|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
17-272 |
3.14e-136 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 391.35 E-value: 3.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKMDcN 94
Cdd:pfam04960 30 YSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQleLENGKPRNPMINAGAIAVTSLIKGA-D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 95 KAEKFDFVLQYLNKMAGNEfMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVM 174
Cdd:pfam04960 109 PEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLDLYFRQCSIEVTCRDLAVM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 175 AATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGN 254
Cdd:pfam04960 186 GATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVVPGKMGIAVFSPPLDEKGN 265
|
250
....*....|....*...
gi 551411515 255 SQRGINFCQKLVSLFNFH 272
Cdd:pfam04960 266 SVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
17-272 |
4.97e-111 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 327.78 E-value: 4.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKmDCN 94
Cdd:COG2066 44 YSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERVGVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 95 KAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVM 174
Cdd:COG2066 123 GDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALAYLLKSFGNLENDVEE--VLDLYFRQCSIEVTCRDLARM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 175 AATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGN 254
Cdd:COG2066 201 GATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGN 280
|
250
....*....|....*...
gi 551411515 255 SQRGINFCQKLVSLFNFH 272
Cdd:COG2066 281 SVRGVKALERLSTELGLS 298
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
17-259 |
1.28e-95 |
|
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: 288.61 E-value: 1.28e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIkMDCN 94
Cdd:TIGR03814 44 FSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERVGVEPSGDPFNSIVQleLEPGKPRNPFINAGAIAVTSLL-PGRT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 95 KAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVM 174
Cdd:TIGR03814 123 SDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 175 AATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGN 254
Cdd:TIGR03814 201 GLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGN 280
|
....*
gi 551411515 255 SQRGI 259
Cdd:TIGR03814 281 SVAGQ 285
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
17-272 |
1.47e-88 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 270.87 E-value: 1.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYN---KLSLnEEGIPHNPMVNAGAIVVSSLIkMDC 93
Cdd:PRK00971 51 YSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRVGKEPSGDPFNslvQLEL-EQGKPRNPMINAGAIVVTDLL-QGR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 94 NKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSV 173
Cdd:PRK00971 129 LSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSFGNIENDVET--VLDTYFHQCALEMSCVDLAR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 174 MAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLG 253
Cdd:PRK00971 207 AGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKG 286
|
250
....*....|....*....
gi 551411515 254 NSQRGINFCQKLVSLFNFH 272
Cdd:PRK00971 287 NSLAGTAALERLSQRLGLS 305
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
301-383 |
4.52e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 78.07 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 380
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202
|
...
gi 551411515 381 KLL 383
Cdd:COG0666 203 KLL 205
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
301-383 |
1.80e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.30 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFVKdrwGNIPLDDAVQFNHLEVV 380
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
|
...
gi 551411515 381 KLL 383
Cdd:pfam12796 78 KLL 80
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
299-386 |
2.25e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.61 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 299 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLE 378
Cdd:PTZ00322 84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162
|
....*...
gi 551411515 379 VVKLLQDY 386
Cdd:PTZ00322 163 VVQLLSRH 170
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
301-383 |
2.61e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.08 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFVKDRW-GNIPLDDAVQFN 375
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100
|
....*...
gi 551411515 376 HLEVVKLL 383
Cdd:cd22192 101 NLNLVREL 108
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
329-352 |
7.63e-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: 7.63e-04
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
17-272 |
3.14e-136 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 391.35 E-value: 3.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKMDcN 94
Cdd:pfam04960 30 YSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQleLENGKPRNPMINAGAIAVTSLIKGA-D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 95 KAEKFDFVLQYLNKMAGNEfMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVM 174
Cdd:pfam04960 109 PEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI--ENDVEEVLDLYFRQCSIEVTCRDLAVM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 175 AATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGN 254
Cdd:pfam04960 186 GATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAKSGVGGGILAVVPGKMGIAVFSPPLDEKGN 265
|
250
....*....|....*...
gi 551411515 255 SQRGINFCQKLVSLFNFH 272
Cdd:pfam04960 266 SVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
17-272 |
4.97e-111 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 327.78 E-value: 4.97e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKmDCN 94
Cdd:COG2066 44 YSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERVGVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 95 KAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVM 174
Cdd:COG2066 123 GDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALAYLLKSFGNLENDVEE--VLDLYFRQCSIEVTCRDLARM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 175 AATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGN 254
Cdd:COG2066 201 GATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGN 280
|
250
....*....|....*...
gi 551411515 255 SQRGINFCQKLVSLFNFH 272
Cdd:COG2066 281 SVRGVKALERLSTELGLS 298
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
17-259 |
1.28e-95 |
|
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: 288.61 E-value: 1.28e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIkMDCN 94
Cdd:TIGR03814 44 FSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERVGVEPSGDPFNSIVQleLEPGKPRNPFINAGAIAVTSLL-PGRT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 95 KAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVM 174
Cdd:TIGR03814 123 SDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 175 AATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGN 254
Cdd:TIGR03814 201 GLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGN 280
|
....*
gi 551411515 255 SQRGI 259
Cdd:TIGR03814 281 SVAGQ 285
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
17-272 |
1.47e-88 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 270.87 E-value: 1.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYN---KLSLnEEGIPHNPMVNAGAIVVSSLIkMDC 93
Cdd:PRK00971 51 YSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRVGKEPSGDPFNslvQLEL-EQGKPRNPMINAGAIVVTDLL-QGR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 94 NKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSV 173
Cdd:PRK00971 129 LSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSFGNIENDVET--VLDTYFHQCALEMSCVDLAR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 174 MAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLG 253
Cdd:PRK00971 207 AGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKG 286
|
250
....*....|....*....
gi 551411515 254 NSQRGINFCQKLVSLFNFH 272
Cdd:PRK00971 287 NSLAGTAALERLSQRLGLS 305
|
|
| PRK12356 |
PRK12356 |
glutaminase; Reviewed |
17-258 |
8.85e-69 |
|
glutaminase; Reviewed
Pssm-ID: 237073 Cd Length: 319 Bit Score: 220.22 E-value: 8.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 17 HSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSLNEE--GIPHNPMVNAGAIVVSSLIKMDcN 94
Cdd:PRK12356 56 YSAGDSDYRFAIESISKVFTLALALEDVGPQAVREKIGADPTGLPFNSVIAIELhgGKPLNPLVNAGAIATTSLVPGA-N 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 95 KAEKFDFVLQYLNKMAGNEfMGFSNATFQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVM 174
Cdd:PRK12356 135 SDERWQRILDGQQRFAGRE-LALSDEVYQSEQTTNFHNRAIAWLLYSYGRL--YCDPMEACDVYTRQCSTLVTARDLATM 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 175 AATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGN 254
Cdd:PRK12356 212 GATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYERSGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGN 291
|
....
gi 551411515 255 SQRG 258
Cdd:PRK12356 292 SVRG 295
|
|
| PRK12357 |
PRK12357 |
glutaminase; Reviewed |
20-269 |
1.07e-55 |
|
glutaminase; Reviewed
Pssm-ID: 237074 Cd Length: 326 Bit Score: 186.47 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 20 GHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYN---KLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKa 96
Cdd:PRK12357 63 GDWEVPFTLQSISKVISFIAACLSRGISYVLERVDVEPTGDAFNsiiRLEIHKPGKPFNPMINAGAITVASLLPGTSVQ- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 97 EKFDFVLQYLNKMAGNEFMgFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDmmAALDLYFQLCSVEVTCESGSVMAA 176
Cdd:PRK12357 142 EKLESLYVLIEKMIGKRPA-INEEVFQSEWETAHRNRALAYYLKETGFLESDVE--ETLEVYLKQCSIEVTTEDIALIGL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 177 TLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVP----------NVMGMMCLS 246
Cdd:PRK12357 219 ILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAAFVGLPAKSGVSGGIMTLVPpksrkdlpfqDGCGIGIYG 298
|
250 260
....*....|....*....|....*...
gi 551411515 247 PPLDKLGNSQRGINFCQKL-----VSLF 269
Cdd:PRK12357 299 PAIDEYGNSLPGIMLLKHIakewdLSIF 326
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
301-383 |
4.52e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 78.07 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 380
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202
|
...
gi 551411515 381 KLL 383
Cdd:COG0666 203 KLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
301-383 |
9.37e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 77.30 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 380
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169
|
...
gi 551411515 381 KLL 383
Cdd:COG0666 170 KLL 172
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
301-383 |
1.80e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.30 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFVKdrwGNIPLDDAVQFNHLEVV 380
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
|
...
gi 551411515 381 KLL 383
Cdd:pfam12796 78 KLL 80
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
301-387 |
3.19e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 69.60 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 380
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235
|
....*..
gi 551411515 381 KLLQDYH 387
Cdd:COG0666 236 KLLLEAG 242
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
301-383 |
1.00e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 65.36 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 380
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIV 136
|
...
gi 551411515 381 KLL 383
Cdd:COG0666 137 KLL 139
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
299-386 |
2.25e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.61 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 299 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLE 378
Cdd:PTZ00322 84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162
|
....*...
gi 551411515 379 VVKLLQDY 386
Cdd:PTZ00322 163 VVQLLSRH 170
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
331-383 |
8.12e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 8.12e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 551411515 331 RTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVVKLL 383
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
277-350 |
1.79e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 1.79e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 551411515 277 LRHCARKLDPRrEGGEVrnktvvnLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLI 350
Cdd:PLN03192 610 LYHFASISDPH-AAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
334-388 |
6.31e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.11 E-value: 6.31e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 551411515 334 LHVAAAEGHIEVVKFLIEaCKVNPFVKDRWGNIPLDDAVQFNHLEVVKLLQDYHD 388
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
301-350 |
6.60e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 6.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLI 350
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
300-387 |
9.53e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.02 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 300 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfVKDRWGNIPLDDAVQFNHLE 378
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605
|
....*....
gi 551411515 379 VVKLLqdYH 387
Cdd:PLN03192 606 IFRIL--YH 612
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
301-361 |
2.41e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 45.49 E-value: 2.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 551411515 301 LLFAAYSGDVSALRrFALSAMDMEQKDYDsRTALHVAAAEGHIEVVKFLIEaCKVNPFVKD 361
Cdd:pfam12796 34 LHLAAKNGHLEIVK-LLLEHADVNLKDNG-RTALHYAARSGHLEIVKLLLE-KGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
295-386 |
1.03e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 47.35 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 295 NKTVVNLLFAAY--SGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHI--EVVKFLIE-------ACKVNPF----- 358
Cdd:PHA03100 104 NNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDkgvdinaKNRVNYLlsygv 183
|
90 100 110
....*....|....*....|....*....|.
gi 551411515 359 ---VKDRWGNIPLDDAVQFNHLEVVKLLQDY 386
Cdd:PHA03100 184 pinIKDVYGFTPLHYAVYNNNPEFVKYLLDL 214
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
321-369 |
1.80e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 551411515 321 MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLD 369
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
301-383 |
2.61e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 43.08 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 301 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFVKDRW-GNIPLDDAVQFN 375
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100
|
....*...
gi 551411515 376 HLEVVKLL 383
Cdd:cd22192 101 NLNLVREL 108
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
319-383 |
3.21e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 42.64 E-value: 3.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 551411515 319 SAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfVKDRWGNIPLDDAVQFNHLEVVKLL 383
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEyGADVN--IEDDNGCYPIHIAIKHNFFDIIKLL 176
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
329-352 |
7.63e-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: 7.63e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
331-362 |
1.13e-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: 36.11 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|...
gi 551411515 331 RTALHVAAAE-GHIEVVKFLIEAcKVNPFVKDR 362
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
300-383 |
4.28e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 38.78 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 551411515 300 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEV 379
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA-GADINAKDDGGNTLLHAAARNGDLEI 102
|
....
gi 551411515 380 VKLL 383
Cdd:COG0666 103 VKLL 106
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
331-351 |
7.48e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 33.77 E-value: 7.48e-03
|
| |
