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Conserved domains on  [gi|1958800985|ref|XP_038938938|]
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glutaminase kidney isoform, mitochondrial isoform X6 [Rattus norvegicus]

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 super family cl46433
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 13-195 4.51e-100

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


The actual alignment was detected with superfamily member pfam04960:

Pssm-ID: 461499  Cd Length: 283  Bit Score: 296.21  E-value: 4.51e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  13 LQGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCFpeGTDMVGILDFYFQLCSIEVTCE 92
Cdd:pfam04960 104 IKGADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLDLYFRQCSIEVTCR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  93 SASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPL 172
Cdd:pfam04960 181 DLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVVPGKMGIAVFSPPL 260

                         170       180
                  ....*....|....*....|...
gi 1958800985 173 DKMGNSVKGIHFCHDLVSLCNFH 195
Cdd:pfam04960 261 DEKGNSVRGVKALERLSEELGLH 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-309 6.17e-14

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 303
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 1958800985 304 KILQEY 309
Cdd:COG0666   203 KLLLEA 208
 
Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 13-195 4.51e-100

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 296.21  E-value: 4.51e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  13 LQGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCFpeGTDMVGILDFYFQLCSIEVTCE 92
Cdd:pfam04960 104 IKGADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLDLYFRQCSIEVTCR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  93 SASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPL 172
Cdd:pfam04960 181 DLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVVPGKMGIAVFSPPL 260

                         170       180
                  ....*....|....*....|...
gi 1958800985 173 DKMGNSVKGIHFCHDLVSLCNFH 195
Cdd:pfam04960 261 DEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
9-195 4.49e-84

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 256.13  E-value: 4.49e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985   9 SSMkLQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIE 88
Cdd:COG2066   115 TSL-LPGRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALAYLLKSFGNLENDVEEV--LDLYFRQCSIE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  89 VTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCW 168
Cdd:COG2066   192 VTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVF 271

                         170       180
                  ....*....|....*....|....*..
gi 1958800985 169 SPPLDKMGNSVKGIHFCHDLVSLCNFH 195
Cdd:COG2066   272 SPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 9-208 6.86e-73

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: 227.75  E-value: 6.86e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985   9 SSMkLQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIE 88
Cdd:TIGR03814 115 TSL-LPGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAYLLKSFGNLENDVEEV--LDVYFKQCSIE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  89 VTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCW 168
Cdd:TIGR03814 192 MTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVW 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958800985 169 SPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 208
Cdd:TIGR03814 272 SPALDEAGNSVAGQKA---------------LELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 13-184 5.52e-67

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 212.71  E-value: 5.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  13 LQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCE 92
Cdd:PRK00971  125 LQGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  93 SASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPL 172
Cdd:PRK00971  203 DLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPEL 282

                         170
                  ....*....|..
gi 1958800985 173 DKMGNSVKGIHF 184
Cdd:PRK00971  283 DAKGNSLAGTAA 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-309 6.17e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 303
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 1958800985 304 KILQEY 309
Cdd:COG0666   203 KLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-316 7.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 7.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 303
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 1958800985 304 KILQEYQVQYTPQ 316
Cdd:pfam12796  78 KLLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 223-320 1.97e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 223 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 301
Cdd:PLN03192  528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605

                          90
                  ....*....|....*....
gi 1958800985 302 VFKILQEYQVQYTPQGDSD 320
Cdd:PLN03192  606 IFRILYHFASISDPHAAGD 624
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 215-275 3.96e-05

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: 45.39  E-value: 3.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800985 215 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 275
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 252-275 7.59e-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: 7.59e-04
                           10        20
                   ....*....|....*....|....
gi 1958800985  252 DSRTALHVAAAEGHVEVVKFLLEA 275
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.
 13-195 4.51e-100

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 296.21  E-value: 4.51e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  13 LQGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCFpeGTDMVGILDFYFQLCSIEVTCE 92
Cdd:pfam04960 104 IKGADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLDLYFRQCSIEVTCR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  93 SASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPL 172
Cdd:pfam04960 181 DLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVVPGKMGIAVFSPPL 260

                         170       180
                  ....*....|....*....|...
gi 1958800985 173 DKMGNSVKGIHFCHDLVSLCNFH 195
Cdd:pfam04960 261 DEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
9-195 4.49e-84

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 256.13  E-value: 4.49e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985   9 SSMkLQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIE 88
Cdd:COG2066   115 TSL-LPGRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALAYLLKSFGNLENDVEEV--LDLYFRQCSIE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  89 VTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCW 168
Cdd:COG2066   192 VTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVF 271

                         170       180
                  ....*....|....*....|....*..
gi 1958800985 169 SPPLDKMGNSVKGIHFCHDLVSLCNFH 195
Cdd:COG2066   272 SPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 9-208 6.86e-73

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: 227.75  E-value: 6.86e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985   9 SSMkLQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIE 88
Cdd:TIGR03814 115 TSL-LPGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAYLLKSFGNLENDVEEV--LDVYFKQCSIE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  89 VTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCW 168
Cdd:TIGR03814 192 MTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVW 271

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958800985 169 SPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 208
Cdd:TIGR03814 272 SPALDEAGNSVAGQKA---------------LELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 13-184 5.52e-67

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 212.71  E-value: 5.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  13 LQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCE 92
Cdd:PRK00971  125 LQGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  93 SASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPL 172
Cdd:PRK00971  203 DLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPEL 282

                         170
                  ....*....|..
gi 1958800985 173 DKMGNSVKGIHF 184
Cdd:PRK00971  283 DAKGNSLAGTAA 294
PRK12356 PRK12356
glutaminase; Reviewed
 13-181 3.97e-49

glutaminase; Reviewed


Pssm-ID: 237073  Cd Length: 319  Bit Score: 167.07  E-value: 3.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  13 LQGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCE 92
Cdd:PRK12356  130 VPGANSDERWQRILDGQQRFAGRE-LALSDEVYQSEQTTNFHNRAIAWLLYSYGRLYCDPMEA--CDVYTRQCSTLVTAR 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  93 SASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPL 172
Cdd:PRK12356  207 DLATMGATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYERSGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPL 286


                  ....*....
gi 1958800985 173 DKMGNSVKG 181
Cdd:PRK12356  287 DSAGNSVRG 295
PRK12357 PRK12357
glutaminase; Reviewed
 9-208 6.29e-44

glutaminase; Reviewed


Pssm-ID: 237074  Cd Length: 326  Bit Score: 153.34  E-value: 6.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985   9 SSMkLQGVNNAEKFDYVMQFLNKMAG-----NEYVgfsnatFQSERESGDRNFAIGYYLKEKKcFPEGtDMVGILDFYFQ 83
Cdd:PRK12357  132 ASL-LPGTSVQEKLESLYVLIEKMIGkrpaiNEEV------FQSEWETAHRNRALAYYLKETG-FLES-DVEETLEVYLK 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985  84 LCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVP--- 160
Cdd:PRK12357  203 QCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAAFVGLPAKSGVSGGIMTLVPpks 282

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958800985 161 -------NVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 208
Cdd:PRK12357  283 rkdlpfqDGCGIGIYGPAIDEYGNSLPGIML---------------LKHIAKEWD 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-309 6.17e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 6.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 303
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                  ....*.
gi 1958800985 304 KILQEY 309
Cdd:COG0666   203 KLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
224-316 7.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 7.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 303
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 1958800985 304 KILQEYQVQYTPQ 316
Cdd:pfam12796  78 KLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-306 2.20e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 2.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 303
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169


                  ...
gi 1958800985 304 KIL 306
Cdd:COG0666   170 KLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-310 2.89e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 303
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235


                  ....*..
gi 1958800985 304 KILQEYQ 310
Cdd:COG0666   236 KLLLEAG 242
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 223-320 1.97e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 223 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 301
Cdd:PLN03192  528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605

                          90
                  ....*....|....*....
gi 1958800985 302 VFKILQEYQVQYTPQGDSD 320
Cdd:PLN03192  606 IFRILYHFASISDPHAAGD 624
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 228-324 4.70e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 228 AYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKILQ 307
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLLS 168

                          90       100
                  ....*....|....*....|..
gi 1958800985 308 EYQVQYTPQG-----DSDDGKE 324
Cdd:PTZ00322  169 RHSQCHFELGanakpDSFTGKP 190
Ank_4 pfam13637
Ankyrin repeats (many copies);
254-306 1.51e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.51e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958800985 254 RTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKIL 306
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
224-306 2.27e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 303
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIV 136


                  ...
gi 1958800985 304 KIL 306
Cdd:COG0666   137 KLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
224-273 5.79e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 5.79e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958800985 224 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 273
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 200-273 7.44e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 7.44e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958800985 200 LRHFAKKLDPRrEGGDQrvksvinLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 273
Cdd:PLN03192  610 LYHFASISDPH-AAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 215-275 3.96e-05

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: 45.39  E-value: 3.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958800985 215 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 275
Cdd:cd22192    12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
Ank_5 pfam13857
Ankyrin repeats (many copies);
244-294 1.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958800985 244 MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEA 294
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 252-275 7.59e-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: 7.59e-04
                           10        20
                   ....*....|....*....|....
gi 1958800985  252 DSRTALHVAAAEGHVEVVKFLLEA 275
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 254-285 1.57e-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. 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: 35.73  E-value: 1.57e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958800985 254 RTALHVAAAE-GHVEVVKFLLEAcKVNPFPKDR 285
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 254-274 4.78e-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: 34.16  E-value: 4.78e-03
                          10        20
                  ....*....|....*....|.
gi 1958800985 254 RTALHVAAAEGHVEVVKFLLE 274
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLE 23
 
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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