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Conserved domains on  [gi|526118222|ref|NP_001267727|]
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glutaminase liver isoform, mitochondrial isoform 4 [Homo sapiens]

Protein Classification

glutaminase( domain architecture ID 12059562)

glutaminase catalyzes the hydrolysis of L-glutamine to form L-glutamate and ammonium, playing an important role in glutamine catabolism and in maintaining acid-base homeostasis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 1-196 3.17e-105

Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.


:

Pssm-ID: 461499  Cd Length: 283  Bit Score: 309.30  E-value: 3.17e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222    1 MVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALD 80
Cdd:pfam04960  92 MINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLD 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:pfam04960 168 LYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVV 247

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 526118222  161 PNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 196
Cdd:pfam04960 248 PGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-307 2.96e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 225 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 304
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ...
gi 526118222 305 KLL 307
Cdd:COG0666  203 KLL 205
 
Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 1-196 3.17e-105

Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.


Pssm-ID: 461499  Cd Length: 283  Bit Score: 309.30  E-value: 3.17e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222    1 MVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALD 80
Cdd:pfam04960  92 MINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLD 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:pfam04960 168 LYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVV 247

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 526118222  161 PNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 196
Cdd:pfam04960 248 PGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
1-196 7.84e-87

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 263.06  E-value: 7.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   1 MVNAGAIVVSSLIKmDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALD 80
Cdd:COG2066  106 MINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALAYLLKSFGNLENDVEE--VLD 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:COG2066  183 LYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEFAYRVGLPAKSGVGGGIVAVV 262

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 526118222 161 PNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 196
Cdd:COG2066  263 PGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 1-183 6.25e-76

glutaminase A; This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2). [Energy metabolism, Amino acids and amines]


Pssm-ID: 274797  Cd Length: 300  Bit Score: 235.46  E-value: 6.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222    1 MVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALD 80
Cdd:TIGR03814 106 FINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAYLLKSFGNL--ENDVEEVLD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:TIGR03814 183 VYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGEFAYRVGLPAKSGVGGGILAVV 262

                         170       180
                  ....*....|....*....|...
gi 526118222  161 PNVMGMMCLSPPLDKLGNSHRGT 183
Cdd:TIGR03814 263 PGKMGIAVWSPALDEAGNSVAGQ 285
PRK00971 PRK00971
glutaminase; Provisional
 1-196 1.48e-67

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 214.25  E-value: 1.48e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   1 MVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALD 80
Cdd:PRK00971 113 MINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSFGNIENDVET--VLD 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:PRK00971 190 TYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGLPAKSGVGGGILAVV 269

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 526118222 161 PNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 196
Cdd:PRK00971 270 PGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-307 2.96e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 225 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 304
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ...
gi 526118222 305 KLL 307
Cdd:COG0666  203 KLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-307 2.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  225 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFAKdrwGNIPLDDAVQFNHLEVV 304
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77


                  ...
gi 526118222  305 KLL 307
Cdd:pfam12796  78 KLL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 223-310 7.39e-11

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 223 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLE 302
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 526118222 303 VVKLLQDY 310
Cdd:PTZ00322 163 VVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 225-307 2.01e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 225 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFAKDRW-GNIPLDDAVQFN 299
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100


                 ....*...
gi 526118222 300 HLEVVKLL 307
Cdd:cd22192  101 NLNLVREL 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 253-276 7.25e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 7.25e-04
                           10        20
                   ....*....|....*....|....
gi 526118222   253 DSRTALHVAAAEGHIEVVKFLIEA 276
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
 
Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 1-196 3.17e-105

Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.


Pssm-ID: 461499  Cd Length: 283  Bit Score: 309.30  E-value: 3.17e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222    1 MVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALD 80
Cdd:pfam04960  92 MINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLD 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:pfam04960 168 LYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVV 247

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 526118222  161 PNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 196
Cdd:pfam04960 248 PGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
1-196 7.84e-87

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 263.06  E-value: 7.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   1 MVNAGAIVVSSLIKmDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALD 80
Cdd:COG2066  106 MINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALAYLLKSFGNLENDVEE--VLD 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:COG2066  183 LYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEFAYRVGLPAKSGVGGGIVAVV 262

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 526118222 161 PNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 196
Cdd:COG2066  263 PGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 1-183 6.25e-76

glutaminase A; This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2). [Energy metabolism, Amino acids and amines]


Pssm-ID: 274797  Cd Length: 300  Bit Score: 235.46  E-value: 6.25e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222    1 MVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALD 80
Cdd:TIGR03814 106 FINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAYLLKSFGNL--ENDVEEVLD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:TIGR03814 183 VYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGEFAYRVGLPAKSGVGGGILAVV 262

                         170       180
                  ....*....|....*....|...
gi 526118222  161 PNVMGMMCLSPPLDKLGNSHRGT 183
Cdd:TIGR03814 263 PGKMGIAVWSPALDEAGNSVAGQ 285
PRK00971 PRK00971
glutaminase; Provisional
 1-196 1.48e-67

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 214.25  E-value: 1.48e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   1 MVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALD 80
Cdd:PRK00971 113 MINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSFGNIENDVET--VLD 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:PRK00971 190 TYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGLPAKSGVGGGILAVV 269

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 526118222 161 PNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 196
Cdd:PRK00971 270 PGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
PRK12356 PRK12356
glutaminase; Reviewed
 1-182 4.40e-55

glutaminase; Reviewed


Pssm-ID: 237073  Cd Length: 319  Bit Score: 182.47  E-value: 4.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   1 MVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALD 80
Cdd:PRK12356 118 LVNAGAIATTSLVPGA-NSDERWQRILDGQQRFAGRE-LALSDEVYQSEQTTNFHNRAIAWLLYSYGRL--YCDPMEACD 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:PRK12356 194 VYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYERSGDWAYTVGLPGKSGVGGGILAVV 273

                        170       180
                 ....*....|....*....|..
gi 526118222 161 PNVMGMMCLSPPLDKLGNSHRG 182
Cdd:PRK12356 274 PGKMGIAAFSPPLDSAGNSVRG 295
PRK12357 PRK12357
glutaminase; Reviewed
 1-193 1.22e-43

glutaminase; Reviewed


Pssm-ID: 237074  Cd Length: 326  Bit Score: 152.95  E-value: 1.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222   1 MVNAGAIVVSSLIKMDCNKaEKFDFVLQYLNKMAGNEYMgFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDmmAALD 80
Cdd:PRK12357 123 MINAGAITVASLLPGTSVQ-EKLESLYVLIEKMIGKRPA-INEEVFQSEWETAHRNRALAYYLKETGFLESDVE--ETLE 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  81 LYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVV 160
Cdd:PRK12357 199 VYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAAFVGLPAKSGVSGGIMTLV 278

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 526118222 161 P----------NVMGMMCLSPPLDKLGNSHRGTSFCQKL-----VSLF 193
Cdd:PRK12357 279 PpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGIMLLKHIakewdLSIF 326
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-307 2.96e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.69  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 225 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 304
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ...
gi 526118222 305 KLL 307
Cdd:COG0666  203 KLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
192-307 4.53e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 4.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 192 LFNFHNYDNLRHCARKLDPRREGAEIRNKTVVNLLF-AAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVV 270
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHaAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 526118222 271 KFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVVKLL 307
Cdd:COG0666  137 KLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-307 2.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222  225 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFAKdrwGNIPLDDAVQFNHLEVV 304
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77


                  ...
gi 526118222  305 KLL 307
Cdd:pfam12796  78 KLL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-311 2.18e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 225 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 304
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235


                 ....*..
gi 526118222 305 KLLQDYQ 311
Cdd:COG0666  236 KLLLEAG 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 223-310 7.39e-11

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 223 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLE 302
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 526118222 303 VVKLLQDY 310
Cdd:PTZ00322 163 VVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
255-307 4.21e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 4.21e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 526118222  255 RTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVVKLL 307
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 174-274 4.61e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 174 DKLGNSHRGTSFCQKLVSLFNFhnydnLRHCARKLDPRREGAEirnktvvnLLFAAYSGDVSALRRFALSAMDMEQKDYD 253
Cdd:PLN03192 588 DANGNTALWNAISAKHHKIFRI-----LYHFASISDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                         90       100
                 ....*....|....*....|.
gi 526118222 254 SRTALHVAAAEGHIEVVKFLI 274
Cdd:PLN03192 655 GATALQVAMAEDHVDMVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
225-274 6.41e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 6.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 526118222  225 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLI 274
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
258-312 7.89e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 7.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 526118222  258 LHVAAAEGHIEVVKFLIEaCKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQD 312
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-285 3.47e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 3.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526118222  225 LLFAAYSGDVSALRrFALSAMDMEQKDYDsRTALHVAAAEGHIEVVKFLIEaCKVNPFAKD 285
Cdd:pfam12796  34 LHLAAKNGHLEIVK-LLLEHADVNLKDNG-RTALHYAARSGHLEIVKLLLE-KGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 224-307 5.31e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 224 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfAKDRWGNIPLDDAVQFNHLE 302
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605


                 ....*
gi 526118222 303 VVKLL 307
Cdd:PLN03192 606 IFRIL 610
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 214-311 8.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 214 GAEIR---NKTVVNLLFAAY--SGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHI--EVVKFLIE-------ACKV 279
Cdd:PHA03100  96 GANVNapdNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDkgvdinaKNRV 175

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 526118222 280 NPF--------AKDRWGNIPLDDAVQFNHLEVVKLLQDYQ 311
Cdd:PHA03100 176 NYLlsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 225-307 2.01e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 225 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFAKDRW-GNIPLDDAVQFN 299
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100


                 ....*...
gi 526118222 300 HLEVVKLL 307
Cdd:cd22192  101 NLNLVREL 108
Ank_5 pfam13857
Ankyrin repeats (many copies);
245-293 2.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 526118222  245 MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLD 293
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 255-286 5.50e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 5.50e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 526118222  255 RTALHVAAAE-GHIEVVKFLIEAcKVNPFAKDR 286
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 253-276 7.25e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 7.25e-04
                           10        20
                   ....*....|....*....|....
gi 526118222   253 DSRTALHVAAAEGHIEVVKFLIEA 276
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 243-307 8.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 8.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526118222 243 SAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfAKDRWGNIPLDDAVQFNHLEVVKLL 307
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEyGADVN--IEDDNGCYPIHIAIKHNFFDIIKLL 176
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-307 3.25e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 38.78  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 224 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEV 303
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA-GADINAKDDGGNTLLHAAARNGDLEI 102


                 ....
gi 526118222 304 VKLL 307
Cdd:COG0666  103 VKLL 106
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 255-275 6.38e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.77  E-value: 6.38e-03
                          10        20
                  ....*....|....*....|.
gi 526118222  255 RTALHVAAAEGHIEVVKFLIE 275
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLE 23
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 217-313 8.55e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 37.82  E-value: 8.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526118222 217 IRNKT--VVNLLFAaYSGDVSALRRFaLSAmDMEQKDYDSRTALHVAAAEGHIEVVKFLIE--------ACKV--NPFAK 284
Cdd:cd22194  105 INENTkeIVRILLA-FAEENGILDRF-INA-EYTEEAYEGQTALNIAIERRQGDIVKLLIAkgadvnahAKGVffNPKYK 181

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 526118222 285 DR---WGNIPLDDAVQFNHLEVVKLLQD-------YQDS 313
Cdd:cd22194  182 HEgfyFGETPLALAACTNQPEIVQLLMEkestditSQDS 220
 
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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