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Conserved domains on  [gi|4503987|ref|NP_003869|]
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gamma-glutamyl hydrolase isoform 1 precursor [Homo sapiens]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 10109835)

type 1 glutamine amidotransferase (GATase1) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 36-306 2.18e-162

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


:

Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 453.32  E-value: 2.18e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   36 IGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFY 115
Cdd:cd01747   1 IGILTQPVDGAGSNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDIDTSGYARTAKIIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987  116 NLSIQSFDDGDYFPVWGTCLGFEELSLLISGEC-LLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANF 194
Cdd:cd01747  81 NLALERNDAGDYFPVWGTCLGFELLTYLTSGETlLLEATEATNSALPLNFTEDALQSRLFKRFPPDLLKSLATEPLTMNN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987  195 HKWSLSVKNFTMNEKLKKFFNVLTTNTD-GKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAE 273
Cdd:cd01747 161 HRYGISPENFTENGLLSDFFNVLTTNDDwNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSSIPHSEEAIRLTQYFAN 240

                       250       260       270
                ....*....|....*....|....*....|...
gi 4503987  274 FFVNEARKNNHHFKSESEEEKALIYQFSPIYTG 306
Cdd:cd01747 241 FFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 36-306 2.18e-162

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 453.32  E-value: 2.18e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   36 IGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFY 115
Cdd:cd01747   1 IGILTQPVDGAGSNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDIDTSGYARTAKIIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987  116 NLSIQSFDDGDYFPVWGTCLGFEELSLLISGEC-LLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANF 194
Cdd:cd01747  81 NLALERNDAGDYFPVWGTCLGFELLTYLTSGETlLLEATEATNSALPLNFTEDALQSRLFKRFPPDLLKSLATEPLTMNN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987  195 HKWSLSVKNFTMNEKLKKFFNVLTTNTD-GKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAE 273
Cdd:cd01747 161 HRYGISPENFTENGLLSDFFNVLTTNDDwNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSSIPHSEEAIRLTQYFAN 240

                       250       260       270
                ....*....|....*....|....*....|...
gi 4503987  274 FFVNEARKNNHHFKSESEEEKALIYQFSPIYTG 306
Cdd:cd01747 241 FFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 34-246 4.87e-20

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 86.54  E-value: 4.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987     34 PIIGIL--MQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGsvdlrrsdyAKVA 111
Cdd:pfam07722   1 PVIGITanEESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGG---------PNVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987    112 KIFYNL-SIQSFDDGD-----------------YFPVWGTCLGFEELSLLISGECLLtatdtvDVAMPLNFTGGQLHSRM 173
Cdd:pfam07722  72 PHFYGEePSESGGPYDpardayelaliraalarGKPILGICRGFQLLNVALGGTLYQ------DIQEQPGFTDHREHCQV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987    174 FQNFPTELL----------LSLAVEPLTANFHkwSLSVKnftmneKLKKFFNVLTTNTDGKIEFIStMEGYKYPVYGVQW 243
Cdd:pfam07722 146 APYAPSHAVnvepgsllasLLGSEEFRVNSLH--HQAID------RLAPGLRVEAVAPDGTIEAIE-SPNAKGFALGVQW 216


                  ...
gi 4503987    244 HPE 246
Cdd:pfam07722 217 HPE 219
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 128-249 7.44e-04

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 40.65  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   128 FPVWGTCLGFeelsLLISgecLLTATDTVDvaMPLNFTGGqlhsrmfqNFPTELLLSLAVEpLTANFHKWSLSVKNFTMN 207
Cdd:PRK12838 238 YPILGICLGH----QLIA---LALGADTEK--LPFGHRGA--------NHPVIDLTTGRVW-MTSQNHGYVVDEDSLDGT 299

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 4503987   208 EKLKKFFNVlttnTDGkiefisTMEGYKY---PVYGVQWHPEKAP 249
Cdd:PRK12838 300 PLSVRFFNV----NDG------SIEGLRHkkkPVLSVQFHPEAHP 334
 
Name Accession Description Interval E-value
GATase1_Glutamyl_Hydrolase cd01747
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ...
 36-306 2.18e-162

Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153218 [Multi-domain]  Cd Length: 273  Bit Score: 453.32  E-value: 2.18e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   36 IGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFY 115
Cdd:cd01747   1 IGILTQPVDGAGSNKTGHSYIAASYVKFLESAGARVVPIWINESEEYYDKLFKSINGILFPGGAVDIDTSGYARTAKIIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987  116 NLSIQSFDDGDYFPVWGTCLGFEELSLLISGEC-LLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANF 194
Cdd:cd01747  81 NLALERNDAGDYFPVWGTCLGFELLTYLTSGETlLLEATEATNSALPLNFTEDALQSRLFKRFPPDLLKSLATEPLTMNN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987  195 HKWSLSVKNFTMNEKLKKFFNVLTTNTD-GKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAE 273
Cdd:cd01747 161 HRYGISPENFTENGLLSDFFNVLTTNDDwNGVEFISTVEAYKYPIYGVQWHPEKNAFEWKKSSSIPHSEEAIRLTQYFAN 240

                       250       260       270
                ....*....|....*....|....*....|...
gi 4503987  274 FFVNEARKNNHHFKSESEEEKALIYQFSPIYTG 306
Cdd:cd01747 241 FFVNEARKSNNRFESAEEETKHLIYNYKPTYTG 273
Peptidase_C26 pfam07722
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ...
 34-246 4.87e-20

Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.


Pssm-ID: 429620 [Multi-domain]  Cd Length: 219  Bit Score: 86.54  E-value: 4.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987     34 PIIGIL--MQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGsvdlrrsdyAKVA 111
Cdd:pfam07722   1 PVIGITanEESLGGHVFHGAGESYLAAGYVEAVEGAGGLPVLLPILGDPEDAAAILDRLDGLLLTGG---------PNVD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987    112 KIFYNL-SIQSFDDGD-----------------YFPVWGTCLGFEELSLLISGECLLtatdtvDVAMPLNFTGGQLHSRM 173
Cdd:pfam07722  72 PHFYGEePSESGGPYDpardayelaliraalarGKPILGICRGFQLLNVALGGTLYQ------DIQEQPGFTDHREHCQV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987    174 FQNFPTELL----------LSLAVEPLTANFHkwSLSVKnftmneKLKKFFNVLTTNTDGKIEFIStMEGYKYPVYGVQW 243
Cdd:pfam07722 146 APYAPSHAVnvepgsllasLLGSEEFRVNSLH--HQAID------RLAPGLRVEAVAPDGTIEAIE-SPNAKGFALGVQW 216


                  ...
gi 4503987    244 HPE 246
Cdd:pfam07722 217 HPE 219
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 47-162 3.77e-07

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 47.98  E-value: 3.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   47 VMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGG--SVDLRRSDYAKVAKIfynlsIQSFDD 124
Cdd:cd01653   4 LLFPGFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGpgTPDDLARDEALLALL-----REAAAA 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4503987  125 GdyFPVWGTCLGFeeLSLLISGECLLTATDTVDVAMPL 162
Cdd:cd01653  79 G--KPILGICLGA--QLLVLGVQFHPEAIDGAEAGARL 112
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 47-137 4.31e-07

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 47.20  E-value: 4.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   47 VMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGG--SVDLRRSDYAKVAKIfynlsIQSFDD 124
Cdd:cd03128   4 LLFGGSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDDYDGLILPGGpgTPDDLAWDEALLALL-----REAAAA 78

                        90
                ....*....|...
gi 4503987  125 GdyFPVWGTCLGF 137
Cdd:cd03128  79 G--KPVLGICLGA 89
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 36-251 1.44e-06

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 47.96  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   36 IGILMqkcRNKVMKNYG--RYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGG-SVDLRRsdyakvak 112
Cdd:cd01745   1 IGITA---RLREEEGGYerRDYLNQYYVDAVRKAGGLPVLLPPVDDEEDLEQYLELLDGLLLTGGgDVDPPL-------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987  113 iFYNLSIQSFDDGDY-----------------FPVWGTCLGFEELSllisgeclltatdtvdVAMplnftGGQLHSRMFQ 175
Cdd:cd01745  70 -YGEEPHPELGPIDPerdafelallraalergKPILGICRGMQLLN----------------VAL-----GGTLYQDIRV 127

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503987  176 NfptelllslavepltaNFHkwSLSVKnftmneKLKKFFNVLTTNTDGKIEFISTMEgyKYPVYGVQWHPEKAPYE 251
Cdd:cd01745 128 N----------------SLH--HQAIK------RLADGLRVEARAPDGVIEAIESPD--RPFVLGVQWHPEWLADT 177
GATase pfam00117
Glutamine amidotransferase class-I;
61-249 4.48e-04

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 40.68  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987     61 VKYLESAGARVVPVRLDltEKDYEILFKSINGILFPGG---------SVDLRRsdYAKVAKIfynlsiqsfddgdyfPVW 131
Cdd:pfam00117  14 ARALRELGVEVTVVPND--TPAEEILEENPDGIILSGGpgspgaaggAIEAIR--EARELKI---------------PIL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987    132 GTCLGFEELSLLISGeclltatdTVDVAMPLNFTGGQLHSRmfqNFPTELLLSLAVEPLTANFHkwSLSVKNFTMNEKLK 211
Cdd:pfam00117  75 GICLGHQLLALAFGG--------KVVKAKKFGHHGKNSPVG---DDGCGLFYGLPNVFIVRRYH--SYAVDPDTLPDGLE 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 4503987    212 kffnVLTTNTDGkiEFISTMEGYKYPVYGVQWHPEKAP 249
Cdd:pfam00117 142 ----VTATSEND--GTIMGIRHKKLPIFGVQFHPESIL 173
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 128-249 7.44e-04

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 40.65  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503987   128 FPVWGTCLGFeelsLLISgecLLTATDTVDvaMPLNFTGGqlhsrmfqNFPTELLLSLAVEpLTANFHKWSLSVKNFTMN 207
Cdd:PRK12838 238 YPILGICLGH----QLIA---LALGADTEK--LPFGHRGA--------NHPVIDLTTGRVW-MTSQNHGYVVDEDSLDGT 299

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 4503987   208 EKLKKFFNVlttnTDGkiefisTMEGYKY---PVYGVQWHPEKAP 249
Cdd:PRK12838 300 PLSVRFFNV----NDG------SIEGLRHkkkPVLSVQFHPEAHP 334
 
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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