  ....*....|....*....|
gi 2793893884 145 LLAPWLNKVLEKRRILEIYI 164
Cdd:COG4953   143 LRALQLERRYSKDEILELYL 162
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 78-167 9.13e-15

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 73.65  E-value: 9.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  78 LIQLLIFIEDRDFYKHSGISYKAIGRGILS-LFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRKFVEILLAPWLNKVLEK 156
Cdd:PRK09506  223 LVDTLLATEDRHFYEHDGISLYSIGRAVLAnLTAGRTVQGGSTLTQQLVKNLF-LSNERSLWRKANEAYMALIMDARYSK 301

                          90
                  ....*....|.
gi 2793893884 157 RRILEIYICSV 167
Cdd:PRK09506  302 DRILELYLNEV 312
PRK13481 PRK13481
glycosyltransferase; Provisional
 56-217 2.05e-14

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 70.60  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  56 YLIYRAN---LATYEADRHKVSLKNLIQLL----IFIEDRDFYKHSGISYKAIGRGILSLFKLKRRSGGSTIQQQLVRTL 128
Cdd:PRK13481   28 FLSTRDNvdeLRKIENKSSFVSADNMPEYVkgafISMEDERFYKHHGFDLKGTTRALFSTISDRDVQGGSTITQQVVKNY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884 129 FiLDLSKTKRRKFVEILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGEIIPNPSKAeafflVERVSNIRR 208
Cdd:PRK13481  108 F-YDNERSFTRKVKELFVAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNKNSTT-----MSHITVLQS 181


                  ....*....
gi 2793893884 209 SLLANKIVA 217
Cdd:PRK13481  182 AILASKVNA 190
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
 76-167 7.41e-13

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 67.95  E-value: 7.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  76 KNLIQLLIFIEDRDFYKHSGISYKAIGRGIL-SLFKLKRRSGGSTIQQQLVRTLFildLSKTKR--RKFVEILLAPWLNK 152
Cdd:PRK14850  167 EMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLvNLMSGHTIQGGSTLTQQLVKNLF---LTNTRSlwRKINEIYMALILDR 243

                          90
                  ....*....|....*
gi 2793893884 153 VLEKRRILEIYICSV 167
Cdd:PRK14850  244 FYSKDRILELYLNEV 258
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 78-185 1.14e-12

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 67.46  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  78 LIQLLIFIEDRDFYKHSGISYKAIGRGI-LSLFKLKRRSGGSTIQQQLVRTLFiLDLSKTKRRKFVEILLAPWLNKVLEK 156
Cdd:PRK11636   78 MVKAFIATEDSRFYEHHGVDPVGIFRAAsVALFSGHASQGASTITQQLARNFF-LSPERTLMRKIKEAFLAIRIEQLLTK 156

                          90       100
                  ....*....|....*....|....*....
gi 2793893884 157 RRILEIYICSVRYENRCFGVLSAMQHFFG 185
Cdd:PRK11636  157 DEILELYLNKIYLGYRAYGVGAAAQVYFG 185
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
 70-199 2.81e-06

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 48.16  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2793893884  70 RHKVSLKNL----IQLLIFIEDRDFYKHSGISYKAIGR-GILSLFKLKRRSGGSTIQQQLVRtlfILD-LSKTKRRKFVE 143
Cdd:PRK11240   62 RYPVTIEDVspryLEALINYEDRWFWKHPGVNPFSVARaAWQDLTSGRVISGGSTLTMQVAR---LLDpHPRTFGGKIRQ 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2793893884 144 ILLAPWLNKVLEKRRILEIYICSVRYENRCFGVLSAMQHFFGEIIPNPSKAEAFFL 199
Cdd:PRK11240  139 LWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALL 194
 
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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