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Conserved domains on  [gi|295789558]
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Chain B, Arginase-1

Protein Classification

arginase-1( domain architecture ID 10184189)

arginase-1 is a liver-type arginase that catalyzes the last step of urea synthesis and is expressed specifically in the liver of ureotelic animals

Graphical summary

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List of domain hits

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 ...
9-303 1.95e-179

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: 497.40  E-value: 1.95e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   9 GIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVK 88
Cdd:cd11587    1 SIIGAPFSLGQPRGGVEHGPGALRKAGLLEKLKELEYNYEDLGDLPFGDYENDSEFQIVRNPKSVGKASEQLAGEVAEVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  89 KNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVpGFSWVTPC 168
Cdd:cd11587   81 KNGRFSLVLGGDHSLAIGSISGHAQVYPDLGVIWIDAHGDINTPETSPSGNLHGMPLAFLLGEGKGKLPDV-GFSWVTPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 169 ISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPV 248
Cdd:cd11587  160 ISPENVVYIGLRDVDPGEKYIIKTLGIKYYTMFEVDKLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPVFAPATGTPV 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295789558 249 VGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLAC 303
Cdd:cd11587  240 VGGLSYREGLLIMEELAETGLLSGMDLVEVNPSLDKTPEEVTKTANTAVALTLAL 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 ...
9-303 1.95e-179

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: 497.40  E-value: 1.95e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   9 GIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVK 88
Cdd:cd11587    1 SIIGAPFSLGQPRGGVEHGPGALRKAGLLEKLKELEYNYEDLGDLPFGDYENDSEFQIVRNPKSVGKASEQLAGEVAEVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  89 KNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVpGFSWVTPC 168
Cdd:cd11587   81 KNGRFSLVLGGDHSLAIGSISGHAQVYPDLGVIWIDAHGDINTPETSPSGNLHGMPLAFLLGEGKGKLPDV-GFSWVTPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 169 ISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPV 248
Cdd:cd11587  160 ISPENVVYIGLRDVDPGEKYIIKTLGIKYYTMFEVDKLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPVFAPATGTPV 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295789558 249 VGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLAC 303
Cdd:cd11587  240 VGGLSYREGLLIMEELAETGLLSGMDLVEVNPSLDKTPEEVTKTANTAVALTLAL 294
rocF_arginase TIGR01229
arginase; This model helps resolve arginases from known and putative agmatinases, ...
9-309 3.60e-170

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: 474.23  E-value: 3.60e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558    9 GIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVK 88
Cdd:TIGR01229   1 GIVGLPFSLGQPRRGVDKGPSRLREAGLLETLRDLEYDMQDLGQLPFAVRPKESPRYAVKNPRYVLAATEQLAPKVYEVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   89 KNGRISLVLGGDHSLAIGSISGHARVHPD--LGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVT 166
Cdd:TIGR01229  81 EEGRFPLVLGGDHSIAIGTISGTARVHPDkkLGVLWLDAHADINTPETSDSGNIHGMPLAFLLGRLKSEFPDSPGLGWVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  167 PCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKrPIHLSFDVDGLDPSFTPATGT 246
Cdd:TIGR01229 161 PEISPKNLVYIGLRSVDPGERKILKELGIKVFSMHEIDELGIGKVVEETLEYLKAEDG-PIHLSLDVDGLDPSLAPATGT 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295789558  247 PVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTpeEVTRTVNTAVAITLACFGLARE 309
Cdd:TIGR01229 240 PVVGGLTFREGLLIMEMLYESGLLTALDVVEVNPTLDIK--HVNETIKTAVEIVRSLLGSTLL 300
Arginase pfam00491
Arginase family;
8-304 7.17e-96

Arginase family;


Pssm-ID: 425716 [Multi-domain]  Cd Length: 272  Bit Score: 284.79  E-value: 7.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558    8 IGIIGAPFSK-GQPRGGVEEGPTVLRKAGLLEKLKE-------QECDVKDYGDLPFadipndspfqivkNPRSVGKASEQ 79
Cdd:pfam00491   2 VAIIGVPFDGtGSGRPGARFGPDAIREASARLEPYSldlgvdlEDLKVVDLGDVPV-------------PPGDNEEVLER 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   80 LAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVH-PDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKElkgkipd 158
Cdd:pfam00491  69 IEEAVAAILKAGKLPIVLGGDHSITLGSLRAVAEHYgGPLGVIHFDAHADLRDPYTTGSGNSHGTPFRRAAEE------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  159 vpgfswvtPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLlgrKKRPIHLSFDVDGLDP 238
Cdd:pfam00491 142 --------GLLDPERIVQIGIRSVDNEEYEYARELGITVITMREIDELGIAAVLEEILDRL---GDDPVYLSFDIDVLDP 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295789558  239 SFTPATGTPVVGGLTYREGLYITEEIYKtGLLSGLDIMEVNPSLGktpEEVTRTVNTAVAITLACF 304
Cdd:pfam00491 211 AFAPGTGTPEPGGLTYREALEILRRLAG-LNVVGADVVEVNPPYD---PSGGITARLAAKLVRELL 272
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
2-306 2.66e-80

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: 245.51  E-value: 2.66e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   2 SAKSRTIGIIGAPFSKGQP-RGGVEEGPTVLRKAGLLekLKEQECDVKDYGDLPFADIPNdspfqIVKNPRSVGKASEQL 80
Cdd:COG0010    7 DLEEADIVLLGVPSDLGVSyRPGARFGPDAIREASLN--LEPYDPGVDPLEDLGVADLGD-----VEVPPGDLEETLAAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  81 AGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTttsGNL-HGQPVSFLLKElkgkipdv 159
Cdd:COG0010   80 AEAVAELLAAGKFPIVLGGDHSITLGTIRALARAYGPLGVIHFDAHADLRDPYE---GNLsHGTPLRRALEE-------- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 160 pgfswvtPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLlgRKKRPIHLSFDVDGLDPS 239
Cdd:COG0010  149 -------GLLDPENVVQIGIRSNDPEEFELARELGVTVFTAREIRERGLAAVLEEALERL--RAGDPVYVSFDIDVLDPA 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295789558 240 FTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTpeevTRTVNTAVAITLACFGL 306
Cdd:COG0010  220 FAPGVGTPEPGGLTPREALELLRALAASGKVVGFDIVEVNPPLDPD----GRTARLAAKLLWELLGG 282
PRK02190 PRK02190
agmatinase; Provisional
21-280 5.03e-19

agmatinase; Provisional


Pssm-ID: 235011  Cd Length: 301  Bit Score: 85.67  E-value: 5.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  21 RGGVEEGPTVLRKA---------------GLLEKLKeqecdVKDYGDLPFAdipndspfqiVKNPRSVgkaSEQLAGKVA 85
Cdd:PRK02190  43 RPGARFGPAAIRQAstnlawedrrypwnfDLFERLA-----VVDYGDLVFD----------YGDAEDF---PEALEAHAE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  86 EVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDintplTTTSGNL---HGqpvSFLLKELKGKIpdvpgf 162
Cdd:PRK02190 105 KILAAGKRMLTLGGDHFITLPLLRAHAKHFGPLALVHFDAHTD-----TWADGGSridHG---TMFYHAPKEGL------ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 163 swvtpcISAKDIVYIGLRdvdpgEHYIlKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRkkrPIHLSFDVDGLDPSFTP 242
Cdd:PRK02190 171 ------IDPAHSVQIGIR-----TEYD-KDNGFTVLDARQVNDRGVDAIIAQIKQIVGDM---PVYLTFDIDCLDPAFAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 295789558 243 ATGTPVVGGLTYREGLYITEEIykTGL-LSGLDIMEVNP 280
Cdd:PRK02190 236 GTGTPVIGGLTSAQALKILRGL--KGLnIVGMDVVEVAP 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 ...
9-303 1.95e-179

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: 497.40  E-value: 1.95e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   9 GIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVK 88
Cdd:cd11587    1 SIIGAPFSLGQPRGGVEHGPGALRKAGLLEKLKELEYNYEDLGDLPFGDYENDSEFQIVRNPKSVGKASEQLAGEVAEVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  89 KNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVpGFSWVTPC 168
Cdd:cd11587   81 KNGRFSLVLGGDHSLAIGSISGHAQVYPDLGVIWIDAHGDINTPETSPSGNLHGMPLAFLLGEGKGKLPDV-GFSWVTPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 169 ISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPV 248
Cdd:cd11587  160 ISPENVVYIGLRDVDPGEKYIIKTLGIKYYTMFEVDKLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPVFAPATGTPV 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 295789558 249 VGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLAC 303
Cdd:cd11587  240 VGGLSYREGLLIMEELAETGLLSGMDLVEVNPSLDKTPEEVTKTANTAVALTLAL 294
rocF_arginase TIGR01229
arginase; This model helps resolve arginases from known and putative agmatinases, ...
9-309 3.60e-170

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: 474.23  E-value: 3.60e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558    9 GIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVK 88
Cdd:TIGR01229   1 GIVGLPFSLGQPRRGVDKGPSRLREAGLLETLRDLEYDMQDLGQLPFAVRPKESPRYAVKNPRYVLAATEQLAPKVYEVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   89 KNGRISLVLGGDHSLAIGSISGHARVHPD--LGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVT 166
Cdd:TIGR01229  81 EEGRFPLVLGGDHSIAIGTISGTARVHPDkkLGVLWLDAHADINTPETSDSGNIHGMPLAFLLGRLKSEFPDSPGLGWVA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  167 PCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKrPIHLSFDVDGLDPSFTPATGT 246
Cdd:TIGR01229 161 PEISPKNLVYIGLRSVDPGERKILKELGIKVFSMHEIDELGIGKVVEETLEYLKAEDG-PIHLSLDVDGLDPSLAPATGT 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295789558  247 PVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTpeEVTRTVNTAVAITLACFGLARE 309
Cdd:TIGR01229 240 PVVGGLTFREGLLIMEMLYESGLLTALDVVEVNPTLDIK--HVNETIKTAVEIVRSLLGSTLL 300
Arginase cd09989
Arginase family; This family includes arginase, also known as arginase-like amidino hydrolase ...
8-303 9.87e-150

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: 421.90  E-value: 9.87e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   8 IGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPF-QIVKNPRSVGKASEQLAGKVAE 86
Cdd:cd09989    1 ISIIGVPFDLGAGKRGVELGPEALREAGLLERLEELGHDVEDLGDLLVPNPEEESPFnGNAKNLDEVLEANEKLAEAVAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  87 VKKNGRISLVLGGDHSLAIGSISGHARV-HPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKgkiPDVPGFSWV 165
Cdd:cd09989   81 ALEEGRFPLVLGGDHSIAIGTIAGVARApYPDLGVIWIDAHADINTPETSPSGNIHGMPLAALLGEGH---PELTNIGGV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 166 TPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLlGRKKRPIHLSFDVDGLDPSFTPATG 245
Cdd:cd09989  158 GPKLKPENLVYIGLRDLDPGERELIKKLGIKVFTMDEIDERGIGAVMEEALEYL-KPGTDGIHVSFDVDVLDPSIAPGTG 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 295789558 246 TPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTpeevTRTVNTAVAITLAC 303
Cdd:cd09989  237 TPVPGGLTYREAHLLLEELAETGRLVSLDIVEVNPLLDKE----NRTAELAVELIASA 290
Ureohydrolase cd09015
Ureohydrolase superfamily includes arginase, formiminoglutamase, agmatinase and proclavaminate ...
10-301 4.47e-106

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: 310.51  E-value: 4.47e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  10 IIGAPFSKGQP-RGGVEEGPTVLRKAGLLEKLK--------EQECDVKDYGDLPFAdipndspfqivknPRSVGKASEQL 80
Cdd:cd09015    2 IIGFPYDAGCEgRPGAKFGPSAIRQALLRLALVftglgktrHHHINIYDAGDIRLE-------------GDELEEAHEKL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  81 AGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTtSGNLHGQPVSFLLKELKgkipdvp 160
Cdd:cd09015   69 ASVVQQVLKRGAFPVVLGGDHSIAIATLRAVARHHPDLGVINLDAHLDVNTPETD-GRNSSGTPFRQLLEELQ------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 161 gfswvtpcISAKDIVYIGLRDVDPGEHY--ILKTLGIKYFSMTEVDRLGIGKVMEETLSYllgRKKRPIHLSFDVDGLDP 238
Cdd:cd09015  141 --------QSPKHIVCIGVRGLDPGPALfeYARKLGVKYVTMDEVDKLGLGGVLEQLFHY---DDGDNVYLSVDVDGLDP 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 295789558 239 SFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLgktpEEVTRTVNTAVAITL 301
Cdd:cd09015  210 ADAPGVSTPAAGGLSYREGLPILERAGKTKKVMGADIVEVNPLL----DEDGRTARLAVRLCW 268
Arginase pfam00491
Arginase family;
8-304 7.17e-96

Arginase family;


Pssm-ID: 425716 [Multi-domain]  Cd Length: 272  Bit Score: 284.79  E-value: 7.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558    8 IGIIGAPFSK-GQPRGGVEEGPTVLRKAGLLEKLKE-------QECDVKDYGDLPFadipndspfqivkNPRSVGKASEQ 79
Cdd:pfam00491   2 VAIIGVPFDGtGSGRPGARFGPDAIREASARLEPYSldlgvdlEDLKVVDLGDVPV-------------PPGDNEEVLER 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   80 LAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVH-PDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKElkgkipd 158
Cdd:pfam00491  69 IEEAVAAILKAGKLPIVLGGDHSITLGSLRAVAEHYgGPLGVIHFDAHADLRDPYTTGSGNSHGTPFRRAAEE------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  159 vpgfswvtPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLlgrKKRPIHLSFDVDGLDP 238
Cdd:pfam00491 142 --------GLLDPERIVQIGIRSVDNEEYEYARELGITVITMREIDELGIAAVLEEILDRL---GDDPVYLSFDIDVLDP 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 295789558  239 SFTPATGTPVVGGLTYREGLYITEEIYKtGLLSGLDIMEVNPSLGktpEEVTRTVNTAVAITLACF 304
Cdd:pfam00491 211 AFAPGTGTPEPGGLTYREALEILRRLAG-LNVVGADVVEVNPPYD---PSGGITARLAAKLVRELL 272
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
75-303 1.55e-84

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: 253.84  E-value: 1.55e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  75 KASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGqpvsfllkelkg 154
Cdd:cd09987    9 EAHELLAGVVVAVLKDGKVPVVLGGDHSIANGAIRAVAELHPDLGVIDVDAHHDVRTPEAFGKGNHHT------------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 155 kipdvPGFSWVTPCISAKDIVYIGLRDVDPGEH--YILKTLGIKYFSMTEVDRLGIGKVMEETLSYLlGRKKRPIHLSFD 232
Cdd:cd09987   77 -----PRHLLCEPLISDVHIVSIGIRGVSNGEAggAYARKLGVVYFSMTEVDKLGLGDVFEEIVSYL-GDKGDNVYLSVD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295789558 233 VDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGktpeEVTRTVNTAVAITLAC 303
Cdd:cd09987  151 VDGLDPSFAPGTGTPGPGGLSYREGLYITERIAKTNLVVGLDIVEVNPLLD----ETGRTARLAAALTLEL 217
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
2-306 2.66e-80

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: 245.51  E-value: 2.66e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   2 SAKSRTIGIIGAPFSKGQP-RGGVEEGPTVLRKAGLLekLKEQECDVKDYGDLPFADIPNdspfqIVKNPRSVGKASEQL 80
Cdd:COG0010    7 DLEEADIVLLGVPSDLGVSyRPGARFGPDAIREASLN--LEPYDPGVDPLEDLGVADLGD-----VEVPPGDLEETLAAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  81 AGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTttsGNL-HGQPVSFLLKElkgkipdv 159
Cdd:COG0010   80 AEAVAELLAAGKFPIVLGGDHSITLGTIRALARAYGPLGVIHFDAHADLRDPYE---GNLsHGTPLRRALEE-------- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 160 pgfswvtPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLlgRKKRPIHLSFDVDGLDPS 239
Cdd:COG0010  149 -------GLLDPENVVQIGIRSNDPEEFELARELGVTVFTAREIRERGLAAVLEEALERL--RAGDPVYVSFDIDVLDPA 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 295789558 240 FTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTpeevTRTVNTAVAITLACFGL 306
Cdd:COG0010  220 FAPGVGTPEPGGLTPREALELLRALAASGKVVGFDIVEVNPPLDPD----GRTARLAAKLLWELLGG 282
Agmatinase-like cd09990
Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as ...
8-304 4.16e-44

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: 151.94  E-value: 4.16e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   8 IGIIGAPFSKGQ-PRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNdspfqIVKNPRSVGKASEQLAGKVAE 86
Cdd:cd09990    1 VAVLGVPFDGGStSRPGARFGPRAIREASAGYSTYSPDLGVDDFDDLTVVDYGD-----VPVDPGDIEKTFDRIREAVAE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  87 VKKNGRISLVLGGDHSLAIGSISGHARVHP-DLGVIWVDAHTDINTPLTTtSGNLHGQPVSFLLKElkgkipdvpgfswv 165
Cdd:cd09990   76 IAEAGAIPIVLGGDHSITYPAVRGLAERHKgKVGVIHFDAHLDTRDTDGG-GELSHGTPFRRLLED-------------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 166 tPCISAKDIVYIGLRDVDPGEHYI--LKTLGIKYFSMTEVDRLGIGKVMEETLSyLLGRKKRPIHLSFDVDGLDPSFTPA 243
Cdd:cd09990  141 -GNVDGENIVQIGIRGFWNSPEYVeyAREQGVTVITMRDVRERGLDAVIEEALE-IASDGTDAVYVSVDIDVLDPAFAPG 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 295789558 244 TGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPeevtRTVNTAVAITLACF 304
Cdd:cd09990  219 TGTPEPGGLTPRELLDAVRALGAEAGVVGMDIVEVSPPLDPTD----ITARLAARAVLEFL 275
Agmatinase-like_2 cd11593
Agmatinase and related proteins; This family includes known and predicted bacterial and ...
8-283 3.65e-42

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: 146.47  E-value: 3.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   8 IGIIGAPFSKGQP-RGGVEEGPTVLRKA--GL-----LEKLKEQECDVKDYGDLPFadipndspfqivkNPRSVGKASEQ 79
Cdd:cd11593    1 FVILGVPYDGTVSyRPGTRFGPAAIREAsyQLelyspYLDRDLEDIPFYDLGDLTL-------------PPGDPEKVLER 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  80 LAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTpltttsgNLHGQP-----VSFLLKELKG 154
Cdd:cd11593   68 IEEAVKELLDDGKFPIVLGGEHSITLGAVRALAEKYPDLGVLHFDAHADLRD-------EYEGSKyshacVMRRILELGG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 155 KIPdvpgfswvtpcisakdIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLsyllgrKKRPIHLSFDVD 234
Cdd:cd11593  141 VKR----------------LVQVGIRSGSKEEFEFAKEKGVRIYTFDDFDLGRWLDELIKVL------PEKPVYISIDID 198
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 295789558 235 GLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLG 283
Cdd:cd11593  199 VLDPAFAPGTGTPEPGGLSWRELLDLLRALAESKNIVGFDVVELSPDYD 247
Arginase-like_1 cd09999
Arginase-like amidino hydrolase family; This family includes arginase, also known as ...
10-283 9.20e-39

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: 138.14  E-value: 9.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  10 IIGAPfskgQPRGGVEEGPTVLRKAGLLEKLKEQEcdVKDYGDLP-FADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVK 88
Cdd:cd09999    2 RLVAP----QWQGGNPPNPGYVLGAELLAWLLPES--ADETVEVPvPPDPAPLDPETGIIGRSALLAQLRAAADIIEAAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  89 KNgRIsLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLkelkGKIPdvPGF-SWVTP 167
Cdd:cd09999   76 PD-RP-VVLGGDCSVSLAPFAYLARKYGDLGLLWIDAHPDFNTPETSPTGYAHGMVLAALL----GEGD--PELtAIVKP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 168 CISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGigkvmEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTP 247
Cdd:cd09999  148 PLSPERVVLAGLRDPDDEEEEFIARLGIRVLRPEGLAASA-----QAVLDWLKEEGLSGVWIHLDLDVLDPAIFPAVDFP 222
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 295789558 248 VVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLG 283
Cdd:cd09999  223 EPGGLSLDELVALLAALAASADLVGLTIAEFDPDLD 258
Agmatinase_PAH cd11592
Agmatinase-like family includes proclavaminic acid amidinohydrolase; This agmatinase subfamily ...
8-281 1.28e-38

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: 137.99  E-value: 1.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   8 IGIIGAPFSKGQP-RGGVEEGPTVLRKAGLLekLKE----------QECDVKDYGDLPFadipndspfqivkNPRSVGKA 76
Cdd:cd11592   19 VAVVGVPFDTGVSyRPGARFGPRAIRQASRL--LRPynpatgvdpfDWLKVVDCGDVPV-------------TPGDIEDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  77 SEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNlHGQPVSFLLKElkgki 156
Cdd:cd11592   84 LEQIEEAYRAILAAGPRPLTLGGDHSITLPILRALAKKHGPVALVHFDAHLDTWDPYFGEKYN-HGTPFRRAVEE----- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 157 pdvpGfswvtpCISAKDIVYIGLR--DVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSyLLGRkkRPIHLSFDVD 234
Cdd:cd11592  158 ----G------LLDPKRSIQIGIRgsLYSPDDLEDDRDLGFRVITADEVDDIGLDAIIEKIRE-RVGD--GPVYLSFDID 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 295789558 235 GLDPSFTPATGTPVVGGLTYREGLYITEEIykTGL-LSGLDIMEVNPS 281
Cdd:cd11592  225 VLDPAFAPGTGTPEIGGLTSREALEILRGL--AGLnIVGADVVEVSPP 270
agmatinase TIGR01230
agmatinase; Members of this family include known and predicted examples of agmatinase ...
10-280 1.43e-24

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: 100.22  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   10 IIGAPFSKGQP-RGGVEEGPTVLRKAGLLEKLKEQECDVkDYGDLPFADIpNDSPFQIVKNPRSVGKASEQLAGKVAEVK 88
Cdd:TIGR01230  17 IYGIPYDATTSyRPGSRHGPNAIREASWNLEWYSNRLDR-DLAMLNVVDA-GDLPLAFGDAREMFEKIQEHAEEFLEEGK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   89 KngriSLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNlHGQPVSFLLKelkgkipdvpgfswvtpc 168
Cdd:TIGR01230  95 F----PVAIGGEHSITLPVIRAMAKKFGKFAVVHFDAHTDLRDEFDGGTLN-HACPMRRVIE------------------ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  169 iSAKDIVYIGLRDVDPGEHYILKTLGIKYF--SMTEVDRLGIGKVMEetlsyllgrkkRPIHLSFDVDGLDPSFTPATGT 246
Cdd:TIGR01230 152 -LGLNVVQFGIRSGFKEENDFARENNIQVLkrEVDDVIAEVKQKVGD-----------KPVYVTIDIDVLDPAFAPGTGT 219
                         250       260       270
                  ....*....|....*....|....*....|....
gi 295789558  247 PVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNP 280
Cdd:TIGR01230 220 PEPGGLTSDELINFFVRALKDDNVVGFDVVEVAP 253
Formimidoylglutamase cd09988
Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate ...
9-282 9.00e-24

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: 97.97  E-value: 9.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   9 GIIGAPFSKG----QPRGGVEEGPTVLRKAglLEKLKEQECDVK--DYGDlpfadipndspfqIVKNPRSVGKASEQLAG 82
Cdd:cd09988    1 ALLGFPEDEGvrrnKGRVGAAQGPDAIRKA--LYNLPPGNWGLKiyDLGD-------------IICDGDSLEDTQQALAE 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  83 KVAEVKKNGRISLVLGGDHSLAIGSISGHAR-VHPDLGVIWVDAHTDINTPLTT-TSGNlhgqPVSFLLKELKGKIpdvp 160
Cdd:cd09988   66 VVAELLKKGIIPIVIGGGHDLAYGHYRGLDKaLEKKIGIINFDAHFDLRPLEEGrHSGT----PFRQILEECPNNL---- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 161 gfswvtpcisaKDIVYIGLRdvdpgEHY-------ILKTLGIKYFSMtevDRLGIGKVMEETLSYLLGRkkRPIHLSFDV 233
Cdd:cd09988  138 -----------FNYSVLGIQ-----EYYntqelfdLAKELGVLYFEA---ERLLGEKILDILEAEPALR--DAIYLSIDL 196
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 295789558 234 DGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSL 282
Cdd:cd09988  197 DVISSSDAPGVSAPSPNGLSPEEACAIARYAGKSGKVRSFDIAELNPSL 245
Agmatinase_like_1 cd11589
Agmatinase and related proteins; This family includes known and predicted bacterial agmatinase ...
8-282 2.25e-19

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: 86.12  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558   8 IGIIGAPFSKG-QPRGGVEEGPTVLRKAGLL--------------EKLKEQECDVKDYGDlpfADIPndspfqivknPRS 72
Cdd:cd11589    1 VAVLGVPYDMGyPFRSGARFAPRAIREASTRfargiggyddddggLLFLGDGVRIVDCGD---VDID----------PTD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  73 VGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARvHPDLGVIWVDAHTD-INTPLTTTSGNlhGQPVSfLLKE 151
Cdd:cd11589   68 PAGNFANIEEAVRKILARGAVPVVLGGDHSVTIPVLRALDE-HGPIHVVQIDAHLDwRDEVNGVRYGN--SSPMR-RASE 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 152 LkgkipdvpgfSWVTPcisakdIVYIGLR--------DVDPGEHYilktlGIKYFSMTEVDRLGIGKVMEETlsyllgRK 223
Cdd:cd11589  144 M----------PHVGR------ITQIGIRglgsarpeDFDDARAY-----GSVIITAREVHRIGIEAVLDQI------PD 196
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 295789558 224 KRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSL 282
Cdd:cd11589  197 GENYYITIDIDGLDPSIAPGVGSPSPGGLTYDQVRDLLHGLAKKGRVVGFDLVEVAPAY 255
PRK02190 PRK02190
agmatinase; Provisional
21-280 5.03e-19

agmatinase; Provisional


Pssm-ID: 235011  Cd Length: 301  Bit Score: 85.67  E-value: 5.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  21 RGGVEEGPTVLRKA---------------GLLEKLKeqecdVKDYGDLPFAdipndspfqiVKNPRSVgkaSEQLAGKVA 85
Cdd:PRK02190  43 RPGARFGPAAIRQAstnlawedrrypwnfDLFERLA-----VVDYGDLVFD----------YGDAEDF---PEALEAHAE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  86 EVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDintplTTTSGNL---HGqpvSFLLKELKGKIpdvpgf 162
Cdd:PRK02190 105 KILAAGKRMLTLGGDHFITLPLLRAHAKHFGPLALVHFDAHTD-----TWADGGSridHG---TMFYHAPKEGL------ 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 163 swvtpcISAKDIVYIGLRdvdpgEHYIlKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRkkrPIHLSFDVDGLDPSFTP 242
Cdd:PRK02190 171 ------IDPAHSVQIGIR-----TEYD-KDNGFTVLDARQVNDRGVDAIIAQIKQIVGDM---PVYLTFDIDCLDPAFAP 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 295789558 243 ATGTPVVGGLTYREGLYITEEIykTGL-LSGLDIMEVNP 280
Cdd:PRK02190 236 GTGTPVIGGLTSAQALKILRGL--KGLnIVGMDVVEVAP 272
PLN02615 PLN02615
arginase
49-280 5.99e-09

arginase


Pssm-ID: 178224  Cd Length: 338  Bit Score: 56.40  E-value: 5.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  49 DYGDLPFADIpndspfqivknpRSVGKASEQLAGKVAE-----VKKNGRISLVLGGDHSLAIGSISGharVHPDLG---- 119
Cdd:PLN02615 112 DVGDVPVQEI------------RDCGVDDDRLMNVISEsvklvMEEEPLRPLVLGGDHSISYPVVRA---VSEKLGgpvd 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 120 VIWVDAHTDINTPLtttSGNLHGQPVSFLlKELKGkipdvpGFswvtpcisAKDIVYIGLRDVDPGEHYILKTLGIKYFS 199
Cdd:PLN02615 177 ILHLDAHPDIYHAF---EGNKYSHASSFA-RIMEG------GY--------ARRLLQVGIRSITKEGREQGKRFGVEQYE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 200 MTEVDRlgiGKVMEETLSylLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIykTGLLSGLDIMEVN 279
Cdd:PLN02615 239 MRTFSK---DREKLENLK--LGEGVKGVYISIDVDCLDPAFAPGVSHIEPGGLSFRDVLNILHNL--QGDVVGADVVEFN 311

                 .
gi 295789558 280 P 280
Cdd:PLN02615 312 P 312
PRK13773 PRK13773
formimidoylglutamase; Provisional
21-298 1.13e-08

formimidoylglutamase; Provisional


Pssm-ID: 237499  Cd Length: 324  Bit Score: 55.52  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558  21 RGGVEEGPTVLRKAGLLEKLKEQEcDVKDYGDlpfadipndspfqIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGD 100
Cdd:PRK13773  63 RVGAAAGPDALRGALGSLALHEPR-RVYDAGT-------------VTVPGGDLEAGQERLGDAVSALLDAGHLPVVLGGG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 101 HSLAIGS---ISGHARVHPD--LGVIWVDAHTDINTPLTTTSGnlhgqpvsfllkelkgkipdvpgfswvTPcisakdIV 175
Cdd:PRK13773 129 HETAFGSylgVAGSERRRPGkrLGILNLDAHFDLRAAPVPSSG---------------------------TP------FR 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 295789558 176 YIGLRDVDPGEHYILKTLGIKYFSMTEV-----DRLGIGKVMEETLSYL-----------LGRKKRPIHLSFDVDGLDPS 239
Cdd:PRK13773 176 QIARAEEAAGRTFQYSVLGISEPNNTRAlfdtaRELGVRYLLDEECQVMdraavrvfvadFLADVDVIYLTIDLDVLPAA 255
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 295789558 240 FTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSL---GKTPEEVTRTVNTAVA 298
Cdd:PRK13773 256 VAPGVSAPAAYGVPLEVIQAVCDRVAASGKLALVDVAELNPRFdidNRTARVAARLIHTIVT 317
 
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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