|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
248-532 |
2.88e-166 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 477.25 E-value: 2.88e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 248 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 327
Cdd:pfam04960 1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 328 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 405
Cdd:pfam04960 81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 406 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 485
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1939402065 486 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 532
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
235-532 |
3.25e-139 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 409.05 E-value: 3.25e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 235 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 313
Cdd:COG2066 1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 314 GKEPSGLRFNKLFL--NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 391
Cdd:COG2066 81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 392 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 471
Cdd:COG2066 160 NRALAYLLKSFGNLENDVEEV--LDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939402065 472 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 532
Cdd:COG2066 238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
235-545 |
2.06e-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: 2.06e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 235 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 313
Cdd:TIGR03814 1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 314 GKEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 391
Cdd:TIGR03814 81 GVEPSGDPFNSIvqLELEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 392 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 471
Cdd:TIGR03814 160 NRALAYLLKSFGNLENDVEEV--LDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402065 472 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 545
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKA---------------LELLSEKLG 296
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
229-521 |
1.42e-115 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 348.68 E-value: 1.42e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 229 MSFTSHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTE 307
Cdd:PRK00971 2 MLMQAILEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 308 YVHRYVGKEPSGLRFNKLFLNEDD--KPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSE 385
Cdd:PRK00971 82 EVWQRVGKEPSGDPFNSLVQLELEqgKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 386 RESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMH 465
Cdd:PRK00971 161 LEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALML 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939402065 466 SCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHF 521
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. |
143-226 |
7.55e-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: 7.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 143 LEDLLFYTIA-EGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQ-----TTSDGVMLDKDLFKKCVQSNIVLLT 216
Cdd:pfam17959 1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQensepTDSETLLLDRETFKKCIGSNIVLIS 80
|
90
....*....|
gi 1939402065 217 QAFRRKFVIP 226
Cdd:pfam17959 81 KALKNQFVIP 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
561-653 |
6.75e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.45 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 640
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
|
90
....*....|...
gi 1939402065 641 KILQEYQVQYTPQ 653
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
561-646 |
2.37e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.14 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 640
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202
|
....*.
gi 1939402065 641 KILQEY 646
Cdd:COG0666 203 KLLLEA 208
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
560-657 |
9.18e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.81 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 560 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 638
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605
|
90
....*....|....*....
gi 1939402065 639 VFKILQEYQVQYTPQGDSD 657
Cdd:PLN03192 606 IFRILYHFASISDPHAAGD 624
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
552-612 |
1.14e-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: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939402065 552 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 612
Cdd:cd22192 12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
589-612 |
5.30e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 5.30e-04
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
248-532 |
2.88e-166 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 477.25 E-value: 2.88e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 248 GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFL 327
Cdd:pfam04960 1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 328 --NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRNFAIGYYLKEKKCF 405
Cdd:pfam04960 81 leLENGKPRNPMINAGAIAVTSLIK-GADPEERFERILDFLRKLAGRE-LTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 406 peGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAK 485
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1939402065 486 SGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 532
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
235-532 |
3.25e-139 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 409.05 E-value: 3.25e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 235 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 313
Cdd:COG2066 1 LEEIYEKVRPYLGeGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 314 GKEPSGLRFNKLFL--NEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 391
Cdd:COG2066 81 GVEPSGDPFNSIVQleLENGIPRNPMINAGAIVVTSLLP-GRSGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 392 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 471
Cdd:COG2066 160 NRALAYLLKSFGNLENDVEEV--LDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939402065 472 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFH 532
Cdd:COG2066 238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
235-545 |
2.06e-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: 2.06e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 235 IDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYV 313
Cdd:TIGR03814 1 LEDIVEEARPLIGeGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 314 GKEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDR 391
Cdd:TIGR03814 81 GVEPSGDPFNSIvqLELEPGKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 392 NFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYD 471
Cdd:TIGR03814 160 NRALAYLLKSFGNLENDVEEV--LDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402065 472 FSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhnydnLRHFAKKLD 545
Cdd:TIGR03814 238 ASGEFAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKA---------------LELLSEKLG 296
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
229-521 |
1.42e-115 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 348.68 E-value: 1.42e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 229 MSFTSHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTE 307
Cdd:PRK00971 2 MLMQAILEEILEEVRPLIGqGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 308 YVHRYVGKEPSGLRFNKLFLNEDD--KPHNPMVNAGAIVVTSLIkQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSE 385
Cdd:PRK00971 82 EVWQRVGKEPSGDPFNSLVQLELEqgKPRNPMINAGAIVVTDLL-QGRLSEEPCERLLEFVRQLAGNPDILYDEVVASSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 386 RESGDRNFAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMH 465
Cdd:PRK00971 161 LEHADRNAAIAYLMKSFGNIENDVETV--LDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALML 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939402065 466 SCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHF 521
Cdd:PRK00971 239 TCGMYDASGEFAYRVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAA 294
|
|
| PRK12356 |
PRK12356 |
glutaminase; Reviewed |
235-518 |
1.03e-92 |
|
glutaminase; Reviewed
Pssm-ID: 237073 Cd Length: 319 Bit Score: 289.94 E-value: 1.03e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 235 IDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVG 314
Cdd:PRK12356 14 VDQAYAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESISKVFTLALALEDVGPQAVREKIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 315 KEPSGLRFNKL--FLNEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAGNEyVGFSNATFQSERESGDRN 392
Cdd:PRK12356 94 ADPTGLPFNSViaIELHGGKPLNPLVNAGAIATTSLVP-GANSDERWQRILDGQQRFAGRE-LALSDEVYQSEQTTNFHN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 393 FAIGYYLKEKKCFPEGTDMVgiLDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDF 472
Cdd:PRK12356 172 RAIAWLLYSYGRLYCDPMEA--CDVYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYER 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1939402065 473 SGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKG 518
Cdd:PRK12356 250 SGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGNSVRG 295
|
|
| PRK12357 |
PRK12357 |
glutaminase; Reviewed |
233-545 |
1.32e-71 |
|
glutaminase; Reviewed
Pssm-ID: 237074 Cd Length: 326 Bit Score: 235.00 E-value: 1.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 233 SHIDELYESAKKQSG-GKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHR 311
Cdd:PRK12357 15 VCLDQWVAHYRTYAAeGRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFTLQSISKVISFIAACLSRGISYVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 312 YVGKEPSGLRFN---KLFLNEDDKPHNPMVNAGAIVVTSLIKqGVNNAEKFDYVMQFLNKMAG-----NEYVgfsnatFQ 383
Cdd:PRK12357 95 RVDVEPTGDAFNsiiRLEIHKPGKPFNPMINAGAITVASLLP-GTSVQEKLESLYVLIEKMIGkrpaiNEEV------FQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 384 SERESGDRNFAIGYYLKEKKcFPEGtDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSL 463
Cdd:PRK12357 168 SEWETAHRNRALAYYLKETG-FLES-DVEETLEVYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 464 MHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVP----------NVMGMMCWSPPLDKMGNSVKGIHFchdlvslcnfhn 533
Cdd:PRK12357 246 MLTCGMYNASGKFAAFVGLPAKSGVSGGIMTLVPpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGIML------------ 313
|
330
....*....|..
gi 1939402065 534 ydnLRHFAKKLD 545
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. |
143-226 |
7.55e-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: 7.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 143 LEDLLFYTIA-EGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQ-----TTSDGVMLDKDLFKKCVQSNIVLLT 216
Cdd:pfam17959 1 LEDLLFDLFRdEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQensepTDSETLLLDRETFKKCIGSNIVLIS 80
|
90
....*....|
gi 1939402065 217 QAFRRKFVIP 226
Cdd:pfam17959 81 KALKNQFVIP 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
561-653 |
6.75e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.45 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRwnnTPMDEALHFGHHDVF 640
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
|
90
....*....|...
gi 1939402065 641 KILQEYQVQYTPQ 653
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
561-646 |
2.37e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 71.14 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 640
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIV 202
|
....*.
gi 1939402065 641 KILQEY 646
Cdd:COG0666 203 KLLLEA 208
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
561-643 |
8.17e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 69.60 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 640
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIV 169
|
...
gi 1939402065 641 KIL 643
Cdd:COG0666 170 KLL 172
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
561-647 |
1.01e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 66.13 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 640
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV 235
|
....*..
gi 1939402065 641 KILQEYQ 647
Cdd:COG0666 236 KLLLEAG 242
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
560-657 |
9.18e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.81 E-value: 9.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 560 NLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLE-ACKVNpfPKDRWNNTPMDEALHFGHHD 638
Cdd:PLN03192 528 NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhACNVH--IRDANGNTALWNAISAKHHK 605
|
90
....*....|....*....
gi 1939402065 639 VFKILQEYQVQYTPQGDSD 657
Cdd:PLN03192 606 IFRILYHFASISDPHAAGD 624
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
591-643 |
1.08e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 1.08e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1939402065 591 RTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKIL 643
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
565-661 |
2.05e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.68 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 565 AYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVFKILQ 644
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
90 100
....*....|....*....|..
gi 1939402065 645 EYQVQYTPQG-----DSDDGKE 661
Cdd:PTZ00322 169 RHSQCHFELGanakpDSFTGKP 190
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
561-643 |
7.04e-09 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 57.66 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEALHFGHHDVF 640
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIV 136
|
...
gi 1939402065 641 KIL 643
Cdd:COG0666 137 KLL 139
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
561-610 |
5.15e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 5.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1939402065 561 LLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 610
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
537-610 |
2.75e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.10 E-value: 2.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939402065 537 LRHFAKKLDPRrEGGDQrvksvinLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLL 610
Cdd:PLN03192 610 LYHFASISDPH-AAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
552-612 |
1.14e-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: 1.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939402065 552 DQRVKSVINLLFAAYTGDVSALRRFALSA-MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEA 612
Cdd:cd22192 12 QQKRISESPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEA 73
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
581-631 |
1.21e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1939402065 581 MDMEQRDYDSRTALHVAAAEGHVEVVKFLLEAcKVNPFPKDRWNNTPMDEA 631
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
589-612 |
5.30e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 5.30e-04
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
591-622 |
1.82e-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: 1.82e-03
10 20 30
....*....|....*....|....*....|...
gi 1939402065 591 RTALHVAAAE-GHVEVVKFLLEAcKVNPFPKDR 622
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSK-GADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
591-611 |
4.99e-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: 4.99e-03
|
| |
