|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
177-461 |
2.74e-156 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 449.52 E-value: 2.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 177 GKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL 256
Cdd:pfam04960 1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 257 --NEEGIPHNPMVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEfMGFSNATFQSEKETGDRNYAIGYYLKEKKCF 334
Cdd:pfam04960 81 leLENGKPRNPMINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 335 pkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 414
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 254826698 415 SAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFH 461
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
164-461 |
2.68e-129 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 381.32 E-value: 2.68e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 164 VDRIFEDAKEPTG-GKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFV 242
Cdd:COG2066 1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 243 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKmDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDR 320
Cdd:COG2066 81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 321 NYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 400
Cdd:COG2066 160 NRALAYLLKSFGNLENDVEE--VLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254826698 401 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFH 461
Cdd:COG2066 238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
164-448 |
1.61e-112 |
|
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: 338.31 E-value: 1.61e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 164 VDRIFEDAKE-PTGGKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFV 242
Cdd:TIGR03814 1 LEDIVEEARPlIGEGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 243 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDR 320
Cdd:TIGR03814 81 GVEPSGDPFNSIVQleLEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 321 NYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 400
Cdd:TIGR03814 160 NRALAYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 254826698 401 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGI 448
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQ 285
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
164-461 |
6.04e-104 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 316.32 E-value: 6.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 164 VDRIFEDAKEPTG-GKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFV 242
Cdd:PRK00971 8 LEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 243 GKEPSGLRYN---KLSLnEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGD 319
Cdd:PRK00971 88 GKEPSGDPFNslvQLEL-EQGKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 320 RNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMY 399
Cdd:PRK00971 166 RNAAIAYLMKSFGNIENDVET--VLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMY 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254826698 400 DFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFH 461
Cdd:PRK00971 244 DASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
|
|
| EF-hand_14 |
pfam17959 |
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme. |
72-155 |
1.47e-29 |
|
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: 111.94 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 72 LGDLLFYTIA-EGQERIPIHKFTTALKATGLQTSDPRLQDCMSKMQRMVQE-----SSSGGLLDRELFQKCVSSNIVLLT 145
Cdd:pfam17959 1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQEnseptDSETLLLDRETFKKCIGSNIVLIS 80
|
90
....*....|
gi 254826698 146 QAFRKKFVIP 155
Cdd:pfam17959 81 KALKNQFVIP 90
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
490-572 |
2.15e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 80.00 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 569
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202
|
...
gi 254826698 570 KLL 572
Cdd:COG0666 203 KLL 205
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
490-572 |
5.70e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFVKdrwGNIPLDDAVQFNHLEVV 569
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
|
...
gi 254826698 570 KLL 572
Cdd:pfam12796 78 KLL 80
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
488-575 |
4.93e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.61 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 488 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLE 567
Cdd:PTZ00322 84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162
|
....*...
gi 254826698 568 VVKLLQDY 575
Cdd:PTZ00322 163 VVQLLSRH 170
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
490-572 |
3.34e-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: 43.46 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFVKDRW-GNIPLDDAVQFN 564
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100
|
....*...
gi 254826698 565 HLEVVKLL 572
Cdd:cd22192 101 NLNLVREL 108
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
518-541 |
4.94e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 4.94e-04
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
177-461 |
2.74e-156 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 449.52 E-value: 2.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 177 GKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSL 256
Cdd:pfam04960 1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 257 --NEEGIPHNPMVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEfMGFSNATFQSEKETGDRNYAIGYYLKEKKCF 334
Cdd:pfam04960 81 leLENGKPRNPMINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 335 pkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 414
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 254826698 415 SAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFH 461
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
164-461 |
2.68e-129 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 381.32 E-value: 2.68e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 164 VDRIFEDAKEPTG-GKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFV 242
Cdd:COG2066 1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 243 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIKmDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDR 320
Cdd:COG2066 81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 321 NYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 400
Cdd:COG2066 160 NRALAYLLKSFGNLENDVEE--VLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254826698 401 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFH 461
Cdd:COG2066 238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
164-448 |
1.61e-112 |
|
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: 338.31 E-value: 1.61e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 164 VDRIFEDAKE-PTGGKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFV 242
Cdd:TIGR03814 1 LEDIVEEARPlIGEGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 243 GKEPSGLRYNKLSL--NEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDR 320
Cdd:TIGR03814 81 GVEPSGDPFNSIVQleLEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 321 NYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYD 400
Cdd:TIGR03814 160 NRALAYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 254826698 401 FSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGI 448
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQ 285
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
164-461 |
6.04e-104 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 316.32 E-value: 6.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 164 VDRIFEDAKEPTG-GKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFV 242
Cdd:PRK00971 8 LEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 243 GKEPSGLRYN---KLSLnEEGIPHNPMVNAGAIVVSSLIkMDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGD 319
Cdd:PRK00971 88 GKEPSGDPFNslvQLEL-EQGKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 320 RNYAIGYYLKEKKCFPKGVDMmaALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMY 399
Cdd:PRK00971 166 RNAAIAYLMKSFGNIENDVET--VLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMY 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254826698 400 DFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFH 461
Cdd:PRK00971 244 DASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
|
|
| PRK12356 |
PRK12356 |
glutaminase; Reviewed |
153-447 |
1.84e-85 |
|
glutaminase; Reviewed
Pssm-ID: 237073 Cd Length: 319 Bit Score: 269.14 E-value: 1.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 153 VIPDFEEFTGHVDRIFEDAKEPTGGKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVST 232
Cdd:PRK12356 3 MLPDAEQLQQAVDQAYAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESISKVFTLALALED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 233 LGTDYVHKFVGKEPSGLRYNKLSLNEE--GIPHNPMVNAGAIVVSSLIKMDcNKAEKFDFVLQYLNKMAGNEfMGFSNAT 310
Cdd:PRK12356 83 VGPQAVREKIGADPTGLPFNSVIAIELhgGKPLNPLVNAGAIATTSLVPGA-NSDERWQRILDGQQRFAGRE-LALSDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 311 FQSEKETGDRNYAIGYYLKEKKCFpkGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTL 390
Cdd:PRK12356 161 YQSEQTTNFHNRAIAWLLYSYGRL--YCDPMEACDVYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPYIL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 254826698 391 SLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRG 447
Cdd:PRK12356 239 AEMTMEGLYERSGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGNSVRG 295
|
|
| PRK12357 |
PRK12357 |
glutaminase; Reviewed |
177-458 |
3.59e-63 |
|
glutaminase; Reviewed
Pssm-ID: 237074 Cd Length: 326 Bit Score: 211.12 E-value: 3.59e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 177 GKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYN---K 253
Cdd:PRK12357 31 GRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFTLQSISKVISFIAACLSRGISYVLERVDVEPTGDAFNsiiR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 254 LSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKaEKFDFVLQYLNKMAGNEFMgFSNATFQSEKETGDRNYAIGYYLKEKKC 333
Cdd:PRK12357 111 LEIHKPGKPFNPMINAGAITVASLLPGTSVQ-EKLESLYVLIEKMIGKRPA-INEEVFQSEWETAHRNRALAYYLKETGF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 334 FPKGVDmmAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPA 413
Cdd:PRK12357 189 LESDVE--ETLEVYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAAFVGLPA 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 414 KSAVSGAILLVVP----------NVMGMMCLSPPLDKLGNSQRGINFCQKL-----VSLF 458
Cdd:PRK12357 267 KSGVSGGIMTLVPpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGIMLLKHIakewdLSIF 326
|
|
| EF-hand_14 |
pfam17959 |
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme. |
72-155 |
1.47e-29 |
|
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: 111.94 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 72 LGDLLFYTIA-EGQERIPIHKFTTALKATGLQTSDPRLQDCMSKMQRMVQE-----SSSGGLLDRELFQKCVSSNIVLLT 145
Cdd:pfam17959 1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQEnseptDSETLLLDRETFKKCIGSNIVLIS 80
|
90
....*....|
gi 254826698 146 QAFRKKFVIP 155
Cdd:pfam17959 81 KALKNQFVIP 90
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
490-572 |
2.15e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 80.00 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 569
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202
|
...
gi 254826698 570 KLL 572
Cdd:COG0666 203 KLL 205
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
490-572 |
4.54e-16 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 79.23 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 569
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169
|
...
gi 254826698 570 KLL 572
Cdd:COG0666 170 KLL 172
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
490-572 |
5.70e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFVKdrwGNIPLDDAVQFNHLEVV 569
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEIV 77
|
...
gi 254826698 570 KLL 572
Cdd:pfam12796 78 KLL 80
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
490-576 |
1.63e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.52 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 569
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235
|
....*..
gi 254826698 570 KLLQDYH 576
Cdd:COG0666 236 KLLLEAG 242
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
490-572 |
5.54e-12 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 66.90 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVV 569
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIV 136
|
...
gi 254826698 570 KLL 572
Cdd:COG0666 137 KLL 139
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
488-575 |
4.93e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.61 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 488 VNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLE 567
Cdd:PTZ00322 84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFRE 162
|
....*...
gi 254826698 568 VVKLLQDY 575
Cdd:PTZ00322 163 VVQLLSRH 170
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
520-572 |
7.38e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 7.38e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 254826698 520 RTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEVVKLL 572
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
523-577 |
3.12e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 51.27 E-value: 3.12e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 254826698 523 LHVAAAEGHIEVVKFLIEaCKVNPFVKDRWGNIPLDDAVQFNHLEVVKLLQDYHD 577
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
466-539 |
3.57e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 3.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254826698 466 LRHCARKLDPRrEGGEVrnktvvnLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLI 539
Cdd:PLN03192 610 LYHFASISDPH-AAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
490-539 |
6.35e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 6.35e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLI 539
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
490-550 |
1.07e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 47.03 E-value: 1.07e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254826698 490 LLFAAYSGDVSALRrFALSAMDMEQKDYDsRTALHVAAAEGHIEVVKFLIEaCKVNPFVKD 550
Cdd:pfam12796 34 LHLAAKNGHLEIVK-LLLEHADVNLKDNG-RTALHYAARSGHLEIVKLLLE-KGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
489-576 |
1.81e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 51.02 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 489 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfVKDRWGNIPLDDAVQFNHLE 567
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605
|
....*....
gi 254826698 568 VVKLLqdYH 576
Cdd:PLN03192 606 IFRIL--YH 612
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
484-575 |
4.22e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 49.28 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 484 NKTVVNLLFAAY--SGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHI--EVVKFLIE-------ACKVNPF----- 547
Cdd:PHA03100 104 NNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDkgvdinaKNRVNYLlsygv 183
|
90 100 110
....*....|....*....|....*....|.
gi 254826698 548 ---VKDRWGNIPLDDAVQFNHLEVVKLLQDY 575
Cdd:PHA03100 184 pinIKDVYGFTPLHYAVYNNNPEFVKYLLDL 214
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
510-558 |
1.29e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 1.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 254826698 510 MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLD 558
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALD 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
490-572 |
3.34e-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: 43.46 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 490 LLFAAYSGDVSALRRFALSA-MDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACK--VN-PFVKDRW-GNIPLDDAVQFN 564
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelVNePMTSDLYqGETALHIAVVNQ 100
|
....*...
gi 254826698 565 HLEVVKLL 572
Cdd:cd22192 101 NLNLVREL 108
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
508-572 |
4.38e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 43.03 E-value: 4.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254826698 508 SAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIE-ACKVNpfVKDRWGNIPLDDAVQFNHLEVVKLL 572
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEyGADVN--IEDDNGCYPIHIAIKHNFFDIIKLL 176
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
518-541 |
4.94e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 4.94e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
520-551 |
1.22e-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: 1.22e-03
10 20 30
....*....|....*....|....*....|...
gi 254826698 520 RTALHVAAAE-GHIEVVKFLIEAcKVNPFVKDR 551
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
489-572 |
3.61e-03 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 39.55 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 489 NLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEAcKVNPFVKDRWGNIPLDDAVQFNHLEV 568
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA-GADINAKDDGGNTLLHAAARNGDLEI 102
|
....
gi 254826698 569 VKLL 572
Cdd:COG0666 103 VKLL 106
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
520-540 |
5.95e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 34.54 E-value: 5.95e-03
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
485-574 |
8.62e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 38.97 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254826698 485 KTVVNLLFAaYSGDVSALRRFaLSAmDMEQKDYDSRTALHVAAAEGHIEVVKFLIE--------ACKV--NPFVKDR--- 551
Cdd:cd22194 110 KEIVRILLA-FAEENGILDRF-INA-EYTEEAYEGQTALNIAIERRQGDIVKLLIAkgadvnahAKGVffNPKYKHEgfy 186
|
90 100
....*....|....*....|...
gi 254826698 552 WGNIPLDDAVQFNHLEVVKLLQD 574
Cdd:cd22194 187 FGETPLALAACTNQPEIVQLLME 209
|
|
| |
