NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1799708356|pdb|6JV0|A]
View 

Chain A, Sll1336 protein

Protein Classification

dimethylarginine dimethylaminohydrolase family protein( domain architecture ID 10004634)

dimethylarginine dimethylaminohydrolase (DdaH) family protein similar to Pseudomonas aeruginosa N(G),N(G)-dimethylarginine dimethylaminohydrolase that hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DdaH COG1834
N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];
27-290 2.13e-110

N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];


:

Pssm-ID: 441439 [Multi-domain]  Cd Length: 264  Bit Score: 320.58  E-value: 2.13e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A       27 RILMCPPDHYDVDYVINpWMEGNI----HKSSQERAVEQWKKLHQTI-KECAIVDLVKPAKGWPDMVFTANAGLVLGENV 101
Cdd:COG1834   1 RVLMCRPDHFGVEYAIN-WMDPLRewagPPPDAERAVAQWDALVDALeALGVEVHRLPPVPGLPDMVFTRDAGLVIGDGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      102 VLSRFYHKERQGEEPYFKAWFEENGFTVYELPQDLPFEGaGDALFDreGRWLWAGYGFRSELDSHPYIAKWLDTEVVSLR 181
Cdd:COG1834  80 ILARMRHPERRGEEAAYREWLEELGIPVVRLPEPGVFEG-GDVLLD--GDTLLVGYGFRTNRAGIEWLARLLGYEVVPLE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      182 LIDERFYHLDTCFCPLSGGYLLYYPPAFDAYSNRVIEMriPPEKRIIVEELDAVNFACNAVNV-NDIIIMNLVSRTLKEK 260
Cdd:COG1834 157 LVDPRFLHLDTAFCPLAPGLALVYPEAFDPESLALLKE--PGWDLIEVPEEEAAWLGCNVLSLgGRRVVSPAGNPRLNAA 234
                       250       260       270
                ....*....|....*....|....*....|
6JV0_A      261 LAEAGFKVRETPLTEFLKAGGAAKCLTLRV 290
Cdd:COG1834 235 LRAAGFEVIEVDLSEFLKGGGGFHCLTLPL 264
 
Name Accession Description Interval E-value
DdaH COG1834
N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];
27-290 2.13e-110

N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];


Pssm-ID: 441439 [Multi-domain]  Cd Length: 264  Bit Score: 320.58  E-value: 2.13e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A       27 RILMCPPDHYDVDYVINpWMEGNI----HKSSQERAVEQWKKLHQTI-KECAIVDLVKPAKGWPDMVFTANAGLVLGENV 101
Cdd:COG1834   1 RVLMCRPDHFGVEYAIN-WMDPLRewagPPPDAERAVAQWDALVDALeALGVEVHRLPPVPGLPDMVFTRDAGLVIGDGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      102 VLSRFYHKERQGEEPYFKAWFEENGFTVYELPQDLPFEGaGDALFDreGRWLWAGYGFRSELDSHPYIAKWLDTEVVSLR 181
Cdd:COG1834  80 ILARMRHPERRGEEAAYREWLEELGIPVVRLPEPGVFEG-GDVLLD--GDTLLVGYGFRTNRAGIEWLARLLGYEVVPLE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      182 LIDERFYHLDTCFCPLSGGYLLYYPPAFDAYSNRVIEMriPPEKRIIVEELDAVNFACNAVNV-NDIIIMNLVSRTLKEK 260
Cdd:COG1834 157 LVDPRFLHLDTAFCPLAPGLALVYPEAFDPESLALLKE--PGWDLIEVPEEEAAWLGCNVLSLgGRRVVSPAGNPRLNAA 234
                       250       260       270
                ....*....|....*....|....*....|
6JV0_A      261 LAEAGFKVRETPLTEFLKAGGAAKCLTLRV 290
Cdd:COG1834 235 LRAAGFEVIEVDLSEFLKGGGGFHCLTLPL 264
DDAH_eukar pfam19420
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G) ...
51-287 1.12e-11

N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G)-dimethylarginine dimethylaminohydrolases (DDAH) from eukaryotes. It also includes arginine deiminases and DDAH from prokaryotes. These enzymes are involved in arginine metabolism and belong to the amidinotransferase (AT) superfamily as they share the alpha/beta propeller fold, which includes structurally important residues (buried hydrophobic residues, buried hydrophilic residues hydrogen-bonded with mainchain groups and the hallmark of three consecutive buried Gly residues near the C-terminus, conserved among its members.


Pssm-ID: 437252 [Multi-domain]  Cd Length: 288  Bit Score: 63.93  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A         51 HKSSQERAVEQWKKLHQTIKECAI-VDLVK-PAKGWPDMVFTANAG-LVLGENVVLSRFYHKERQGEEPYFKAWFEEN-- 125
Cdd:pfam19420  21 EDEIQERALKEFDAMVQALRQNGIeVIVLDdTEPKTPDAVFPNNWFsTHADGTVFLYPMYAENRRLERREDLLELLLEkg 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A        126 -------GFTVYELPQDLpFEGAGDALFDREGRWLWAGYGFRSELDSHPYIAKWLDTEVV---SLRLIDER---FYHLDT 192
Cdd:pfam19420 101 favykvlDYSGFEDESKF-LEGTGDMVFDHENKIAYGALSPRADEEVLEEVCREIGYKPVtfhSEVIVDRKgkpIYHTNV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A        193 CFCPLSGGYLLYYPPAFDAYSNRVIEMRIPPEKRIIVE--ELDAVNFACNAVNVNDIIIMNLVSRT-------LKEKLAE 263
Cdd:pfam19420 180 MMNVGEDLAVVCLESIPDRKERELVLRALTQSGKEIIDisEEQIFHFAGNVLELCNGNKNLIMSVTaydsltpVQEQLIE 259
                         250       260
                  ....*....|....*....|....*
6JV0_A        264 AGFKVRETPLTEFL-KAGGAAKCLT 287
Cdd:pfam19420 260 KYCEVISVDIPTIErLGGGSARCMI 284
amidinotransferase-like cd21113
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
56-290 1.88e-07

L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar proteins; This family contains amidinotransferase enzymes known to catalyze the transfer of the amidino group from a donor molecule (usually arginine) to an acceptor molecule bearing a primary amine. They are widespread in nature, occurring in essential metabolic pathways in eukaryotes as well as in biosynthetic pathways for antibiotics and virulence factors in prokaryotes. This family includes L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase, arginine-glycine amidinotransferase, or arginine-glycine transamidinase), inosamine-phosphate amidinotransferase (EC 2.1.4.2; also called inosamine amidinotransferase, inosamine-P amidinotransferase, or scyllo-inosamine-4-phosphate amidinotransferase or L-arginine:inosamine phosphate amidinotransferase), and similar proteins. L-arginine:glycine amidinotransferase (AT or AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. This family also includes L-arginine:inosamine-phosphate Streptomyces griseus amidinotransferase StrB1, which is structurally similar to human L-arginine:glycine amidinotransferase; AT and StrB1 share conserved residues involved in substrate binding and catalysis at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases.


Pssm-ID: 439146  Cd Length: 336  Bit Score: 51.74  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A       56 ERAVEQWKKLHQTIKECAI-------VD--LVKPAKGWPDMVFTANAGLVLGENVVLSRFYHKERQGEE----PYFKAWF 122
Cdd:cd21113  56 KKAVAELENLASILEKEGVrvrrpkeVDhlPAKTPDGETTGVMPRDILFVIGNKIIEAPMAWPSRFFEElayrDILEDYG 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      123 EENGFTVYELPQdlpFEGAGDALFDREGRWLWAGYGFRSELDSHPYI------------------AKWL------DTEVV 178
Cdd:cd21113 136 ESGLYRVMRAPK---PEGGDDLYDGQAPAGEDIITETEPLFDAADFMrfgkdiigqrsqvtnmkgIEWLreylgdDYTVH 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      179 SLRLIDERFYHLDTCFCPLSGGYLLYYPpafdaysNRVIEMR-----------IPPEKRIIVEELD----AVNFACNAVN 243
Cdd:cd21113 213 IIELDDPHPMHLDCTFLPLREGLALIYP-------SRVVEPRqipdffkgwelINVPEYPEPDDHPlymcSNWLGTNVLS 285
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
6JV0_A      244 VN-DIIIMNLVSRTLKEKLAEAGFKVRETPLTEFLKAGGAAKCLTLRV 290
Cdd:cd21113 286 LDeKTIIVERREVHLNRQLRKLGMNVIEIPFYHAISLGGGFHCATMDL 333
 
Name Accession Description Interval E-value
DdaH COG1834
N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];
27-290 2.13e-110

N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];


Pssm-ID: 441439 [Multi-domain]  Cd Length: 264  Bit Score: 320.58  E-value: 2.13e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A       27 RILMCPPDHYDVDYVINpWMEGNI----HKSSQERAVEQWKKLHQTI-KECAIVDLVKPAKGWPDMVFTANAGLVLGENV 101
Cdd:COG1834   1 RVLMCRPDHFGVEYAIN-WMDPLRewagPPPDAERAVAQWDALVDALeALGVEVHRLPPVPGLPDMVFTRDAGLVIGDGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      102 VLSRFYHKERQGEEPYFKAWFEENGFTVYELPQDLPFEGaGDALFDreGRWLWAGYGFRSELDSHPYIAKWLDTEVVSLR 181
Cdd:COG1834  80 ILARMRHPERRGEEAAYREWLEELGIPVVRLPEPGVFEG-GDVLLD--GDTLLVGYGFRTNRAGIEWLARLLGYEVVPLE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      182 LIDERFYHLDTCFCPLSGGYLLYYPPAFDAYSNRVIEMriPPEKRIIVEELDAVNFACNAVNV-NDIIIMNLVSRTLKEK 260
Cdd:COG1834 157 LVDPRFLHLDTAFCPLAPGLALVYPEAFDPESLALLKE--PGWDLIEVPEEEAAWLGCNVLSLgGRRVVSPAGNPRLNAA 234
                       250       260       270
                ....*....|....*....|....*....|
6JV0_A      261 LAEAGFKVRETPLTEFLKAGGAAKCLTLRV 290
Cdd:COG1834 235 LRAAGFEVIEVDLSEFLKGGGGFHCLTLPL 264
DDAH_eukar pfam19420
N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G) ...
51-287 1.12e-11

N,N dimethylarginine dimethylhydrolase, eukaryotic; This family contains N(G),N(G)-dimethylarginine dimethylaminohydrolases (DDAH) from eukaryotes. It also includes arginine deiminases and DDAH from prokaryotes. These enzymes are involved in arginine metabolism and belong to the amidinotransferase (AT) superfamily as they share the alpha/beta propeller fold, which includes structurally important residues (buried hydrophobic residues, buried hydrophilic residues hydrogen-bonded with mainchain groups and the hallmark of three consecutive buried Gly residues near the C-terminus, conserved among its members.


Pssm-ID: 437252 [Multi-domain]  Cd Length: 288  Bit Score: 63.93  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A         51 HKSSQERAVEQWKKLHQTIKECAI-VDLVK-PAKGWPDMVFTANAG-LVLGENVVLSRFYHKERQGEEPYFKAWFEEN-- 125
Cdd:pfam19420  21 EDEIQERALKEFDAMVQALRQNGIeVIVLDdTEPKTPDAVFPNNWFsTHADGTVFLYPMYAENRRLERREDLLELLLEkg 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A        126 -------GFTVYELPQDLpFEGAGDALFDREGRWLWAGYGFRSELDSHPYIAKWLDTEVV---SLRLIDER---FYHLDT 192
Cdd:pfam19420 101 favykvlDYSGFEDESKF-LEGTGDMVFDHENKIAYGALSPRADEEVLEEVCREIGYKPVtfhSEVIVDRKgkpIYHTNV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A        193 CFCPLSGGYLLYYPPAFDAYSNRVIEMRIPPEKRIIVE--ELDAVNFACNAVNVNDIIIMNLVSRT-------LKEKLAE 263
Cdd:pfam19420 180 MMNVGEDLAVVCLESIPDRKERELVLRALTQSGKEIIDisEEQIFHFAGNVLELCNGNKNLIMSVTaydsltpVQEQLIE 259
                         250       260
                  ....*....|....*....|....*
6JV0_A        264 AGFKVRETPLTEFL-KAGGAAKCLT 287
Cdd:pfam19420 260 KYCEVISVDIPTIErLGGGSARCMI 284
amidinotransferase-like cd21113
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
56-290 1.88e-07

L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar proteins; This family contains amidinotransferase enzymes known to catalyze the transfer of the amidino group from a donor molecule (usually arginine) to an acceptor molecule bearing a primary amine. They are widespread in nature, occurring in essential metabolic pathways in eukaryotes as well as in biosynthetic pathways for antibiotics and virulence factors in prokaryotes. This family includes L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase, arginine-glycine amidinotransferase, or arginine-glycine transamidinase), inosamine-phosphate amidinotransferase (EC 2.1.4.2; also called inosamine amidinotransferase, inosamine-P amidinotransferase, or scyllo-inosamine-4-phosphate amidinotransferase or L-arginine:inosamine phosphate amidinotransferase), and similar proteins. L-arginine:glycine amidinotransferase (AT or AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. This family also includes L-arginine:inosamine-phosphate Streptomyces griseus amidinotransferase StrB1, which is structurally similar to human L-arginine:glycine amidinotransferase; AT and StrB1 share conserved residues involved in substrate binding and catalysis at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases.


Pssm-ID: 439146  Cd Length: 336  Bit Score: 51.74  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A       56 ERAVEQWKKLHQTIKECAI-------VD--LVKPAKGWPDMVFTANAGLVLGENVVLSRFYHKERQGEE----PYFKAWF 122
Cdd:cd21113  56 KKAVAELENLASILEKEGVrvrrpkeVDhlPAKTPDGETTGVMPRDILFVIGNKIIEAPMAWPSRFFEElayrDILEDYG 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      123 EENGFTVYELPQdlpFEGAGDALFDREGRWLWAGYGFRSELDSHPYI------------------AKWL------DTEVV 178
Cdd:cd21113 136 ESGLYRVMRAPK---PEGGDDLYDGQAPAGEDIITETEPLFDAADFMrfgkdiigqrsqvtnmkgIEWLreylgdDYTVH 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6JV0_A      179 SLRLIDERFYHLDTCFCPLSGGYLLYYPpafdaysNRVIEMR-----------IPPEKRIIVEELD----AVNFACNAVN 243
Cdd:cd21113 213 IIELDDPHPMHLDCTFLPLREGLALIYP-------SRVVEPRqipdffkgwelINVPEYPEPDDHPlymcSNWLGTNVLS 285
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
6JV0_A      244 VN-DIIIMNLVSRTLKEKLAEAGFKVRETPLTEFLKAGGAAKCLTLRV 290
Cdd:cd21113 286 LDeKTIIVERREVHLNRQLRKLGMNVIEIPFYHAISLGGGFHCATMDL 333
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH