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Conserved domains on  [gi|1840587955|ref|WP_170323343|]
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transglycosylase domain-containing protein [Bradyrhizobium sp. STM 3809]

Protein Classification

biosynthetic peptidoglycan transglycosylase( domain architecture ID 1001727)

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
PRK13481 super family cl29529
glycosyltransferase; Provisional
 44-227 4.09e-60

glycosyltransferase; Provisional


The actual alignment was detected with superfamily member TIGR02070:

Pssm-ID: 475222 [Multi-domain]  Cd Length: 224  Bit Score: 188.82  E-value: 4.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  44 PVSTLMLWRTMTGR-------PVERRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDWGALREVMDDAED-GEVSRGGSTI 115
Cdd:TIGR02070  31 PSTAFMVAEKLALWgqgdptcGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNEKsGKVVRGGSTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 116 TQQVAKNLFLWPGRSYVRKALELPLALWIDLVLPKRRILEIYLNIAELGPaGQFGVEAGANYAFNRSAAGLGPREAALMA 195
Cdd:TIGR02070 111 SQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN-GVFGAEAAARYYFKRSASNLTRGQAARLA 189

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1840587955 196 SILPNPVRRSARTPGPGVRRlAATYIMRAQAQ 227
Cdd:TIGR02070 190 AVLPNPKYYDENRPGPYVRR-KATWILKQMGY 220
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 44-227 4.09e-60

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: 188.82  E-value: 4.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  44 PVSTLMLWRTMTGR-------PVERRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDWGALREVMDDAED-GEVSRGGSTI 115
Cdd:TIGR02070  31 PSTAFMVAEKLALWgqgdptcGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNEKsGKVVRGGSTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 116 TQQVAKNLFLWPGRSYVRKALELPLALWIDLVLPKRRILEIYLNIAELGPaGQFGVEAGANYAFNRSAAGLGPREAALMA 195
Cdd:TIGR02070 111 SQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN-GVFGAEAAARYYFKRSASNLTRGQAARLA 189

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1840587955 196 SILPNPVRRSARTPGPGVRRlAATYIMRAQAQ 227
Cdd:TIGR02070 190 AVLPNPKYYDENRPGPYVRR-KATWILKQMGY 220
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 57-205 1.34e-57

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: 180.80  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  57 RPVERRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDWGAL-REVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKA 135
Cdd:pfam00912   9 GEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIaRALLSNLRSGRIVQGGSTITQQLAKNLFLTPERTLTRKL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 136 LELPLALWIDLVLPKRRILEIYLNIAELGPaGQFGVEAGANYAFNRSAAGLGPREAALMASILPNPVRRS 205
Cdd:pfam00912  89 KEAVLALKLERRYSKDEILEAYLNTVYFGR-GAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYN 157
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 61-215 1.09e-56

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 190.52  E-value: 1.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  61 RRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDW-GALREVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKALELP 139
Cdd:COG0744    74 REWVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPkGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEAL 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840587955 140 LALWIDLVLPKRRILEIYLNIAELGpAGQFGVEAGANYAFNRSAAGLGPREAALMASILPNPVRRSARTPGPGVRR 215
Cdd:COG0744   154 LALKLERKYSKDEILELYLNTVYFG-RGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKE 228
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 60-225 5.55e-23

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 97.12  E-value: 5.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  60 ERRWI--DLAAMSPYLPRSVVAAEDAKFCTHHGID-WGALREVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKAL 136
Cdd:PRK11636   63 EKRRIplTLDQIPPEMVKAFIATEDSRFYEHHGVDpVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 137 ELPLALWIDLVLPKRRILEIYLNIAELGPAGqFGVEAGANYAFNRSAAGLGPREAALMASiLP------NPV----RRSA 206
Cdd:PRK11636  143 EAFLAIRIEQLLTKDEILELYLNKIYLGYRA-YGVGAAAQVYFGKTVDQLTLSEMAVIAG-LPkapstfNPLysmdRAVA 220

                         170
                  ....*....|....*....
gi 1840587955 207 RTPGPGVRRLAATYIMRAQ 225
Cdd:PRK11636  221 RRNVVLSRMLDEGYITQAQ 239
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 44-227 4.09e-60

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: 188.82  E-value: 4.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  44 PVSTLMLWRTMTGR-------PVERRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDWGALREVMDDAED-GEVSRGGSTI 115
Cdd:TIGR02070  31 PSTAFMVAEKLALWgqgdptcGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNEKsGKVVRGGSTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 116 TQQVAKNLFLWPGRSYVRKALELPLALWIDLVLPKRRILEIYLNIAELGPaGQFGVEAGANYAFNRSAAGLGPREAALMA 195
Cdd:TIGR02070 111 SQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN-GVFGAEAAARYYFKRSASNLTRGQAARLA 189

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1840587955 196 SILPNPVRRSARTPGPGVRRlAATYIMRAQAQ 227
Cdd:TIGR02070 190 AVLPNPKYYDENRPGPYVRR-KATWILKQMGY 220
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 57-205 1.34e-57

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: 180.80  E-value: 1.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  57 RPVERRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDWGAL-REVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKA 135
Cdd:pfam00912   9 GEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIaRALLSNLRSGRIVQGGSTITQQLAKNLFLTPERTLTRKL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 136 LELPLALWIDLVLPKRRILEIYLNIAELGPaGQFGVEAGANYAFNRSAAGLGPREAALMASILPNPVRRS 205
Cdd:pfam00912  89 KEAVLALKLERRYSKDEILEAYLNTVYFGR-GAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYN 157
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 61-215 1.09e-56

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 190.52  E-value: 1.09e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  61 RRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDW-GALREVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKALELP 139
Cdd:COG0744    74 REWVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPkGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEAL 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840587955 140 LALWIDLVLPKRRILEIYLNIAELGpAGQFGVEAGANYAFNRSAAGLGPREAALMASILPNPVRRSARTPGPGVRR 215
Cdd:COG0744   154 LALKLERKYSKDEILELYLNTVYFG-RGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKE 228
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 61-201 3.62e-41

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: 147.02  E-value: 3.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  61 RRWIDLAAMSPYLPRSVVAAEDAKFCTHHGID-WGALREVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKALELP 139
Cdd:TIGR02074   2 REYVPIDDIPENLINAFLAIEDRRFYDHFGIDlKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEAL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840587955 140 LALWIDLVLPKRRILEIYLNIAELGpAGQFGVEAGANYAFNRSAAGLGPREAALMASILPNP 201
Cdd:TIGR02074  82 LALKLEQKLSKDEILELYLNRIYFG-NGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAP 142
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
59-207 2.05e-37

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


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 138.75  E-value: 2.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  59 VERR-WIDLAAMSPYLPRSVVAAEDAKFCTHHGIDW-GALREVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKAL 136
Cdd:COG5009    63 EERRiPVPIEEIPPLLINAFLAAEDKRFYEHPGVDPiGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIK 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840587955 137 ELPLALWIDLVLPKRRILEIYLNIAELGpAGQFGVEAGANYAFNRSAAGLGPREAALMASILP-----NPVRRSAR 207
Cdd:COG5009   143 EAILALRIEQELSKDEILELYLNKIYLG-HRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKapsryNPIRNPER 217
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
 50-204 2.38e-23

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


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 97.98  E-value: 2.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  50 LWRTMTGRPVERRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDWGAL-REVMDDAEDGEVSRGGSTITQQVAKnlFLWPG 128
Cdd:COG4953    54 LRAFLAADGQWRLPVPLDEVSPRYLQALLAYEDRRFYYHPGVNPLALlRAAWQNLRSGRIVSGGSTLTMQVAR--LLEPR 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1840587955 129 -RSYVRKALELPLALWIDLVLPKRRILEIYLNIAELGPAGQfGVEAGANYAFNRSAAGLGPREAALMAsILPN-PVRR 204
Cdd:COG4953   132 pRTLSGKLRQILRALQLERRYSKDEILELYLNLAPYGGNIE-GVEAASLAYFGKPPSRLSLAEAALLA-VLPQaPSRR 207
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 60-225 5.55e-23

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 97.12  E-value: 5.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  60 ERRWI--DLAAMSPYLPRSVVAAEDAKFCTHHGID-WGALREVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKAL 136
Cdd:PRK11636   63 EKRRIplTLDQIPPEMVKAFIATEDSRFYEHHGVDpVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 137 ELPLALWIDLVLPKRRILEIYLNIAELGPAGqFGVEAGANYAFNRSAAGLGPREAALMASiLP------NPV----RRSA 206
Cdd:PRK11636  143 EAFLAIRIEQLLTKDEILELYLNKIYLGYRA-YGVGAAAQVYFGKTVDQLTLSEMAVIAG-LPkapstfNPLysmdRAVA 220

                         170
                  ....*....|....*....
gi 1840587955 207 RTPGPGVRRLAATYIMRAQ 225
Cdd:PRK11636  221 RRNVVLSRMLDEGYITQAQ 239
PRK13481 PRK13481
glycosyltransferase; Provisional
 69-182 1.09e-18

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 81.39  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  69 MSPYLPRSVVAAEDAKFCTHHGIDW-GALREVMDDAEDGEVsRGGSTITQQVAKNLFLWPGRSYVRKALELPLALWIDLV 147
Cdd:PRK13481   53 MPEYVKGAFISMEDERFYKHHGFDLkGTTRALFSTISDRDV-QGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQ 131

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1840587955 148 LPKRRILEIYLNIAELGpAGQFGVEAGANYAFNRS 182
Cdd:PRK13481  132 YSKNEILSFYLNNIYFG-DNQYTLEGAANHYFGTT 165
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 72-167 4.31e-16

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 76.73  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  72 YLPRS---------VVAAEDAKFCTHHGID-WGALREVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKALELPLA 141
Cdd:PRK09506  213 FVPRSgfpdllvdtLLATEDRHFYEHDGISlYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMA 292

                          90       100
                  ....*....|....*....|....*.
gi 1840587955 142 LWIDLVLPKRRILEIYLNIAELGPAG 167
Cdd:PRK09506  293 LIMDARYSKDRILELYLNEVYLGQSG 318
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
 73-194 3.71e-14

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 71.03  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  73 LPRSVVAAEDAKFCTHHGIDWGAL-REVMDDAEDGEVSRGGSTITQQVAKNLFLWPGRSYVRKALELPLALWIDLVLPKR 151
Cdd:PRK14850  169 LIKTLLAIEDKYFYEHDGIHLSSIgRAFLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEIYMALILDRFYSKD 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1840587955 152 RILEIYLNIAELGPAGQ---FGVEAGANYAFNRSAAGLGPREAALM 194
Cdd:PRK14850  249 RILELYLNEVYLGQDGNeqiRGFPLASIYYFGRPINELNLDQYALL 294
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
 50-209 3.66e-10

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 59.33  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955  50 LWRTMTGRPVERRWIDLAAMSPYLPRSVVAAEDAKFCTHHGIDWGAL-REVMDDAEDGEVSRGGSTITQQVAKNLFLWPg 128
Cdd:PRK11240   51 LWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVaRAAWQDLTSGRVISGGSTLTMQVARLLDPHP- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840587955 129 RSYVRKALELPLALWIDLVLPKRRILEIYLNIAELGPAGQfGVEAGANYAFNRSAAGLGPREAALMASILPNPVR-RSAR 207
Cdd:PRK11240  130 RTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQ-GIGAASWAYLGKSPANLSYAEAALLAVLPQAPSRlRPDR 208


                  ..
gi 1840587955 208 TP 209
Cdd:PRK11240  209 WP 210
 
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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