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Conserved domains on  [gi|320461543|ref|NP_001073933|]
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60 kDa lysophospholipase isoform 1 [Homo sapiens]

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) ...
 9-361 5.61e-128

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: 378.16  E-value: 5.61e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   9 RRLLAVYTGGTIGM-RSELGvLVPGTG-LAAILRTLPMFHDEEhararglsedtlvLPpasrnqriLYTVLECQPLFDSS 86
Cdd:PRK09461   4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE-------------MP--------DFTIHEYTPLIDSS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  87 DMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461  62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 167 YVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKvDGKAGLVVHSSMEQDVGLLRLYPG 246
Cdd:PRK09461 142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAP-HGEGELIVHPITPQPIGVVTIYPG 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 247 IPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDM 325
Cdd:PRK09461 221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGADM 300

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 320461543 326 TSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 361
Cdd:PRK09461 301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
384-564 2.12e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 2.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 384 LLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTR 463
Cdd:COG0666   70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 464 DTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEEaGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEA 543
Cdd:COG0666  150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                        170       180
                 ....*....|....*....|.
gi 320461543 544 AGNLAVVAFLQSLEGAVGAQA 564
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKD 249
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 9-361 5.61e-128

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 378.16  E-value: 5.61e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   9 RRLLAVYTGGTIGM-RSELGvLVPGTG-LAAILRTLPMFHDEEhararglsedtlvLPpasrnqriLYTVLECQPLFDSS 86
Cdd:PRK09461   4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE-------------MP--------DFTIHEYTPLIDSS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  87 DMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461  62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 167 YVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKvDGKAGLVVHSSMEQDVGLLRLYPG 246
Cdd:PRK09461 142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAP-HGEGELIVHPITPQPIGVVTIYPG 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 247 IPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDM 325
Cdd:PRK09461 221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGADM 300

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 320461543 326 TSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 361
Cdd:PRK09461 301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 8.81e-100

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: 305.60  E-value: 8.81e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543    11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPmfhdeehararglsedtlvlppaSRNQRILYTVLECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLALLP-----------------------ALPELADDIEVEQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543    89 TIAEWVCLAQTIK--RHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   167 Y--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAG---LVVHSSMEQDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSpflLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   242 RLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVI 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDPGyYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 320461543   321 SGFDMTSEAALAKLSYVLGQpGLSLDVRK 349
Cdd:smart00870 296 SAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 3.39e-96

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: 296.27  E-value: 3.39e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  10 RLLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFHDEEHararglsedtlvlppasrnqrilYTVLECQPLfDSSD 87
Cdd:COG0252    5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAELAD-----------------------IEVEQFANI-DSSN 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  88 MTIAEWVCLAQTIKRHY-EQYHGFVVIHGTDTMAFAASMLSFMLEnLQKTVILTGAQVPIHALWSDGRENLLGALLMA-- 164
Cdd:COG0252   61 MTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 165 GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGAD-ITINRELVRKVDGKagLVVHSSMEQDVGLLRL 243
Cdd:COG0252  140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRPESE--LDLAPALLPRVAILKL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 244 YPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGF 323
Cdd:COG0252  218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                        330       340       350
                 ....*....|....*....|....*....|.
gi 320461543 324 DMTSEAALAKLSYVLGQpGLSLDVRKELLTK 354
Cdd:COG0252  296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 9-341 1.63e-95

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: 294.10  E-value: 1.63e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   9 RRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPmfHDEEHARarglsedtlvlppasrnqrilyTVLECQPLFDSSDM 88
Cdd:cd08963    1 KKILLLYTGGTIASVKTEGGLAPALTAEELLSYLP--ELLEDCF----------------------IEVEQLPNIDSSNM 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:cd08963   57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 169 IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLvvHSSMEQDVGLLRLYPGIP 248
Cdd:cd08963  137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLL 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 249 AALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDMTS 327
Cdd:cd08963  215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALLEAGVIPGGDMTT 294

                        330
                 ....*....|....
gi 320461543 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 4.42e-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: 268.22  E-value: 4.42e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   11 LLAVYTGGTIGM-RSE-LGVLVPGTGLAAILRTLPMFHDEEHARARGLsedtlvlppasrnqrilytvlecqPLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPVFTADELLSAVPELLDIANIDGEAL------------------------MNILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  169 ------IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  243 LYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTkpDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVIS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 320461543  322 GFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMTP 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 7.15e-67

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 215.10  E-value: 7.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFhdEEHARARGlsedtlvlppasrnqrilytvlECQPLFDSSDM 88
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPALTGEELLAAVPEL--ADIAEIEA----------------------EQVANIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQY- 167
Cdd:pfam00710  57 TPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPa 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 320461543  168 -VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRE 217
Cdd:pfam00710 137 aRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
384-564 2.12e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 2.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 384 LLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTR 463
Cdd:COG0666   70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 464 DTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEEaGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEA 543
Cdd:COG0666  150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                        170       180
                 ....*....|....*....|.
gi 320461543 544 AGNLAVVAFLQSLEGAVGAQA 564
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKD 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
408-496 2.34e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRgVDVNTRDtDGFSPLLLAVRGRHPGVIGLLR 487
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81


                  ....*....
gi 320461543  488 EAGASLSTQ 496
Cdd:pfam12796  82 EKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 407-553 3.31e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 486
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320461543 487 REAgASLSTQELeeAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFL 553
Cdd:PLN03192 611 YHF-ASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 433-461 1.33e-05

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: 42.19  E-value: 1.33e-05
                           10        20
                   ....*....|....*....|....*....
gi 320461543   433 NGQTPLHAAARGGHTEAVTMLLQRGVDVN 461
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 434-509 1.45e-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: 44.69  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  434 GQTPLHAAARGGHTEAVTMLLQRGVDVNTR----------DTDGF----SPLLLAVRGRHPGVIGLLREAGASLSTQelE 499
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA--D 205

                          90
                  ....*....|
gi 320461543  500 EAGTELCRLA 509
Cdd:TIGR00870 206 SLGNTLLHLL 215
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 408-497 1.52e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 408 AAHAGDVEALQALVE---------LGSDLglvdFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT-RDTDGF---SPLLLA 474
Cdd:cd22192   58 AALYDNLEAAVVLMEaapelvnepMTSDL----YQGETALHIAVVNQNLNLVRELIARGADVVSpRATGTFfrpGPKNLI 133

                         90       100       110
                 ....*....|....*....|....*....|...
gi 320461543 475 VRGRHP----------GVIGLLREAGASLSTQE 497
Cdd:cd22192  134 YYGEHPlsfaacvgneEIVRLLIEHGADIRAQD 166
 
Name Accession Description Interval E-value
ansA PRK09461
cytoplasmic asparaginase I; Provisional
 9-361 5.61e-128

cytoplasmic asparaginase I; Provisional


Pssm-ID: 181876 [Multi-domain]  Cd Length: 335  Bit Score: 378.16  E-value: 5.61e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   9 RRLLAVYTGGTIGM-RSELGvLVPGTG-LAAILRTLPMFHDEEhararglsedtlvLPpasrnqriLYTVLECQPLFDSS 86
Cdd:PRK09461   4 KSIYVAYTGGTIGMqRSDQG-YIPVSGhLQRQLALMPEFHRPE-------------MP--------DFTIHEYTPLIDSS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  87 DMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:PRK09461  62 DMTPEDWQHIADDIKANYDDYDGFVILHGTDTMAYTASALSFMLENLGKPVIVTGSQIPLAELRSDGQTNLLNALYVAAN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 167 YVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKvDGKAGLVVHSSMEQDVGLLRLYPG 246
Cdd:PRK09461 142 YPINEVTLFFNNKLFRGNRTTKAHADGFDAFASPNLPPLLEAGIHIRRLNTPPAP-HGEGELIVHPITPQPIGVVTIYPG 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 247 IPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDM 325
Cdd:PRK09461 221 ISAEVVRNFLRQPVKALILRSYGVGNAPQNPALLQELKEASERGIVVVNLTQCMSGKVNMGgYATGNALAHAGVISGADM 300

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 320461543 326 TSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMT 361
Cdd:PRK09461 301 TVEAALTKLHYLLSQE-LSTEEIRQAMQQNLRGELT 335
Asparaginase smart00870
Asparaginase, found in various plant, animal and bacterial cells; Asparaginase catalyses the ...
 11-349 8.81e-100

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: 305.60  E-value: 8.81e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543    11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPmfhdeehararglsedtlvlppaSRNQRILYTVLECQPLFDSSDM 88
Cdd:smart00870   1 ILVLYTGGTIAMKadPSTGAVGPTAGAEELLALLP-----------------------ALPELADDIEVEQVANIDSSNM 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543    89 TIAEWVCLAQTIK--RHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQ 166
Cdd:smart00870  58 TPEDWLKLAKRINeaLADDGYDGVVVTHGTDTLEETAYFLSLTLDSLDKPVVLTGAMRPATALSSDGPANLLDAVRVAAS 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   167 Y--VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAG---LVVHSSMEQDVGLL 241
Cdd:smart00870 138 PeaRGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNFGPLGYVDEGGVVYYTRPTRRHTKRSpflLDLKDALLPKVAIV 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   242 RLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVI 320
Cdd:smart00870 218 KAYPGMDAELLDALLDSGAKGLVLEGTGAGNVP--PDLLEALKEALERGIPVVRTSRCLSGRVDPGyYATGRDLAKAGVI 295

                          330       340
                   ....*....|....*....|....*....
gi 320461543   321 SGFDMTSEAALAKLSYVLGQpGLSLDVRK 349
Cdd:smart00870 296 SAGDLTPEKARIKLMLALGK-GLDPEEIR 323
AnsA COG0252
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ...
 10-354 3.39e-96

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: 296.27  E-value: 3.39e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  10 RLLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFHDEEHararglsedtlvlppasrnqrilYTVLECQPLfDSSD 87
Cdd:COG0252    5 KILVLATGGTIAMRadPAGYAVAPALSAEELLAAVPELAELAD-----------------------IEVEQFANI-DSSN 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  88 MTIAEWVCLAQTIKRHY-EQYHGFVVIHGTDTMAFAASMLSFMLEnLQKTVILTGAQVPIHALWSDGRENLLGALLMA-- 164
Cdd:COG0252   61 MTPADWLALARRIEEALaDDYDGVVVTHGTDTLEETAYALSLMLD-LPKPVVLTGAQRPADAPSSDGPANLLDAVRVAas 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 165 GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGAD-ITINRELVRKVDGKagLVVHSSMEQDVGLLRL 243
Cdd:COG0252  140 PEARGRGVLVVFNDEIHRARRVTKTHTSRVDAFQSPNYGPLGEVDEGrVRFYRRPPRRPESE--LDLAPALLPRVAILKL 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 244 YPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDYAAGMAMAGAGVISGF 323
Cdd:COG0252  218 YPGMDPALLDALLAAGVKGIVLEGTGAGNVP--PALLPALKRAIERGVPVVVTSRCPEGRVNGVYGGGRDLAEAGVISGG 295

                        330       340       350
                 ....*....|....*....|....*....|.
gi 320461543 324 DMTSEAALAKLSYVLGQpGLSLDVRKELLTK 354
Cdd:COG0252  296 DLTPEKARIKLMLALGQ-GLDPEEIRRLFET 325
L-asparaginase_I cd08963
Type I (cytosolic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) are ...
 9-341 1.63e-95

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: 294.10  E-value: 1.63e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   9 RRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPmfHDEEHARarglsedtlvlppasrnqrilyTVLECQPLFDSSDM 88
Cdd:cd08963    1 KKILLLYTGGTIASVKTEGGLAPALTAEELLSYLP--ELLEDCF----------------------IEVEQLPNIDSSNM 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:cd08963   57 TPEDWLRIARAIAENYDGYDGFVITHGTDTMAYTAAALSFLLQNLPKPVVLTGSQLPLGEPGSDARRNLRDALRAASSGS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 169 IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLvvHSSMEQDVGLLRLYPGIP 248
Cdd:cd08963  137 IRGVYVAFNGKLIRGTRARKVRTTSFDAFESINYPLLAEIGAGGLTLERLLQYEPLPSLF--YPDLDPNVFLLKLIPGLL 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 249 AALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVISGFDMTS 327
Cdd:cd08963  215 PAILDALLEKYPRGLILEGFGAGNIPYDGDLLAALEEATARGKPVVVTTQCPYGGSDLSvYAVGQALLEAGVIPGGDMTT 294

                        330
                 ....*....|....
gi 320461543 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 4.42e-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: 268.22  E-value: 4.42e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   11 LLAVYTGGTIGM-RSE-LGVLVPGTGLAAILRTLPMFHDEEHARARGLsedtlvlppasrnqrilytvlecqPLFDSSDM 88
Cdd:TIGR00519   4 ISIISTGGTIASkVDYrTGAVHPVFTADELLSAVPELLDIANIDGEAL------------------------MNILSENM 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYV 168
Cdd:TIGR00519  60 KPEYWVEIAEAVKKEYDDYDGFVITHGTDTMAYTAAALSFMLET-PKPVVFTGAQRSSDRPSSDAALNLLCAVRAATEYI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  169 ------IPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGLLR 242
Cdd:TIGR00519 139 aevtvcMHGVTLDFNCRLHRGVKVRKAHTSRRDAFASINAPPLAEINPDGIEYLNEVYRPRGEDELEVHDRLEEKVALIK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  243 LYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTkpDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMAGAGVIS 321
Cdd:TIGR00519 219 IYPGISPDIIRNYLSKGYKGIVIEGTGLGHAPQ--NKLQELQEASDRGVVVVMTTQCLNGRVNMNvYSTGRRLLQAGVIG 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 320461543  322 GFDMTSEAALAKLSYVLGQPgLSLDVRKELLTKDLRGEMTP 362
Cdd:TIGR00519 297 GEDMLPEVALVKLMWLLGQY-SDPEEAKKMMSKNIAGEIEP 336
Asparaginase pfam00710
Asparaginase, N-terminal; This is the N-terminal domain of this enzyme.
 11-217 7.15e-67

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


Pssm-ID: 459913 [Multi-domain]  Cd Length: 188  Bit Score: 215.10  E-value: 7.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   11 LLAVYTGGTIGMR--SELGVLVPGTGLAAILRTLPMFhdEEHARARGlsedtlvlppasrnqrilytvlECQPLFDSSDM 88
Cdd:pfam00710   1 VLILATGGTIASRadSSGGAVVPALTGEELLAAVPEL--ADIAEIEA----------------------EQVANIDSSNM 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   89 TIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQY- 167
Cdd:pfam00710  57 TPADWLRLARRIAEALDDYDGVVVTHGTDTLEETASALSFMLKNLGKPVVLTGSQRPSDEPSSDGPMNLLAALRVAASPa 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 320461543  168 -VIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRE 217
Cdd:pfam00710 137 aRGPGVLVVFNDKLHRARRVTKTHTSSLDAFDSPNFGPLGEVdGGQVELYRE 188
gatD_arch TIGR02153
glutamyl-tRNA(Gln) amidotransferase, subunit D; This peptide is found only in the Archaea. It ...
 74-365 1.93e-46

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: 167.94  E-value: 1.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   74 YTVLECQPLFD--SSDMTIAEWVCLAQTIKRHYEQYH-GFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALW 150
Cdd:TIGR02153 104 IANIKARAVFNilSENMKPEYWIKIAEAVAKALKEGAdGVVVAHGTDTMAYTAAALSFMFETLPVPVVLVGAQRSSDRPS 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  151 SDGRENLLGALLMAGQyVIPEV------------CLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATVGAD--ITINR 216
Cdd:TIGR02153 184 SDAALNLICAVRAATS-PIAEVtvvmhgetsdtyCL-----VHRGVKVRKMHTSRRDAFQSINDIPIAKIDPDegIEKLR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  217 ELVRKvDGKAGLVVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNC 296
Cdd:TIGR02153 258 IDYRR-RGEKELELDDKFEEKVALVKFYPGISPEIIEFLVDKGYKGIVIE--GTGLGHVSEDWIPSIKRATDDGVPVVMT 334

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  297 THCLQGAVTTD-YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDLRGEMTPPSV 365
Cdd:TIGR02153 335 SQCLYGRVNLNvYSTGRELLKAGVIPCEDMLPEVAYVKLMWVLGQTD-DLEEVRKMMRTNIAGEINERTL 403
GatD cd08962
GatD subunit of archaeal Glu-tRNA amidotransferase; GatD is involved in the alternative ...
 85-356 3.22e-44

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: 162.02  E-value: 3.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  85 SSDMTIAEWVCLAQTIKRHYEQ-YHGFVVIHGTDTMAFAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLM 163
Cdd:cd08962  125 SENMTPEYWVKIAEAVYKEIKEgADGVVVAHGTDTMHYTASALSFMLETLPVPVVFVGAQRSSDRPSSDAAMNLIAAVLV 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 164 AGQYvIPEV------------CLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATV---GADITINRELVRKvdGKAGL 228
Cdd:cd08962  205 AASD-IAEVvvvmhgttsddyCL-----LHRGTRVRKMHTSRRDAFQSINDEPLAKVdppGKIEKLSKDYRKR--GDEEL 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 229 VVHSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD- 307
Cdd:cd08962  277 ELNDKLEEKVALIKFYPGMDPEIIDFYVDKGYKGIVIE--GTGLGHVSEDLIPSIKKAIDDGIPVVMTSQCIYGRVNLNv 354

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 320461543 308 YAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDL 356
Cdd:cd08962  355 YSTGRELLKAGVIPGEDMLPETAYVKLMWVLGNTD-DLEEVRKLMLTNL 402
PRK04183 PRK04183
Glu-tRNA(Gln) amidotransferase subunit GatD;
14-365 4.64e-43

Glu-tRNA(Gln) amidotransferase subunit GatD;


Pssm-ID: 235245 [Multi-domain]  Cd Length: 419  Bit Score: 159.24  E-value: 4.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  14 VYTGGTIGMRSELgvlvpgtglaailRT---LPMFHDEEHARARGLSEDtlvlpPASRNQRILYTVLecqplfdSSDMTI 90
Cdd:PRK04183  81 LSTGGTIASKVDY-------------RTgavTPAFTAEDLLRAVPELLD-----IANIRGRVLFNIL-------SENMTP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  91 AEWVCLAQTIKRHYEQ-YHGFVVIHGTDTMAFAASMLSFMLeNLQKTVILTGAQ----VPIhalwSDGRENLLGALLMA- 164
Cdd:PRK04183 136 EYWVEIAEAVYEEIKNgADGVVVAHGTDTMHYTAAALSFML-KTPVPIVFVGAQrssdRPS----SDAAMNLICAVLAAt 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 165 ---GQYVI-------PEVCLffqnqLFRGNRATKVDARRFAAFCSPNLLPLATV----GADITINRELVRKVDGKagLVV 230
Cdd:PRK04183 211 sdiAEVVVvmhgttsDDYCA-----LHRGTRVRKMHTSRRDAFQSINDKPLAKVdykeGKIEFLRKDYRKRGEKE--LEL 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 231 HSSMEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YA 309
Cdd:PRK04183 284 NDKLEEKVALIKFYPGMDPEILDFYVDKGYKGIVIE--GTGLGHVSTDLIPSIKRATDDGIPVVMTSQCLYGRVNMNvYS 361

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 320461543 310 AGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGlSLDVRKELLTKDLRGEMTPPSV 365
Cdd:PRK04183 362 TGRDLLKAGVIPGEDMLPEVAYVKLMWVLGNTY-DLEEVRELMLTNLAGEINERSR 416
L-asparaginase_like cd00411
Bacterial L-asparaginases and related enzymes; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 10-340 1.43e-36

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: 138.80  E-value: 1.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  10 RLLAVYTGGTI----GMRSELGVLVPGTGLAAILRTLPMFHDEEHARARGLSEdtlvlppasrnqrilytvlecqplFDS 85
Cdd:cd00411    2 NITILATGGTIagvgDSATYSAYVAGALGVEKLIKAVPELKELANVKGEQLMN------------------------IAS 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  86 SDMTIAEWVCLAQTI-KRHYEQYHGFVVIHGTDTMAFAASMLSFMLENlQKTVILTGAQVPIHALWSDGRENLLGALLMA 164
Cdd:cd00411   58 EDITPDDWLKLAKEVaKLLDSDVDGIVITHGTDT*EETAYFLSLTLKN-DKPVVLVGAMRPSTAMSADGPFNLYNAVRVA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 165 --GQYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATVGADITI--NRELVRKVDGKAGLVVHSSMEQDVGL 240
Cdd:cd00411  137 kdKDSRGRGVLVVMNDKVHSGRDVSKTNTSGFDAFRSINYGPLGEIKDNKIYyqRKPARKHTDESEFDVSDIKSLPKVDI 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 241 LRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTDyaAGMAMAGAGVI 320
Cdd:cd00411  217 VYLYPGLSDDIYDALVDLGYKGIVLA--GTGNGSVPYDVFPVLSSASKRGVAVVRSSQVIYGGVDLN--AEKVDLKAGVI 292

                        330       340
                 ....*....|....*....|
gi 320461543 321 SGFDMTSEAALAKLSYVLGQ 340
Cdd:cd00411  293 PAGDLNPEKARVLLMWALTH 312
L-asparaginase_II cd08964
Type II (periplasmic) bacterial L-asparaginase; Asparaginases (amidohydrolases, E.C. 3.5.1.1) ...
 16-308 1.61e-35

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: 135.72  E-value: 1.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  16 TGGTIGMR--SELGVLVPGTGLAAILRTLPMFHDEEHARARGLSedtlvlppasrNQrilytvlecqplfDSSDMTIAEW 93
Cdd:cd08964    8 TGGTIAGTadSSGAYAAPTLSGEELLAAVPGLADVADVEVEQVS-----------NL-------------PSSDMTPADW 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  94 VCLAQTIKRHYEQ--YHGFVVIHGTDTM---AFAASMLsfmlENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQyv 168
Cdd:cd08964   64 LALAARVNEALADpdVDGVVVTHGTDTLeetAYFLDLT----LDSDKPVVLTGAMRPADAPSADGPANLLDAVRVAAS-- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 169 iPE-----VCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRKvdgKAGLVVHSSMEQDVGLLR 242
Cdd:cd08964  138 -PEargrgVLVVFNDEIHAARDVTKTHTTSLDAFASPGFGPLGYVdGGKVRFYRRPARP---HTLPSEFDDELPRVDIVY 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320461543 243 LYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTDY 308
Cdd:cd08964  214 AYAGADGALLDAAVAAGAKGIVIAGFGAGNVP--PALVEALERAVAKGIPVVRSSRVGNGRVLPVY 277
Asparaginase_C pfam17763
Glutaminase/Asparaginase C-terminal domain; This domain is found at the C-terminus of ...
 237-351 8.46e-29

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: 110.26  E-value: 8.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  237 DVGLLRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPtkPDLLQELRVATERGLVIVNCTHCLQGAVTTD-YAAGMAMA 315
Cdd:pfam17763   1 RVDILYLYPGMDPELLDAALAAGAKGIVIAGFGAGNVP--SALLDALKEAVARGIPVVRSSRCGSGRVNLGyYETGRDLL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 320461543  316 GAGVISGFDMTSEAALAKLSYVLGQpGLSLDVRKEL 351
Cdd:pfam17763  79 EAGVISGGDLTPEKARIKLMLALGK-GLDPEEIREL 113
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
384-564 2.12e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 2.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 384 LLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTR 463
Cdd:COG0666   70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 464 DTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEEaGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEA 543
Cdd:COG0666  150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG-ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                        170       180
                 ....*....|....*....|.
gi 320461543 544 AGNLAVVAFLQSLEGAVGAQA 564
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKD 249
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-554 3.97e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 3.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 486
Cdd:COG0666  126 LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320461543 487 REAGASLSTQElEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFLQ 554
Cdd:COG0666  206 LEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
383-553 1.66e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 1.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 383 WLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT 462
Cdd:COG0666   36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 463 RDTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQElEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAE 542
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                        170
                 ....*....|.
gi 320461543 543 AAGNLAVVAFL 553
Cdd:COG0666  195 ENGHLEIVKLL 205
asnASE_II TIGR00520
L-asparaginase, type II; Two related families of asparaginase (L-asparagine amidohydrolase, EC ...
 84-307 1.42e-16

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: 81.35  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543   84 DSSDMTIAEWVCLAQTIKRHYE--QYHGFVVIHGTDTMAFAASMLSFMLeNLQKTVILTGAQVPIHALWSDGRENLLGAL 161
Cdd:TIGR00520  81 GSQDMNEEVLLKLAKGINELLAsdDYDGIVITHGTDTLEETAYFLDLTV-KSDKPVVIVGAMRPATSVSADGPMNLYNAV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  162 LMAGQyviPE-----VCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRK--VDGKAGLVVHSS 233
Cdd:TIGR00520 160 SVAAN---PKsagrgVLVVLNDRIASGRYVTKTNTTSLDTFKSRNQGYLGYIhNGKIDYYYPPVRKhtCDTPFSVSNLDE 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 320461543  234 MEQDVGLLRLYPGIPAALVRAFLQPPLKGVVMEtfGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD 307
Cdd:TIGR00520 237 PLPKVDIIYAYQNAPPLIVNAVLDAGAKGIVLA--GVGNGSLSAAGLKVNETAAKLGVPIVRSSRVGDGMVTPD 308
ansB PRK11096
L-asparaginase II; Provisional
 85-307 2.15e-16

L-asparaginase II; Provisional


Pssm-ID: 182958 [Multi-domain]  Cd Length: 347  Bit Score: 80.92  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  85 SSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMAFAASMLSfMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMA 164
Cdd:PRK11096  79 SQDMNDEVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLD-LTVKCDKPVVLVGAMRPSTAMSADGPLNLYNAVVTA 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 165 G--QYVIPEVCLFFQNQLFRGNRATKVDARRFAAFCSPNLLPLATV-GADITINRELVRKVDGKAGLVVhSSMEQ--DVG 239
Cdd:PRK11096 158 AdkASANRGVLVAMNDTVLDGRDVTKTNTTDVQTFQSPNYGPLGYIhNGKVDYQRTPARKHTTDTPFDV-SKLNElpKVG 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320461543 240 LLRLYPGIPAALVRAFLQPPLKGVVmeTFGSGNGPTKPDLLQELRVATERGLVIVNCTHCLQGAVTTD 307
Cdd:PRK11096 237 IVYNYANASDLPAKALVDAGYDGIV--SAGVGNGNLYKTVFDTLATAAKNGVAVVRSSRVPTGATTQD 302
Ank_2 pfam12796
Ankyrin repeats (3 copies);
408-496 2.34e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRgVDVNTRDtDGFSPLLLAVRGRHPGVIGLLR 487
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81


                  ....*....
gi 320461543  488 EAGASLSTQ 496
Cdd:pfam12796  82 EKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
393-553 2.89e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 2.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 393 ADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLL 472
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 473 LAVRGRHPGVIGLLREAGASLSTQElEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAF 552
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171


                 .
gi 320461543 553 L 553
Cdd:COG0666  172 L 172
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 407-553 3.31e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.67  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 486
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 320461543 487 REAgASLSTQELeeAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFL 553
Cdd:PLN03192 611 YHF-ASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 406-486 2.74e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 406 CAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGL 485
Cdd:PTZ00322  87 CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 .
gi 320461543 486 L 486
Cdd:PTZ00322 167 L 167
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
407-491 4.20e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 4.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 407 AAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 486
Cdd:COG0666  192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271


                 ....*
gi 320461543 487 REAGA 491
Cdd:COG0666  272 LLALL 276
Ank_4 pfam13637
Ankyrin repeats (many copies);
403-454 1.35e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 1.35e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 320461543  403 SLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLL 454
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
407-464 1.37e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 1.37e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 320461543  407 AAAHAGDVEALQALVELGSdlGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRD 464
Cdd:pfam12796  36 LAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
436-486 1.10e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 320461543  436 TPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 486
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 413-493 2.37e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 413 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVT-MLLQRGVDVNTRDTDGFSPLLLAVRGR--HPGVIGLLREA 489
Cdd:PHA03095  62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK 141


                 ....
gi 320461543 490 GASL 493
Cdd:PHA03095 142 GADV 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
438-553 2.74e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  438 LHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLreagaslstqeLEEAGTELCrlayradlegl 517
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-----------LEHADVNLK----------- 58

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 320461543  518 qvwwqagadlgqpgYDGHSALHVAEAAGNLAVVAFL 553
Cdd:pfam12796  59 --------------DNGRTALHYAARSGHLEIVKLL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 381-495 1.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 381 VSWLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTE------------ 448
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgv 167

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 320461543 449 ------AVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLST 495
Cdd:PHA03100 168 dinaknRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 420-495 2.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 2.16e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 320461543 420 LVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLST 495
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 404-495 3.08e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 404 LACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGG--HTEAVTMLLQRGVDVNTRDTDGFSPL--LLAVRGRH 479
Cdd:PHA03095  87 LHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNAN 166

                         90
                 ....*....|....*.
gi 320461543 480 PGVIGLLREAGASLST 495
Cdd:PHA03095 167 VELLRLLIDAGADVYA 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
420-474 5.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 5.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 320461543  420 LVELGS-DLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLA 474
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 433-464 5.62e-07

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.13  E-value: 5.62e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 320461543  433 NGQTPLHAAA-RGGHTEAVTMLLQRGVDVNTRD 464
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 396-476 1.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 396 LRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198


                 .
gi 320461543 476 R 476
Cdd:PHA02874 199 E 199
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 415-497 1.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 415 EALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLS 494
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184


                 ...
gi 320461543 495 TQE 497
Cdd:PHA02874 185 VKD 187
PHA03095 PHA03095
ankyrin-like protein; Provisional
 420-476 1.91e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.91e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 320461543 420 LVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 408-508 3.84e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 408 AAHAGDVEALQALVELGSDLGLVDF-NGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 486
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110
                 ....*....|....*....|....*....|..
gi 320461543 487 REAGASLSTQE----------LEEAGTELCRL 508
Cdd:PHA02875 155 IDHKACLDIEDccgctpliiaMAKGDIAICKM 186
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 404-473 4.46e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 4.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320461543 404 LACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDT-DGFSPLLL 473
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPTEL 695
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 433-461 1.33e-05

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: 42.19  E-value: 1.33e-05
                           10        20
                   ....*....|....*....|....*....
gi 320461543   433 NGQTPLHAAARGGHTEAVTMLLQRGVDVN 461
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 417-494 2.02e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 417 LQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTM--LLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLS 494
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 433-462 3.20e-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: 3.20e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 320461543  433 NGQTPLHAAARGGHTEAVTMLLQRGVDVNT 462
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 413-541 3.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 413 DVEALQALVELGSDLGLVDFN-GQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGA 491
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 320461543 492 slSTQELEEAGTELCRLA--YRADLEGLQVWWQAGADLGQPGY-DGHSALHVA 541
Cdd:PHA02878 226 --STDARDKCGNTPLHISvgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 418-548 3.58e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 418 QALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLSTQE 497
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND 241

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 320461543 498 LeeagtELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLA 548
Cdd:PHA02876 242 L-----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLS 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 420-546 6.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 420 LVELGSDLGLVDFNGQTPLHAAARGGH-TEAVTMLLQRGVDVNTRDTDGFSPLLLA-VRGRHPGVIGLLREAGASLSTQE 497
Cdd:PHA02876 293 LLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARD 372

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 320461543 498 LEEAgTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGN 546
Cdd:PHA02876 373 YCDK-TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTN 420
PHA03095 PHA03095
ankyrin-like protein; Provisional
 413-493 1.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 413 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGH---TEAVTMLLQRGVDVNTRDTDGFSPLLLAVR-GRHPGVIGLLRE 488
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIK 105


                 ....*
gi 320461543 489 AGASL 493
Cdd:PHA03095 106 AGADV 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 434-509 1.45e-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: 44.69  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543  434 GQTPLHAAARGGHTEAVTMLLQRGVDVNTR----------DTDGF----SPLLLAVRGRHPGVIGLLREAGASLSTQelE 499
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTA--D 205

                          90
                  ....*....|
gi 320461543  500 EAGTELCRLA 509
Cdd:TIGR00870 206 SLGNTLLHLL 215
PHA02741 PHA02741
hypothetical protein; Provisional
 414-492 2.26e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.34  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 414 VEALQALVELGSDL-GLVDFNGQTPLHAAA-RGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGA 491
Cdd:PHA02741  77 AEIIDHLIELGADInAQEMLEGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVA 156


                 .
gi 320461543 492 S 492
Cdd:PHA02741 157 T 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 408-553 3.75e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVD-----------------------VNTRD 464
Cdd:PHA02874  42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmiktildcgidVNIKD 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 465 TDGFSPLLLAVRGRHPGVIGLLREAGASLSTQELEeaGTELCRLAYRAD-LEGLQVWWQAGADLGQPGYDGHSALHVAEA 543
Cdd:PHA02874 122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN--GCYPIHIAIKHNfFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                        170
                 ....*....|
gi 320461543 544 AGNLAVVAFL 553
Cdd:PHA02874 200 YGDYACIKLL 209
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 410-553 4.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 410 HAGDVEALQALVEL-GSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLRE 488
Cdd:PHA02874  10 YSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 489 AGASLSTQELEEAGTELCR-------------------LAY---RADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGN 546
Cdd:PHA02874  90 NGVDTSILPIPCIEKDMIKtildcgidvnikdaelktfLHYaikKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169


                 ....*..
gi 320461543 547 LAVVAFL 553
Cdd:PHA02874 170 FDIIKLL 176
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 415-475 5.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 5.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320461543 415 EALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 504-553 7.41e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 7.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 320461543 504 ELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHVAEAAGNLAVVAFL 553
Cdd:PTZ00322  85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
PHA02917 PHA02917
ankyrin-like protein; Provisional
 426-475 1.06e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.91  E-value: 1.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 320461543 426 DLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAV 475
Cdd:PHA02917 444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 408-462 1.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 320461543 408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT 462
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 408-497 1.52e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 408 AAHAGDVEALQALVE---------LGSDLglvdFNGQTPLHAAARGGHTEAVTMLLQRGVDVNT-RDTDGF---SPLLLA 474
Cdd:cd22192   58 AALYDNLEAAVVLMEaapelvnepMTSDL----YQGETALHIAVVNQNLNLVRELIARGADVVSpRATGTFfrpGPKNLI 133

                         90       100       110
                 ....*....|....*....|....*....|...
gi 320461543 475 VRGRHP----------GVIGLLREAGASLSTQE 497
Cdd:cd22192  134 YYGEHPlsfaacvgneEIVRLLIEHGADIRAQD 166
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 408-493 5.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAAR-GGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLL 486
Cdd:PHA02876 315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394


                 ....*..
gi 320461543 487 REAGASL 493
Cdd:PHA02876 395 LDYGADI 401
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 408-492 6.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.20  E-value: 6.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 408 AAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLR 487
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188


                 ....*
gi 320461543 488 EAGAS 492
Cdd:PHA02875 189 DSGAN 193
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 442-513 7.16e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 7.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320461543 442 ARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHPGVIGLLREAGASLSTqeLEEAGTELCRLAYRAD 513
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL--LDKDGKTPLELAEENG 159
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 392-493 7.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320461543 392 EADALRNALVPSLACAAAHAGDVEALQALVELGSDLGLVDFNGQTPLHAAARGG-HTEAVTMLLQRGVDVNTRDTDGFSP 470
Cdd:PHA02876 400 DIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP 479

                         90       100
                 ....*....|....*....|...
gi 320461543 471 LLLAVrGRHpGVIGLLREAGASL 493
Cdd:PHA02876 480 LLIAL-EYH-GIVNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 413-476 9.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 9.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 320461543 413 DVEALQALVELGSDLGLVDFNGQTPLHAAARGGH-TEAVTMLLQRGVDVNTRDTDGFSPLLLAVR 476
Cdd:PHA02876 252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
 
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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