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Conserved domains on  [gi|1907131464|ref|XP_036017269|]
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carnosine synthase 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
658-934 1.72e-39

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 147.33  E-value: 1.72e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  658 NALLLAELVRARNLKLDGCFSFWDDCLVLTALLCRELGLPCSPPAAMCLAKQKSRTQLHLLRcQGPPwpstslhAVACCP 737
Cdd:COG0439      3 DAIIAAAAELARETGIDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAA-AGVP-------VPGFAL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  738 LENEADVERAIYQVPLPGVMKLEFGSGAVGVQLVKDGPQCREHFSRILHDLQGEADHPGiglgwgnaMLLMEFVEGTEHD 817
Cdd:COG0439     75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGE--------VLVEEFLEGREYS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  818 VDLVVFGGRLLAAFVSDNGPTRlPGFTETAACMPTGLAPEQEAQVVQAAFRCCLGCGLLDGVFNVELKMTGAG-PRLIEI 896
Cdd:COG0439    147 VEGLVRDGEVVVCSITRKHQKP-PYFVELGHEAPSPLPEELRAEIGELVARALRALGYRRGAFHTEFLLTPDGePYLIEI 225
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907131464  897 NPRMGGFYLRDWILELYGVDLLLASTMVACGLQPALPA 934
Cdd:COG0439    226 NARLGGEHIPPLTELATGVDLVREQIRLALGEPRILDP 263
ATPgrasp_N super family cl39516
ATP-grasp N-terminal domain; This is the N-terminal domain found in BL00235 present in ...
617-697 1.83e-07

ATP-grasp N-terminal domain; This is the N-terminal domain found in BL00235 present in Bacillus licheniformis. BL00235 is a ATP-grasp superfamily protein that catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner. BL00235 has a highly restricted substrate specificity: the N-terminal substrate is confined to L-methionine an L-leucine, while the C-terminal substrates include small residues such as L-alanine, L-serine, L-threonine and L-cysteine.


The actual alignment was detected with superfamily member pfam18130:

Pssm-ID: 407962 [Multi-domain]  Cd Length: 81  Bit Score: 49.57  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  617 EAARDYGLTLHLV----ESDPNHFASqlVQTFIHFDVTEhrrDEENAL-LLAELVRARnlKLDGCFSFWDDCLVLTALLC 691
Cdd:pfam18130    2 EAARALGIDVTVVdepgEWAPGHLPA--VEEFIPLDLAD---DPDRALeIVRALHRAR--PVDGVVTFTDPFLPFVARAA 74

                   ....*.
gi 1907131464  692 RELGLP 697
Cdd:pfam18130   75 EALGLP 80
 
Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
658-934 1.72e-39

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 147.33  E-value: 1.72e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  658 NALLLAELVRARNLKLDGCFSFWDDCLVLTALLCRELGLPCSPPAAMCLAKQKSRTQLHLLRcQGPPwpstslhAVACCP 737
Cdd:COG0439      3 DAIIAAAAELARETGIDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAA-AGVP-------VPGFAL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  738 LENEADVERAIYQVPLPGVMKLEFGSGAVGVQLVKDGPQCREHFSRILHDLQGEADHPGiglgwgnaMLLMEFVEGTEHD 817
Cdd:COG0439     75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGE--------VLVEEFLEGREYS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  818 VDLVVFGGRLLAAFVSDNGPTRlPGFTETAACMPTGLAPEQEAQVVQAAFRCCLGCGLLDGVFNVELKMTGAG-PRLIEI 896
Cdd:COG0439    147 VEGLVRDGEVVVCSITRKHQKP-PYFVELGHEAPSPLPEELRAEIGELVARALRALGYRRGAFHTEFLLTPDGePYLIEI 225
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907131464  897 NPRMGGFYLRDWILELYGVDLLLASTMVACGLQPALPA 934
Cdd:COG0439    226 NARLGGEHIPPLTELATGVDLVREQIRLALGEPRILDP 263
PRK02186 PRK02186
argininosuccinate lyase; Provisional
688-941 2.89e-21

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 100.31  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  688 ALLCRELGLPCSPPAAMCLAKQKSRTQlHLLRCQGPPWPSTslHAVAccpleNEADVERAIYQVPLPGVMKLEFGSGAVG 767
Cdd:PRK02186    86 SEVARRLGLPAANTEAIRTCRDKKRLA-RTLRDHGIDVPRT--HALA-----LRAVALDALDGLTYPVVVKPRMGSGSVG 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  768 VQLVKDGPQCREHFSRILHDLqgeadhpgiglgwGNAMLLMEFVEGTEHDVDLVVFGGRLLAAFVSDNGPTRLPGFTETA 847
Cdd:PRK02186   158 VRLCASVAEAAAHCAALRRAG-------------TRAALVQAYVEGDEYSVETLTVARGHQVLGITRKHLGPPPHFVEIG 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  848 ACMPTGLAPEQEAQVVQAAFRCCLGCGLLDGVFNVELKMTGAGPRLIEINPRMGGFYLRDWILELYGVDLLLASTMVACG 927
Cdd:PRK02186   225 HDFPAPLSAPQRERIVRTVLRALDAVGYAFGPAHTELRVRGDTVVIIEINPRLAGGMIPVLLEEAFGVDLLDHVIDLHLG 304
                          250
                   ....*....|....
gi 1907131464  928 LQPALPahPRARGY 941
Cdd:PRK02186   305 VAAFAD--PTAKRY 316
ATPgrasp_Ter pfam15632
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ...
804-937 2.25e-14

ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434824 [Multi-domain]  Cd Length: 131  Bit Score: 70.72  E-value: 2.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  804 AMLLMEFVEGTEHDVDLVVFGGRLLAAFVSDNGPTRLPGFtetaacmptglapEQEAQVVQAAFRCCLGCGLlDGVFNVE 883
Cdd:pfam15632    4 PLLVMEYLPGPEYSVDCLAGHGELIAAVPRRKGDGGIQTL-------------EDDPELIEAARRLAEAFGL-DGLFNVQ 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907131464  884 LKMTGAGPRLIEINPRM-GGFYLrdwiLELYGVDLLLASTMVACGLQPALPAHPR 937
Cdd:pfam15632   70 FRYDGDGPKLLEINPRMsGGIGY----SCLAGVNLPYLALKLLLGLETPDPVEPR 120
ATPgrasp_N pfam18130
ATP-grasp N-terminal domain; This is the N-terminal domain found in BL00235 present in ...
617-697 1.83e-07

ATP-grasp N-terminal domain; This is the N-terminal domain found in BL00235 present in Bacillus licheniformis. BL00235 is a ATP-grasp superfamily protein that catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner. BL00235 has a highly restricted substrate specificity: the N-terminal substrate is confined to L-methionine an L-leucine, while the C-terminal substrates include small residues such as L-alanine, L-serine, L-threonine and L-cysteine.


Pssm-ID: 407962 [Multi-domain]  Cd Length: 81  Bit Score: 49.57  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  617 EAARDYGLTLHLV----ESDPNHFASqlVQTFIHFDVTEhrrDEENAL-LLAELVRARnlKLDGCFSFWDDCLVLTALLC 691
Cdd:pfam18130    2 EAARALGIDVTVVdepgEWAPGHLPA--VEEFIPLDLAD---DPDRALeIVRALHRAR--PVDGVVTFTDPFLPFVARAA 74

                   ....*.
gi 1907131464  692 RELGLP 697
Cdd:pfam18130   75 EALGLP 80
 
Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
658-934 1.72e-39

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 147.33  E-value: 1.72e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  658 NALLLAELVRARNLKLDGCFSFWDDCLVLTALLCRELGLPCSPPAAMCLAKQKSRTQLHLLRcQGPPwpstslhAVACCP 737
Cdd:COG0439      3 DAIIAAAAELARETGIDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAA-AGVP-------VPGFAL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  738 LENEADVERAIYQVPLPGVMKLEFGSGAVGVQLVKDGPQCREHFSRILHDLQGEADHPGiglgwgnaMLLMEFVEGTEHD 817
Cdd:COG0439     75 VDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGE--------VLVEEFLEGREYS 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  818 VDLVVFGGRLLAAFVSDNGPTRlPGFTETAACMPTGLAPEQEAQVVQAAFRCCLGCGLLDGVFNVELKMTGAG-PRLIEI 896
Cdd:COG0439    147 VEGLVRDGEVVVCSITRKHQKP-PYFVELGHEAPSPLPEELRAEIGELVARALRALGYRRGAFHTEFLLTPDGePYLIEI 225
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907131464  897 NPRMGGFYLRDWILELYGVDLLLASTMVACGLQPALPA 934
Cdd:COG0439    226 NARLGGEHIPPLTELATGVDLVREQIRLALGEPRILDP 263
PRK02186 PRK02186
argininosuccinate lyase; Provisional
688-941 2.89e-21

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 100.31  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  688 ALLCRELGLPCSPPAAMCLAKQKSRTQlHLLRCQGPPWPSTslHAVAccpleNEADVERAIYQVPLPGVMKLEFGSGAVG 767
Cdd:PRK02186    86 SEVARRLGLPAANTEAIRTCRDKKRLA-RTLRDHGIDVPRT--HALA-----LRAVALDALDGLTYPVVVKPRMGSGSVG 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  768 VQLVKDGPQCREHFSRILHDLqgeadhpgiglgwGNAMLLMEFVEGTEHDVDLVVFGGRLLAAFVSDNGPTRLPGFTETA 847
Cdd:PRK02186   158 VRLCASVAEAAAHCAALRRAG-------------TRAALVQAYVEGDEYSVETLTVARGHQVLGITRKHLGPPPHFVEIG 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  848 ACMPTGLAPEQEAQVVQAAFRCCLGCGLLDGVFNVELKMTGAGPRLIEINPRMGGFYLRDWILELYGVDLLLASTMVACG 927
Cdd:PRK02186   225 HDFPAPLSAPQRERIVRTVLRALDAVGYAFGPAHTELRVRGDTVVIIEINPRLAGGMIPVLLEEAFGVDLLDHVIDLHLG 304
                          250
                   ....*....|....
gi 1907131464  928 LQPALPahPRARGY 941
Cdd:PRK02186   305 VAAFAD--PTAKRY 316
ATPgrasp_Ter pfam15632
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ...
804-937 2.25e-14

ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434824 [Multi-domain]  Cd Length: 131  Bit Score: 70.72  E-value: 2.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  804 AMLLMEFVEGTEHDVDLVVFGGRLLAAFVSDNGPTRLPGFtetaacmptglapEQEAQVVQAAFRCCLGCGLlDGVFNVE 883
Cdd:pfam15632    4 PLLVMEYLPGPEYSVDCLAGHGELIAAVPRRKGDGGIQTL-------------EDDPELIEAARRLAEAFGL-DGLFNVQ 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907131464  884 LKMTGAGPRLIEINPRM-GGFYLrdwiLELYGVDLLLASTMVACGLQPALPAHPR 937
Cdd:pfam15632   70 FRYDGDGPKLLEINPRMsGGIGY----SCLAGVNLPYLALKLLLGLETPDPVEPR 120
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
714-917 3.60e-13

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 71.13  E-value: 3.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  714 QLHLLRCQGPPWPSTSLhavaccpLENEADVERAIYQVPLPGVMKLEFGSGAVGVQLVKDgpqcREHFSRILHDLQGEAD 793
Cdd:COG0189    100 TLQLLARAGIPVPPTLV-------TRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVED----EDALESILEALTELGS 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  794 HPgiglgwgnaMLLMEFVEGTE-HDVDLVVFGGRLLAAF--VSDNGPTR----LPGFTETAAcmptgLAPEQEAQVVQAA 866
Cdd:COG0189    169 EP---------VLVQEFIPEEDgRDIRVLVVGGEPVAAIrrIPAEGEFRtnlaRGGRAEPVE-----LTDEERELALRAA 234
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907131464  867 frcclgcGLLDGVFN-VELKMTGAGPRLIEINPRMGgfyLRdWILELYGVDL 917
Cdd:COG0189    235 -------PALGLDFAgVDLIEDDDGPLVLEVNVTPG---FR-GLERATGVDI 275
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
751-902 5.27e-08

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 53.44  E-value: 5.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  751 VPLPGVMKLEFGSGAVGVQLVKDGPQCREHFSRILHDLQGEADHPGIGLGWGNAMLLMEFVEGTEHDVDlvvfggrllaA 830
Cdd:pfam13535    1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEIEQWKEMYPEAVVDGGSFLVEEYIEGEEFAVD----------A 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  831 FVSDNGPTRL-----------PGFTETAACMPTGLAPEQEAQVVQAAFRCCLGCGLLDGVFNVELKMTGAGP-RLIEINP 898
Cdd:pfam13535   71 YFDENGEPVIlnilkhdfassEDVSDRIYVTSASIIRETQAAFTEFLKRINALLGLKNFPVHIELRVDEDGQiIPIEVNP 150

                   ....*
gi 1907131464  899 -RMGG 902
Cdd:pfam13535  151 lRFAG 155
ATPgrasp_N pfam18130
ATP-grasp N-terminal domain; This is the N-terminal domain found in BL00235 present in ...
617-697 1.83e-07

ATP-grasp N-terminal domain; This is the N-terminal domain found in BL00235 present in Bacillus licheniformis. BL00235 is a ATP-grasp superfamily protein that catalyzes the formation of an alpha-peptide bond between two L-amino acids in an ATP-dependent manner. BL00235 has a highly restricted substrate specificity: the N-terminal substrate is confined to L-methionine an L-leucine, while the C-terminal substrates include small residues such as L-alanine, L-serine, L-threonine and L-cysteine.


Pssm-ID: 407962 [Multi-domain]  Cd Length: 81  Bit Score: 49.57  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  617 EAARDYGLTLHLV----ESDPNHFASqlVQTFIHFDVTEhrrDEENAL-LLAELVRARnlKLDGCFSFWDDCLVLTALLC 691
Cdd:pfam18130    2 EAARALGIDVTVVdepgEWAPGHLPA--VEEFIPLDLAD---DPDRALeIVRALHRAR--PVDGVVTFTDPFLPFVARAA 74

                   ....*.
gi 1907131464  692 RELGLP 697
Cdd:pfam18130   75 EALGLP 80
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
751-902 5.55e-05

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 44.68  E-value: 5.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  751 VPLPGVMKLEFGSGAVGVQLVKDGPQcrehfsrilhdlqgeaDHPGIglgwgNAMLLMEFVEGTEHDVDLVVFGGRllAA 830
Cdd:pfam02655   30 EEKKYVVKPRDGCGGEGVRKVENGRE----------------DEAFI-----ENVLVQEFIEGEPLSVSLLSDGEK--AL 86
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907131464  831 FVSDNgpTRLPGFTETAACMPTGLAP---EQEAQVVQAAFRCCLGCGLLDGVFNVELKMTGAGPRLIEINPRMGG 902
Cdd:pfam02655   87 PLSVN--RQYIDNGGSGFVYAGNVTPsrtELKEEIIELAEEVVECLPGLRGYVGVDLVLKDNEPYVIEVNPRITT 159
PylC COG2232
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ...
597-942 1.34e-03

Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];


Pssm-ID: 441833 [Multi-domain]  Cd Length: 370  Bit Score: 42.21  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  597 MDGKQ-LLVIGaggVSKKFVWEAARDYGLTLHLVEsdpnHFA----SQLVQTFIHFDVTEHRRDEENaLLLAELVRARNL 671
Cdd:COG2232      1 MSSPPdLLIAG---FSARALAQSARRAGYRVYAVD----LFAdldtRALAERWVRLDAESCGFDLED-LPAALLELAAAD 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  672 KLDG--CFSFWDDCLVLTALLCRELGLPCSPPAAMCLAKQKSRTQlHLLRCQGPPWPSTSLhavaccplENEADVERAIy 749
Cdd:COG2232     73 DPDGlvYGSGFENFPELLERLARRLPLLGNPPEVVRRVKDPLRFF-ALLDELGIPHPETRF--------EPPPDPGPWL- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  750 qvplpgvMKLEFGSGAVGVQLVKDGPQCREHFsrilhdlqgeadhpgiglgwgnamLLMEFVEGTEHDVdlvvfggrlla 829
Cdd:COG2232    143 -------VKPIGGAGGWHIRPADSEAPPAPGR------------------------YFQRYVEGTPASV----------- 180
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131464  830 AFVSDNGPTRLPGFTE----TAACM---------PTGLAPEQEAQVVQAAFRCCLGCGLLdGVFNVELKMTGAGPRLIEI 896
Cdd:COG2232    181 LFLADGSDARVLGFNRqligPAGERpfryggnigPLALPPALAEEMRAIAEALVAALGLV-GLNGVDFILDGDGPYVLEV 259
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907131464  897 NPRMGGfylrdwILELYGVDL---LLASTMVACG-----LQPALPAHPRARGYL 942
Cdd:COG2232    260 NPRPQA------SLDLYEDATggnLFDAHLRACRgelpeVPRPKPRRVAAKAIL 307
 
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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