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Conserved domains on  [gi|1958643125|ref|XP_038959290|]
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arginase-1 isoform X2 [Rattus norvegicus]

Protein Classification

arginase family protein( domain architecture ID 98571)

arginase family protein is a metal-dependent enzyme that catalyzes the hydrolysis of an amide bond, such as arginase-like amidino hydrolases and histone/histone-like deacetylases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arginase_HDAC super family cl17011
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 1-201 6.31e-123

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


The actual alignment was detected with superfamily member cd11587:

Pssm-ID: 450134  Cd Length: 294  Bit Score: 350.25  E-value: 6.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVpGFSWVTPCISAKDIVYIGLRDV 80
Cdd:cd11587    95 LAIGSISGHAQVYPDLGVIWIDAHGDINTPETSPSGNLHGMPLAFLLGEGKGKLPDV-GFSWVTPLISPENVVYIGLRDV 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:cd11587   174 DPGEKYIIKTLGIKYYTMFEVDKLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPVFAPATGTPVVGGLSYREGLLIME 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958643125 161 EIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSC 201
Cdd:cd11587   254 ELAETGLLSGMDLVEVNPSLDKTPEEVTKTANTAVALTLAL 294
 
Name Accession Description Interval E-value
Arginase-like cd11587
Arginase types I and II and arginase-like family; This family includes arginase, also known as ...
 1-201 6.31e-123

Arginase types I and II and arginase-like family; This family includes arginase, also known as arginase-like amidino hydrolase family, and related proteins, found in bacteria, archaea and eykaryotes. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid. In vertebrates, at least two isozymes have been identified: type I cytoplasmic or hepatic liver-type arginase and type II mitochondrial or non-hepatic arginase. Point mutations in human arginase gene lead to hyperargininemia with consequent mental disorders, retarded development and early death. Arginase is a therapeutic target to treat asthma, erectile dysfunction, atherosclerosis and cancer.


Pssm-ID: 212536  Cd Length: 294  Bit Score: 350.25  E-value: 6.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVpGFSWVTPCISAKDIVYIGLRDV 80
Cdd:cd11587    95 LAIGSISGHAQVYPDLGVIWIDAHGDINTPETSPSGNLHGMPLAFLLGEGKGKLPDV-GFSWVTPLISPENVVYIGLRDV 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:cd11587   174 DPGEKYIIKTLGIKYYTMFEVDKLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPVFAPATGTPVVGGLSYREGLLIME 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958643125 161 EIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSC 201
Cdd:cd11587   254 ELAETGLLSGMDLVEVNPSLDKTPEEVTKTANTAVALTLAL 294
rocF_arginase TIGR01229
arginase; This model helps resolve arginases from known and putative agmatinases, ...
 1-207 8.25e-113

arginase; This model helps resolve arginases from known and putative agmatinases, formiminoglutamases, and other related proteins of unknown specifity. The pathway from arginine to the polyamine putrescine may procede by hydrolysis to remove urea (arginase) followed by decarboxylation (ornithine decarboxylase), or by decarboxylation first (arginine decarboxylase) followed by removal of urea (agmatinase).


Pssm-ID: 162262  Cd Length: 300  Bit Score: 324.77  E-value: 8.25e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARVHPD--LCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLR 78
Cdd:TIGR01229  95 IAIGTISGTARVHPDkkLGVLWLDAHADINTPETSDSGNIHGMPLAFLLGRLKSEFPDSPGLGWVAPEISPKNLVYIGLR 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  79 DVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKrPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYI 158
Cdd:TIGR01229 175 SVDPGERKILKELGIKVFSMHEIDELGIGKVVEETLEYLKAEDG-PIHLSLDVDGLDPSLAPATGTPVVGGLTFREGLLI 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958643125 159 TEEIYKTGLLSGLDIMEVNPTLGKTpeEVTRTVNTAVALTLSCFGTKRE 207
Cdd:TIGR01229 254 MEMLYESGLLTALDVVEVNPTLDIK--HVNETIKTAVEIVRSLLGSTLL 300
Arginase pfam00491
Arginase family;
2-202 4.87e-69

Arginase family;


Pssm-ID: 425716 [Multi-domain]  Cd Length: 272  Bit Score: 212.38  E-value: 4.87e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   2 AIGSISGHARVH-PDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKElkgkfpdvpgfswvtPCISAKDIVYIGLRDV 80
Cdd:pfam00491  93 TLGSLRAVAEHYgGPLGVIHFDAHADLRDPYTTGSGNSHGTPFRRAAEE---------------GLLDPERIVQIGIRSV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLlgrKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:pfam00491 158 DNEEYEYARELGITVITMREIDELGIAAVLEEILDRL---GDDPVYLSFDIDVLDPAFAPGTGTPEPGGLTYREALEILR 234

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958643125 161 EIYKtGLLSGLDIMEVNPTLGktpEEVTRTVNTAVALTLSCF 202
Cdd:pfam00491 235 RLAG-LNVVGADVVEVNPPYD---PSGGITARLAAKLVRELL 272
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
 2-203 9.44e-56

Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase family enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 439781 [Multi-domain]  Cd Length: 283  Bit Score: 178.87  E-value: 9.44e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   2 AIGSISGHARVHPDLCVIWVDAHTDINTPLTtssGNL-HGQPVAFLLKElkgkfpdvpgfswvtPCISAKDIVYIGLRDV 80
Cdd:COG0010   103 TLGTIRALARAYGPLGVIHFDAHADLRDPYE---GNLsHGTPLRRALEE---------------GLLDPENVVQIGIRSN 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLlgRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:COG0010   165 DPEEFELARELGVTVFTAREIRERGLAAVLEEALERL--RAGDPVYVSFDIDVLDPAFAPGVGTPEPGGLTPREALELLR 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958643125 161 EIYKTGLLSGLDIMEVNPTLGKTpeevTRTVNTAVALTLSCFG 203
Cdd:COG0010   243 ALAASGKVVGFDIVEVNPPLDPD----GRTARLAAKLLWELLG 281
PRK02190 PRK02190
agmatinase; Provisional
 9-178 7.95e-13

agmatinase; Provisional


Pssm-ID: 235011  Cd Length: 301  Bit Score: 66.02  E-value: 7.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   9 HARVHPDLCVIWVDAHTDintplTTSSGNL---HGQPVAFLLKElkgkfpdvpGFswvtpcISAKDIVYIGLRdvdpgEH 85
Cdd:PRK02190  130 HAKHFGPLALVHFDAHTD-----TWADGGSridHGTMFYHAPKE---------GL------IDPAHSVQIGIR-----TE 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  86 YIiKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRkkrPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIykT 165
Cdd:PRK02190  185 YD-KDNGFTVLDARQVNDRGVDAIIAQIKQIVGDM---PVYLTFDIDCLDPAFAPGTGTPVIGGLTSAQALKILRGL--K 258

                         170
                  ....*....|....
gi 1958643125 166 GL-LSGLDIMEVNP 178
Cdd:PRK02190  259 GLnIVGMDVVEVAP 272
 
Name Accession Description Interval E-value
Arginase-like cd11587
Arginase types I and II and arginase-like family; This family includes arginase, also known as ...
 1-201 6.31e-123

Arginase types I and II and arginase-like family; This family includes arginase, also known as arginase-like amidino hydrolase family, and related proteins, found in bacteria, archaea and eykaryotes. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid. In vertebrates, at least two isozymes have been identified: type I cytoplasmic or hepatic liver-type arginase and type II mitochondrial or non-hepatic arginase. Point mutations in human arginase gene lead to hyperargininemia with consequent mental disorders, retarded development and early death. Arginase is a therapeutic target to treat asthma, erectile dysfunction, atherosclerosis and cancer.


Pssm-ID: 212536  Cd Length: 294  Bit Score: 350.25  E-value: 6.31e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVpGFSWVTPCISAKDIVYIGLRDV 80
Cdd:cd11587    95 LAIGSISGHAQVYPDLGVIWIDAHGDINTPETSPSGNLHGMPLAFLLGEGKGKLPDV-GFSWVTPLISPENVVYIGLRDV 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:cd11587   174 DPGEKYIIKTLGIKYYTMFEVDKLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPVFAPATGTPVVGGLSYREGLLIME 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958643125 161 EIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSC 201
Cdd:cd11587   254 ELAETGLLSGMDLVEVNPSLDKTPEEVTKTANTAVALTLAL 294
rocF_arginase TIGR01229
arginase; This model helps resolve arginases from known and putative agmatinases, ...
 1-207 8.25e-113

arginase; This model helps resolve arginases from known and putative agmatinases, formiminoglutamases, and other related proteins of unknown specifity. The pathway from arginine to the polyamine putrescine may procede by hydrolysis to remove urea (arginase) followed by decarboxylation (ornithine decarboxylase), or by decarboxylation first (arginine decarboxylase) followed by removal of urea (agmatinase).


Pssm-ID: 162262  Cd Length: 300  Bit Score: 324.77  E-value: 8.25e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARVHPD--LCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLR 78
Cdd:TIGR01229  95 IAIGTISGTARVHPDkkLGVLWLDAHADINTPETSDSGNIHGMPLAFLLGRLKSEFPDSPGLGWVAPEISPKNLVYIGLR 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  79 DVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKrPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYI 158
Cdd:TIGR01229 175 SVDPGERKILKELGIKVFSMHEIDELGIGKVVEETLEYLKAEDG-PIHLSLDVDGLDPSLAPATGTPVVGGLTFREGLLI 253

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958643125 159 TEEIYKTGLLSGLDIMEVNPTLGKTpeEVTRTVNTAVALTLSCFGTKRE 207
Cdd:TIGR01229 254 MEMLYESGLLTALDVVEVNPTLDIK--HVNETIKTAVEIVRSLLGSTLL 300
Arginase cd09989
Arginase family; This family includes arginase, also known as arginase-like amidino hydrolase ...
 1-201 1.48e-106

Arginase family; This family includes arginase, also known as arginase-like amidino hydrolase family, and related proteins. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid. In vertebrates, at least two isozymes have been identified: type I (ARG1) cytoplasmic or hepatic liver-type arginase and type II (ARG2) mitochondrial or non-hepatic arginase. Point mutations in human arginase ARG1 gene lead to hyperargininemia with consequent mental disorders, retarded development and early death. Hyperargininemia is associated with a several-fold increase in the activity of the mitochondrial arginase (ARG2), causing persistent ureagenesis in patients. ARG2 overexpression plays a critical role in the pathophysiology of cholesterol mediated endothelial dysfunction. Thus, arginase is a therapeutic target to treat asthma, erectile dysfunction, atherosclerosis and cancer.


Pssm-ID: 212515  Cd Length: 290  Bit Score: 308.27  E-value: 1.48e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARV-HPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKgkfPDVPGFSWVTPCISAKDIVYIGLRD 79
Cdd:cd09989    97 IAIGTIAGVARApYPDLGVIWIDAHADINTPETSPSGNIHGMPLAALLGEGH---PELTNIGGVGPKLKPENLVYIGLRD 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  80 VDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLlGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYIT 159
Cdd:cd09989   174 LDPGERELIKKLGIKVFTMDEIDERGIGAVMEEALEYL-KPGTDGIHVSFDVDVLDPSIAPGTGTPVPGGLTYREAHLLL 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958643125 160 EEIYKTGLLSGLDIMEVNPTLGKTpeevTRTVNTAVALTLSC 201
Cdd:cd09989   253 EELAETGRLVSLDIVEVNPLLDKE----NRTAELAVELIASA 290
Ureohydrolase cd09015
Ureohydrolase superfamily includes arginase, formiminoglutamase, agmatinase and proclavaminate ...
 1-200 4.33e-81

Ureohydrolase superfamily includes arginase, formiminoglutamase, agmatinase and proclavaminate amidinohydrolase (PAH); This family, also known as arginase-like amidino hydrolase family, includes Mn-dependent enzymes: arginase (Arg, EC 3.5.3.1), formimidoylglutamase (HutG, EC 3.5.3.8 ), agmatinase (SpeB, EC 3.5.3.11), guanidinobutyrase (Gbh, EC=3.5.3.7), proclavaminate amidinohydrolase (PAH, EC 3.5.3.22) and related proteins. These enzymes catalyze hydrolysis of amide bond. They are involved in control of cellular levels of arginine and ornithine (both involved in protein biosynthesis, and production of creatine, polyamines, proline and nitric acid), in histidine and arginine degradation, and in clavulanic acid biosynthesis.


Pssm-ID: 212511 [Multi-domain]  Cd Length: 270  Bit Score: 243.10  E-value: 4.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARVHPDLCVIWVDAHTDINTPLTtSSGNLHGQPVAFLLKELKgkfpdvpgfswvtpcISAKDIVYIGLRDV 80
Cdd:cd09015    91 IAIATLRAVARHHPDLGVINLDAHLDVNTPET-DGRNSSGTPFRQLLEELQ---------------QSPKHIVCIGVRGL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHY--IIKTLGIKYFSMTEVDKLGIGKVMEETFSYllgRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYI 158
Cdd:cd09015   155 DPGPALfeYARKLGVKYVTMDEVDKLGLGGVLEQLFHY---DDGDNVYLSVDVDGLDPADAPGVSTPAAGGLSYREGLPI 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958643125 159 TEEIYKTGLLSGLDIMEVNPTLgktpEEVTRTVNTAVALTLS 200
Cdd:cd09015   232 LERAGKTKKVMGADIVEVNPLL----DEDGRTARLAVRLCWE 269
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
 1-201 7.59e-72

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212513  Cd Length: 217  Bit Score: 217.63  E-value: 7.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   1 MAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGqpvafllkelkgkfpdvPGFSWVTPCISAKDIVYIGLRDV 80
Cdd:cd09987    37 IANGAIRAVAELHPDLGVIDVDAHHDVRTPEAFGKGNHHT-----------------PRHLLCEPLISDVHIVSIGIRGV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEH--YIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLlGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYI 158
Cdd:cd09987   100 SNGEAggAYARKLGVVYFSMTEVDKLGLGDVFEEIVSYL-GDKGDNVYLSVDVDGLDPSFAPGTGTPGPGGLSYREGLYI 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958643125 159 TEEIYKTGLLSGLDIMEVNPTLGktpeEVTRTVNTAVALTLSC 201
Cdd:cd09987   179 TERIAKTNLVVGLDIVEVNPLLD----ETGRTARLAAALTLEL 217
Arginase pfam00491
Arginase family;
2-202 4.87e-69

Arginase family;


Pssm-ID: 425716 [Multi-domain]  Cd Length: 272  Bit Score: 212.38  E-value: 4.87e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   2 AIGSISGHARVH-PDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKElkgkfpdvpgfswvtPCISAKDIVYIGLRDV 80
Cdd:pfam00491  93 TLGSLRAVAEHYgGPLGVIHFDAHADLRDPYTTGSGNSHGTPFRRAAEE---------------GLLDPERIVQIGIRSV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLlgrKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:pfam00491 158 DNEEYEYARELGITVITMREIDELGIAAVLEEILDRL---GDDPVYLSFDIDVLDPAFAPGTGTPEPGGLTYREALEILR 234

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958643125 161 EIYKtGLLSGLDIMEVNPTLGktpEEVTRTVNTAVALTLSCF 202
Cdd:pfam00491 235 RLAG-LNVVGADVVEVNPPYD---PSGGITARLAAKLVRELL 272
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
 2-203 9.44e-56

Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase family enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 439781 [Multi-domain]  Cd Length: 283  Bit Score: 178.87  E-value: 9.44e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   2 AIGSISGHARVHPDLCVIWVDAHTDINTPLTtssGNL-HGQPVAFLLKElkgkfpdvpgfswvtPCISAKDIVYIGLRDV 80
Cdd:COG0010   103 TLGTIRALARAYGPLGVIHFDAHADLRDPYE---GNLsHGTPLRRALEE---------------GLLDPENVVQIGIRSN 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLlgRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:COG0010   165 DPEEFELARELGVTVFTAREIRERGLAAVLEEALERL--RAGDPVYVSFDIDVLDPAFAPGVGTPEPGGLTPREALELLR 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958643125 161 EIYKTGLLSGLDIMEVNPTLGKTpeevTRTVNTAVALTLSCFG 203
Cdd:COG0010   243 ALAASGKVVGFDIVEVNPPLDPD----GRTARLAAKLLWELLG 281
Arginase-like_1 cd09999
Arginase-like amidino hydrolase family; This family includes arginase, also known as ...
 3-181 3.32e-31

Arginase-like amidino hydrolase family; This family includes arginase, also known as arginase-like amidino hydrolase family, as well as arginase-like proteins and are found in bacteria, archaea and eykaryotes, but does not include metazoan arginases. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid.


Pssm-ID: 212523  Cd Length: 272  Bit Score: 115.03  E-value: 3.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   3 IGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLkelkGKFPdvPGF-SWVTPCISAKDIVYIGLRDVD 81
Cdd:cd09999    90 LAPFAYLARKYGDLGLLWIDAHPDFNTPETSPTGYAHGMVLAALL----GEGD--PELtAIVKPPLSPERVVLAGLRDPD 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  82 PGEHYIIKTLGIKYFSmTEVDKLGIGKVMEEtfsyLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEE 161
Cdd:cd09999   164 DEEEEFIARLGIRVLR-PEGLAASAQAVLDW----LKEEGLSGVWIHLDLDVLDPAIFPAVDFPEPGGLSLDELVALLAA 238

                         170       180
                  ....*....|....*....|
gi 1958643125 162 IYKTGLLSGLDIMEVNPTLG 181
Cdd:cd09999   239 LAASADLVGLTIAEFDPDLD 258
Agmatinase-like_2 cd11593
Agmatinase and related proteins; This family includes known and predicted bacterial and ...
 3-178 9.21e-29

Agmatinase and related proteins; This family includes known and predicted bacterial and archaeal agmatinase (agmatine ureohydrolase; AUH; SpeB; EC=3.5.3.11), a binuclear manganese metalloenzyme that belongs to the ureohydrolase superfamily. It is a key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield urea and putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. As compared to E. coli where two paths to putrescine exist, via decarboxylation of an amino acid, ornithine or arginine, a single path is found in Bacillus subtilis, where polyamine synthesis starts with agmatine; the speE and speB encode spermidine synthase and agmatinase, respectively. The level of agmatinase synthesis is very low, allowing strict control on the synthesis of putrescine and therefore, of all polyamines, consistent with polyamine levels in the cell. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.


Pssm-ID: 212539 [Multi-domain]  Cd Length: 263  Bit Score: 108.33  E-value: 9.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   3 IGSISGHARVHPDLCVIWVDAHTDI-----NTPLTTSSgnlhgqpVAFLLKELKGKFPdvpgfswvtpcisakdIVYIGL 77
Cdd:cd11593    93 LGAVRALAEKYPDLGVLHFDAHADLrdeyeGSKYSHAC-------VMRRILELGGVKR----------------LVQVGI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  78 RDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFsyllgrKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLY 157
Cdd:cd11593   150 RSGSKEEFEFAKEKGVRIYTFDDFDLGRWLDELIKVL------PEKPVYISIDIDVLDPAFAPGTGTPEPGGLSWRELLD 223

                         170       180
                  ....*....|....*....|.
gi 1958643125 158 ITEEIYKTGLLSGLDIMEVNP 178
Cdd:cd11593   224 LLRALAESKNIVGFDVVELSP 244
Agmatinase-like cd09990
Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as ...
 5-202 1.68e-25

Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as agmatinase, guanidinobutyrase, guanidopropionase, formimidoylglutamase and proclavaminate amidinohydrolase. Agmatinase (agmatine ureohydrolase; SpeB; EC=3.5.3.11) is the key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield putrescine and urea. This enzyme has been found in bacteria, archaea and eukaryotes, requiring divalent Mn and sometimes Zn, Co or Ca for activity. In mammals, the highest level of agmatinase mRNA was found in liver and kidney. However, catabolism of agmatine via agmatinase apparently is a not major path; it is mostly catabolized via diamine oxidase. Agmatinase has been shown to be down-regulated in tumor renal cells. Guanidinobutyrase (Gbh, EC=3.5.3.7) catalyzes hydrolysis of 4-guanidinobutanoate to yield 4-aminobutanoate and urea in arginine degradation pathway. Activity has been shown for purified enzyme from Arthrobacter sp. KUJ 8602. Additionally, guanidinobutyrase is able to hydrolyze D-arginine, 3-guanidinopropionate, 5-guanidinovaleriate and L-arginine with much less affinity, having divalent Zn ions for catalysis. Proclavaminate amidinohydrolase (Pah, EC 3.5.3.22) hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Activity has been shown for purified enzyme from Streptomyces clavuligerus. Clavulanic acid is the effective inhibitor of beta-lactamases. This acid is used in combination with the penicillin amoxicillin to prevent antibiotic's beta-lactam rings from hydrolysis, thus keeping the antibiotics biologically active.


Pssm-ID: 212516 [Multi-domain]  Cd Length: 275  Bit Score: 100.32  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   5 SISGHARVHP-DLCVIWVDAHTDINTPLTtSSGNLHGQPVAFLLKElkgkfpdvpgfswvtPCISAKDIVYIGLRDVDPG 83
Cdd:cd09990    96 AVRGLAERHKgKVGVIHFDAHLDTRDTDG-GGELSHGTPFRRLLED---------------GNVDGENIVQIGIRGFWNS 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  84 EHYI--IKTLGIKYFSMTEVDKLGIGKVMEETFSyLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEE 161
Cdd:cd09990   160 PEYVeyAREQGVTVITMRDVRERGLDAVIEEALE-IASDGTDAVYVSVDIDVLDPAFAPGTGTPEPGGLTPRELLDAVRA 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958643125 162 IYKTGLLSGLDIMEVNPTLGKTPeevtRTVNTAVALTLSCF 202
Cdd:cd09990   239 LGAEAGVVGMDIVEVSPPLDPTD----ITARLAARAVLEFL 275
Agmatinase_PAH cd11592
Agmatinase-like family includes proclavaminic acid amidinohydrolase; This agmatinase subfamily ...
 9-178 3.86e-25

Agmatinase-like family includes proclavaminic acid amidinohydrolase; This agmatinase subfamily contains bacterial and fungal/metazoan enzymes, including proclavaminic acid amidinohydrolase (PAH, EC 3.5.3.22) and Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA). PAH hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Clavulanic acid is an effective inhibitor of beta-lactamases and is used in combination with amoxicillin to prevent the beta-lactam rings of the antibiotic from hydrolysis and, thus keeping the antibiotic biologically active. GbuA hydrolyzes 4-guanidinobutyrate (4-GB) into 4-aminobutyrate and urea while GpuA hydrolyzes 3-guanidinopropionate (3-GP) into beta-alanine and urea. Mutation studies show that significant variations in two active site loops in these two enzymes may be important for substrate specificity. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.


Pssm-ID: 212538 [Multi-domain]  Cd Length: 289  Bit Score: 99.47  E-value: 3.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   9 HARVHPDLCVIWVDAHTDINTPLTTSSGNlHGQPVAFLLKElkgkfpdvpGfswvtpCISAKDIVYIGLR--DVDPGEHY 86
Cdd:cd11592   118 LAKKHGPVALVHFDAHLDTWDPYFGEKYN-HGTPFRRAVEE---------G------LLDPKRSIQIGIRgsLYSPDDLE 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  87 IIKTLGIKYFSMTEVDKLGIGKVMEETFSyLLGRkkRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIykTG 166
Cdd:cd11592   182 DDRDLGFRVITADEVDDIGLDAIIEKIRE-RVGD--GPVYLSFDIDVLDPAFAPGTGTPEIGGLTSREALEILRGL--AG 256

                         170
                  ....*....|...
gi 1958643125 167 L-LSGLDIMEVNP 178
Cdd:cd11592   257 LnIVGADVVEVSP 269
agmatinase TIGR01230
agmatinase; Members of this family include known and predicted examples of agmatinase ...
 4-199 1.47e-17

agmatinase; Members of this family include known and predicted examples of agmatinase (agmatine ureohydrolase). The seed includes members of archaea, for which no definitive agmatinase sequence has yet been made available. However, archaeal sequences are phylogenetically close to the experimentally verified B. subtilis sequence. One species of Halobacterium has been demonstrated in vitro to produce agmatine from arginine, but no putrescine from ornithine, suggesting that arginine decarboxylase and agmatinase, rather than arginase and ornithine decarboxylase, lead from Arg to polyamine biosynthesis. Note: a history of early misannotation of members of this family is detailed in PUBMED:10931887.


Pssm-ID: 273514 [Multi-domain]  Cd Length: 275  Bit Score: 79.03  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   4 GSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNlHGQPVAFLLKelkgkfpdvpgfswvtpciSAKDIVYIGLRDVDPG 83
Cdd:TIGR01230 108 PVIRAMAKKFGKFAVVHFDAHTDLRDEFDGGTLN-HACPMRRVIE-------------------LGLNVVQFGIRSGFKE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  84 EHYIIKTLGIKYFSMTEVDKlgIGKVMEETFSyllgrkkRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIY 163
Cdd:TIGR01230 168 ENDFARENNIQVLKREVDDV--IAEVKQKVGD-------KPVYVTIDIDVLDPAFAPGTGTPEPGGLTSDELINFFVRAL 238

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958643125 164 KTGLLSGLDIMEVNPTLGKTpeEVTRTVNTAVALTL 199
Cdd:TIGR01230 239 KDDNVVGFDVVEVAPVYDQS--EVTALTAAKIALEM 272
PRK02190 PRK02190
agmatinase; Provisional
 9-178 7.95e-13

agmatinase; Provisional


Pssm-ID: 235011  Cd Length: 301  Bit Score: 66.02  E-value: 7.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125   9 HARVHPDLCVIWVDAHTDintplTTSSGNL---HGQPVAFLLKElkgkfpdvpGFswvtpcISAKDIVYIGLRdvdpgEH 85
Cdd:PRK02190  130 HAKHFGPLALVHFDAHTD-----TWADGGSridHGTMFYHAPKE---------GL------IDPAHSVQIGIR-----TE 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  86 YIiKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRkkrPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIykT 165
Cdd:PRK02190  185 YD-KDNGFTVLDARQVNDRGVDAIIAQIKQIVGDM---PVYLTFDIDCLDPAFAPGTGTPVIGGLTSAQALKILRGL--K 258

                         170
                  ....*....|....
gi 1958643125 166 GL-LSGLDIMEVNP 178
Cdd:PRK02190  259 GLnIVGMDVVEVAP 272
Agmatinase_like_1 cd11589
Agmatinase and related proteins; This family includes known and predicted bacterial agmatinase ...
 13-178 2.66e-11

Agmatinase and related proteins; This family includes known and predicted bacterial agmatinase (agmatine ureohydrolase; AUH; SpeB; EC=3.5.3.11), a binuclear manganese metalloenzyme, belonging to the ureohydrolase superfamily. It is a key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield urea and putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. Agmatinase from Deinococcus radiodurans shows approximately 33% of sequence identity to human mitochondrial agmatinase. An analysis of the evolutionary relationship among ureohydrolase superfamily enzymes indicates the pathway involving arginine decarboxylase and agmatinase evolved earlier than the arginase pathway of polyamine.


Pssm-ID: 212537  Cd Length: 274  Bit Score: 61.47  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  13 HPDLCVIWVDAHTD----INtPLTTSsgnlHGQPVAfLLKELkgkfpdvpgfSWVTPcisakdIVYIGLR--------DV 80
Cdd:cd11589   109 HGPIHVVQIDAHLDwrdeVN-GVRYG----NSSPMR-RASEM----------PHVGR------ITQIGIRglgsarpeDF 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  81 DPGEHYiiktlGIKYFSMTEVDKLGIGKVMEETfsyllgRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITE 160
Cdd:cd11589   167 DDARAY-----GSVIITAREVHRIGIEAVLDQI------PDGENYYITIDIDGLDPSIAPGVGSPSPGGLTYDQVRDLLH 235

                         170
                  ....*....|....*...
gi 1958643125 161 EIYKTGLLSGLDIMEVNP 178
Cdd:cd11589   236 GLAKKGRVVGFDLVEVAP 253
Formimidoylglutamase cd09988
Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate ...
 88-180 6.79e-09

Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate formimidoylhydrolase; formiminoglutamase; N-formiminoglutamate hydrolase; N-formimino-L-glutamate formiminohydrolase; HutE; EC 3.5.3.8) is a metalloenzyme that catalyzes hydrolysis of N-formimidoyl-L-glutamate to L-glutamate and formamide. This enzyme is involved in histidine degradation, requiring Mn as a cofactor while glutathione may be required for maximal activity. In Pseudomonas PAO1, mutation studies show that histidine degradation proceeds via a 'four-step' pathway if the 'five-step' route is absent and vice versa; in the four-step pathway, formiminoglutaminase (HutE, EC 3.5.3.8) directly converts formiminoglutamate (FIGLU) to L-glutamate and formamide in a single step. Formiminoglutamase has traditionally also been referred to as HutG; however, formiminoglutamase is structurally and mechanistically unrelated to N-formyl-glutamate deformylase (also called HutG). Phylogenetic analysis has suggested that HutE was acquired by horizontal gene transfer from a Ralstonia-like ancestor.


Pssm-ID: 212514 [Multi-domain]  Cd Length: 262  Bit Score: 54.45  E-value: 6.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  88 IKTLGIKYFSMTEVDklgIGKVMEETFSYLLGRkkRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIYKTGL 167
Cdd:cd09988   158 AKELGVLYFEAERLL---GEKILDILEAEPALR--DAIYLSIDLDVISSSDAPGVSAPSPNGLSPEEACAIARYAGKSGK 232

                          90
                  ....*....|...
gi 1958643125 168 LSGLDIMEVNPTL 180
Cdd:cd09988   233 VRSFDIAELNPSL 245
PLN02615 PLN02615
arginase
 69-178 2.96e-06

arginase


Pssm-ID: 178224  Cd Length: 338  Bit Score: 47.16  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  69 AKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKlgiGKVMEETFSylLGRKKRPIHLSFDVDGLDPVFTPATGTPVVG 148
Cdd:PLN02615  210 ARRLLQVGIRSITKEGREQGKRFGVEQYEMRTFSK---DREKLENLK--LGEGVKGVYISIDVDCLDPAFAPGVSHIEPG 284

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958643125 149 GLSYREGLYITEEIykTGLLSGLDIMEVNP 178
Cdd:PLN02615  285 GLSFRDVLNILHNL--QGDVVGADVVEFNP 312
PRK13773 PRK13773
formimidoylglutamase; Provisional
 91-200 5.87e-04

formimidoylglutamase; Provisional


Pssm-ID: 237499  Cd Length: 324  Bit Score: 40.11  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643125  91 LGIKYFSMTEVDKLGIGKVMEETFSYLLGRKkrPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIYKTGLLSG 170
Cdd:PRK13773  211 LGVRYLLDEECQVMDRAAVRVFVADFLADVD--VIYLTIDLDVLPAAVAPGVSAPAAYGVPLEVIQAVCDRVAASGKLAL 288

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958643125 171 LDIMEVNPTL---GKTPEEVTRTVNTAVALTLS 200
Cdd:PRK13773  289 VDVAELNPRFdidNRTARVAARLIHTIVTAHLP 321
 
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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