|
Name |
Accession |
Description |
Interval |
E-value |
| ansA |
PRK09461 |
cytoplasmic asparaginase I; Provisional |
56-414 |
3.15e-136 |
|
cytoplasmic asparaginase I; Provisional
Pssm-ID: 181876 [Multi-domain] Cd Length: 335 Bit Score: 401.66 E-value: 3.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 56 RVLVINTGGTIGMTLHDNVLAPKANAFVKQMRKLPvvhdelyaqqtrlyDYYGSEntlvLPLskdnkriiYTILEYKPLL 135
Cdd:PRK09461 5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP--------------EFHRPE----MPD--------FTIHEYTPLI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 136 DSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALLI 215
Cdd:PRK09461 59 DSSDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 216 AGQFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVwRANTTAKFQVSTELNRNVGLLRL 295
Cdd:PRK09461 139 AANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPP-APHGEGELIVHPITPQPIGVVTI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 296 FPGITAATVRAFLQPPMEGVVLETYGSGNAPDNRlDLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVLIDAGLIA 374
Cdd:PRK09461 218 YPGISAEVVRNFLRQPVKALILRSYGVGNAPQNP-ALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVIS 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1880388717 375 GGDMTPEAALSKLSYVLAkKDLDLAAKKKMMAQNLRGEMS 414
Cdd:PRK09461 297 GADMTVEAALTKLHYLLS-QELSTEEIRQAMQQNLRGELT 335
|
|
| AnsA |
COG0252 |
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ... |
56-407 |
8.19e-116 |
|
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];
Pssm-ID: 440022 [Multi-domain] Cd Length: 325 Bit Score: 349.05 E-value: 8.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 56 RVLVINTGGTIGMTLHDNVLAPKANAFVkqmrklpvvhDELYAQqtrlydyygsentlVLPLSKDNKriiYTILEYkPLL 135
Cdd:COG0252 5 KILVLATGGTIAMRADPAGYAVAPALSA----------EELLAA--------------VPELAELAD---IEVEQF-ANI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 136 DSSNMTTDDWGRIGKDIEKNY-ENYDGFVILHGTDTMAYTASALSFMCEhLGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:COG0252 57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 215 IA--GQFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDiTINWDTVWRANTTAKFQVSTELNRNVGL 292
Cdd:COG0252 136 VAasPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 293 LRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCLRGTVSASYATGKVLIDAGL 372
Cdd:COG0252 215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291
|
330 340 350
....*....|....*....|....*....|....*
gi 1880388717 373 IAGGDMTPEAALSKLSYVLAKKdLDLAAKKKMMAQ 407
Cdd:COG0252 292 ISGGDLTPEKARIKLMLALGQG-LDPEEIRRLFET 325
|
|
| L-asparaginase_I |
cd08963 |
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ... |
56-393 |
8.42e-114 |
|
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.
Pssm-ID: 199207 [Multi-domain] Cd Length: 316 Bit Score: 343.41 E-value: 8.42e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 56 RVLVINTGGTIGMTLHDNVLAPKANAfVKQMRKLPVVHDelyaqqtrlydyygsentlvlplskdnkrIIYTILEYKPLL 135
Cdd:cd08963 2 KILLLYTGGTIASVKTEGGLAPALTA-EELLSYLPELLE-----------------------------DCFIEVEQLPNI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 136 DSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALLI 215
Cdd:cd08963 52 DSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 216 AGQFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQvsTELNRNVGLLRL 295
Cdd:cd08963 132 ASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLFY--PDLDPNVFLLKL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 296 FPGITAATVRAFLQPPMEGVVLETYGSGNAPDNRlDLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVLIDAGLIA 374
Cdd:cd08963 210 IPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALLEAGVIP 288
|
330
....*....|....*....
gi 1880388717 375 GGDMTPEAALSKLSYVLAK 393
Cdd:cd08963 289 GGDMTTEAAVAKLMWLLGQ 307
|
|
| Asparaginase |
smart00870 |
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ... |
57-395 |
1.01e-113 |
|
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.
Pssm-ID: 214873 [Multi-domain] Cd Length: 323 Bit Score: 343.73 E-value: 1.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 57 VLVINTGGTIGMTLHDNVLAPKANAFVKQMRKlpvvhdelyaqqtrlydyygsentLVLPLSKDNKRIIYtilEYKPLLD 136
Cdd:smart00870 1 ILVLYTGGTIAMKADPSTGAVGPTAGAEELLA------------------------LLPALPELADDIEV---EQVANID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 137 SSNMTTDDWGRIGKDIEK--NYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:smart00870 54 SSNMTPEDWLKLAKRINEalADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 215 IAG--QFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQV---STELNRN 289
Cdd:smart00870 134 VAAspEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPFLldlKDALLPK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 290 VGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVLI 368
Cdd:smart00870 214 VAIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVDPGyYATGRDLA 290
|
330 340
....*....|....*....|....*..
gi 1880388717 369 DAGLIAGGDMTPEAALSKLSYVLAKKD 395
Cdd:smart00870 291 KAGVISAGDLTPEKARIKLMLALGKGL 317
|
|
| asnASE_I |
TIGR00519 |
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ... |
57-413 |
5.50e-96 |
|
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.
Pssm-ID: 129610 [Multi-domain] Cd Length: 336 Bit Score: 298.27 E-value: 5.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 57 VLVINTGGTIGMtlhdnVLAPKANAFVkqmrklPVVH-DELYAQQTRLYDyygsentlvlplskdnkriIYTI-LEYKPL 134
Cdd:TIGR00519 4 ISIISTGGTIAS-----KVDYRTGAVH------PVFTaDELLSAVPELLD-------------------IANIdGEALMN 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 135 LDSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHlGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:TIGR00519 54 ILSENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 215 IAGQFV------IPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQVSTELNR 288
Cdd:TIGR00519 133 AATEYIaevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 289 NVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDNrldLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVL 367
Cdd:TIGR00519 213 KVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQN---KLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRRL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1880388717 368 IDAGLIAGGDMTPEAALSKLSYVLAKKDlDLAAKKKMMAQNLRGEM 413
Cdd:TIGR00519 290 LQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEI 334
|
|
| Asparaginase |
pfam00710 |
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme. |
57-269 |
2.21e-73 |
|
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
Pssm-ID: 459913 [Multi-domain] Cd Length: 188 Bit Score: 233.97 E-value: 2.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 57 VLVINTGGTIGMTLHDN--VLAPKANAfvkqmrklpvvhDELYAQqtrlydyygsentlvLPLSKDNKRIIYtilEYKPL 134
Cdd:pfam00710 1 VLILATGGTIASRADSSggAVVPALTG------------EELLAA---------------VPELADIAEIEA---EQVAN 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 135 LDSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:pfam00710 51 IDSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALR 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880388717 215 IAGQF--VIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLAT-AEVDITINWD 269
Cdd:pfam00710 131 VAASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEvDGGQVELYRE 188
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
366-607 |
2.81e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 106.19 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 366 VLIDAGLIAGGDMTPEAALSKLSYVLAKKDLDLAAKKKMMAQNLRGEMSADLAGAKLCLSDSRFIQVIAKSLSISCKEEL 445
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 446 EAIRDALTPPLAcAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSN 525
Cdd:COG0666 81 NAKDDGGNTLLH-AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 526 AVRFRHKEVVKLLRKTGAHF-SRDKLEEagTELCSLAASGDLEGLEIwsL--AGADLNETGYDGQTAIQVAQACGQKKVV 602
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVnARDNDGE--TPLHLAAENGHLEIVKL--LleAGADVNAKDNDGKTALDLAAENGNLEIV 235
|
....*
gi 1880388717 603 AFLVQ 607
Cdd:COG0666 236 KLLLE 240
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
459-606 |
4.78e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 88.39 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 459 AAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLL 538
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880388717 539 RktgaHFSR-DKLEEAGTELCSLAASGDLEGLEIWSLAGADLNETGYDGQTAIQVAQACGQKKVVAFLV 606
Cdd:PLN03192 611 Y----HFASiSDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
460-547 |
7.82e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 460 AAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATvyAKDRYGDTPLSNAVRFRHKEVVKLLR 539
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLL 81
|
....*...
gi 1880388717 540 KTGAHFSR 547
Cdd:pfam12796 82 EKGADINV 89
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
469-543 |
9.67e-07 |
|
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: 51.94 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 469 LEAIREMGGNLFLGD-YDGRTPLHIATCEGHFELVEYLLNHGATVyAKDR---------------YGDTPLSNAVRFRHK 532
Cdd:cd22192 71 MEAAPELVNEPMTSDlYQGETALHIAVVNQNLNLVRELIARGADV-VSPRatgtffrpgpknliyYGEHPLSFAACVGNE 149
|
90
....*....|.
gi 1880388717 533 EVVKLLRKTGA 543
Cdd:cd22192 150 EIVRLLIEHGA 160
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
485-514 |
1.24e-06 |
|
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: 44.89 E-value: 1.24e-06
10 20 30
....*....|....*....|....*....|
gi 1880388717 485 DGRTPLHIATCEGHFELVEYLLNHGATVYA 514
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
442-546 |
3.75e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.45 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 442 KEELEAIRDALTPPLAcAAAKIGDKEalEAIREMGGNLflgdYDGRTPLHIATCEGHFELVEYLLNHGATVYAKD----- 516
Cdd:TIGR00870 91 LEYVDAVEAILLHLLA-AFRKSGPLE--LANDQYTSEF----TPGITALHLAAHRQNYEIVKLLLERGASVPARAcgdff 163
|
90 100 110
....*....|....*....|....*....|....*....
gi 1880388717 517 ---------RYGDTPLSNAVRFRHKEVVKLLRKTGAHFS 546
Cdd:TIGR00870 164 vksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ansA |
PRK09461 |
cytoplasmic asparaginase I; Provisional |
56-414 |
3.15e-136 |
|
cytoplasmic asparaginase I; Provisional
Pssm-ID: 181876 [Multi-domain] Cd Length: 335 Bit Score: 401.66 E-value: 3.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 56 RVLVINTGGTIGMTLHDNVLAPKANAFVKQMRKLPvvhdelyaqqtrlyDYYGSEntlvLPLskdnkriiYTILEYKPLL 135
Cdd:PRK09461 5 SIYVAYTGGTIGMQRSDQGYIPVSGHLQRQLALMP--------------EFHRPE----MPD--------FTIHEYTPLI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 136 DSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALLI 215
Cdd:PRK09461 59 DSSDMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 216 AGQFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVwRANTTAKFQVSTELNRNVGLLRL 295
Cdd:PRK09461 139 AANYPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPP-APHGEGELIVHPITPQPIGVVTI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 296 FPGITAATVRAFLQPPMEGVVLETYGSGNAPDNRlDLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVLIDAGLIA 374
Cdd:PRK09461 218 YPGISAEVVRNFLRQPVKALILRSYGVGNAPQNP-ALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVIS 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1880388717 375 GGDMTPEAALSKLSYVLAkKDLDLAAKKKMMAQNLRGEMS 414
Cdd:PRK09461 297 GADMTVEAALTKLHYLLS-QELSTEEIRQAMQQNLRGELT 335
|
|
| AnsA |
COG0252 |
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ... |
56-407 |
8.19e-116 |
|
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];
Pssm-ID: 440022 [Multi-domain] Cd Length: 325 Bit Score: 349.05 E-value: 8.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 56 RVLVINTGGTIGMTLHDNVLAPKANAFVkqmrklpvvhDELYAQqtrlydyygsentlVLPLSKDNKriiYTILEYkPLL 135
Cdd:COG0252 5 KILVLATGGTIAMRADPAGYAVAPALSA----------EELLAA--------------VPELAELAD---IEVEQF-ANI 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 136 DSSNMTTDDWGRIGKDIEKNY-ENYDGFVILHGTDTMAYTASALSFMCEhLGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:COG0252 57 DSSNMTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 215 IA--GQFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDiTINWDTVWRANTTAKFQVSTELNRNVGL 292
Cdd:COG0252 136 VAasPEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEG-RVRFYRRPPRRPESELDLAPALLPRVAI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 293 LRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCLRGTVSASYATGKVLIDAGL 372
Cdd:COG0252 215 LKLYPGMDPALLDALLAAGVKGIVLEGTGAGNVPP---ALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGV 291
|
330 340 350
....*....|....*....|....*....|....*
gi 1880388717 373 IAGGDMTPEAALSKLSYVLAKKdLDLAAKKKMMAQ 407
Cdd:COG0252 292 ISGGDLTPEKARIKLMLALGQG-LDPEEIRRLFET 325
|
|
| L-asparaginase_I |
cd08963 |
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ... |
56-393 |
8.42e-114 |
|
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type I L-asparaginases, which are highly specific for asparagine and localized in the cytosol. Type I L-asparaginase acts as a dimer. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. One example of an enzyme with no L-glutaminase activity is the type I L-asparaginase from Wolinella succinogenes.
Pssm-ID: 199207 [Multi-domain] Cd Length: 316 Bit Score: 343.41 E-value: 8.42e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 56 RVLVINTGGTIGMTLHDNVLAPKANAfVKQMRKLPVVHDelyaqqtrlydyygsentlvlplskdnkrIIYTILEYKPLL 135
Cdd:cd08963 2 KILLLYTGGTIASVKTEGGLAPALTA-EELLSYLPELLE-----------------------------DCFIEVEQLPNI 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 136 DSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALLI 215
Cdd:cd08963 52 DSSNMTPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 216 AGQFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQvsTELNRNVGLLRL 295
Cdd:cd08963 132 ASSGSIRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLFY--PDLDPNVFLLKL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 296 FPGITAATVRAFLQPPMEGVVLETYGSGNAPDNRlDLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVLIDAGLIA 374
Cdd:cd08963 210 IPGLLPAILDALLEKYPRGLILEGFGAGNIPYDG-DLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALLEAGVIP 288
|
330
....*....|....*....
gi 1880388717 375 GGDMTPEAALSKLSYVLAK 393
Cdd:cd08963 289 GGDMTTEAAVAKLMWLLGQ 307
|
|
| Asparaginase |
smart00870 |
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ... |
57-395 |
1.01e-113 |
|
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.
Pssm-ID: 214873 [Multi-domain] Cd Length: 323 Bit Score: 343.73 E-value: 1.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 57 VLVINTGGTIGMTLHDNVLAPKANAFVKQMRKlpvvhdelyaqqtrlydyygsentLVLPLSKDNKRIIYtilEYKPLLD 136
Cdd:smart00870 1 ILVLYTGGTIAMKADPSTGAVGPTAGAEELLA------------------------LLPALPELADDIEV---EQVANID 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 137 SSNMTTDDWGRIGKDIEK--NYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:smart00870 54 SSNMTPEDWLKLAKRINEalADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 215 IAG--QFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQV---STELNRN 289
Cdd:smart00870 134 VAAspEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSPFLldlKDALLPK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 290 VGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVLI 368
Cdd:smart00870 214 VAIVKAYPGMDAELLDALLDSGAKGLVLEGTGAGNVPP---DLLEALKEALERGIPVVRTSRCLSGRVDPGyYATGRDLA 290
|
330 340
....*....|....*....|....*..
gi 1880388717 369 DAGLIAGGDMTPEAALSKLSYVLAKKD 395
Cdd:smart00870 291 KAGVISAGDLTPEKARIKLMLALGKGL 317
|
|
| asnASE_I |
TIGR00519 |
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ... |
57-413 |
5.50e-96 |
|
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity secreted enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type I of E. coli. Archaeal putative asparaginases are of this type but contain an extra ~ 80 residues in a conserved N-terminal region. These archaeal homologs are included in this model.
Pssm-ID: 129610 [Multi-domain] Cd Length: 336 Bit Score: 298.27 E-value: 5.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 57 VLVINTGGTIGMtlhdnVLAPKANAFVkqmrklPVVH-DELYAQQTRLYDyygsentlvlplskdnkriIYTI-LEYKPL 134
Cdd:TIGR00519 4 ISIISTGGTIAS-----KVDYRTGAVH------PVFTaDELLSAVPELLD-------------------IANIdGEALMN 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 135 LDSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHlGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:TIGR00519 54 ILSENMKPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 215 IAGQFV------IPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQVSTELNR 288
Cdd:TIGR00519 133 AATEYIaevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 289 NVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDNrldLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVL 367
Cdd:TIGR00519 213 KVALIKIYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQN---KLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRRL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1880388717 368 IDAGLIAGGDMTPEAALSKLSYVLAKKDlDLAAKKKMMAQNLRGEM 413
Cdd:TIGR00519 290 LQAGVIGGEDMLPEVALVKLMWLLGQYS-DPEEAKKMMSKNIAGEI 334
|
|
| Asparaginase |
pfam00710 |
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme. |
57-269 |
2.21e-73 |
|
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
Pssm-ID: 459913 [Multi-domain] Cd Length: 188 Bit Score: 233.97 E-value: 2.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 57 VLVINTGGTIGMTLHDN--VLAPKANAfvkqmrklpvvhDELYAQqtrlydyygsentlvLPLSKDNKRIIYtilEYKPL 134
Cdd:pfam00710 1 VLILATGGTIASRADSSggAVVPALTG------------EELLAA---------------VPELADIAEIEA---EQVAN 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 135 LDSSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:pfam00710 51 IDSSNMTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALR 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880388717 215 IAGQF--VIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLAT-AEVDITINWD 269
Cdd:pfam00710 131 VAASPaaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEvDGGQVELYRE 188
|
|
| gatD_arch |
TIGR02153 |
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ... |
123-414 |
5.18e-60 |
|
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It is part of a heterodimer, with GatE (TIGR00134), that acts as an amidotransferase on misacylated Glu-tRNA(Gln) to produce Gln-tRNA(Gln). The analogous amidotransferase found in bacteria is the GatABC system, although GatABC homologs in the Archaea appear to act instead on Asp-tRNA(Asn). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 274001 [Multi-domain] Cd Length: 404 Bit Score: 206.08 E-value: 5.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 123 RIIYTILeykplldSSNMTTDDWGRIGKDIEKNYEN-YDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQVPIYEM 201
Cdd:TIGR02153 110 RAVFNIL-------SENMKPEYWIKIAEAVAKALKEgADGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRSSDRP 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 202 RNDGRDNLLGALLIAGQfVIPEV--CLY-----FYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITIN-WDTVWR 273
Cdd:TIGR02153 183 SSDAALNLICAVRAATS-PIAEVtvVMHgetsdTYCLVHRGVKVRKMHTSRRDAFQSINDIPIAKIDPDEGIEkLRIDYR 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 274 ANTTAKFQVSTELNRNVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCL 353
Cdd:TIGR02153 262 RRGEKELELDDKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIEGTGLGHVSE---DWIPSIKRATDDGVPVVMTSQCL 338
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880388717 354 RGTVSAS-YATGKVLIDAGLIAGGDMTPEAALSKLSYVLAKKDlDLAAKKKMMAQNLRGEMS 414
Cdd:TIGR02153 339 YGRVNLNvYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAGEIN 399
|
|
| GatD |
cd08962 |
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ... |
126-409 |
2.99e-57 |
|
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative synthesis of Gln-tRNA(Gln) in archaea via the transamidation of incorrectly charged Glu-tRNA(Gln). GatD is active as a dimer, and it provides the amino group required for this reaction. GatD is related to bacterial L-asparaginases (amidohydrolases), which catalyze the hydrolysis of asparagine to aspartic acid and ammonia. This CD spans both the L-asparaginase_like domain and an N-terminal supplementary domain.
Pssm-ID: 199206 [Multi-domain] Cd Length: 402 Bit Score: 198.61 E-value: 2.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 126 YTILEYKPLLD--SSNMTTDDWGRIGKDIEKNYEN-YDGFVILHGTDTMAYTASALSFMCEHLGKPIILTGSQvpiyemR 202
Cdd:cd08962 112 IANIKAEVLFNilSENMTPEYWVKIAEAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQ------R 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 203 N------DGRDNLLGALLIAGQfVIPEV--CLY-----FYNKLYRGNRVTKVDAGSFNAFSSPNLAPLA---TAEVDITI 266
Cdd:cd08962 186 SsdrpssDAAMNLIAAVLVAAS-DIAEVvvVMHgttsdDYCLLHRGTRVRKMHTSRRDAFQSINDEPLAkvdPPGKIEKL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 267 NWDTVWRANTTAKFqvSTELNRNVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVII 346
Cdd:cd08962 265 SKDYRKRGDEELEL--NDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIEGTGLGHVSE---DLIPSIKKAIDDGIPV 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1880388717 347 INCTQCLRGTVSAS-YATGKVLIDAGLIAGGDMTPEAALSKLSYVLAKKDlDLAAKKKMMAQNL 409
Cdd:cd08962 340 VMTSQCIYGRVNLNvYSTGRELLKAGVIPGEDMLPETAYVKLMWVLGNTD-DLEEVRKLMLTNL 402
|
|
| PRK04183 |
PRK04183 |
Glu-tRNA(Gln) amidotransferase subunit GatD; |
123-414 |
1.85e-56 |
|
Glu-tRNA(Gln) amidotransferase subunit GatD;
Pssm-ID: 235245 [Multi-domain] Cd Length: 419 Bit Score: 196.99 E-value: 1.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 123 RIIYTILeykplldSSNMTTDDWGRIGKDIEKNYEN-YDGFVILHGTDTMAYTASALSFMCEhLGKPIILTGSQvpiyem 201
Cdd:PRK04183 123 RVLFNIL-------SENMTPEYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFMLK-TPVPIVFVGAQ------ 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 202 RNDGR---D---NLLGALLIA----GQFVI-------PEVCLyfynkLYRGNRVTKVDAGSFNAFSSPNLAPLA-----T 259
Cdd:PRK04183 189 RSSDRpssDaamNLICAVLAAtsdiAEVVVvmhgttsDDYCA-----LHRGTRVRKMHTSRRDAFQSINDKPLAkvdykE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 260 AEVDItINWDtvWRANTTAKFQVSTELNRNVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKA 339
Cdd:PRK04183 264 GKIEF-LRKD--YRKRGEKELELNDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIEGTGLGHVST---DLIPSIKRA 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880388717 340 TDSGVIIINCTQCLRGTVSAS-YATGKVLIDAGLIAGGDMTPEAALSKLSYVLAKKDlDLAAKKKMMAQNLRGEMS 414
Cdd:PRK04183 338 TDDGIPVVMTSQCLYGRVNMNvYSTGRDLLKAGVIPGEDMLPEVAYVKLMWVLGNTY-DLEEVRELMLTNLAGEIN 412
|
|
| L-asparaginase_like |
cd00411 |
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ... |
135-393 |
2.05e-42 |
|
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are dimeric or tetrameric enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases, one highly specific for asparagine and localized to the periplasm (type II L-asparaginase), and a second (asparaginase- glutaminase) present in the cytosol (type I L-asparaginase) that hydrolyzes both asparagine and glutamine with similar specificities and has a lower affinity for its substrate. Bacterial L-asparaginases (type II) are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL). A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase. This wider family also includes a subunit of an archaeal Glu-tRNA amidotransferase.
Pssm-ID: 199205 [Multi-domain] Cd Length: 320 Bit Score: 155.75 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 135 LDSSNMTTDDWGRIGKDIEKN-YENYDGFVILHGTDTMAYTASALSFMCEHlGKPIILTGSQVPIYEMRNDGRDNLLGAL 213
Cdd:cd00411 55 IASEDITPDDWLKLAKEVAKLlDSDVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 214 LIA--GQFVIPEVCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQVSTELNR--N 289
Cdd:cd00411 134 RVAkdKDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYYQRKPARKHTDESEFDVSDIKSlpK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 290 VGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCLRGTVSASyaTGKVLID 369
Cdd:cd00411 214 VDIVYLYPGLSDDIYDALVDLGYKGIVLAGTGNGSVPY---DVFPVLSSASKRGVAVVRSSQVIYGGVDLN--AEKVDLK 288
|
250 260
....*....|....*....|....
gi 1880388717 370 AGLIAGGDMTPEAALSKLSYVLAK 393
Cdd:cd00411 289 AGVIPAGDLNPEKARVLLMWALTH 312
|
|
| L-asparaginase_II |
cd08964 |
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ... |
56-393 |
1.05e-40 |
|
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type II L-asparaginases, which tend to be highly specific for asparagine and localized to the periplasm. They are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL), but not without severe side effects. Tumor cells appear to have a heightened dependence on exogenous L-aspartate, and depleting their surroundings of L-aspartate may starve cancerous ALL cells. Type II L-asparaginase acts as a tetramer, which is actually a dimer of two tightly bound dimers. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase.
Pssm-ID: 199208 [Multi-domain] Cd Length: 319 Bit Score: 150.74 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 56 RVLVINTGGTIGMTLHD--NVLAPKANAfvkqmrklpvvhDELYAQqtrlydyygsentlvLPLSKDNKRIiytilEYKP 133
Cdd:cd08964 2 RIAVLATGGTIAGTADSsgAYAAPTLSG------------EELLAA---------------VPGLADVADV-----EVEQ 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 134 L--LDSSNMTTDDWGRIGKDIEK--NYENYDGFVILHGTDTMAYTASALSFMCEHlGKPIILTGSQVPIYEMRNDGRDNL 209
Cdd:cd08964 50 VsnLPSSDMTPADWLALAARVNEalADPDVDGVVVTHGTDTLEETAYFLDLTLDS-DKPVVLTGAMRPADAPSADGPANL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 210 LGALLIAGQfviPE-------VClyFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLATAEVDITINWDTVWRANTTAKFQV 282
Cdd:cd08964 129 LDAVRVAAS---PEargrgvlVV--FNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVDGGKVRFYRRPARPHTLPSEFD 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 283 STElnRNVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCLRGTVSASYA 362
Cdd:cd08964 204 DEL--PRVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVPP---ALVEALERAVAKGIPVVRSSRVGNGRVLPVYG 278
|
330 340 350
....*....|....*....|....*....|...
gi 1880388717 363 --TGKVLIDAGLIAGGDMTPEAALSKLSYVLAK 393
Cdd:cd08964 279 ygGGADLAEAGAIFAGDLSPQKARILLMLALAA 311
|
|
| Asparaginase_C |
pfam17763 |
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ... |
289-405 |
4.84e-38 |
|
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of asparaginase enzymes.
Pssm-ID: 465490 [Multi-domain] Cd Length: 114 Bit Score: 136.46 E-value: 4.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 289 NVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDnrlDLLEELKKATDSGVIIINCTQCLRGTVSAS-YATGKVL 367
Cdd:pfam17763 1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVPS---ALLDALKEAVARGIPVVRSSRCGSGRVNLGyYETGRDL 77
|
90 100 110
....*....|....*....|....*....|....*...
gi 1880388717 368 IDAGLIAGGDMTPEAALSKLSYVLAKKdLDLAAKKKMM 405
Cdd:pfam17763 78 LEAGVISGGDLTPEKARIKLMLALGKG-LDPEEIRELF 114
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
366-607 |
2.81e-25 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 106.19 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 366 VLIDAGLIAGGDMTPEAALSKLSYVLAKKDLDLAAKKKMMAQNLRGEMSADLAGAKLCLSDSRFIQVIAKSLSISCKEEL 445
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 446 EAIRDALTPPLAcAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSN 525
Cdd:COG0666 81 NAKDDGGNTLLH-AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 526 AVRFRHKEVVKLLRKTGAHF-SRDKLEEagTELCSLAASGDLEGLEIwsL--AGADLNETGYDGQTAIQVAQACGQKKVV 602
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVnARDNDGE--TPLHLAAENGHLEIVKL--LleAGADVNAKDNDGKTALDLAAENGNLEIV 235
|
....*
gi 1880388717 603 AFLVQ 607
Cdd:COG0666 236 KLLLE 240
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
448-605 |
6.17e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 96.56 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 448 IRDALTPPLACAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAV 527
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1880388717 528 RFRHKEVVKLLRKTGAHFSrDKLEEAGTELCSLAASGDLEGLEIWSLAGADLNETGYDGQTAIQVAQACGQKKVVAFL 605
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| asnASE_II |
TIGR00520 |
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ... |
135-397 |
1.27e-19 |
|
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) are designated type I and type II according to the terminology in E. coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-asparaginase II is a high-affinity periplasmic enzyme synthesized with a cleavable signal sequence. This model describes L-asparaginases related to type II of E. coli. Both the cytoplasmic and the cell wall asparaginases of Saccharomyces cerevisiae belong to this set. Members of this set from Acinetobacter glutaminasificans and Pseudomonas fluorescens are described as having both glutaminase and asparaginase activitities. All members are homotetrameric. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273115 [Multi-domain] Cd Length: 349 Bit Score: 90.60 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 135 LDSSNMTTDDWGRIGKDIEKNYE--NYDGFVILHGTDTMAYTASALSFM--CEhlgKPIILTGSQVPIYEMRNDGRDNLL 210
Cdd:TIGR00520 80 VGSQDMNEEVLLKLAKGINELLAsdDYDGIVITHGTDTLEETAYFLDLTvkSD---KPVVIVGAMRPATSVSADGPMNLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 211 GALLIAGQfviPE-----VCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLAT-AEVDITINWDTVWRANTTAKFQVSt 284
Cdd:TIGR00520 157 NAVSVAAN---PKsagrgVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYiHNGKIDYYYPPVRKHTCDTPFSVS- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 285 ELNRN---VGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDNRLDLLEELKKatdSGVIIINCTQCLRGTVSASY 361
Cdd:TIGR00520 233 NLDEPlpkVDIIYAYQNAPPLIVNAVLDAGAKGIVLAGVGNGSLSAAGLKVNETAAK---LGVPIVRSSRVGDGMVTPDA 309
|
250 260 270
....*....|....*....|....*....|....*..
gi 1880388717 362 ATgkvlidAGLIAGGDMTPEAALSKLSYVLAK-KDLD 397
Cdd:TIGR00520 310 EP------DGFIASGYLNPQKARVLLQLALTKtYDPE 340
|
|
| ansB |
PRK11096 |
L-asparaginase II; Provisional |
137-383 |
5.80e-19 |
|
L-asparaginase II; Provisional
Pssm-ID: 182958 [Multi-domain] Cd Length: 347 Bit Score: 88.62 E-value: 5.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 137 SSNMTTDDWGRIGKDIEKNYENYDGFVILHGTDTMAYTASALSFM--CEhlgKPIILTGSQVPIYEMRNDGRDNLLGALL 214
Cdd:PRK11096 79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTvkCD---KPVVLVGAMRPSTAMSADGPLNLYNAVV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 215 IAGQfviPE-----VCLYFYNKLYRGNRVTKVDAGSFNAFSSPNLAPLA---TAEVDitINWDTVWRANTTAKFQVS--T 284
Cdd:PRK11096 156 TAAD---KAsanrgVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGyihNGKVD--YQRTPARKHTTDTPFDVSklN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 285 ELNRnVGLLRLFPGITAATVRAFLQPPMEGVVLETYGSGNAPDNRLDLLEelkKATDSGVIIINctqclrgtvSASYATG 364
Cdd:PRK11096 231 ELPK-VGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKTVFDTLA---TAAKNGVAVVR---------SSRVPTG 297
|
250 260
....*....|....*....|....*.
gi 1880388717 365 KVLIDA-------GLIAGGDMTPEAA 383
Cdd:PRK11096 298 ATTQDAevddakyGFVASGTLNPQKA 323
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
459-606 |
4.78e-18 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 88.39 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 459 AAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLL 538
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1880388717 539 RktgaHFSR-DKLEEAGTELCSLAASGDLEGLEIWSLAGADLNETGYDGQTAIQVAQACGQKKVVAFLV 606
Cdd:PLN03192 611 Y----HFASiSDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
460-547 |
7.82e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 460 AAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATvyAKDRYGDTPLSNAVRFRHKEVVKLLR 539
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLL 81
|
....*...
gi 1880388717 540 KTGAHFSR 547
Cdd:pfam12796 82 EKGADINV 89
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
458-548 |
4.59e-11 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 66.07 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 458 CAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKL 537
Cdd:PTZ00322 87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|..
gi 1880388717 538 L-RKTGAHFSRD 548
Cdd:PTZ00322 167 LsRHSQCHFELG 178
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
486-538 |
1.91e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.51 E-value: 1.91e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1880388717 486 GRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLL 538
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
448-546 |
2.36e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.06 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 448 IRDALTPPLACAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAV 527
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
|
90
....*....|....*....
gi 1880388717 528 RFRHKEVVKLLRKTGAHFS 546
Cdd:PHA02874 199 EYGDYACIKLLIDHGNHIM 217
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
490-607 |
5.21e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 490 LHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLLrktgahfsrdkleeagtelcslaasgdlegl 569
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL------------------------------- 49
|
90 100 110
....*....|....*....|....*....|....*...
gi 1880388717 570 eiwsLAGADLNETGYdGQTAIQVAQACGQKKVVAFLVQ 607
Cdd:pfam12796 50 ----LEHADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
452-543 |
1.72e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 60.45 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 452 LTPPLACAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFEL------------------VEYLLNHGATVY 513
Cdd:PHA03100 107 ITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPIN 186
|
90 100 110
....*....|....*....|....*....|
gi 1880388717 514 AKDRYGDTPLSNAVRFRHKEVVKLLRKTGA 543
Cdd:PHA03100 187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGA 216
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
459-516 |
5.57e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.88 E-value: 5.57e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1880388717 459 AAAKIGDKEALEA-IREMGGNLflgDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKD 516
Cdd:pfam12796 36 LAAKNGHLEIVKLlLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
474-608 |
7.20e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 55.42 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 474 EMGGNLFLGDYDGRTPLHIATC--EGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHK--EVVKLLRKTGAH-FSRD 548
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADvYAVD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 549 -------------------KLEEAGTELCSLAASGDLEGLEIWSLA----------------GADLNETGYDGQTAIQVA 593
Cdd:PHA03095 185 drfrsllhhhlqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMAtgssckrslvlplliaGISINARNRYGQTPLHYA 264
|
170
....*....|....*
gi 1880388717 594 QACGQKKVVAFLVQL 608
Cdd:PHA03095 265 AVFNNPRACRRLIAL 279
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
455-544 |
1.87e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.03 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 455 PLACAAAKiGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEV 534
Cdd:COG0666 189 PLHLAAEN-GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
|
90
....*....|
gi 1880388717 535 VKLLRKTGAH 544
Cdd:COG0666 268 VKLLLLALLL 277
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
485-517 |
5.23e-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: 46.13 E-value: 5.23e-07
10 20 30
....*....|....*....|....*....|....
gi 1880388717 485 DGRTPLHIA-TCEGHFELVEYLLNHGATVYAKDR 517
Cdd:pfam00023 1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
486-543 |
7.00e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.97 E-value: 7.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1880388717 486 GRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLLRKTGA 543
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
469-543 |
9.67e-07 |
|
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: 51.94 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 469 LEAIREMGGNLFLGD-YDGRTPLHIATCEGHFELVEYLLNHGATVyAKDR---------------YGDTPLSNAVRFRHK 532
Cdd:cd22192 71 MEAAPELVNEPMTSDlYQGETALHIAVVNQNLNLVRELIARGADV-VSPRatgtffrpgpknliyYGEHPLSFAACVGNE 149
|
90
....*....|.
gi 1880388717 533 EVVKLLRKTGA 543
Cdd:cd22192 150 EIVRLLIEHGA 160
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
485-514 |
1.24e-06 |
|
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: 44.89 E-value: 1.24e-06
10 20 30
....*....|....*....|....*....|
gi 1880388717 485 DGRTPLHIATCEGHFELVEYLLNHGATVYA 514
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
465-544 |
1.73e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 50.82 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 465 DKEALEAIREMGGNLFLGDYDGRTPLHIA--TCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRH--KEVVKLLRK 540
Cdd:PHA03100 85 VKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLID 164
|
....
gi 1880388717 541 TGAH 544
Cdd:PHA03100 165 KGVD 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
556-619 |
4.57e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 4.57e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1880388717 556 ELCSLAASGDLEGLEIWSLAGADLNETGYDGQTAIQVAQACGQKKVVAFLVQLMSTRSKTVFDG 619
Cdd:PTZ00322 85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG 148
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
486-593 |
9.54e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 48.72 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 486 GRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLLRKTGAhfSRDKLEEAGTELCSLAASG- 564
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA--STDARDKCGNTPLHISVGYc 245
|
90 100 110
....*....|....*....|....*....|.
gi 1880388717 565 -DLEGLEIWSLAGADLNETGY-DGQTAIQVA 593
Cdd:PHA02878 246 kDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
456-520 |
1.25e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.33 E-value: 1.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1880388717 456 LACAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGD 520
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
449-580 |
1.56e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 47.68 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 449 RDALTPplACAAAKIGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVR 528
Cdd:PHA02875 100 KDGMTP--LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1880388717 529 FRHKEVVKLLRKTGAHFSRDKLEEAGTELCSLAASGDLEGLEIWSLAGADLN 580
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
485-514 |
1.59e-05 |
|
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: 41.86 E-value: 1.59e-05
10 20 30
....*....|....*....|....*....|
gi 1880388717 485 DGRTPLHIATCEGHFELVEYLLNHGATVYA 514
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
467-538 |
2.55e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 47.27 E-value: 2.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1880388717 467 EALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVrFRHKEVVKLL 538
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELL 241
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
453-506 |
2.76e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 2.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1880388717 453 TPPLACAAAKiGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLL 506
Cdd:pfam13637 2 LTALHAAAAS-GHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
478-523 |
3.49e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 3.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1880388717 478 NLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPL 523
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
476-523 |
9.17e-05 |
|
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: 9.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1880388717 476 GGNLFlgdYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPL 523
Cdd:cd22192 129 PKNLI---YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
465-544 |
1.34e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 44.95 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 465 DKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLLRKTGAH 544
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
555-606 |
2.03e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 2.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1880388717 555 TELCSLAASGDLEGLEIWSLAGADLNETGYDGQTAIQVAQACGQKKVVAFLV 606
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
499-592 |
3.12e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 43.67 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 499 FELVEYLLNHGATVYAKDRYGDTP----LSNAVRFRHK-EVVKLLRKTGAHFSRdKLEEAGTELCSLAASGDLEGLEIWS 573
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPlctiLSNIKDYKHMlDIVKILIENGADINK-KNSDGETPLYCLLSNGYINNLEILL 129
|
90 100
....*....|....*....|..
gi 1880388717 574 LA---GADLNETGYDGQTAIQV 592
Cdd:PHA02798 130 FMienGADTTLLDKDGFTMLQV 151
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
499-606 |
5.55e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 42.70 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 499 FELVEYLLNHGATVYAKDRYGDTPLSNAVRFRH---KEVVKLLRKTGAHFsrDKLEEAG-TEL-CSLAASGDLEGLEIWS 573
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADV--NAPERCGfTPLhLYLYNATTLDVIKLLI 104
|
90 100 110
....*....|....*....|....*....|....*
gi 1880388717 574 LAGADLNETGYDGQTAIQV--AQACGQKKVVAFLV 606
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLL 139
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
482-538 |
2.35e-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: 40.90 E-value: 2.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1880388717 482 GDYDGRTPLHIATCEGHFELVEYLLNHGATVYA---------KDRY-----GDTPLSNAVRFRHKEVVKLL 538
Cdd:cd22194 137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLL 207
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
449-593 |
3.19e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 40.63 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 449 RDALTPPLACAAAKiGDKEALEAIREMGGNLFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAV- 527
Cdd:PHA02878 165 RHKGNTALHYATEN-KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVg 243
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880388717 528 RFRHKEVVKLLRKTGAHFSRDKLEEAGTELCSLAASGDLegLEIWSLAGADLNETGYDGQTAIQVA 593
Cdd:PHA02878 244 YCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
487-545 |
3.20e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 40.42 E-value: 3.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1880388717 487 RTPLHIATCEGH-----FELVEYLLNHGATVYAKDRYGDTPLSNAV--RFRHKEVVKLLRKTGAHF 545
Cdd:PHA03100 69 STPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANV 134
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
442-546 |
3.75e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.45 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 442 KEELEAIRDALTPPLAcAAAKIGDKEalEAIREMGGNLflgdYDGRTPLHIATCEGHFELVEYLLNHGATVYAKD----- 516
Cdd:TIGR00870 91 LEYVDAVEAILLHLLA-AFRKSGPLE--LANDQYTSEF----TPGITALHLAAHRQNYEIVKLLLERGASVPARAcgdff 163
|
90 100 110
....*....|....*....|....*....|....*....
gi 1880388717 517 ---------RYGDTPLSNAVRFRHKEVVKLLRKTGAHFS 546
Cdd:TIGR00870 164 vksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
464-607 |
5.09e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 39.56 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 464 GDKEALEAIREMGGN-LFLGDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRHKEVVKLLRKTG 542
Cdd:PHA02874 12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 543 AHFS----------------------RDKLEEAGTELCSLAASGDLEGLEIWSLAGADLNETGYDGQTAIQVAQACGQKK 600
Cdd:PHA02874 92 VDTSilpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
|
....*..
gi 1880388717 601 VVAFLVQ 607
Cdd:PHA02874 172 IIKLLLE 178
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
561-615 |
6.40e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 36.25 E-value: 6.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1880388717 561 AASGDLEGLEIWSLAGADLNETGYDGQTAIQVAQACGQKKVVAFLVQLMSTRSKT 615
Cdd:pfam12796 5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD 59
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
482-607 |
6.68e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 39.26 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1880388717 482 GDYDGRTPLHIATCEGHFELVEYLLNHGATVYAKDRYGDTPLSNAVRFRH-----KEVVKLLRKTGAHFsrDKLEEAGTE 556
Cdd:PHA03100 31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANV--NAPDNNGIT 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1880388717 557 LCSLAASGDLEGLEIWSL---AGADLNETGYDGQTAIQVAQACGQ--KKVVAFLVQ 607
Cdd:PHA03100 109 PLLYAISKKSNSYSIVEYlldNGANVNIKNSDGENLLHLYLESNKidLKILKLLID 164
|
|
| |
