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Conserved domains on  [gi|229891187|sp|B6QS64|]
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RecName: Full=Amino-acid acetyltransferase, mitochondrial; AltName: Full=Arginine-requiring protein 2; AltName: Full=Glutamate N-acetyltransferase; AltName: Full=N-acetylglutamate synthase; Short=AGS; Short=NAGS; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF619-like super family cl14605
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 573-691 1.29e-52

DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; DUF619-like: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. This subgroup also includes the DUF619 domain of the FABP N-acetylglutamate kinase (NAGK), the enzyme that catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-acetylglutamate phosphate reductase). The DUF619 domain function has yet to be characterized.


The actual alignment was detected with superfamily member cd04266:

Pssm-ID: 417472  Cd Length: 108  Bit Score: 177.26  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 573 QDYLNRVNGRLAGLIIAGEYEGGAILTWETPPsipesernnpENLPRLVPYLDKFAVLKRSQGAGGVADIVFNAMVRTcL 652
Cdd:cd04266    1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPD----------GSTPEKIAYLDKFAVLPKAQGSDGIADILFNAMLDG-F 69

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 229891187 653 PQGVCWRSRMDNPVNKWYFERSRGTWKLDGSNWAMFWTT 691
Cdd:cd04266   70 PNELIWRSRKDNPVNKWYFERSVGVLKLSGSQWKLFWTG 108
 
Name Accession Description Interval E-value
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 573-691 1.29e-52

DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; DUF619-NAGS-FABP: This family includes the DUF619 domain of N-acetylglutamate synthase (NAGS) of the fungal arginine-biosynthetic pathway (FABP). This NAGS (also known as arginine-requiring protein 2 or ARG2) consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. NAGS catalyzes the formation of NAG from acetylcoenzyme A and L-glutamate. The DUF619 domain, yet to be characterized, is predicted to function in NAGS association in fungi.


Pssm-ID: 176268  Cd Length: 108  Bit Score: 177.26  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 573 QDYLNRVNGRLAGLIIAGEYEGGAILTWETPPsipesernnpENLPRLVPYLDKFAVLKRSQGAGGVADIVFNAMVRTcL 652
Cdd:cd04266    1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPD----------GSTPEKIAYLDKFAVLPKAQGSDGIADILFNAMLDG-F 69

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 229891187 653 PQGVCWRSRMDNPVNKWYFERSRGTWKLDGSNWAMFWTT 691
Cdd:cd04266   70 PNELIWRSRKDNPVNKWYFERSVGVLKLSGSQWKLFWTG 108
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 517-712 1.12e-42

NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696.


Pssm-ID: 398437  Cd Length: 166  Bit Score: 152.02  E-value: 1.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187  517 TFLKRGMPLTilpdpritpwspnspdsRHLTLDDpRIDLSRLVHLIEDSFNRKLDVQDYLNRVNGRLAGLIIAGEYEGGA 596
Cdd:pfam04768  14 TLIRRGYKVL-----------------RRTSLEE-LIDIERLRNLIERSFDGRLSVADYLDRLKGRLFKIYVDEPYEALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187  597 ILTWETPPsipesernnpenlprlVPYLDKFAVLKRSQGAgGVADIVFNAMVRTcLPQGVcWRSRMDNPVNKWYFERSRG 676
Cdd:pfam04768  76 IVTKEDGG----------------VPYLDKFAVSKSGWGN-GVSDNVFNAIKKD-FPKLV-WRSREDNPNNKWYFERSDG 136

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 229891187  677 TWKldGSNWAMFWTtpGVpeEDSLRFKDYEAVCRSI 712
Cdd:pfam04768 137 SLL--KNGWVLFWY--GI--KDLNEVSELVASFRDI 166
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 553-689 1.01e-22

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 101.28  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 553 IDLSRLVHLIEDSFNRKLdVQDYLNRVngRLAGLIIAGEYEGGAILTwETPpsipesernnpenlprLVPYLDKFAVLKR 632
Cdd:PRK04531 262 LDLERLNLLIESSFGRTL-KPDYFDTT--QLLRAYVSENYRAAAILT-ETG----------------GGPYLDKFAVLDD 321

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 229891187 633 SQGAGgVADIVFNAMVRTClPQgVCWRSRMDNPVNKWYFERSRGTWKldGSNWAMFW 689
Cdd:PRK04531 322 ARGEG-LGRAVWNVMREET-PQ-LFWRSRHNNTINKFYYAESDGCIK--QEKWKVFW 373
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
544-689 1.77e-20

N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 94.77  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 544 RHLTLDDprIDLSRLVHLIEDSFNRKLdVQDYLNRVngRLAGLIIAGEYEGGAILTWETPpsipesernnpenlprlVPY 623
Cdd:COG5630  294 RHDSWDG--LDLPRLRDLIESSFGRKL-VEGYFDKT--KFYRAYVSESYRAAAILTLEDG-----------------VPY 351

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229891187 624 LDKFAVLKRSQGAGgVADIVFNAMVRTcLPQgVCWRSRMDNPVNKWYFERSRGTWKLDgsNWAMFW 689
Cdd:COG5630  352 LDKFAVLDDAQGEG-LGRAVWQRMREE-NPQ-LFWRSRHDNPVNGFYFAEADGCYKQE--KWTVFW 412
 
Name Accession Description Interval E-value
DUF619-NAGS-FABP cd04266
DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; ...
 573-691 1.29e-52

DUF619 domain of N-acetylglutamate Synthase of the fungal arginine-biosynthetic pathway; DUF619-NAGS-FABP: This family includes the DUF619 domain of N-acetylglutamate synthase (NAGS) of the fungal arginine-biosynthetic pathway (FABP). This NAGS (also known as arginine-requiring protein 2 or ARG2) consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. NAGS catalyzes the formation of NAG from acetylcoenzyme A and L-glutamate. The DUF619 domain, yet to be characterized, is predicted to function in NAGS association in fungi.


Pssm-ID: 176268  Cd Length: 108  Bit Score: 177.26  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 573 QDYLNRVNGRLAGLIIAGEYEGGAILTWETPPsipesernnpENLPRLVPYLDKFAVLKRSQGAGGVADIVFNAMVRTcL 652
Cdd:cd04266    1 EKYLDRLKNSLATVIIAGDYEGAAILTWEGPD----------GSTPEKIAYLDKFAVLPKAQGSDGIADILFNAMLDG-F 69

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 229891187 653 PQGVCWRSRMDNPVNKWYFERSRGTWKLDGSNWAMFWTT 691
Cdd:cd04266   70 PNELIWRSRKDNPVNKWYFERSVGVLKLSGSQWKLFWTG 108
NAT pfam04768
NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or ...
 517-712 1.12e-42

NAT, N-acetyltransferase, of N-acetylglutamate synthase; This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region (pfam00696) in some fungal acetylglutamate kinase enzymes. it stabilizes the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-temrinal domain pfam00696.


Pssm-ID: 398437  Cd Length: 166  Bit Score: 152.02  E-value: 1.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187  517 TFLKRGMPLTilpdpritpwspnspdsRHLTLDDpRIDLSRLVHLIEDSFNRKLDVQDYLNRVNGRLAGLIIAGEYEGGA 596
Cdd:pfam04768  14 TLIRRGYKVL-----------------RRTSLEE-LIDIERLRNLIERSFDGRLSVADYLDRLKGRLFKIYVDEPYEALA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187  597 ILTWETPPsipesernnpenlprlVPYLDKFAVLKRSQGAgGVADIVFNAMVRTcLPQGVcWRSRMDNPVNKWYFERSRG 676
Cdd:pfam04768  76 IVTKEDGG----------------VPYLDKFAVSKSGWGN-GVSDNVFNAIKKD-FPKLV-WRSREDNPNNKWYFERSDG 136

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 229891187  677 TWKldGSNWAMFWTtpGVpeEDSLRFKDYEAVCRSI 712
Cdd:pfam04768 137 SLL--KNGWVLFWY--GI--KDLNEVSELVASFRDI 166
DUF619-NAGS cd04264
DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic ...
 574-690 1.25e-25

DUF619 domain of various N-acetylglutamate Synthases of the fungal arginine-biosynthetic pathway and urea cycle found in humans and fish; DUF619-NAGS: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176266  Cd Length: 99  Bit Score: 101.29  E-value: 1.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 574 DYLNRVNgRLAGLIIAGEYEGGAILTWETPPSipesernnpenlprLVPYLDKFAVLKRSQGAGgVADIVFNAMVRtcLP 653
Cdd:cd04264    2 DYIDRLQ-RLHAIYLSEGYNAAAIVTYEGVNN--------------GVPYLDKFAVSSSAQGEG-TSDALWRRLRR--DF 63

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 229891187 654 QGVCWRSRMDNPVNKWYFERSRGTWKLDgsNWAMFWT 690
Cdd:cd04264   64 PKLFWRSRKTNPINPWYFKRSDGSFKNG--QWKVFWY 98
PRK04531 PRK04531
acetylglutamate kinase; Provisional
 553-689 1.01e-22

acetylglutamate kinase; Provisional


Pssm-ID: 235306 [Multi-domain]  Cd Length: 398  Bit Score: 101.28  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 553 IDLSRLVHLIEDSFNRKLdVQDYLNRVngRLAGLIIAGEYEGGAILTwETPpsipesernnpenlprLVPYLDKFAVLKR 632
Cdd:PRK04531 262 LDLERLNLLIESSFGRTL-KPDYFDTT--QLLRAYVSENYRAAAILT-ETG----------------GGPYLDKFAVLDD 321

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 229891187 633 SQGAGgVADIVFNAMVRTClPQgVCWRSRMDNPVNKWYFERSRGTWKldGSNWAMFW 689
Cdd:PRK04531 322 ARGEG-LGRAVWNVMREET-PQ-LFWRSRHNNTINKFYYAESDGCIK--QEKWKVFW 373
ARG2 COG5630
N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];
544-689 1.77e-20

N-acetylglutamate synthase (arginine biosynthesis) [Amino acid transport and metabolism];


Pssm-ID: 444357 [Multi-domain]  Cd Length: 437  Bit Score: 94.77  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 544 RHLTLDDprIDLSRLVHLIEDSFNRKLdVQDYLNRVngRLAGLIIAGEYEGGAILTWETPpsipesernnpenlprlVPY 623
Cdd:COG5630  294 RHDSWDG--LDLPRLRDLIESSFGRKL-VEGYFDKT--KFYRAYVSESYRAAAILTLEDG-----------------VPY 351

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 229891187 624 LDKFAVLKRSQGAGgVADIVFNAMVRTcLPQgVCWRSRMDNPVNKWYFERSRGTWKLDgsNWAMFW 689
Cdd:COG5630  352 LDKFAVLDDAQGEG-LGRAVWQRMREE-NPQ-LFWRSRHDNPVNGFYFAEADGCYKQE--KWTVFW 412
DUF619-NAGS-U cd04265
DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans ...
 574-689 5.05e-20

DUF619 domain of various N-acetylglutamate Synthases (NAGS) of the urea (U) cycle of humans and fish; This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present in C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176267  Cd Length: 99  Bit Score: 85.50  E-value: 5.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 574 DYLNRVNGRLAGLIIAGEYEGGAILTWETPPSipesernnpenlprlVPYLDKFAVLKRSQGAGgVADIVFNAMVRTcLP 653
Cdd:cd04265    2 DYFDSLQGRLHTIYLSEGYNAAAIVTNEEVDG---------------VPYLDKFAVSSSAQGEG-TGEALWRRLRRD-FP 64

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 229891187 654 QgVCWRSRMDNPVNKWYFERSRGTWKLDgsNWAMFW 689
Cdd:cd04265   65 K-LFWRSRSTNPINPWYFKRCDGSFKNG--HWTVFW 97
DUF619-like cd03173
DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; ...
 574-689 2.46e-14

DUF619 domain of various N-acetylglutamate Kinases and N-acetylglutamate Synthases; DUF619-like: This family includes the DUF619 domain of various N-acetylglutamate synthases (NAGS) of the urea cycle found in humans and fish, the DUF619 domain of the NAGS of the fungal arginine-biosynthetic pathway (FABP), as well as the DUF619 domain present C-terminal of a NAG kinase-like domain in a limited number of predicted NAGSs found in bacteria and Dictyostelium. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate. NAGS is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Domain architecture of ureogenic and fungal NAGS consists of an N-terminal NAG kinase-like domain and a C-terminal DUF619 domain. This subgroup also includes the DUF619 domain of the FABP N-acetylglutamate kinase (NAGK), the enzyme that catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-acetylglutamate phosphate reductase). The DUF619 domain function has yet to be characterized.


Pssm-ID: 176264  Cd Length: 98  Bit Score: 69.05  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229891187 574 DYLNRVNGRLAGLIIAGEYEGGAILTWETPPsipesernnpenlprlVPYLDKFAVLKrSQGAGGVADIVFNAMVRTclP 653
Cdd:cd03173    2 SYLKRLKNGKFASYADEPLEGVAIVTYEGNS----------------IPYLDKFAVSD-HLWLNNVTDNIFNLIRKD--F 62

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 229891187 654 QGVCWRSRMDNPVNKWYFERSRGTwkLDGSNWAMFW 689
Cdd:cd03173   63 PSLLWRVRENDANLKWYFSKSVGS--LDKNGFILFW 96
DUF619-NAGK-FABP cd04263
DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; ...
 621-689 3.16e-06

DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway; DUF619-NAGK-FABP: DUF619 domain of N-acetylglutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (FABP). The nuclear-encoded, mitochondrial polyprotein precursor (ARG5,6) consists of an N-terminal NAGK (ArgB) domain, a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved into two distinct enzymes (NAGK-DUF619 and NAGPR) in the mitochondria. Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. Arg5,6 catalyzes the second reaction of arginine biosynthesis; the phosphorylation of the gamma-carboxyl group of NAG to produce N-acetylglutamylphosphate (NAGP) which is subsequently converted to ornithine in two more steps. It also binds and regulates the promoters of nuclear and mitochondrial genes, and may possibly regulate precursor mRNA metabolism. The DUF619 domain function has yet to be characterized.


Pssm-ID: 176265  Cd Length: 98  Bit Score: 46.16  E-value: 3.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 229891187 621 VPYLDKFaVLKRSQGAGGVADIVFNAMVRTcLPQgVCWRSRMDNPVNKWYFERSRGTWKLDGsnWAMFW 689
Cdd:cd04263   33 VATLATF-TITKSGWLNNVADNIFTAIKKD-HPK-LVWTVREDDENLKWHFEKADGSFTRNG--KVLFW 96
 
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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