|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
497-783 |
2.96e-154 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 454.91 E-value: 2.96e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 497 GNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGREPSGVRFNELT- 575
Cdd:pfam04960 1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 576 LNHEH-KPHNPMINSGAIMTCSLIQPEmDMADRFTYVVEKWTAMAGGgRIGFSNATYLSERQTADRNFALAYFMRENHGF 654
Cdd:pfam04960 81 LELENgKPRNPMINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGR-ELTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 655 PVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYDFSGEFAFKIGIP 734
Cdd:pfam04960 159 ENDVE----EVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 754347469 735 AKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFH 783
Cdd:pfam04960 235 AKSGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
486-785 |
2.30e-131 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 396.34 E-value: 2.30e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 486 DIFETTKRFT-SGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGR 564
Cdd:COG2066 3 EIYEKVRPYLgEGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 565 EPSGVRFNELT-LNHEH-KPHNPMINSGAIMTCSLIQPEmDMADRFTYVVEKWTAMAGGGRIGFSNATYLSERQTADRNF 642
Cdd:COG2066 83 EPSGDPFNSIVqLELENgIPRNPMINAGAIVVTSLLPGR-SGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 643 ALAYFMRENHGFPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYD 722
Cdd:COG2066 162 ALAYLLKSFGNLENDVE----EVLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754347469 723 FSGEFAFKIGIPAKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFHNF 785
Cdd:COG2066 238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLSIF 300
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
489-785 |
8.06e-110 |
|
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: 340.23 E-value: 8.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 489 ETTKRFTSGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGREPSG 568
Cdd:TIGR03814 7 EARPLIGEGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERVGVEPSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 569 VRFNELT-LNHEH-KPHNPMINSGAIMTCSLIqPEMDMADRFTYVVEKWTAMAGGGRIGFSNATYLSERQTADRNFALAY 646
Cdd:TIGR03814 87 DPFNSIVqLELEPgKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 647 FMRENHGFPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYDFSGE 726
Cdd:TIGR03814 166 LLKSFGNLENDVE----EVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 754347469 727 FAFKIGIPAKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFHNF 785
Cdd:TIGR03814 242 FAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKALELLSEKLGLSIF 300
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
492-785 |
2.80e-107 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 333.66 E-value: 2.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 492 KRFTSGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGREPSGVRF 571
Cdd:PRK00971 17 PLIGQGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRVGKEPSGDPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 572 NELT-LNHEH-KPHNPMINSGAIMTCSLIQPEmDMADRFTYVVEKWTAMAGGGRIGFSNATYLSERQTADRNFALAYFMR 649
Cdd:PRK00971 97 NSLVqLELEQgKPRNPMINAGAIVVTDLLQGR-LSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 650 ENHGFPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYDFSGEFAF 729
Cdd:PRK00971 176 SFGNIENDVE----TVLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAY 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 754347469 730 KIGIPAKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFHNF 785
Cdd:PRK00971 252 RVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLSIF 307
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
802-898 |
2.72e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.41 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 802 NHQRHRQMIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDA 881
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
|
90
....*....|....*..
gi 754347469 882 KREQRVDVVELLFDNGA 898
Cdd:COG0666 194 AENGHLEIVKLLLEAGA 210
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
812-898 |
3.18e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHgAHINPMDRwGNTPLDDAKREQRVDVVE 891
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*..
gi 754347469 892 LLFDNGA 898
Cdd:pfam12796 79 LLLEKGA 85
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
806-893 |
4.47e-16 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 82.64 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 806 HRQMIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQ 885
Cdd:PTZ00322 80 HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
....*...
gi 754347469 886 RVDVVELL 893
Cdd:PTZ00322 160 FREVVQLL 167
|
|
| EF-hand_14 |
pfam17959 |
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme. |
402-475 |
7.87e-08 |
|
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: 50.70 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 402 FKSFREPKLQKVSRSTFLAALASNGILEDDPRLQSVIASMRKFDD-----------LMDYEQFSQAIWPEHRFLCEILQG 470
Cdd:pfam17959 6 FDLFRDEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQenseptdsetlLLDRETFKKCIGSNIVLISKALKN 85
|
....*
gi 754347469 471 NLAIP 475
Cdd:pfam17959 86 QFVIP 90
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
840-868 |
4.61e-07 |
|
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: 46.81 E-value: 4.61e-07
10 20
....*....|....*....|....*....
gi 754347469 840 DGRTPLHLAASEGHTRVVKYLFQHGAHIN 868
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
839-878 |
2.04e-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: 45.00 E-value: 2.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 754347469 839 YDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPL 878
Cdd:cd22192 134 YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glutaminase |
pfam04960 |
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2. |
497-783 |
2.96e-154 |
|
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
Pssm-ID: 461499 Cd Length: 283 Bit Score: 454.91 E-value: 2.96e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 497 GNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGREPSGVRFNELT- 575
Cdd:pfam04960 1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 576 LNHEH-KPHNPMINSGAIMTCSLIQPEmDMADRFTYVVEKWTAMAGGgRIGFSNATYLSERQTADRNFALAYFMRENHGF 654
Cdd:pfam04960 81 LELENgKPRNPMINAGAIAVTSLIKGA-DPEERFERILDFLRKLAGR-ELTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 655 PVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYDFSGEFAFKIGIP 734
Cdd:pfam04960 159 ENDVE----EVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 754347469 735 AKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFH 783
Cdd:pfam04960 235 AKSGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
|
|
| GlsA |
COG2066 |
Glutaminase [Amino acid transport and metabolism]; |
486-785 |
2.30e-131 |
|
Glutaminase [Amino acid transport and metabolism];
Pssm-ID: 441669 Cd Length: 300 Bit Score: 396.34 E-value: 2.30e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 486 DIFETTKRFT-SGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGR 564
Cdd:COG2066 3 EIYEKVRPYLgEGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERVGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 565 EPSGVRFNELT-LNHEH-KPHNPMINSGAIMTCSLIQPEmDMADRFTYVVEKWTAMAGGGRIGFSNATYLSERQTADRNF 642
Cdd:COG2066 83 EPSGDPFNSIVqLELENgIPRNPMINAGAIVVTSLLPGR-SGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 643 ALAYFMRENHGFPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYD 722
Cdd:COG2066 162 ALAYLLKSFGNLENDVE----EVLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754347469 723 FSGEFAFKIGIPAKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFHNF 785
Cdd:COG2066 238 ASGEFAYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLSIF 300
|
|
| Gln_ase |
TIGR03814 |
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ... |
489-785 |
8.06e-110 |
|
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: 340.23 E-value: 8.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 489 ETTKRFTSGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGREPSG 568
Cdd:TIGR03814 7 EARPLIGEGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERVGVEPSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 569 VRFNELT-LNHEH-KPHNPMINSGAIMTCSLIqPEMDMADRFTYVVEKWTAMAGGGRIGFSNATYLSERQTADRNFALAY 646
Cdd:TIGR03814 87 DPFNSIVqLELEPgKPRNPFINAGAIAVTSLL-PGRTSDEKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRALAY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 647 FMRENHGFPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYDFSGE 726
Cdd:TIGR03814 166 LLKSFGNLENDVE----EVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGE 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 754347469 727 FAFKIGIPAKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFHNF 785
Cdd:TIGR03814 242 FAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKALELLSEKLGLSIF 300
|
|
| PRK00971 |
PRK00971 |
glutaminase; Provisional |
492-785 |
2.80e-107 |
|
glutaminase; Provisional
Pssm-ID: 234880 Cd Length: 307 Bit Score: 333.66 E-value: 2.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 492 KRFTSGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGREPSGVRF 571
Cdd:PRK00971 17 PLIGQGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRVGKEPSGDPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 572 NELT-LNHEH-KPHNPMINSGAIMTCSLIQPEmDMADRFTYVVEKWTAMAGGGRIGFSNATYLSERQTADRNFALAYFMR 649
Cdd:PRK00971 97 NSLVqLELEQgKPRNPMINAGAIVVTDLLQGR-LSEEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 650 ENHGFPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYDFSGEFAF 729
Cdd:PRK00971 176 SFGNIENDVE----TVLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAY 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 754347469 730 KIGIPAKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFHNF 785
Cdd:PRK00971 252 RVGLPAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLSIF 307
|
|
| PRK12356 |
PRK12356 |
glutaminase; Reviewed |
474-769 |
3.25e-77 |
|
glutaminase; Reviewed
Pssm-ID: 237073 Cd Length: 319 Bit Score: 254.51 E-value: 3.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 474 IPDFEYFRQEICDIFETTKRFTSGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEER 553
Cdd:PRK12356 4 LPDAEQLQQAVDQAYAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESISKVFTLALALEDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 554 GHDKVHQHVGREPSGVRFNELT--LNHEHKPHNPMINSGAIMTCSLIQPEmDMADRFTYVVEKWTAMAGGgRIGFSNATY 631
Cdd:PRK12356 84 GPQAVREKIGADPTGLPFNSVIaiELHGGKPLNPLVNAGAIATTSLVPGA-NSDERWQRILDGQQRFAGR-ELALSDEVY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 632 LSERQTADRNFALAYFMrENHG-FPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRA 710
Cdd:PRK12356 162 QSEQTTNFHNRAIAWLL-YSYGrLYCDPM----EACDVYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPY 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 754347469 711 VLSMMYSCGTYDFSGEFAFKIGIPAKSGVAGALMVVVPNIMGLCIWSPRLDKLGNSVRG 769
Cdd:PRK12356 237 ILAEMTMEGLYERSGDWAYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGNSVRG 295
|
|
| PRK12357 |
PRK12357 |
glutaminase; Reviewed |
496-785 |
4.73e-64 |
|
glutaminase; Reviewed
Pssm-ID: 237074 Cd Length: 326 Bit Score: 218.82 E-value: 4.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 496 SGNVASYIPQLARVNPEQYAAAICTIDGQRFAVGDTKAEFCVQSCSKPISYALALEERGHDKVHQHVGREPSGVRFN--- 572
Cdd:PRK12357 30 EGRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFTLQSISKVISFIAACLSRGISYVLERVDVEPTGDAFNsii 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 573 ELTLNHEHKPHNPMINSGAIMTCSLIqPEMDMADRFTY---VVEKWTamagGGRIGFSNATYLSERQTADRNFALAYFMR 649
Cdd:PRK12357 110 RLEIHKPGKPFNPMINAGAITVASLL-PGTSVQEKLESlyvLIEKMI----GKRPAINEEVFQSEWETAHRNRALAYYLK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 650 ENHGFPVEVEknltEILEFYFQCCSLECNVQTLSVIAGTLANGGICPITNEQVLRPETVRAVLSMMYSCGTYDFSGEFAF 729
Cdd:PRK12357 185 ETGFLESDVE----ETLEVYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAA 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754347469 730 KIGIPAKSGVAGALMVVVP----------NIMGLCIWSPRLDKLGNSVRGIEFCKELCNRFNFHNF 785
Cdd:PRK12357 261 FVGLPAKSGVSGGIMTLVPpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGIMLLKHIAKEWDLSIF 326
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
802-898 |
2.72e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.41 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 802 NHQRHRQMIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDA 881
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
|
90
....*....|....*..
gi 754347469 882 KREQRVDVVELLFDNGA 898
Cdd:COG0666 194 AENGHLEIVKLLLEAGA 210
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
786-898 |
3.71e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.02 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 786 DESVHARGKIDPRLPKNHQRHRQMIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGA 865
Cdd:COG0666 65 GDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
|
90 100 110
....*....|....*....|....*....|...
gi 754347469 866 HINPMDRWGNTPLDDAKREQRVDVVELLFDNGA 898
Cdd:COG0666 145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
812-898 |
3.18e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHgAHINPMDRwGNTPLDDAKREQRVDVVE 891
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*..
gi 754347469 892 LLFDNGA 898
Cdd:pfam12796 79 LLLEKGA 85
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
812-899 |
7.79e-18 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 85.01 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVE 891
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
|
....*...
gi 754347469 892 LLFDNGAL 899
Cdd:COG0666 237 LLLEAGAD 244
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
806-893 |
4.47e-16 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 82.64 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 806 HRQMIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQ 885
Cdd:PTZ00322 80 HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
....*...
gi 754347469 886 RVDVVELL 893
Cdd:PTZ00322 160 FREVVQLL 167
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
814-898 |
1.64e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 72.29 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 814 FAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELL 893
Cdd:COG0666 60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
|
....*
gi 754347469 894 FDNGA 898
Cdd:COG0666 140 LEAGA 144
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
812-871 |
6.19e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.74 E-value: 6.19e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGlnECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMD 871
Cdd:pfam12796 34 LHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
841-893 |
1.44e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 1.44e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 754347469 841 GRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELL 893
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
812-860 |
3.02e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.51 E-value: 3.02e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYL 860
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
812-909 |
8.33e-10 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 61.12 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVE 891
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
|
90
....*....|....*...
gi 754347469 892 LLFDNGALTGAELMERHA 909
Cdd:COG0666 270 LLLLALLLLAAALLDLLT 287
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
748-902 |
4.74e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 56.43 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 748 PNIMGL--CIWSPRLDKLGNSVRGIefcKELCNRFNFHNFDESVHARGKidprlpknHQRHRQMIELCFAASQGDLSA-- 823
Cdd:PHA02878 81 PNKLGMkeMIRSINKCSVFYTLVAI---KDAFNNRNVEIFKIILTNRYK--------NIQTIDLVYIDKKSKDDIIEAei 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 824 IRRALQKGGGLNECDYD-GRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELLFDNGALTGA 902
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
|
|
| EF-hand_14 |
pfam17959 |
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme. |
402-475 |
7.87e-08 |
|
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: 50.70 E-value: 7.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 402 FKSFREPKLQKVSRSTFLAALASNGILEDDPRLQSVIASMRKFDD-----------LMDYEQFSQAIWPEHRFLCEILQG 470
Cdd:pfam17959 6 FDLFRDEETDKLSVAKFLKALAATGIRKDDPRLAELMKNLKKADQenseptdsetlLLDRETFKKCIGSNIVLISKALKN 85
|
....*
gi 754347469 471 NLAIP 475
Cdd:pfam17959 86 QFVIP 90
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
840-872 |
2.25e-07 |
|
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: 47.67 E-value: 2.25e-07
10 20 30
....*....|....*....|....*....|....
gi 754347469 840 DGRTPLHLAA-SEGHTRVVKYLFQHGAHINPMDR 872
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
845-899 |
2.40e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 49.34 E-value: 2.40e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 754347469 845 LHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELLFDNGAL 899
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV 55
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
824-899 |
2.78e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.20 E-value: 2.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754347469 824 IRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRvDVVELLFDNGAL 899
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASI 247
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
812-897 |
3.43e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.81 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVE 891
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
....*.
gi 754347469 892 LLFDNG 897
Cdd:PHA02874 208 LLIDHG 213
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
840-868 |
4.61e-07 |
|
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: 46.81 E-value: 4.61e-07
10 20
....*....|....*....|....*....
gi 754347469 840 DGRTPLHLAASEGHTRVVKYLFQHGAHIN 868
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
812-884 |
5.68e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 53.72 E-value: 5.68e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGA---HINPMDRWGNTPLDD--AKRE 884
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAdvdKANTDDDFSPTELREllQKRE 703
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
805-903 |
8.66e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.57 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 805 RHRQMIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDA-KR 883
Cdd:PHA02878 165 RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGY 244
|
90 100
....*....|....*....|
gi 754347469 884 EQRVDVVELLFDNGALTGAE 903
Cdd:PHA02878 245 CKDYDILKLLLEHGVDVNAK 264
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
840-868 |
9.82e-07 |
|
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: 45.71 E-value: 9.82e-07
10 20
....*....|....*....|....*....
gi 754347469 840 DGRTPLHLAASEGHTRVVKYLFQHGAHIN 868
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
838-879 |
1.38e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 754347469 838 DYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLD 879
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
828-898 |
2.57e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.18 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754347469 828 LQKGGGLNECDYDGRTPLH--LAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDV--VELLFDNGA 898
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGA 178
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
815-881 |
1.05e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.48 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754347469 815 AASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDA 881
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
778-896 |
2.03e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.52 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 778 NRFNFHNFDESVHARGKIDPRLPKNHQRHRQMIelcfaasqgdlsairraLQKGGGLNECDYDGRTPLHLAASEGHTRVV 857
Cdd:PHA02876 132 NDIHYDKINESIEYMKLIKERIQQDELLIAEML-----------------LEGGADVNAKDIYCITPIHYAAERGNAKMV 194
|
90 100 110
....*....|....*....|....*....|....*....
gi 754347469 858 KYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELLFDN 896
Cdd:PHA02876 195 NLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
824-898 |
2.85e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 47.65 E-value: 2.85e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754347469 824 IRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELLFDNGA 898
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
828-898 |
3.17e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 47.35 E-value: 3.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754347469 828 LQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELLFDNGA 898
Cdd:PHA03100 179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
812-898 |
3.83e-05 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 46.49 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVE 891
Cdd:COG0666 25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
|
....*..
gi 754347469 892 LLFDNGA 898
Cdd:COG0666 105 LLLEAGA 111
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
824-898 |
4.43e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.97 E-value: 4.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754347469 824 IRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLD--DAKREQRVDVVELLFDNGA 898
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLLVQYGA 131
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
816-898 |
5.95e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.56 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 816 ASQGDLSAIRRALQKGGGLNECDYDGRTPLHL---AASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQ-RVDVVE 891
Cdd:PHA03095 22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIK 101
|
....*..
gi 754347469 892 LLFDNGA 898
Cdd:PHA03095 102 LLIKAGA 108
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
819-898 |
7.61e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.20 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 819 GDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRV------------------VKYLFQHGAHINPMDRWGNTPLDD 880
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHY 198
|
90
....*....|....*...
gi 754347469 881 AKREQRVDVVELLFDNGA 898
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGA 216
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
802-897 |
9.80e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.75 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 802 NHQrhrqmIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDA 881
Cdd:PHA02875 1 MDQ-----VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDA 75
|
90
....*....|....*.
gi 754347469 882 KREQRVDVVELLFDNG 897
Cdd:PHA02875 76 VEEGDVKAVEELLDLG 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
778-881 |
1.73e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 45.02 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 778 NRFN--FHNFDESVHARGKI---------DPRLPKNHqrHRQMIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLH 846
Cdd:PHA03095 185 DRFRslLHHHLQSFKPRARIvreliragcDPAATDML--GNTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLH 262
|
90 100 110
....*....|....*....|....*....|....*
gi 754347469 847 LAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDA 881
Cdd:PHA03095 263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
839-878 |
2.04e-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: 45.00 E-value: 2.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 754347469 839 YDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPL 878
Cdd:cd22192 134 YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
819-900 |
2.21e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.57 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 819 GDLSAIRRALQ-KGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELLFDNG 897
Cdd:PHA02874 12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
...
gi 754347469 898 ALT 900
Cdd:PHA02874 92 VDT 94
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
816-898 |
2.62e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 44.63 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 816 ASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHT-RVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVD--VVEL 892
Cdd:PHA03095 58 SSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRL 137
|
....*.
gi 754347469 893 LFDNGA 898
Cdd:PHA03095 138 LLRKGA 143
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
824-898 |
3.60e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 44.28 E-value: 3.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754347469 824 IRRALQKGGGLNECDYDGRTPLHLAASEGH-TRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRV-DVVELLFDNGA 898
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGA 366
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
809-898 |
3.98e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 43.83 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 809 MIELCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVD 888
Cdd:PHA02875 103 MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182
|
90
....*....|
gi 754347469 889 VVELLFDNGA 898
Cdd:PHA02875 183 ICKMLLDSGA 192
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
836-902 |
4.53e-04 |
|
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: 43.98 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 836 ECDYDGRTPLHLAASEGHTRVVKYLFQHGAHI---------NPMDR-----WGNTPLDDAKREQRVDVVELLFDNGALTG 901
Cdd:cd22194 136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVnahakgvffNPKYKhegfyFGETPLALAACTNQPEIVQLLMEKESTDI 215
|
.
gi 754347469 902 A 902
Cdd:cd22194 216 T 216
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
828-898 |
8.43e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 42.73 E-value: 8.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754347469 828 LQKGGGLNECDYDGRTPLHLAASEGHT-----RVVKYLFQHGAHINPMDRWGNTPLDDA--KREQRVDVVELLFDNGA 898
Cdd:PHA03100 55 LDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGA 132
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
812-898 |
1.37e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.29 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 812 LCFAASQGDLSAIRRALQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHINPMDRWGN-TPLDDAKREQRVDVV 890
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIV 218
|
....*...
gi 754347469 891 ELLFDNGA 898
Cdd:PHA02875 219 RLFIKRGA 226
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
811-903 |
3.31e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 40.74 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 811 ELCFAASQGDLSAIRRALQKGGGLNECDY-DGRTPLHLAASEGHTRVVKYLFQHGA--HINPMDRWgnTPLDDAKREQRV 887
Cdd:PHA02875 71 ELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDI 148
|
90
....*....|....*.
gi 754347469 888 DVVELLFDNGALTGAE 903
Cdd:PHA02875 149 KGIELLIDHKACLDIE 164
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
820-898 |
6.02e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.43 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 820 DLSAIRRALQKGGGLNECDYDGRTPLHLAAS-EGHTRVVKYLFQHGAHINPMDRWGNTPLDDAKREQRVDVVELLFDNGA 898
Cdd:PHA02876 320 DTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
828-898 |
7.51e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.05 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347469 828 LQKGGGLNECDYDGRTPLHLAASEGHTRVVKYLFQHGAHI------------------NP-------MDRWGN------- 875
Cdd:PHA02876 362 LELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIealsqkigtalhfalcgtNPymsvktlIDRGANvnsknkd 441
|
90 100
....*....|....*....|....*.
gi 754347469 876 --TPLDDA-KREQRVDVVELLFDNGA 898
Cdd:PHA02876 442 lsTPLHYAcKKNCKLDVIEMLLDNGA 467
|
|
| |
