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Conserved domains on  [gi|21426773|ref|NP_653351|]
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60 kDa lysophospholipase [Rattus norvegicus]

Protein Classification

L-asparaginase family protein( domain architecture ID 13049359)

L-asparaginase family protein containing ankyrin (ANK) repeats, may catalyze the deamination of asparagine to yield aspartic acid and ammonium

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
L-asparaginase_like super family cl00216
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 15-361 4.90e-131

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.


The actual alignment was detected with superfamily member PRK09461:

Pssm-ID: 469665 [Multi-domain]  Cd Length: 335  Bit Score: 385.86  E-value: 4.90e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   15 YTGGTIGM-RSEGGvLVPGRG-LAAVLRTLHMLHDEEyarahsLPEdtlvlppassdqriiYKVLECQPLFDSSDMTITE 92
Cdd:PRK09461  10 YTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE------MPD---------------FTIHEYTPLIDSSDMTPED 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   93 WVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYVIPEV 172
Cdd:PRK09461  68 WQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  173 CLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASwKSHLVVHSNMEPDVGLLRLYPGIPASLV 252
Cdd:PRK09461 148 TLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHG-EGELIVHPITPQPIGVVTIYPGISAEVV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  253 RTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMAGAGIISGFDMTSEAAL 331
Cdd:PRK09461 227 RNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADMTVEAAL 306

                        330       340       350
                 ....*....|....*....|....*....|
gi 21426773  332 AKLSYVLGQPgLSLSDRKKLLAKDLRGEMT 361
Cdd:PRK09461 307 TKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-559 1.68e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLS 491
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21426773 492 PQELEDvGTELCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSLEDRVSA 559
Cdd:COG0666 181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 15-361 4.90e-131

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 385.86  E-value: 4.90e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   15 YTGGTIGM-RSEGGvLVPGRG-LAAVLRTLHMLHDEEyarahsLPEdtlvlppassdqriiYKVLECQPLFDSSDMTITE 92
Cdd:PRK09461  10 YTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE------MPD---------------FTIHEYTPLIDSSDMTPED 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   93 WVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYVIPEV 172
Cdd:PRK09461  68 WQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  173 CLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASwKSHLVVHSNMEPDVGLLRLYPGIPASLV 252
Cdd:PRK09461 148 TLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHG-EGELIVHPITPQPIGVVTIYPGISAEVV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  253 RTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMAGAGIISGFDMTSEAAL 331
Cdd:PRK09461 227 RNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADMTVEAAL 306

                        330       340       350
                 ....*....|....*....|....*....|
gi 21426773  332 AKLSYVLGQPgLSLSDRKKLLAKDLRGEMT 361
Cdd:PRK09461 307 TKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 7.42e-108

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: 325.93  E-value: 7.42e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  10 RLLAIYTGGTIGMR--SEGGVLVPGRGLAAVLRTLHMLHDEEYARAHSLPedtlvlppassdqriiykvlecqpLFDSSD 87
Cdd:COG0252   5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAELADIEVEQFA------------------------NIDSSN 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  88 MTITEWVQIAQTIERHYTQ-YQGFVVIHGTDTMAFAASVLSFMLEnLQKPVILTGAQVPIHELWSDGRENLLGALLMA-- 164
Cdd:COG0252  61 MTPADWLALARRIEEALADdYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 165 GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKAswKSHLVVHSNMEPDVGLLRL 243
Cdd:COG0252 140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRP--ESELDLAPALLPRVAILKL 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 244 YPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYAPGMAMAGAGIISGF 323
Cdd:COG0252 218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                       330       340       350
                ....*....|....*....|....*....|.
gi 21426773 324 DMTSEAALAKLSYVLGQpGLSLSDRKKLLAK 354
Cdd:COG0252 296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 1.07e-107

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: 325.63  E-value: 1.07e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773     11 LLAIYTGGTIGMR--SEGGVLVPGRGLAAVLRtlhmLHDEeyarahsLPEDtlvlppassDQRIIYkvlECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLA----LLPA-------LPEL---------ADDIEV---EQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773     89 TITEWVQIAQTIE--RHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    167 Y--VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKASWKS--HLVVHSNMEPDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGgVVYYTRPTRRHTKRSpfLLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    242 RLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMAGAGII 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 21426773    321 SGFDMTSEAALAKLSYVLGQpGLSLSDRK 349
Cdd:smart00870 296 SAGDLTPEKARIKLMLALGK-GLDPEEIR 323
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 9-341 1.78e-107

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: 324.53  E-value: 1.78e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   9 QRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLRtlhmlhdeeyarahslpedtlVLPPASSDQRIIykvLECQPLFDSSDM 88
Cdd:cd08963   1 KKILLLYTGGTIASVKTEGGLAPALTAEELLS---------------------YLPELLEDCFIE---VEQLPNIDSSNM 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  89 TITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYV 168
Cdd:cd08963  57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 169 IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASWKSHLVVHSNmePDVGLLRLYPGIP 248
Cdd:cd08963 137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLFYPDLD--PNVFLLKLIPGLL 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 249 ASLVRTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAV-TSDYAPGMAMAGAGIISGFDMTS 327
Cdd:cd08963 215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIPGGDMTT 294

                       330
                ....*....|....
gi 21426773 328 EAALAKLSYVLGQP 341
Cdd:cd08963 295 EAAVAKLMWLLGQT 308
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 11-362 1.13e-85

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: 269.38  E-value: 1.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    11 LLAIYTGGTIGM-RSE-GGVLVPGRGLAAVLRTLHMLHDEEYARAHSLPedtlvlppassdqriiykvlecqpLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPVFTADELLSAVPELLDIANIDGEALM------------------------NILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    89 TITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENlQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   169 ------IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASWKSHLVVHSNMEPDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   243 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTkpDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMAGAGIIS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNmNVYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 21426773   322 GFDMTSEAALAKLSYVLGQPgLSLSDRKKLLAKDLRGEMTL 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 1.97e-70

Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 224.34  E-value: 1.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    11 LLAIYTGGTIGMR--SEGGVLVPGrglaavlrtlhmLHDEEYARAhslpedtlvLPPASSDQRIIYkvlECQPLFDSSDM 88
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPA------------LTGEELLAA---------VPELADIAEIEA---EQVANIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    89 TITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQY- 167
Cdd:pfam00710  57 TPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPa 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21426773   168 -VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRE 217
Cdd:pfam00710 137 aRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-559 1.68e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLS 491
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21426773 492 PQELEDvGTELCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSLEDRVSA 559
Cdd:COG0666 181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 381-550 2.82e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 85.69  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  381 LLSMNGSQDADAMKDVLLPGLALAAAHAGDLDTLQAfvelGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDAC 460
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA----KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  461 NEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELEDVgteLCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEA 540
Cdd:PLN03192 588 DANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664

                        170
                 ....*....|
gi 21426773  541 AGNADVVALL 550
Cdd:PLN03192 665 EDHVDMVRLL 674
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-490 9.35e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 9.35e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773   412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKgVDVDACNeDGQSPLLLAVRGRHQSVIRLLRAAGAHL 490
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 431-459 4.30e-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: 43.35  E-value: 4.30e-06
                           10        20
                   ....*....|....*....|....*....
gi 21426773    431 GQTPLHVAARRGHASVVAMLLQKGVDVDA 459
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 412-459 7.42e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.49  E-value: 7.42e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773 412 DTLQAFVELGRDL-NLKD----------YSGQTPLHVAARRGHASVVAMLLQKGVDVDA 459
Cdd:cd22196  64 DTISLLLDIAEKTgNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHA 122
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 429-506 1.42e-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: 41.61  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   429 YSGQTPLHVAARRGHASVVAMLLQKGVDVDA-CNED-------------GQSPLLLAVRGRHQSVIRLLRAAGAHLSPQe 494
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPArACGDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA- 204

                          90
                  ....*....|..
gi 21426773   495 lEDVGTELCRLA 506
Cdd:TIGR00870 205 -DSLGNTLLHLL 215
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 15-361 4.90e-131

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 385.86  E-value: 4.90e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   15 YTGGTIGM-RSEGGvLVPGRG-LAAVLRTLHMLHDEEyarahsLPEdtlvlppassdqriiYKVLECQPLFDSSDMTITE 92
Cdd:PRK09461  10 YTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE------MPD---------------FTIHEYTPLIDSSDMTPED 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   93 WVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYVIPEV 172
Cdd:PRK09461  68 WQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAANYPINEV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  173 CLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASwKSHLVVHSNMEPDVGLLRLYPGIPASLV 252
Cdd:PRK09461 148 TLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHG-EGELIVHPITPQPIGVVTIYPGISAEVV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  253 RTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMAGAGIISGFDMTSEAAL 331
Cdd:PRK09461 227 RNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADMTVEAAL 306

                        330       340       350
                 ....*....|....*....|....*....|
gi 21426773  332 AKLSYVLGQPgLSLSDRKKLLAKDLRGEMT 361
Cdd:PRK09461 307 TKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 7.42e-108

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: 325.93  E-value: 7.42e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  10 RLLAIYTGGTIGMR--SEGGVLVPGRGLAAVLRTLHMLHDEEYARAHSLPedtlvlppassdqriiykvlecqpLFDSSD 87
Cdd:COG0252   5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAELADIEVEQFA------------------------NIDSSN 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  88 MTITEWVQIAQTIERHYTQ-YQGFVVIHGTDTMAFAASVLSFMLEnLQKPVILTGAQVPIHELWSDGRENLLGALLMA-- 164
Cdd:COG0252  61 MTPADWLALARRIEEALADdYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 165 GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKAswKSHLVVHSNMEPDVGLLRL 243
Cdd:COG0252 140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRP--ESELDLAPALLPRVAILKL 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 244 YPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYAPGMAMAGAGIISGF 323
Cdd:COG0252 218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                       330       340       350
                ....*....|....*....|....*....|.
gi 21426773 324 DMTSEAALAKLSYVLGQpGLSLSDRKKLLAK 354
Cdd:COG0252 296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 1.07e-107

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: 325.63  E-value: 1.07e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773     11 LLAIYTGGTIGMR--SEGGVLVPGRGLAAVLRtlhmLHDEeyarahsLPEDtlvlppassDQRIIYkvlECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLA----LLPA-------LPEL---------ADDIEV---EQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773     89 TITEWVQIAQTIE--RHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    167 Y--VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKASWKS--HLVVHSNMEPDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGgVVYYTRPTRRHTKRSpfLLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    242 RLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMAGAGII 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 21426773    321 SGFDMTSEAALAKLSYVLGQpGLSLSDRK 349
Cdd:smart00870 296 SAGDLTPEKARIKLMLALGK-GLDPEEIR 323
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 9-341 1.78e-107

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: 324.53  E-value: 1.78e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   9 QRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLRtlhmlhdeeyarahslpedtlVLPPASSDQRIIykvLECQPLFDSSDM 88
Cdd:cd08963   1 KKILLLYTGGTIASVKTEGGLAPALTAEELLS---------------------YLPELLEDCFIE---VEQLPNIDSSNM 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  89 TITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYV 168
Cdd:cd08963  57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 169 IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASWKSHLVVHSNmePDVGLLRLYPGIP 248
Cdd:cd08963 137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLFYPDLD--PNVFLLKLIPGLL 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 249 ASLVRTFLQPPLKGVVMETFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAV-TSDYAPGMAMAGAGIISGFDMTS 327
Cdd:cd08963 215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIPGGDMTT 294

                       330
                ....*....|....
gi 21426773 328 EAALAKLSYVLGQP 341
Cdd:cd08963 295 EAAVAKLMWLLGQT 308
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 11-362 1.13e-85

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: 269.38  E-value: 1.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    11 LLAIYTGGTIGM-RSE-GGVLVPGRGLAAVLRTLHMLHDEEYARAHSLPedtlvlppassdqriiykvlecqpLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPVFTADELLSAVPELLDIANIDGEALM------------------------NILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    89 TITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENlQKPVILTGAQVPIHELWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   169 ------IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKASWKSHLVVHSNMEPDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   243 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTkpDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMAGAGIIS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNmNVYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 21426773   322 GFDMTSEAALAKLSYVLGQPgLSLSDRKKLLAKDLRGEMTL 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 1.97e-70

Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 224.34  E-value: 1.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    11 LLAIYTGGTIGMR--SEGGVLVPGrglaavlrtlhmLHDEEYARAhslpedtlvLPPASSDQRIIYkvlECQPLFDSSDM 88
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPA------------LTGEELLAA---------VPELADIAEIEA---EQVANIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    89 TITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQY- 167
Cdd:pfam00710  57 TPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPa 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21426773   168 -VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRE 217
Cdd:pfam00710 137 aRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 10-340 4.02e-51

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: 180.51  E-value: 4.02e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  10 RLLAIYTGGTIGMR---SEGGVlvpgrglaavlrtlHMLHD-EEYARAhsLPEdtlVLPPASSDQRIIYKVLecqplfdS 85
Cdd:cd08962  72 KVSIISTGGTIASRvdyRTGAV--------------SPAFTaEELLRA--IPE---LLDIANIKAEVLFNIL-------S 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  86 SDMTITEWVQIAQTIERHYTQ-YQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMA 164
Cdd:cd08962 126 ENMTPEYWVKIAEAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLVA 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 165 GQYvIPEV------------CLffqnqLFRGNRTTKVDARRFAAFCSPNLPPLATV---GADVTINRELVRKASWKshLV 229
Cdd:cd08962 206 ASD-IAEVvvvmhgttsddyCL-----LHRGTRVRKMHTSRRDAFQSINDEPLAKVdppGKIEKLSKDYRKRGDEE--LE 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 230 VHSNMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSD-Y 308
Cdd:cd08962 278 LNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIE--GTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRVNLNvY 355

                       330       340       350
                ....*....|....*....|....*....|..
gi 21426773 309 APGMAMAGAGIISGFDMTSEAALAKLSYVLGQ 340
Cdd:cd08962 356 STGRELLKAGVIPGEDMLPETAYVKLMWVLGN 387
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
14-361 2.96e-50

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 178.50  E-value: 2.96e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   14 IYTGGTIGMRSE---GGVlvpgrglAAVLRTlhmlhdEEYARAhsLPEdtlVLPPASSDQRIIYKVLecqplfdSSDMTI 90
Cdd:PRK04183  81 LSTGGTIASKVDyrtGAV-------TPAFTA------EDLLRA--VPE---LLDIANIRGRVLFNIL-------SENMTP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   91 TEWVQIAQTIERHYTQ-YQGFVVIHGTDTMAFAASVLSFMLeNLQKPVILTGAQ----VPIhelwSDGRENLLGALLMA- 164
Cdd:PRK04183 136 EYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFML-KTPVPIVFVGAQrssdRPS----SDAAMNLICAVLAAt 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  165 ---GQYVI-------PEVCLffqnqLFRGNRTTKVDARRFAAFCSPNLPPLATV----GADVTINRELVRKASWKshLVV 230
Cdd:PRK04183 211 sdiAEVVVvmhgttsDDYCA-----LHRGTRVRKMHTSRRDAFQSINDKPLAKVdykeGKIEFLRKDYRKRGEKE--LEL 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  231 HSNMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSD-YA 309
Cdd:PRK04183 284 NDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIE--GTGLGHVSTDLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYS 361

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 21426773  310 PGMAMAGAGIISGFDMTSEAALAKLSYVLGQPGlSLSDRKKLLAKDLRGEMT 361
Cdd:PRK04183 362 TGRDLLKAGVIPGEDMLPEVAYVKLMWVLGNTY-DLEEVRELMLTNLAGEIN 412
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
 14-361 9.65e-48

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: 171.41  E-value: 9.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    14 IYTGGTIGMR--SEGGVLVPgrglaavlrtlhMLHDEEYARAhsLPEDTLVlppASSDQRIIYKVLecqplfdSSDMTIT 91
Cdd:TIGR02153  68 ISTGGTIASRvdYETGAVYP------------AFTAEELARA--VPELLEI---ANIKARAVFNIL-------SENMKPE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    92 EWVQIAQTIERHYTQ-YQGFVVIHGTDTMAFAASVLSFMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMAGQyVIP 170
Cdd:TIGR02153 124 YWIKIAEAVAKALKEgADGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRSSDRPSSDAALNLICAVRAATS-PIA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   171 EV------------CLffqnqLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTIN--RELVRKASWKShLVVHSNMEP 236
Cdd:TIGR02153 203 EVtvvmhgetsdtyCL-----VHRGVKVRKMHTSRRDAFQSINDIPIAKIDPDEGIEklRIDYRRRGEKE-LELDDKFEE 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   237 DVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSD-YAPGMAMA 315
Cdd:TIGR02153 277 KVALVKFYPGISPEIIEFLVDKGYKGIVIE--GTGLGHVSEDWIPSIKRATDDGVPVVMTSQCLYGRVNLNvYSTGRELL 354

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 21426773   316 GAGIISGFDMTSEAALAKLSYVLGQPGlSLSDRKKLLAKDLRGEMT 361
Cdd:TIGR02153 355 KAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAGEIN 399
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 84-340 5.00e-41

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: 150.74  E-value: 5.00e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  84 DSSDMTITEWVQIAQTIERH-YTQYQGFVVIHGTDTMAFAASVLSFMLENlQKPVILTGAQVPIHELWSDGRENLLGALL 162
Cdd:cd00411  56 ASEDITPDDWLKLAKEVAKLlDSDVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAVR 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 163 MA--GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTI-NRELVRKASWKSHLVVHS-NMEPDV 238
Cdd:cd00411 135 VAkdKDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYyQRKPARKHTDESEFDVSDiKSLPKV 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 239 GLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYAPGMAMAGaG 318
Cdd:cd00411 215 DIVYLYPGLSDDIYDALVDLGYKGIVLA--GTGNGSVPYDVFPVLSSASKRGVAVVRSSQVIYGGVDLNAEKVDLKAG-V 291

                       250       260
                ....*....|....*....|..
gi 21426773 319 IISGfDMTSEAALAKLSYVLGQ 340
Cdd:cd00411 292 IPAG-DLNPEKARVLLMWALTH 312
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 10-340 2.77e-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: 148.81  E-value: 2.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  10 RLLAIYTGGTIGMR--SEGGVLVPGRGLAAVLRTLHMLhdEEYARAHslPEDTLVLPpassdqriiykvlecqplfdSSD 87
Cdd:cd08964   2 RIAVLATGGTIAGTadSSGAYAAPTLSGEELLAAVPGL--ADVADVE--VEQVSNLP--------------------SSD 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  88 MTITEWVQIAQTIERHYTQ--YQGFVVIHGTDTM---AFAASvlsfMLENLQKPVILTGAQVPIHELWSDGRENLLGALL 162
Cdd:cd08964  58 MTPADWLALAARVNEALADpdVDGVVVTHGTDTLeetAYFLD----LTLDSDKPVVLTGAMRPADAPSADGPANLLDAVR 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 163 MAGQyviPE-----VCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRELVRKASWKShlvVHSNMEP 236
Cdd:cd08964 134 VAAS---PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVdGGKVRFYRRPARPHTLPS---EFDDELP 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 237 DVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYA--PGMAM 314
Cdd:cd08964 208 RVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVP--PALVEALERAVAKGIPVVRSSRVGNGRVLPVYGygGGADL 285

                       330       340
                ....*....|....*....|....*.
gi 21426773 315 AGAGIISGFDMTSEAALAKLSYVLGQ 340
Cdd:cd08964 286 AEAGAIFAGDLSPQKARILLMLALAA 311
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 237-351 1.27e-32

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: 121.05  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   237 DVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLIQELRAAAERGLIIVNCTHCLQGAVT-SDYAPGMAMA 315
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNlGYYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 21426773   316 GAGIISGFDMTSEAALAKLSYVLGQpGLSLSDRKKL 351
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-559 1.68e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLS 491
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21426773 492 PQELEDvGTELCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSLEDRVSA 559
Cdd:COG0666 181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
 84-315 1.50e-21

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: 96.37  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773    84 DSSDMTITEWVQIAQTIERHY--TQYQGFVVIHGTDTMAFAASVLSFMLeNLQKPVILTGAQVPIHELWSDGRENLLGAL 161
Cdd:TIGR00520  81 GSQDMNEEVLLKLAKGINELLasDDYDGIVITHGTDTLEETAYFLDLTV-KSDKPVVIVGAMRPATSVSADGPMNLYNAV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   162 LMAGQyviPE-----VCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRELVRKASWKSHLVVhSNME 235
Cdd:TIGR00520 160 SVAAN---PKsagrgVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIhNGKIDYYYPPVRKHTCDTPFSV-SNLD 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   236 ---PDVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSDYAPGM 312
Cdd:TIGR00520 236 eplPKVDIIYAYQNAPPLIVNAVLDAGAKGIVLA--GVGNGSLSAAGLKVNETAAKLGVPIVRSSRVGDGMVTPDAEPDG 313


                  ...
gi 21426773   313 AMA 315
Cdd:TIGR00520 314 FIA 316
ansB PRK11096
L-asparaginase II; Provisional
 85-307 2.00e-18

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 86.70  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   85 SSDMTITEWVQIAQTIERHYTQYQGFVVIHGTDTMAFAASVLSfMLENLQKPVILTGAQVPIHELWSDGRENLLGALLMA 164
Cdd:PRK11096  79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  165 G--QYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRELVRKASWKSHL-VVHSNMEPDVGL 240
Cdd:PRK11096 158 AdkASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIhNGKVDYQRTPARKHTTDTPFdVSKLNELPKVGI 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21426773  241 LRLYPGIPASLVRTFLQPPLKGVVmeTFGSGNGPTKPDLIQELRAAAERGLIIVNCTHCLQGAVTSD 307
Cdd:PRK11096 238 VYNYANASDLPAKALVDAGYDGIV--SAGVGNGNLYKTVFDTLATAAKNGVAVVRSSRVPTGATTQD 302
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
345-550 2.79e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.39  E-value: 2.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 345 LSDRKKLLAKDLRGEMTLPTTDDLLGDDMLGCRATWLLSMNGSQDADAMKDVLLPGLALAAAHAGDLDTLQAFVELGRDL 424
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773 425 NLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELEDVgTELCR 504
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHL 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 21426773 505 LASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 550
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 381-550 2.82e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 85.69  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  381 LLSMNGSQDADAMKDVLLPGLALAAAHAGDLDTLQAfvelGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDAC 460
Cdd:PLN03192 512 LLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA----KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  461 NEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELEDVgteLCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEA 540
Cdd:PLN03192 588 DANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664

                        170
                 ....*....|
gi 21426773  541 AGNADVVALL 550
Cdd:PLN03192 665 EDHVDMVRLL 674
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-490 9.35e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 9.35e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773   412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKgVDVDACNeDGQSPLLLAVRGRHQSVIRLLRAAGAHL 490
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 421-498 2.80e-11

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.07  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  421 GRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRA-------AGAHLSPQ 493
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPD 184


                 ....*
gi 21426773  494 ELEDV 498
Cdd:PTZ00322 185 SFTGK 189
Ank_4 pfam13637
Ankyrin repeats (many copies);
433-483 1.95e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 21426773   433 TPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLL 483
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
422-471 3.54e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 3.54e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 21426773   422 RDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLA 471
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
435-483 3.61e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 3.61e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 21426773   435 LHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLL 483
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-491 3.49e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAAR--RGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSV--IRLLRAAG 487
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAG 177


                 ....
gi 21426773  488 AHLS 491
Cdd:PHA03095 178 ADVY 181
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 417-488 1.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.07e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21426773  417 FVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGA 488
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 412-491 3.60e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLS 491
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-490 4.48e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.88  E-value: 4.48e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773 412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHL 490
Cdd:COG0666 200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 431-462 6.53e-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: 45.74  E-value: 6.53e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 21426773   431 GQTPLHVAA-RRGHASVVAMLLQKGVDVDACNE 462
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 418-488 9.08e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 9.08e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21426773  418 VELGRDLNLKDYSGQTPLHVAARRG--HASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGA 488
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
PHA03095 PHA03095
ankyrin-like protein; Provisional
 417-486 1.24e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 1.24e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  417 FVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHqsvIRLLRAA 486
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN---GRAVRAA 309
PHA02741 PHA02741
hypothetical protein; Provisional
 414-484 1.45e-06

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 48.50  E-value: 1.45e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21426773  414 LQAFVELGRDLNLKD-YSGQTPLHVAA-RRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLR 484
Cdd:PHA02741  80 IDHLIELGADINAQEmLEGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILR 152
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-524 2.79e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGH-ASVVAMLLQKGVDVDACNEDGQSPLLLAVRGR--HQSVIRLLRAAGA 488
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGA 143

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 21426773  489 HLSPQELEDVGTELCRLASR-ADSEGLRAWWQAGADL 524
Cdd:PHA03095 144 DVNALDLYGMTPLAVLLKSRnANVELLRLLIDAGADV 180
Ank_4 pfam13637
Ankyrin repeats (many copies);
412-451 3.80e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 3.80e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 21426773   412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLL 451
Cdd:pfam13637  15 ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 431-459 4.30e-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: 43.35  E-value: 4.30e-06
                           10        20
                   ....*....|....*....|....*....
gi 21426773    431 GQTPLHVAARRGHASVVAMLLQKGVDVDA 459
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 412-491 8.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLS 491
Cdd:PHA02874 138 ESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM 217
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 415-481 1.15e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 1.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21426773  415 QAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIR 481
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 413-490 1.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 1.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773  413 TLQAFVELGRDLNLKDYSGQTPLHVAARRG-HASVVAMLLQKGVDVDACNEDGQSPLLLAVrgRHQSVIRLLRAAGAHL 490
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
423-459 1.76e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 1.76e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 21426773   423 DLNLKDYsGQTPLHVAARRGHASVVAMLLQKGVDVDA 459
Cdd:pfam12796  54 DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 431-459 2.56e-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: 41.09  E-value: 2.56e-05
                          10        20
                  ....*....|....*....|....*....
gi 21426773   431 GQTPLHVAARRGHASVVAMLLQKGVDVDA 459
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 412-474 7.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 7.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRG 474
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCG 418
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 490-550 1.32e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21426773  490 LSPQELED------VGTELCRLASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 550
Cdd:PTZ00322  68 LTTEEVIDpvvahmLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 431-555 1.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  431 GQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRaagAHLSPQELEDV--GTELCRLASR 508
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCcgCTPLIIAMAK 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 21426773  509 ADSEGLRAWWQAGADlgqPDYDGHcalqvaeaagNADVVALLQSLED 555
Cdd:PHA02875 179 GDIAICKMLLDSGAN---IDYFGK----------NGCVAALCYAIEN 212
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 424-550 2.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  424 LNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELEDVGTELC 503
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMI 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773  504 RL----------------------ASRADSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 550
Cdd:PHA02874 108 KTildcgidvnikdaelktflhyaIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 412-483 5.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 5.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRgRHQSVIRLL 483
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELL 241
PHA02946 PHA02946
ankyin-like protein; Provisional
 414-468 5.27e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 5.27e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21426773  414 LQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPL 468
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL 109
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-487 6.07e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 6.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASV--VAMLLQKGVDVDACNEDGQSPL---LLAVRGRhQSVIRLLRAA 486
Cdd:PHA03095 133 KVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLhhhLQSFKPR-ARIVRELIRA 211


                 .
gi 21426773  487 G 487
Cdd:PHA03095 212 G 212
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 412-512 6.78e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACN-EDGQSPLLL--AVRGRHQSVIRLLRAAGA 488
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPTELreLLQKRELGHSITIVDSVP 715

                         90       100
                 ....*....|....*....|....
gi 21426773  489 HLSPQELEDVGTELCRLASRADSE 512
Cdd:PLN03192 716 ADEPDLGRDGGSRPGRLQGTSSDN 739
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 412-459 7.42e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.49  E-value: 7.42e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773 412 DTLQAFVELGRDL-NLKD----------YSGQTPLHVAARRGHASVVAMLLQKGVDVDA 459
Cdd:cd22196  64 DTISLLLDIAEKTgNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHA 122
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 417-488 9.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 9.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  417 FVELGRDLNLKDYSGQTPLHVAARRGHASV------------------VAMLLQKGVDVDACNEDGQSPLLLAVRGRHQS 478
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                         90
                 ....*....|
gi 21426773  479 VIRLLRAAGA 488
Cdd:PHA03100 207 FVKYLLDLGA 216
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 412-462 9.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 9.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 21426773  412 DTLQAFVELGRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNE 462
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 427-483 1.02e-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: 42.05  E-value: 1.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21426773 427 KDYSGQTPLHVAARRGHASVVAMLLQKGVDVDAC----------NED----GQSPLLLAVRGRHQSVIRLL 483
Cdd:cd22194 137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLL 207
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 429-506 1.42e-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: 41.61  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773   429 YSGQTPLHVAARRGHASVVAMLLQKGVDVDA-CNED-------------GQSPLLLAVRGRHQSVIRLLRAAGAHLSPQe 494
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPArACGDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA- 204

                          90
                  ....*....|..
gi 21426773   495 lEDVGTELCRLA 506
Cdd:TIGR00870 205 -DSLGNTLLHLL 215
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 429-505 1.68e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 1.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21426773  429 YSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGAHLSPQELED--VGTELCRL 505
Cdd:PLN03192 620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdfSPTELREL 698
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 421-488 1.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21426773  421 GRDLNLKDYSGQTPLHVAARRGHAS-VVAMLLQKGVDVDACNEDGQSPL-LLAVRGRHQSVIRLLRAAGA 488
Cdd:PHA02876 263 GFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGA 332
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 414-488 2.05e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 2.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21426773  414 LQAFVELGRDLNLKD-YSGQTPLHVAARRGHASVVAMLL-QKGVDVDACNEDGQSPLLLAVRGRHQSVIRLLRAAGA 488
Cdd:PHA02736  74 LKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 412-475 3.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 3.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21426773  412 DTLQAFVELGRDLNLKDY-SGQTPLHVAARrgHASVVAMLLQKGVDVDACNEDGQSPLLLAVRGR 475
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
PHA02917 PHA02917
ankyrin-like protein; Provisional
 422-483 8.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.21  E-value: 8.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21426773  422 RDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAV-RGRHQSVIRLL 483
Cdd:PHA02917 443 KDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKML 505
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 421-493 9.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 9.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21426773  421 GRDLNLKDYSGQTPLHVAARRGHASVVAMLLQKGVDVDACNEDGQSPLLLAV-RGRHQSVIRLLRAAGAHLSPQ 493
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAK 264
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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