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Conserved domains on  [gi|568905794|ref|XP_006495765|]
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glutaminase kidney isoform, mitochondrial isoform X2 [Mus musculus]

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.
 20-304 4.45e-169

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


:

Pssm-ID: 461499  Cd Length: 283  Bit Score: 475.71  E-value: 4.45e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   20 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 99
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  100 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 177
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  178 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 257
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568905794  258 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 304
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
333-425 6.57e-14

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 6.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 412
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 568905794  413 KILQEYQVQYTPQ 425
Cdd:pfam12796  78 KLLLEKGADINVK 90
 
Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 20-304 4.45e-169

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 475.71  E-value: 4.45e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   20 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 99
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  100 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 177
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  178 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 257
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568905794  258 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 304
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
7-304 2.94e-142

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 408.28  E-value: 2.94e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   7 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 85
Cdd:COG2066    1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  86 GKEPSGLRFNKLFL--NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 163
Cdd:COG2066   81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 164 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 243
Cdd:COG2066  160 NRALAYLLKSFGNLENDVEEV--LDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568905794 244 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 304
Cdd:COG2066  238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 7-317 1.57e-125

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: 366.04  E-value: 1.57e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794    7 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 85
Cdd:TIGR03814   1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   86 GKEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 163
Cdd:TIGR03814  81 GVEPSGDPFNSIvqLELEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  164 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 243
Cdd:TIGR03814 160 NRALAYLLKSFGNLENDVEEV--LDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568905794  244 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 317
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKA---------------LELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 1-293 1.16e-118

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 348.68  E-value: 1.16e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   1 MSFTSHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTE 79
Cdd:PRK00971   2 MLMQAILEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  80 YVHRYVGKEPSGLRFNKLFLNEDD--KPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSE 157
Cdd:PRK00971  82 EVWQRVGKEPSGDPFNSLVQLELEqgKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 158 RESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMH 237
Cdd:PRK00971 161 LEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALML 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568905794 238 SCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHF 293
Cdd:PRK00971 239 TCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAA 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
333-425 6.57e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 6.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 412
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 568905794  413 KILQEYQVQYTPQ 425
Cdd:pfam12796  78 KLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
333-418 1.23e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 412
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ....*.
gi 568905794 413 KILQEY 418
Cdd:COG0666  203 KLLLEA 208
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 332-429 4.24e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 332 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 410
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605

                         90
                 ....*....|....*....
gi 568905794 411 VFKILQEYQVQYTPQGDSD 429
Cdd:PLN03192 606 IFRILYHFASISDPHAAGD 624
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 324-384 6.22e-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: 6.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905794 324 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 384
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 361-384 7.37e-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: 36.80  E-value: 7.37e-04
                           10        20
                   ....*....|....*....|....
gi 568905794   361 DSRTALHVAAAEGHVEVVKFLLEA 384
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.
 20-304 4.45e-169

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 475.71  E-value: 4.45e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   20 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 99
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  100 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 177
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  178 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 257
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568905794  258 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 304
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
7-304 2.94e-142

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 408.28  E-value: 2.94e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   7 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 85
Cdd:COG2066    1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  86 GKEPSGLRFNKLFL--NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 163
Cdd:COG2066   81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 164 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 243
Cdd:COG2066  160 NRALAYLLKSFGNLENDVEEV--LDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568905794 244 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 304
Cdd:COG2066  238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 7-317 1.57e-125

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: 366.04  E-value: 1.57e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794    7 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 85
Cdd:TIGR03814   1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   86 GKEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 163
Cdd:TIGR03814  81 GVEPSGDPFNSIvqLELEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  164 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 243
Cdd:TIGR03814 160 NRALAYLLKSFGNLENDVEEV--LDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568905794  244 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 317
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKA---------------LELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 1-293 1.16e-118

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 348.68  E-value: 1.16e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   1 MSFTSHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTE 79
Cdd:PRK00971   2 MLMQAILEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  80 YVHRYVGKEPSGLRFNKLFLNEDD--KPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSE 157
Cdd:PRK00971  82 EVWQRVGKEPSGDPFNSLVQLELEqgKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 158 RESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMH 237
Cdd:PRK00971 161 LEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALML 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568905794 238 SCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHF 293
Cdd:PRK00971 239 TCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAA 294
PRK12356 PRK12356
glutaminase; Reviewed
 7-290 1.73e-95

glutaminase; Reviewed


Pssm-ID: 237073  Cd Length: 319  Bit Score: 289.94  E-value: 1.73e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   7 IDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVG 86
Cdd:PRK12356  14 VDQAYAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESISKVFTLALALEDVGPQAVREKIG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  87 KEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRN 164
Cdd:PRK12356  94 ADPTGLPFNSViaIELHGGKPLNPLVNAGAIATTSLVP-GANSDERWQRILDGQQRFAGRE-LALSDEVYQSEQTTNFHN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 165 FAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDF 244
Cdd:PRK12356 172 RAIAWLLYSYGRLYCDPMEA--CDVYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYER 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568905794 245 SGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKG 290
Cdd:PRK12356 250 SGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGNSVRG 295
PRK12357 PRK12357
glutaminase; Reviewed
 5-317 5.38e-74

glutaminase; Reviewed


Pssm-ID: 237074  Cd Length: 326  Bit Score: 235.00  E-value: 5.38e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794   5 SHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHR 83
Cdd:PRK12357  15 VCLDQWVAHYRTYAAeGRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFTLQSISKVISFIAACLSRGISYVLE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  84 YVGKEPSGLRFN---KLFLNEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAG-----NEYVgfsnatFQ 155
Cdd:PRK12357  95 RVDVEPTGDAFNsiiRLEIHKPGKPFNPMINAGAITVASLLP-GTSVQEKLESLYVLIEKMIGkrpaiNEEV------FQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 156 SERESGDRNFAIGYYLKEKKcFPEGtDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSL 235
Cdd:PRK12357 168 SEWETAHRNRALAYYLKETG-FLES-DVEETLEVYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKAL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 236 MHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVP----------NVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhn 305
Cdd:PRK12357 246 MLTCGMYNASGKFAAFVGLPAKSGVSGGIMTLVPpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGIML------------ 313

                        330
                 ....*....|..
gi 568905794 306 ydnLRHFAKKLD 317
Cdd:PRK12357 314 ---LKHIAKEWD 322
Ank_2 pfam12796
Ankyrin repeats (3 copies);
333-425 6.57e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 6.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794  333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 412
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 568905794  413 KILQEYQVQYTPQ 425
Cdd:pfam12796  78 KLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
333-418 1.23e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 412
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ....*.
gi 568905794 413 KILQEY 418
Cdd:COG0666  203 KLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
333-415 4.28e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 4.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 412
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169


                 ...
gi 568905794 413 KIL 415
Cdd:COG0666  170 KLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
333-419 5.34e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 5.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 412
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235


                 ....*..
gi 568905794 413 KILQEYQ 419
Cdd:COG0666  236 KLLLEAG 242
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 332-429 4.24e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 4.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 332 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 410
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605

                         90
                 ....*....|....*....
gi 568905794 411 VFKILQEYQVQYTPQGDSD 429
Cdd:PLN03192 606 IFRILYHFASISDPHAAGD 624
Ank_4 pfam13637
Ankyrin repeats (many copies);
363-415 1.10e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 1.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568905794  363 RTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKIL 415
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 337-432 2.23e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 337 AYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKILQ 416
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLLS 168

                         90       100
                 ....*....|....*....|.
gi 568905794 417 EYQVQYTPQG-----DSDDGK 432
Cdd:PTZ00322 169 RHSQCHFELGanakpDSFTGK 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
333-415 3.83e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 412
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIV 136


                 ...
gi 568905794 413 KIL 415
Cdd:COG0666  137 KLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
333-382 4.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 4.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568905794  333 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 382
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 309-382 1.39e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 1.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568905794 309 LRHFAKKLDPRrEGGDQrvksvinLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 382
Cdd:PLN03192 610 LYHFASISDPH-AAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 324-384 6.22e-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: 6.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905794 324 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 384
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
Ank_5 pfam13857
Ankyrin repeats (many copies);
353-403 9.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 9.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568905794  353 MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEA 403
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 361-384 7.37e-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: 36.80  E-value: 7.37e-04
                           10        20
                   ....*....|....*....|....
gi 568905794   361 DSRTALHVAAAEGHVEVVKFLLEA 384
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 363-394 1.70e-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: 1.70e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568905794  363 RTALHVAAAE-GHVEVVKFLLEAcKVNPFPKDR 394
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 363-383 4.50e-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: 4.50e-03
                          10        20
                  ....*....|....*....|.
gi 568905794  363 RTALHVAAAEGHVEVVKFLLE 383
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLE 23
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 227-438 9.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 9.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 227 EAVRNTLSLMHSCGMYDFSGQFAFHvglpaksgvaggILLVVPNVMGM--MCWSPPLDKMGNSVKGIHfchdlvSLCNFH 304
Cdd:PHA02878  51 DVVKSLLTRGHNVNQPDHRDLTPLH------------IICKEPNKLGMkeMIRSINKCSVFYTLVAIK------DAFNNR 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905794 305 N-----------YDNLRHFAKKLDPRREGGDQRVKSVINLLFAaYTGDVsalrrfalsamDMEQRDYDSrTALHVAAAEG 373
Cdd:PHA02878 113 NveifkiiltnrYKNIQTIDLVYIDKKSKDDIIEAEITKLLLS-YGADI-----------NMKDRHKGN-TALHYATENK 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568905794 374 HVEVVKFLL-EACKVNPfpKDRWNNTPMDEALHFGHHDVFKILqeyqVQYTPQGDSDDGKGNQTVH 438
Cdd:PHA02878 180 DQRLTELLLsYGANVNI--PDKTNNSPLHHAVKHYNKPIVHIL----LENGASTDARDKCGNTPLH 239
 
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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