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Conserved domains on  [gi|530400087|ref|XP_005268854|]
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glutaminase liver isoform, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

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.
 141-425 3.68e-158

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


:

Pssm-ID: 461499  Cd Length: 283  Bit Score: 452.98  E-value: 3.68e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  141 GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFVGKEPSGLRYNKLSL 220
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  221 --NEEGIPHNPMVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNATFQSEKETGDRNYAIGYYLKEKKCF 298
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  299 pkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 378
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 530400087  379 SAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 425
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
EF-hand_14 pfam17959
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 36-119 8.86e-30

EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.


:

Pssm-ID: 465587  Cd Length: 90  Bit Score: 112.33  E-value: 8.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087   36 LGDLLFYTIA-EGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQE-----SSSGGLLDRDLFRKCVSSNIVLLT 109
Cdd:pfam17959   1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQEnseptDSETLLLDRETFKKCIGSNIVLIS 80

                          90
                  ....*....|
gi 530400087  110 QAFRKKFVIP 119
Cdd:pfam17959  81 KALKNQFVIP 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-536 8.15e-17

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 8.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 454 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 533
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ...
gi 530400087 534 KLL 536
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.
 141-425 3.68e-158

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 452.98  E-value: 3.68e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  141 GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFVGKEPSGLRYNKLSL 220
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  221 --NEEGIPHNPMVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNATFQSEKETGDRNYAIGYYLKEKKCF 298
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  299 pkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 378
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 530400087  379 SAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 425
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
128-425 4.14e-132

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 387.10  E-value: 4.14e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 128 VDRIFEDVKELTG-GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFV 206
Cdd:COG2066    1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 207 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKmDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDR 284
Cdd:COG2066   81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 285 NYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 364
Cdd:COG2066  160 NRALAYLLKSFGNLENDVEE--VLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530400087 365 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 425
Cdd:COG2066  238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 128-412 7.85e-115

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: 342.93  E-value: 7.85e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  128 VDRIFEDVKELTG-GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFV 206
Cdd:TIGR03814   1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  207 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDR 284
Cdd:TIGR03814  81 GVEPSGDPFNSIVQleLEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  285 NYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 364
Cdd:TIGR03814 160 NRALAYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 530400087  365 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGT 412
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQ 285
PRK00971 PRK00971
glutaminase; Provisional
 128-425 4.48e-108

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 325.95  E-value: 4.48e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 128 VDRIFEDVKELTG-GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFV 206
Cdd:PRK00971   8 LEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 207 GKEPSGLRYN---KLSLnEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGD 283
Cdd:PRK00971  88 GKEPSGDPFNslvQLEL-EQGKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHAD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 284 RNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMY 363
Cdd:PRK00971 166 RNAAIAYLMKSFGNIENDVET--VLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMY 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400087 364 DFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 425
Cdd:PRK00971 244 DASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
EF-hand_14 pfam17959
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 36-119 8.86e-30

EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.


Pssm-ID: 465587  Cd Length: 90  Bit Score: 112.33  E-value: 8.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087   36 LGDLLFYTIA-EGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQE-----SSSGGLLDRDLFRKCVSSNIVLLT 109
Cdd:pfam17959   1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQEnseptDSETLLLDRETFKKCIGSNIVLIS 80

                          90
                  ....*....|
gi 530400087  110 QAFRKKFVIP 119
Cdd:pfam17959  81 KALKNQFVIP 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-536 8.15e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 8.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 454 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 533
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ...
gi 530400087 534 KLL 536
Cdd:COG0666  203 KLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
454-536 6.12e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  454 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFAKdrwGNIPLDDAVQFNHLEVV 533
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77


                  ...
gi 530400087  534 KLL 536
Cdd:pfam12796  78 KLL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 452-539 2.57e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 452 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLE 531
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 530400087 532 VVKLLQDY 539
Cdd:PTZ00322 163 VVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 454-536 4.37e-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: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 454 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFAKDRW-GNIPLDDAVQFN 528
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100


                 ....*...
gi 530400087 529 HLEVVKLL 536
Cdd:cd22192  101 NLNLVREL 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 482-505 5.08e-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: 37.57  E-value: 5.08e-04
                           10        20
                   ....*....|....*....|....
gi 530400087   482 DSRTALHVAAAEGHIEVVKFLIEA 505
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.
 141-425 3.68e-158

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 452.98  E-value: 3.68e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  141 GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFVGKEPSGLRYNKLSL 220
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  221 --NEEGIPHNPMVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNATFQSEKETGDRNYAIGYYLKEKKCF 298
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  299 pkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 378
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 530400087  379 SAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 425
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
128-425 4.14e-132

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 387.10  E-value: 4.14e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 128 VDRIFEDVKELTG-GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFV 206
Cdd:COG2066    1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 207 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKmDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDR 284
Cdd:COG2066   81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 285 NYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 364
Cdd:COG2066  160 NRALAYLLKSFGNLENDVEE--VLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530400087 365 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 425
Cdd:COG2066  238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 128-412 7.85e-115

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: 342.93  E-value: 7.85e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  128 VDRIFEDVKELTG-GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFV 206
Cdd:TIGR03814   1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  207 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGDR 284
Cdd:TIGR03814  81 GVEPSGDPFNSIVQleLEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  285 NYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 364
Cdd:TIGR03814 160 NRALAYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 530400087  365 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGT 412
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQ 285
PRK00971 PRK00971
glutaminase; Provisional
 128-425 4.48e-108

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 325.95  E-value: 4.48e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 128 VDRIFEDVKELTG-GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFV 206
Cdd:PRK00971   8 LEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 207 GKEPSGLRYN---KLSLnEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEYMGFSNATFQSEKETGD 283
Cdd:PRK00971  88 GKEPSGDPFNslvQLEL-EQGKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHAD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 284 RNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMY 363
Cdd:PRK00971 166 RNAAIAYLMKSFGNIENDVET--VLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMY 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530400087 364 DFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRGTSFCQKLVSLFNFH 425
Cdd:PRK00971 244 DASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
PRK12356 PRK12356
glutaminase; Reviewed
 117-411 1.88e-86

glutaminase; Reviewed


Pssm-ID: 237073  Cd Length: 319  Bit Score: 270.68  E-value: 1.88e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 117 VIPDFEEFTGHVDRIFEDVKELTGGKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISIST 196
Cdd:PRK12356   3 MLPDAEQLQQAVDQAYAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESISKVFTLALALED 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 197 LGTDYVHKFVGKEPSGLRYNKLSLNEE--GIPHNPMVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEyMGFSNAT 274
Cdd:PRK12356  83 VGPQAVREKIGADPTGLPFNSVIAIELhgGKPLNPLVNAGAIATTSLVPGA-NSDERWQRILDGQQRFAGRE-LALSDEV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 275 FQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTL 354
Cdd:PRK12356 161 YQSEQTTNFHNRAIAWLLYSYGRL--YCDPMEACDVYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPYIL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530400087 355 SLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSHRG 411
Cdd:PRK12356 239 AEMTMEGLYERSGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGNSVRG 295
PRK12357 PRK12357
glutaminase; Reviewed
 141-422 2.78e-63

glutaminase; Reviewed


Pssm-ID: 237074  Cd Length: 326  Bit Score: 210.73  E-value: 2.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 141 GKVAAYIPQLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISISTLGTDYVHKFVGKEPSGLRYN---K 217
Cdd:PRK12357  31 GRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFTLQSISKVISFIAACLSRGISYVLERVDVEPTGDAFNsiiR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 218 LSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKaEKFDFVLQYLNKMAGNEYMgFSNATFQSEKETGDRNYAIGYYLKEKKC 297
Cdd:PRK12357 111 LEIHKPGKPFNPMINAGAITVASLLPGTSVQ-EKLESLYVLIEKMIGKRPA-INEEVFQSEWETAHRNRALAYYLKETGF 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 298 FPKGVDmmAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPA 377
Cdd:PRK12357 189 LESDVE--ETLEVYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAAFVGLPA 266

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 378 KSAVSGAILLVVP----------NVMGMMCLSPPLDKLGNSHRGTSFCQKL-----VSLF 422
Cdd:PRK12357 267 KSGVSGGIMTLVPpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGIMLLKHIakewdLSIF 326
EF-hand_14 pfam17959
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 36-119 8.86e-30

EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.


Pssm-ID: 465587  Cd Length: 90  Bit Score: 112.33  E-value: 8.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087   36 LGDLLFYTIA-EGQERIPIHKFTTALKATGLQTSDPRLRDCMSEMHRVVQE-----SSSGGLLDRDLFRKCVSSNIVLLT 109
Cdd:pfam17959   1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQEnseptDSETLLLDRETFKKCIGSNIVLIS 80

                          90
                  ....*....|
gi 530400087  110 QAFRKKFVIP 119
Cdd:pfam17959  81 KALKNQFVIP 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-536 8.15e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 8.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 454 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 533
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ...
gi 530400087 534 KLL 536
Cdd:COG0666  203 KLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-536 1.08e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 421 LFNFHNYDNLRHCARKLDPRREGAEIRNKTVVNLLF-AAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVV 499
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHaAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530400087 500 KFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVVKLL 536
Cdd:COG0666  137 KLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
454-536 6.12e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087  454 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFAKdrwGNIPLDDAVQFNHLEVV 533
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77


                  ...
gi 530400087  534 KLL 536
Cdd:pfam12796  78 KLL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-540 6.19e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 6.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 454 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVV 533
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235


                 ....*..
gi 530400087 534 KLLQDYQ 540
Cdd:COG0666  236 KLLLEAG 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 452-539 2.57e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 452 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLE 531
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 530400087 532 VVKLLQDY 539
Cdd:PTZ00322 163 VVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
484-536 2.66e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 2.66e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530400087  484 RTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEVVKLL 536
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
487-541 3.32e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 3.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530400087  487 LHVAAAEGHIEVVKFLIEaCKVNPFAKDRWGNIPLDDAVQFNHLEVVKLLQDYQD 541
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
454-503 5.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 5.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530400087  454 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLI 503
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 403-503 1.24e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 403 DKLGNSHRGTSFCQKLVSLFNFhnydnLRHCARKLDPRREGAEirnktvvnLLFAAYSGDVSALRRFALSAMDMEQKDYD 482
Cdd:PLN03192 588 DANGNTALWNAISAKHHKIFRI-----LYHFASISDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                         90       100
                 ....*....|....*....|.
gi 530400087 483 SRTALHVAAAEGHIEVVKFLI 503
Cdd:PLN03192 655 GATALQVAMAEDHVDMVRLLI 675
Ank_2 pfam12796
Ankyrin repeats (3 copies);
454-514 1.22e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530400087  454 LLFAAYSGDVSALRrFALSAMDMEQKDYDsRTALHVAAAEGHIEVVKFLIEaCKVNPFAKD 514
Cdd:pfam12796  34 LHLAAKNGHLEIVK-LLLEHADVNLKDNG-RTALHYAARSGHLEIVKLLLE-KGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 443-540 7.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 7.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 443 GAEIR---NKTVVNLLFAAY--SGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHI--EVVKFLIE-------ACKV 508
Cdd:PHA03100  96 GANVNapdNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDkgvdinaKNRV 175

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530400087 509 NPF--------AKDRWGNIPLDDAVQFNHLEVVKLLQDYQ 540
Cdd:PHA03100 176 NYLlsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 453-536 1.30e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 453 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfAKDRWGNIPLDDAVQFNHLE 531
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605


                 ....*
gi 530400087 532 VVKLL 536
Cdd:PLN03192 606 IFRIL 610
Ank_5 pfam13857
Ankyrin repeats (many copies);
474-522 1.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530400087  474 MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLD 522
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 484-515 4.02e-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: 38.04  E-value: 4.02e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 530400087  484 RTALHVAAAE-GHIEVVKFLIEAcKVNPFAKDR 515
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 454-536 4.37e-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: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 454 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFAKDRW-GNIPLDDAVQFN 528
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100


                 ....*...
gi 530400087 529 HLEVVKLL 536
Cdd:cd22192  101 NLNLVREL 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 482-505 5.08e-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: 37.57  E-value: 5.08e-04
                           10        20
                   ....*....|....*....|....
gi 530400087   482 DSRTALHVAAAEGHIEVVKFLIEA 505
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 472-536 1.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530400087 472 SAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfAKDRWGNIPLDDAVQFNHLEVVKLL 536
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEyGADVN--IEDDNGCYPIHIAIKHNFFDIIKLL 176
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
453-536 1.94e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400087 453 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFAKDRWGNIPLDDAVQFNHLEV 532
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA-GADINAKDDGGNTLLHAAARNGDLEI 102


                 ....
gi 530400087 533 VKLL 536
Cdd:COG0666  103 VKLL 106
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 484-504 5.60e-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: 34.54  E-value: 5.60e-03
                          10        20
                  ....*....|....*....|.
gi 530400087  484 RTALHVAAAEGHIEVVKFLIE 504
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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