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Conserved domains on  [gi|156104878|ref|NP_055720|]
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glutaminase kidney isoform, mitochondrial isoform 1 precursor [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.
 244-528 1.88e-166

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


:

Pssm-ID: 461499  Cd Length: 283  Bit Score: 477.64  E-value: 1.88e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  244 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 323
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  324 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 401
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  402 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 481
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 156104878  482 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 528
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.
 139-222 7.48e-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: 113.10  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  139 LEDLLFYTIA-EGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQ-----TTSDGVMLDKDLFKKCVQSNIVLLT 212
Cdd:pfam17959   1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQensepTDSETLLLDRETFKKCIGSNIVLIS 80

                          90
                  ....*....|
gi 156104878  213 QAFRRKFVIP 222
Cdd:pfam17959  81 KALKNQFVIP 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
557-649 6.71e-14

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 6.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 636
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 156104878  637 KILQEYQVQYTPQ 649
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.
 244-528 1.88e-166

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 477.64  E-value: 1.88e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  244 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 323
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  324 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 401
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  402 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 481
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 156104878  482 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 528
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
231-528 1.57e-139

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 409.82  E-value: 1.57e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 231 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 309
Cdd:COG2066    1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 310 GKEPSGLRFNKLFL--NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 387
Cdd:COG2066   81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 388 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 467
Cdd:COG2066  160 NRALAYLLKSFGNLENDVEEV--LDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156104878 468 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 528
Cdd:COG2066  238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 231-541 1.86e-122

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: 1.86e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  231 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 309
Cdd:TIGR03814   1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  310 GKEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 387
Cdd:TIGR03814  81 GVEPSGDPFNSIvqLELEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  388 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 467
Cdd:TIGR03814 160 NRALAYLLKSFGNLENDVEEV--LDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156104878  468 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 541
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKA---------------LELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 225-517 2.36e-115

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 347.91  E-value: 2.36e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 225 MSFTSHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTE 303
Cdd:PRK00971   2 MLMQAILEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 304 YVHRYVGKEPSGLRFNKLFLNEDD--KPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSE 381
Cdd:PRK00971  82 EVWQRVGKEPSGDPFNSLVQLELEqgKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 382 RESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMH 461
Cdd:PRK00971 161 LEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALML 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156104878 462 SCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHF 517
Cdd:PRK00971 239 TCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAA 294
EF-hand_14 pfam17959
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 139-222 7.48e-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: 113.10  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  139 LEDLLFYTIA-EGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQ-----TTSDGVMLDKDLFKKCVQSNIVLLT 212
Cdd:pfam17959   1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQensepTDSETLLLDRETFKKCIGSNIVLIS 80

                          90
                  ....*....|
gi 156104878  213 QAFRRKFVIP 222
Cdd:pfam17959  81 KALKNQFVIP 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
557-649 6.71e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 6.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 636
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 156104878  637 KILQEYQVQYTPQ 649
Cdd:pfam12796  78 KLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
557-642 2.35e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 2.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 636
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ....*.
gi 156104878 637 KILQEY 642
Cdd:COG0666  203 KLLLEA 208
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 556-653 9.09e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 9.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 556 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 634
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605

                         90
                 ....*....|....*....
gi 156104878 635 VFKILQEYQVQYTPQGDSD 653
Cdd:PLN03192 606 IFRILYHFASISDPHAAGD 624
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 548-608 1.13e-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: 45.39  E-value: 1.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156104878 548 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 608
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 585-608 4.97e-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: 37.95  E-value: 4.97e-04
                           10        20
                   ....*....|....*....|....
gi 156104878   585 DSRTALHVAAAEGHVEVVKFLLEA 608
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.
 244-528 1.88e-166

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


Pssm-ID: 461499  Cd Length: 283  Bit Score: 477.64  E-value: 1.88e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  244 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 323
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  324 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 401
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  402 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 481
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 156104878  482 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 528
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
231-528 1.57e-139

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 409.82  E-value: 1.57e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 231 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 309
Cdd:COG2066    1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 310 GKEPSGLRFNKLFL--NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 387
Cdd:COG2066   81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 388 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 467
Cdd:COG2066  160 NRALAYLLKSFGNLENDVEEV--LDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156104878 468 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 528
Cdd:COG2066  238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 231-541 1.86e-122

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: 1.86e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  231 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 309
Cdd:TIGR03814   1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  310 GKEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 387
Cdd:TIGR03814  81 GVEPSGDPFNSIvqLELEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  388 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 467
Cdd:TIGR03814 160 NRALAYLLKSFGNLENDVEEV--LDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156104878  468 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 541
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKA---------------LELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 225-517 2.36e-115

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 347.91  E-value: 2.36e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 225 MSFTSHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTE 303
Cdd:PRK00971   2 MLMQAILEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 304 YVHRYVGKEPSGLRFNKLFLNEDD--KPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSE 381
Cdd:PRK00971  82 EVWQRVGKEPSGDPFNSLVQLELEqgKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 382 RESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMH 461
Cdd:PRK00971 161 LEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALML 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 156104878 462 SCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHF 517
Cdd:PRK00971 239 TCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAA 294
PRK12356 PRK12356
glutaminase; Reviewed
 231-514 4.51e-93

glutaminase; Reviewed


Pssm-ID: 237073  Cd Length: 319  Bit Score: 290.71  E-value: 4.51e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 231 IDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVG 310
Cdd:PRK12356  14 VDQAYAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESISKVFTLALALEDVGPQAVREKIG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 311 KEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRN 388
Cdd:PRK12356  94 ADPTGLPFNSViaIELHGGKPLNPLVNAGAIATTSLVP-GANSDERWQRILDGQQRFAGRE-LALSDEVYQSEQTTNFHN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 389 FAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDF 468
Cdd:PRK12356 172 RAIAWLLYSYGRLYCDPMEA--CDVYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYER 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 156104878 469 SGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKG 514
Cdd:PRK12356 250 SGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGNSVRG 295
PRK12357 PRK12357
glutaminase; Reviewed
 229-541 5.12e-72

glutaminase; Reviewed


Pssm-ID: 237074  Cd Length: 326  Bit Score: 236.16  E-value: 5.12e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 229 SHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHR 307
Cdd:PRK12357  15 VCLDQWVAHYRTYAAeGRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFTLQSISKVISFIAACLSRGISYVLE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 308 YVGKEPSGLRFN---KLFLNEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAG-----NEYVgfsnatFQ 379
Cdd:PRK12357  95 RVDVEPTGDAFNsiiRLEIHKPGKPFNPMINAGAITVASLLP-GTSVQEKLESLYVLIEKMIGkrpaiNEEV------FQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 380 SERESGDRNFAIGYYLKEKKcFPEGtDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSL 459
Cdd:PRK12357 168 SEWETAHRNRALAYYLKETG-FLES-DVEETLEVYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKAL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 460 MHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVP----------NVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhn 529
Cdd:PRK12357 246 MLTCGMYNASGKFAAFVGLPAKSGVSGGIMTLVPpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGIML------------ 313

                        330
                 ....*....|..
gi 156104878 530 ydnLRHFAKKLD 541
Cdd:PRK12357 314 ---LKHIAKEWD 322
EF-hand_14 pfam17959
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 139-222 7.48e-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: 113.10  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  139 LEDLLFYTIA-EGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQ-----TTSDGVMLDKDLFKKCVQSNIVLLT 212
Cdd:pfam17959   1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQensepTDSETLLLDRETFKKCIGSNIVLIS 80

                          90
                  ....*....|
gi 156104878  213 QAFRRKFVIP 222
Cdd:pfam17959  81 KALKNQFVIP 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
557-649 6.71e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 6.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878  557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 636
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 156104878  637 KILQEYQVQYTPQ 649
Cdd:pfam12796  78 KLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
557-642 2.35e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 2.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 636
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202


                 ....*.
gi 156104878 637 KILQEY 642
Cdd:COG0666  203 KLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
557-639 8.10e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 636
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169


                 ...
gi 156104878 637 KIL 639
Cdd:COG0666  170 KLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
557-643 9.99e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 9.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 636
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235


                 ....*..
gi 156104878 637 KILQEYQ 643
Cdd:COG0666  236 KLLLEAG 242
Ank_4 pfam13637
Ankyrin repeats (many copies);
587-639 8.71e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 8.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156104878  587 RTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKIL 639
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 556-653 9.09e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 9.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 556 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 634
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605

                         90
                 ....*....|....*....
gi 156104878 635 VFKILQEYQVQYTPQGDSD 653
Cdd:PLN03192 606 IFRILYHFASISDPHAAGD 624
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 561-642 4.93e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 561 AYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKILQ 640
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLLS 168


                 ..
gi 156104878 641 EY 642
Cdd:PTZ00322 169 RH 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
557-639 6.98e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 6.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104878 557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 636
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIV 136


                 ...
gi 156104878 637 KIL 639
Cdd:COG0666  137 KLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
557-606 4.29e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 4.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 156104878  557 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 606
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 533-606 2.72e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 2.72e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156104878 533 LRHFAKKLDPRrEGGDQrvksvinLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 606
Cdd:PLN03192 610 LYHFASISDPH-AAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_5 pfam13857
Ankyrin repeats (many copies);
577-627 8.79e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 8.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156104878  577 MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEA 627
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 548-608 1.13e-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: 45.39  E-value: 1.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156104878 548 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 608
Cdd:cd22192   12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 585-608 4.97e-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: 37.95  E-value: 4.97e-04
                           10        20
                   ....*....|....*....|....
gi 156104878   585 DSRTALHVAAAEGHVEVVKFLLEA 608
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 587-618 1.50e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 156104878  587 RTALHVAAAE-GHVEVVKFLLEAcKVNPFPKDR 618
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 587-607 4.96e-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: 34.93  E-value: 4.96e-03
                          10        20
                  ....*....|....*....|.
gi 156104878  587 RTALHVAAAEGHVEVVKFLLE 607
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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