NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|124487183|ref|NP_001074638|]
View 

60 kDa lysophospholipase [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 9-361 4.90e-132

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: 388.18  E-value: 4.90e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   9 RRLLAIYTGGTIGM-RSEGGvLVPGRG-LAAVLKTLHMFHDEEyaqahsLPEdtlvlppaspdqriiYTVLECQPLFDSS 86
Cdd:PRK09461   4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE------MPD---------------FTIHEYTPLIDSS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  87 DMTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461  62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 167 YVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRLYPG 246
Cdd:PRK09461 142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTIYPG 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 247 IPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDM 325
Cdd:PRK09461 221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADM 300

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 124487183 326 TSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMT 361
Cdd:PRK09461 301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-551 3.21e-23

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 3.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 491
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 492 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 551
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 9-361 4.90e-132

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 388.18  E-value: 4.90e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   9 RRLLAIYTGGTIGM-RSEGGvLVPGRG-LAAVLKTLHMFHDEEyaqahsLPEdtlvlppaspdqriiYTVLECQPLFDSS 86
Cdd:PRK09461   4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE------MPD---------------FTIHEYTPLIDSS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  87 DMTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461  62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 167 YVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRLYPG 246
Cdd:PRK09461 142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTIYPG 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 247 IPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDM 325
Cdd:PRK09461 221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADM 300

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 124487183 326 TSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMT 361
Cdd:PRK09461 301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 1.26e-108

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: 327.94  E-value: 1.26e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183    11 LLAIYTGGTIGMR--SEGGVLVPGRGLAAVLKTLhmfhdeeyaqahslpedtlvlpPASPDqRIIYTVLECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLALL----------------------PALPE-LADDIEVEQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183    89 TITEWVQIAQTIERHYAQ--YQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   167 Y--VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKS---HLVVHSSMEPDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRspfLLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   242 RLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIV 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 124487183   321 SGFDMTSEAALAKLSYVLGQpGLSLNDRK 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 9.01e-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: 322.99  E-value: 9.01e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   9 RRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLKtlhmfhdeeyaqahslpedtlVLPPASPDQRIIytvLECQPLFDSSDM 88
Cdd:cd08963    1 KKILLLYTGGTIASVKTEGGLAPALTAEELLS---------------------YLPELLEDCFIE---VEQLPNIDSSNM 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  89 TITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:cd08963   57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 169 IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLvvHSSMEPDVGLLRLYPGIP 248
Cdd:cd08963  137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLL 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 249 ASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAV-TSDYASGMAMAGAGIVSGFDMTS 327
Cdd:cd08963  215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIPGGDMTT 294

                        330
                 ....*....|....
gi 124487183 328 EAALAKLSYVLGQP 341
Cdd:cd08963  295 EAAVAKLMWLLGQT 308
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 3.90e-106

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: 321.70  E-value: 3.90e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  10 RLLAIYTGGTIGMR--SEGGVLVPGRGLAAVLKTLHMFHDeeYAQahslpedtlvlppaspdqriiYTVLECQPLfDSSD 87
Cdd:COG0252    5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAE--LAD---------------------IEVEQFANI-DSSN 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  88 MTITEWVQIAQTIERHYAQ-YQGFVVIHGTDTMAFAASVLSFMLEnLQKPVVLTGAQVPIHALWSDGRENLLGALLMA-- 164
Cdd:COG0252   61 MTPADWLALARRIEEALADdYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 165 GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKacGKSHLVVHSSMEPDVGLLRL 243
Cdd:COG0252  140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRR--PESELDLAPALLPRVAILKL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 244 YPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSGF 323
Cdd:COG0252  218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                        330       340       350
                 ....*....|....*....|....*....|.
gi 124487183 324 DMTSEAALAKLSYVLGQpGLSLNDRKKLLAK 354
Cdd:COG0252  296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 11-362 4.66e-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: 267.84  E-value: 4.66e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   11 LLAIYTGGTIGM-RSE-GGVLVPGrglaavlktlhmFHDEEyaQAHSLPEdtlVLPPASPDQRIIytvlecqPLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPV------------FTADE--LLSAVPE---LLDIANIDGEAL-------MNILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   89 TITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENlQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  169 ------IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLVVHSSMEPDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  243 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTkpDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNmNVYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 124487183  322 GFDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMTL 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 6.85e-71

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 225.50  E-value: 6.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   11 LLAIYTGGTIGMR--SEGGVLVPGRGLAAVLKTLhmfhdeeyaqahslpedtlvlppasPDQRIIYTV-LECQPLFDSSD 87
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPALTGEELLAAV-------------------------PELADIAEIeAEQVANIDSSN 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   88 MTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQY 167
Cdd:pfam00710  56 MTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASP 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124487183  168 --VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRE 217
Cdd:pfam00710 136 aaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-551 3.21e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 3.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 491
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 492 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 551
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 373-550 9.53e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 87.23  E-value: 9.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 373 MLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAfvELDRDLNlkDYSGQTPLHVAARRGHAAVVTMLLQ 452
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLK 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 453 RGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgteLCRLASRGDSEGLRAWWQAGADLGQPDYDGH 532
Cdd:PLN03192 580 HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                        170
                 ....*....|....*...
gi 124487183 533 CALQVAEAAGNADVVALL 550
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLL 674
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-490 2.80e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 2.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487183  412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRgADVDARNeDGQSPLLLAVRGRHQSVIGLLRAAGARL 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 3.36e-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: 43.73  E-value: 3.36e-06
                           10        20
                   ....*....|....*....|....*....
gi 124487183   431 GQTPLHVAARRGHAAVVTMLLQRGADVDA 459
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 412-460 4.48e-05

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: 46.34  E-value: 4.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVEL-DRDLNLKD----------YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 460
Cdd:cd22196   64 DTISLLLDIaEKTGNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHAR 123
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 429-460 4.64e-04

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: 43.15  E-value: 4.64e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 124487183  429 YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 460
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 9-361 4.90e-132

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 388.18  E-value: 4.90e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   9 RRLLAIYTGGTIGM-RSEGGvLVPGRG-LAAVLKTLHMFHDEEyaqahsLPEdtlvlppaspdqriiYTVLECQPLFDSS 86
Cdd:PRK09461   4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE------MPD---------------FTIHEYTPLIDSS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  87 DMTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461  62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 167 YVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKShLVVHSSMEPDVGLLRLYPG 246
Cdd:PRK09461 142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAPHGEGE-LIVHPITPQPIGVVTIYPG 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 247 IPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVSGFDM 325
Cdd:PRK09461 221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNmGGYATGNALAHAGVISGADM 300

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 124487183 326 TSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMT 361
Cdd:PRK09461 301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 1.26e-108

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: 327.94  E-value: 1.26e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183    11 LLAIYTGGTIGMR--SEGGVLVPGRGLAAVLKTLhmfhdeeyaqahslpedtlvlpPASPDqRIIYTVLECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLALL----------------------PALPE-LADDIEVEQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183    89 TITEWVQIAQTIERHYAQ--YQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINEALADdgYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   167 Y--VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKS---HLVVHSSMEPDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRspfLLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   242 RLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIV 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDpGYYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 124487183   321 SGFDMTSEAALAKLSYVLGQpGLSLNDRK 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 9.01e-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: 322.99  E-value: 9.01e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   9 RRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLKtlhmfhdeeyaqahslpedtlVLPPASPDQRIIytvLECQPLFDSSDM 88
Cdd:cd08963    1 KKILLLYTGGTIASVKTEGGLAPALTAEELLS---------------------YLPELLEDCFIE---VEQLPNIDSSNM 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  89 TITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:cd08963   57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 169 IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLvvHSSMEPDVGLLRLYPGIP 248
Cdd:cd08963  137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLL 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 249 ASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAV-TSDYASGMAMAGAGIVSGFDMTS 327
Cdd:cd08963  215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSdLSVYAVGQALLEAGVIPGGDMTT 294

                        330
                 ....*....|....
gi 124487183 328 EAALAKLSYVLGQP 341
Cdd:cd08963  295 EAAVAKLMWLLGQT 308
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 3.90e-106

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: 321.70  E-value: 3.90e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  10 RLLAIYTGGTIGMR--SEGGVLVPGRGLAAVLKTLHMFHDeeYAQahslpedtlvlppaspdqriiYTVLECQPLfDSSD 87
Cdd:COG0252    5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAE--LAD---------------------IEVEQFANI-DSSN 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  88 MTITEWVQIAQTIERHYAQ-YQGFVVIHGTDTMAFAASVLSFMLEnLQKPVVLTGAQVPIHALWSDGRENLLGALLMA-- 164
Cdd:COG0252   61 MTPADWLALARRIEEALADdYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 165 GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGAD-VTINRELVRKacGKSHLVVHSSMEPDVGLLRL 243
Cdd:COG0252  140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRR--PESELDLAPALLPRVAILKL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 244 YPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIVSGF 323
Cdd:COG0252  218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                        330       340       350
                 ....*....|....*....|....*....|.
gi 124487183 324 DMTSEAALAKLSYVLGQpGLSLNDRKKLLAK 354
Cdd:COG0252  296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
asnASE_I TIGR00519
L-asparaginase, type I; Two related families of asparaginase are designated type I and type II ...
 11-362 4.66e-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: 267.84  E-value: 4.66e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   11 LLAIYTGGTIGM-RSE-GGVLVPGrglaavlktlhmFHDEEyaQAHSLPEdtlVLPPASPDQRIIytvlecqPLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPV------------FTADE--LLSAVPE---LLDIANIDGEAL-------MNILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   89 TITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENlQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  169 ------IPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLVVHSSMEPDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  243 LYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTkpDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMAGAGIVS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNmNVYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 124487183  322 GFDMTSEAALAKLSYVLGQPgLSLNDRKKLLAKDLRGEMTL 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 6.85e-71

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 225.50  E-value: 6.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   11 LLAIYTGGTIGMR--SEGGVLVPGRGLAAVLKTLhmfhdeeyaqahslpedtlvlppasPDQRIIYTV-LECQPLFDSSD 87
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPALTGEELLAAV-------------------------PELADIAEIeAEQVANIDSSN 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   88 MTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQY 167
Cdd:pfam00710  56 MTPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASP 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124487183  168 --VIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRE 217
Cdd:pfam00710 136 aaRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 8-340 8.51e-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: 179.74  E-value: 8.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   8 ERRLLAIYTGGTIGMR---SEGGVlvpgrglAAVLKTlhmfhdEEYAQAhsLPEdtlVLPPASPDQRIIYTVLecqplfd 84
Cdd:cd08962   70 LPKVSIISTGGTIASRvdyRTGAV-------SPAFTA------EELLRA--IPE---LLDIANIKAEVLFNIL------- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  85 SSDMTITEWVQIAQTIERHY-AQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLM 163
Cdd:cd08962  125 SENMTPEYWVKIAEAVYKEIkEGADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLV 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 164 AGQYvIPEV------------CLffqnqLFRGNRTTKVDARRFAAFCSPNLPPLATV---GADVTINRELVRKacGKSHL 228
Cdd:cd08962  205 AASD-IAEVvvvmhgttsddyCL-----LHRGTRVRKMHTSRRDAFQSINDEPLAKVdppGKIEKLSKDYRKR--GDEEL 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 229 VVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD- 307
Cdd:cd08962  277 ELNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIE--GTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRVNLNv 354

                        330       340       350
                 ....*....|....*....|....*....|...
gi 124487183 308 YASGMAMAGAGIVSGFDMTSEAALAKLSYVLGQ 340
Cdd:cd08962  355 YSTGRELLKAGVIPGEDMLPETAYVKLMWVLGN 387
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
14-361 6.12e-49

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 175.03  E-value: 6.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  14 IYTGGTIGMRSE---GGVLvpgrglAAvlktlhmFHDEEYAQAhsLPEdtlVLPPASPDQRIIYTVLecqplfdSSDMTI 90
Cdd:PRK04183  81 LSTGGTIASKVDyrtGAVT------PA-------FTAEDLLRA--VPE---LLDIANIRGRVLFNIL-------SENMTP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  91 TEWVQIAQTIERHY-AQYQGFVVIHGTDTMAFAASVLSFMLeNLQKPVVLTGAQ----VPIhalwSDGRENLLGALLMA- 164
Cdd:PRK04183 136 EYWVEIAEAVYEEIkNGADGVVVAHGTDTMHYTAAALSFML-KTPVPIVFVGAQrssdRPS----SDAAMNLICAVLAAt 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 165 ---GQYVI-------PEVCLffqnqLFRGNRTTKVDARRFAAFCSPNLPPLATV----GADVTINRELVRKacGKSHLVV 230
Cdd:PRK04183 211 sdiAEVVVvmhgttsDDYCA-----LHRGTRVRKMHTSRRDAFQSINDKPLAKVdykeGKIEFLRKDYRKR--GEKELEL 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 231 HSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD-YA 309
Cdd:PRK04183 284 NDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIE--GTGLGHVSTDLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYS 361

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124487183 310 SGMAMAGAGIVSGFDMTSEAALAKLSYVLGQPGlSLNDRKKLLAKDLRGEMT 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 2.07e-47

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: 170.64  E-value: 2.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   14 IYTGGTIGMR--SEGGVLVPgrglaavlktlhMFHDEEYAQAhsLPEDTLVlppASPDQRIIYTVLecqplfdSSDMTIT 91
Cdd:TIGR02153  68 ISTGGTIASRvdYETGAVYP------------AFTAEELARA--VPELLEI---ANIKARAVFNIL-------SENMKPE 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   92 EWVQIAQTIERHY-AQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQyVIP 170
Cdd:TIGR02153 124 YWIKIAEAVAKALkEGADGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRSSDRPSSDAALNLICAVRAATS-PIA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  171 EV------------CLffqnqLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINR-ELVRKACGKSHLVVHSSMEPD 237
Cdd:TIGR02153 203 EVtvvmhgetsdtyCL-----VHRGVKVRKMHTSRRDAFQSINDIPIAKIDPDEGIEKlRIDYRRRGEKELELDDKFEEK 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  238 VGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD-YASGMAMAG 316
Cdd:TIGR02153 278 VALVKFYPGISPEIIEFLVDKGYKGIVIE--GTGLGHVSEDWIPSIKRATDDGVPVVMTSQCLYGRVNLNvYSTGRELLK 355

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 124487183  317 AGIVSGFDMTSEAALAKLSYVLGQPGlSLNDRKKLLAKDLRGEMT 361
Cdd:TIGR02153 356 AGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAGEIN 399
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 84-340 4.95e-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: 4.95e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  84 DSSDMTITEWVQIAQTIERHYAQ-YQGFVVIHGTDTMAFAASVLSFMLENlQKPVVLTGAQVPIHALWSDGRENLLGALL 162
Cdd:cd00411   56 ASEDITPDDWLKLAKEVAKLLDSdVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAVR 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 163 MA--GQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTI--NRELVRKACGKSHLVVHSSMEPDV 238
Cdd:cd00411  135 VAkdKDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYyqRKPARKHTDESEFDVSDIKSLPKV 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 239 GLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGaG 318
Cdd:cd00411  215 DIVYLYPGLSDDIYDALVDLGYKGIVLA--GTGNGSVPYDVFPVLSSASKRGVAVVRSSQVIYGGVDLNAEKVDLKAG-V 291

                        250       260
                 ....*....|....*....|..
gi 124487183 319 IVSGfDMTSEAALAKLSYVLGQ 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 6.54e-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: 147.66  E-value: 6.54e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  10 RLLAIYTGGTIGMRSEGGVLvpgrglaavlktlhmfhdeeyAQAHSLPEDTLV--LPPASPDQRIIYtvlecQPLF--DS 85
Cdd:cd08964    2 RIAVLATGGTIAGTADSSGA---------------------YAAPTLSGEELLaaVPGLADVADVEV-----EQVSnlPS 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  86 SDMTITEWVQIAQTIERHYAQ--YQGFVVIHGTDTM---AFAASvlsfMLENLQKPVVLTGAQVPIHALWSDGRENLLGA 160
Cdd:cd08964   56 SDMTPADWLALAARVNEALADpdVDGVVVTHGTDTLeetAYFLD----LTLDSDKPVVLTGAMRPADAPSADGPANLLDA 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 161 LLMAGQyviPE-----VCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRELVRKACGKShlvVHSSM 234
Cdd:cd08964  132 VRVAAS---PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVdGGKVRFYRRPARPHTLPS---EFDDE 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 235 EPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYA--SGM 312
Cdd:cd08964  206 LPRVDIVYAYAGADGALLDAAVAAGAKGIVIAGFGAGNVP--PALVEALERAVAKGIPVVRSSRVGNGRVLPVYGygGGA 283

                        330       340
                 ....*....|....*....|....*...
gi 124487183 313 AMAGAGIVSGFDMTSEAALAKLSYVLGQ 340
Cdd:cd08964  284 DLAEAGAIFAGDLSPQKARILLMLALAA 311
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 237-351 5.69e-31

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: 116.43  E-value: 5.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  237 DVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPtkPDLLQELRVAAEQGLIIVNCTHCLQGAVT-SDYASGMAMA 315
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNlGYYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 124487183  316 GAGIVSGFDMTSEAALAKLSYVLGQpGLSLNDRKKL 351
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-551 3.21e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 3.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 491
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 492 PQELEDvGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 551
Cdd:COG0666  181 ARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
423-551 1.98e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 423 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDvGTEL 502
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-KTAL 223

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 124487183 503 CRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQ 551
Cdd:COG0666  224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
 84-307 2.76e-20

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: 92.52  E-value: 2.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183   84 DSSDMTITEWVQIAQTIERHYA--QYQGFVVIHGTDTMAFAASVLSFMLeNLQKPVVLTGAQVPIHALWSDGRENLLGAL 161
Cdd:TIGR00520  81 GSQDMNEEVLLKLAKGINELLAsdDYDGIVITHGTDTLEETAYFLDLTV-KSDKPVVIVGAMRPATSVSADGPMNLYNAV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  162 LMAGQyviPE-----VCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRELVRKACGKSHLVVHSSME 235
Cdd:TIGR00520 160 SVAAN---PKsagrgVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIhNGKIDYYYPPVRKHTCDTPFSVSNLDE 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487183  236 --PDVGLLRLYPGIPASLVRTFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD 307
Cdd:TIGR00520 237 plPKVDIIYAYQNAPPLIVNAVLDAGAKGIVLA--GVGNGSLSAAGLKVNETAAKLGVPIVRSSRVGDGMVTPD 308
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
345-550 9.01e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 9.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 345 LNDRKKLLAKDLRGEMTLPATDVLLQDGMLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAFVELDRDL 424
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 425 NLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgTELCR 504
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLHL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 124487183 505 LASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 550
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ansB PRK11096
L-asparaginase II; Provisional
 85-307 2.15e-19

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 89.78  E-value: 2.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183  85 SSDMTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSfMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMA 164
Cdd:PRK11096  79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 165 G--QYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATV-GADVTINRELVRKACGKSHL-VVHSSMEPDVGL 240
Cdd:PRK11096 158 AdkASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIhNGKVDYQRTPARKHTTDTPFdVSKLNELPKVGI 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487183 241 LRLYPGIPASLVRTFLQPPLKGVVmeTFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSD 307
Cdd:PRK11096 238 VYNYANASDLPAKALVDAGYDGIV--SAGVGNGNLYKTVFDTLATAAKNGVAVVRSSRVPTGATTQD 302
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 373-550 9.53e-18

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 87.23  E-value: 9.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 373 MLGCRVAWLLSMNGSQEADTMKDVLLPGLALAAAHAGDLDTLQAfvELDRDLNlkDYSGQTPLHVAARRGHAAVVTMLLQ 452
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKA--KLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLK 579

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 453 RGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVgteLCRLASRGDSEGLRAWWQAGADLGQPDYDGH 532
Cdd:PLN03192 580 HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                        170
                 ....*....|....*...
gi 124487183 533 CALQVAEAAGNADVVALL 550
Cdd:PLN03192 657 TALQVAMAEDHVDMVRLL 674
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 423-498 9.62e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.62  E-value: 9.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 423 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRA-------AGARLSPQEL 495
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPDSF 186


                 ...
gi 124487183 496 EDV 498
Cdd:PTZ00322 187 TGK 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-490 2.80e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 2.80e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487183  412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRgADVDARNeDGQSPLLLAVRGRHQSVIGLLRAAGARL 490
Cdd:pfam12796  11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
Ank_5 pfam13857
Ankyrin repeats (many copies);
421-471 1.20e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 1.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124487183  421 DRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLA 471
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
433-483 8.46e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 8.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 124487183  433 TPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLL 483
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 431-462 8.52e-08

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: 48.44  E-value: 8.52e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 124487183  431 GQTPLHVAA-RRGHAAVVTMLLQRGADVDARNE 462
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
435-483 1.10e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.73  E-value: 1.10e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 124487183  435 LHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLL 483
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
412-490 6.54e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.11  E-value: 6.54e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARL 490
Cdd:COG0666  200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 417-488 1.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 1.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487183 417 FVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGA 488
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
423-461 1.55e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.55e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 124487183  423 DLNLKDYsGQTPLHVAARRGHAAVVTMLLQRGADVDARN 461
Cdd:pfam12796  54 DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 412-491 1.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 491
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
PHA03095 PHA03095
ankyrin-like protein; Provisional
 423-473 1.58e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 1.58e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124487183 423 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVR 473
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 431-459 3.36e-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: 43.73  E-value: 3.36e-06
                           10        20
                   ....*....|....*....|....*....
gi 124487183   431 GQTPLHVAARRGHAAVVTMLLQRGADVDA 459
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 490-553 6.49e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 6.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 490 LSPQELED------VGTELCRLASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALLQSF 553
Cdd:PTZ00322  68 LTTEEVIDpvvahmLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF 137
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-491 1.60e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAAR--RGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSV--IGLLRAAG 487
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAG 177


                 ....
gi 124487183 488 ARLS 491
Cdd:PHA03095 178 ADVY 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 431-552 1.85e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 431 GQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLspqELEDV--GTELCRLASR 508
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL---DIEDCcgCTPLIIAMAK 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 124487183 509 GDSEGLRAWWQAGADlgqPDYDGH--CALQVAEAAGN--ADVVALLQS 552
Cdd:PHA02875 179 GDIAICKMLLDSGAN---IDYFGKngCVAALCYAIENnkIDIVRLFIK 223
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 431-459 2.39e-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: 41.47  E-value: 2.39e-05
                          10        20
                  ....*....|....*....|....*....
gi 124487183  431 GQTPLHVAARRGHAAVVTMLLQRGADVDA 459
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 423-480 3.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 3.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 124487183 423 DLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVI 480
Cdd:PHA02876 170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTI 227
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 412-460 4.48e-05

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: 46.34  E-value: 4.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVEL-DRDLNLKD----------YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 460
Cdd:cd22196   64 DTISLLLDIaEKTGNLKEfvnaaytdsyYKGQTALHIAIERRNMHLVELLVQNGADVHAR 123
Ank_4 pfam13637
Ankyrin repeats (many copies);
412-451 4.61e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.61e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 124487183  412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLL 451
Cdd:pfam13637  15 ELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 424-550 7.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 7.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 424 LNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELEDVGTELC 503
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMI 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487183 504 RL----------------------ASRGDSEGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADVVALL 550
Cdd:PHA02874 108 KTildcgidvnikdaelktflhyaIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
 418-491 8.05e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 8.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487183 418 VELDRDLNLKDYSGQTPLHVAARRG--HAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLS 491
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 412-474 8.07e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 8.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRG 474
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCG 418
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 413-490 8.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 8.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487183 413 TLQAFVELDRDLNLKDYSGQTPLHVAARRG-HAAVVTMLLQRGADVDARNEDGQSPLLLAVrgRHQSVIGLLRAAGARL 490
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-488 1.25e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGH-AAVVTMLLQRGADVDARNEDGQSPLLLAVRGR--HQSVIGLLRAAGA 488
Cdd:PHA03095  64 DIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGA 143
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 412-473 2.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.34e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVR 473
Cdd:PHA02874 138 ESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 412-483 3.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 3.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRgRHQSVIGLL 483
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELL 241
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 429-460 4.64e-04

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: 43.15  E-value: 4.64e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 124487183  429 YSGQTPLHVAARRGHAAVVTMLLQRGADVDAR 460
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02917 PHA02917
ankyrin-like protein; Provisional
 422-472 7.50e-04

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 42.29  E-value: 7.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124487183 422 RDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAV 472
Cdd:PHA02917 443 KDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 412-512 9.55e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARN-EDGQSPLLL--AVRGRHQSVIGLLRAAGA 488
Cdd:PLN03192 636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPTELreLLQKRELGHSITIVDSVP 715

                         90       100
                 ....*....|....*....|....
gi 124487183 489 RLSPQELEDVGTELCRLASRGDSE 512
Cdd:PLN03192 716 ADEPDLGRDGGSRPGRLQGTSSDN 739
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 413-471 1.46e-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: 41.67  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 413 TLQAFVE----LDRDLNL----KDYSGQTPLHVAARRGHAAVVTMLLQRGADVDAR----------NED----GQSPLLL 470
Cdd:cd22194  115 ILLAFAEengiLDRFINAeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLAL 194


                 .
gi 124487183 471 A 471
Cdd:cd22194  195 A 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 412-462 2.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 2.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNE 462
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02741 PHA02741
hypothetical protein; Provisional
 414-484 2.99e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 2.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124487183 414 LQAFVELDRDLNLKD-YSGQTPLHVAA-RRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLR 484
Cdd:PHA02741  80 IDHLIELGADINAQEmLEGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILR 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 425-493 3.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 3.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 425 NLKDYSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAV-RGRHQSVIGLLRAAGARLSPQ 493
Cdd:PHA02878 195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAK 264
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 429-497 5.29e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. 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. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.48  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 429 YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNED-------------GQSPLLLAVRGRHQSVIGLLRAAGARLSPQEL 495
Cdd:cd21882   71 YQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEA 150


                 ..
gi 124487183 496 ED 497
Cdd:cd21882  151 QD 152
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 424-488 6.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 6.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487183 424 LNLKDYSGQTPLHVAARRGH-AAVVTMLLQRGADVDARNEDGQSPL-LLAVRGRHQSVIGLLRAAGA 488
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGA 332
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 429-505 7.22e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 7.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487183 429 YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGARLSPQELED--VGTELCRL 505
Cdd:PLN03192 620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdfSPTELREL 698
PHA03095 PHA03095
ankyrin-like protein; Provisional
 412-550 7.61e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 7.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 412 DTLQAFVELDRDLNLKDYSGQTPLHVAARRGH---AAVVTMLLQRGADVDARNEDGQSPLLLAVrgRHQSVIGLLR---A 485
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYL--YNATTLDVIKlliK 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487183 486 AGARLSpqELEDVGTELCRLASRGDS---EGLRAWWQAGADLGQPDYDGHCALQVAEAAGNADV--VALL 550
Cdd:PHA03095 106 AGADVN--AKDKVGRTPLHVYLSGFNinpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLL 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 423-488 7.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 7.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487183 423 DLNLKD-YSGQTPLHVAARRGHAAVVTMLLQRGADVDARNEDGQSPLLLAVRGRHQSVIGLLRAAGA 488
Cdd:PHA02878 159 DINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH