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Conserved domains on  [gi|754347355|ref|XP_004347874|]
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glutaminase [Capsaspora owczarzaki ATCC 30864]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 157-441 1.48e-157

Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.


:

Pssm-ID: 461499  Cd Length: 283  Bit Score: 451.44  E-value: 1.48e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  157 GTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPSGRGFNSLTL 236
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  237 --NEAGRPHNPLINAGAIMICSLLHPlIELSDRFDHVIKMYRKMAGgKRVGFSNSTYLSERQTADRNFALGHYMKEKGAF 314
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIKG-ADPEERFERILDFLRKLAG-RELTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  315 ptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEFAFQIGLPAK 394
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 754347355  395 SGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYNFH 441
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
464-564 7.25e-19

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 7.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 464 ARDDELVTLLF-AASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEvIDINVLDRWGGTPLDDA 542
Cdd:COG0666   82 AKDDGGNTLLHaAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA 160

                         90       100
                 ....*....|....*....|..
gi 754347355 543 IRENHPAVIALLRTHGGKQNAR 564
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNAR 182
EF-hand_14 super family cl39396
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 58-135 1.49e-18

EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.


The actual alignment was detected with superfamily member pfam17959:

Pssm-ID: 465587  Cd Length: 90  Bit Score: 80.74  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355   58 QED-IFQSLAQNDAHHISKTDFLRALVSTGLLPDDPRLKEsmlLMQSVPEM--------------MDLATFKRCIAPNIL 122
Cdd:pfam17959   1 LEDlLFDLFRDEETDKLSVAKFLKALAATGIRKDDPRLAE---LMKNLKKAdqenseptdsetllLDRETFKKCIGSNIV 77

                          90
                  ....*....|...
gi 754347355  123 LIDRAFQGDLVIP 135
Cdd:pfam17959  78 LISKALKNQFVIP 90
 
Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 157-441 1.48e-157

Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.


Pssm-ID: 461499  Cd Length: 283  Bit Score: 451.44  E-value: 1.48e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  157 GTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPSGRGFNSLTL 236
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  237 --NEAGRPHNPLINAGAIMICSLLHPlIELSDRFDHVIKMYRKMAGgKRVGFSNSTYLSERQTADRNFALGHYMKEKGAF 314
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIKG-ADPEERFERILDFLRKLAG-RELTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  315 ptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEFAFQIGLPAK 394
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 754347355  395 SGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYNFH 441
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
149-441 6.88e-136

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 396.73  E-value: 6.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 149 DKVRA-NKSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPS 227
Cdd:COG2066    6 EKVRPyLGEGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERVGVEPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 228 GRGFNSLTL--NEAGRPHNPLINAGAIMICSLLHPLiELSDRFDHVIKMYRKMAGGKRVGFSNSTYLSERQTADRNFALG 305
Cdd:COG2066   86 GDPFNSIVQleLENGIPRNPMINAGAIVVTSLLPGR-SGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 306 HYMKEKGAFptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEF 385
Cdd:COG2066  165 YLLKSFGNL--ENDVEEVLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEF 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 754347355 386 AFQIGLPAKSGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYNFH 441
Cdd:COG2066  243 AYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 149-439 1.81e-118

glutaminase A; This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2). [Energy metabolism, Amino acids and amines]


Pssm-ID: 274797  Cd Length: 300  Bit Score: 352.56  E-value: 1.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  149 DKVRA-NKSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPS 227
Cdd:TIGR03814   6 EEARPlIGEGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERVGVEPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  228 GRGFNSLTL--NEAGRPHNPLINAGAIMICSLLHplIELSD-RFDHVIKMYRKMAGGKRVGFSNSTYLSERQTADRNFAL 304
Cdd:TIGR03814  86 GDPFNSIVQleLEPGKPRNPFINAGAIAVTSLLP--GRTSDeKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  305 GHYMKEKGAFptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGE 384
Cdd:TIGR03814 164 AYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 754347355  385 FAFQIGLPAKSGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYN 439
Cdd:TIGR03814 242 FAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKALELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 155-441 1.30e-109

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 329.81  E-value: 1.30e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 155 KSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPSGRGFNSL 234
Cdd:PRK00971  20 GQGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRVGKEPSGDPFNSL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 235 TLNEA--GRPHNPLINAGAIMICSLLhpLIELS-DRFDHVIKMYRKMAGGKRVGFSNSTYLSERQTADRNFALGHYMKEK 311
Cdd:PRK00971 100 VQLELeqGKPRNPMINAGAIVVTDLL--QGRLSeEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSF 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 312 GAFPTgtNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEFAFQIGL 391
Cdd:PRK00971 178 GNIEN--DVETVLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGL 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 754347355 392 PAKSGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYNFH 441
Cdd:PRK00971 256 PAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
464-564 7.25e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 7.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 464 ARDDELVTLLF-AASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEvIDINVLDRWGGTPLDDA 542
Cdd:COG0666   82 AKDDGGNTLLHaAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA 160

                         90       100
                 ....*....|....*....|..
gi 754347355 543 IRENHPAVIALLRTHGGKQNAR 564
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNAR 182
EF-hand_14 pfam17959
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 58-135 1.49e-18

EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.


Pssm-ID: 465587  Cd Length: 90  Bit Score: 80.74  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355   58 QED-IFQSLAQNDAHHISKTDFLRALVSTGLLPDDPRLKEsmlLMQSVPEM--------------MDLATFKRCIAPNIL 122
Cdd:pfam17959   1 LEDlLFDLFRDEETDKLSVAKFLKALAATGIRKDDPRLAE---LMKNLKKAdqenseptdsetllLDRETFKKCIGSNIV 77

                          90
                  ....*....|...
gi 754347355  123 LIDRAFQGDLVIP 135
Cdd:pfam17959  78 LISKALKNQFVIP 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
472-564 3.09e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  472 LLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLscEVIDINVLDRwGGTPLDDAIRENHPAVI 551
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 754347355  552 ALLRTHGGKQNAR 564
Cdd:pfam12796  78 KLLLEKGADINVK 90
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 470-557 3.50e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.07  E-value: 3.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 470 VTLLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEViDINVLDRWGGTPLDDAIRENHPA 549
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 754347355 550 VIALLRTH 557
Cdd:PTZ00322 163 VVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 500-530 2.49e-04

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: 38.34  E-value: 2.49e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 754347355   500 DGRTAIHLAASEGHLKVVEFLLScEVIDINV 530
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD-KGADINA 30
 
Name Accession Description Interval E-value
Glutaminase pfam04960
Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.
 157-441 1.48e-157

Glutaminase; This family of enzymes deaminates glutamine to glutamate EC:3.5.1.2.


Pssm-ID: 461499  Cd Length: 283  Bit Score: 451.44  E-value: 1.48e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  157 GTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPSGRGFNSLTL 236
Cdd:pfam04960   1 GKVADYIPELAKVDPDLFGIAICTVDGQVYSAGDADVPFTIQSISKVFTLALALEDLGGEEVFERVGVEPSGDPFNSLVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  237 --NEAGRPHNPLINAGAIMICSLLHPlIELSDRFDHVIKMYRKMAGgKRVGFSNSTYLSERQTADRNFALGHYMKEKGAF 314
Cdd:pfam04960  81 leLENGKPRNPMINAGAIAVTSLIKG-ADPEERFERILDFLRKLAG-RELTIDEEVYLSEKETGDRNRALAYLLKSFGNI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  315 ptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEFAFQIGLPAK 394
Cdd:pfam04960 159 --ENDVEEVLDLYFRQCSIEVTCRDLAVMGATLANGGVNPITGERVLSPEVVRRVLALMLTCGMYDASGEFAFRVGLPAK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 754347355  395 SGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYNFH 441
Cdd:pfam04960 237 SGVGGGILAVVPGKMGIAVFSPPLDEKGNSVRGVKALERLSEELGLH 283
GlsA COG2066
Glutaminase [Amino acid transport and metabolism];
149-441 6.88e-136

Glutaminase [Amino acid transport and metabolism];


Pssm-ID: 441669  Cd Length: 300  Bit Score: 396.73  E-value: 6.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 149 DKVRA-NKSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPS 227
Cdd:COG2066    6 EKVRPyLGEGKVADYIPELAKVDPDLFGIAVVTVDGEVYSAGDADTPFSIQSISKVFTLALALEDLGGEEVWERVGVEPS 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 228 GRGFNSLTL--NEAGRPHNPLINAGAIMICSLLHPLiELSDRFDHVIKMYRKMAGGKRVGFSNSTYLSERQTADRNFALG 305
Cdd:COG2066   86 GDPFNSIVQleLENGIPRNPMINAGAIVVTSLLPGR-SGDERFERILDFLRRLAGNRELSVDEEVYASEKATGDRNRALA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 306 HYMKEKGAFptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEF 385
Cdd:COG2066  165 YLLKSFGNL--ENDVEEVLDLYFRQCSIEVTCRDLARMGATLANGGVNPVTGERVISPEVARRVLALMLTCGMYDASGEF 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 754347355 386 AFQIGLPAKSGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYNFH 441
Cdd:COG2066  243 AYRVGLPAKSGVGGGIVAVVPGKMGIAVFSPRLDEKGNSVRGVKALERLSTELGLS 298
Gln_ase TIGR03814
glutaminase A; This family describes the enzyme glutaminase, from a larger family that ...
 149-439 1.81e-118

glutaminase A; This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2). [Energy metabolism, Amino acids and amines]


Pssm-ID: 274797  Cd Length: 300  Bit Score: 352.56  E-value: 1.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  149 DKVRA-NKSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPS 227
Cdd:TIGR03814   6 EEARPlIGEGKVADYIPALAKVDPNQFGIAVVTLDGEVFSAGDADVPFSIQSISKVFTLALALEDLGEDEVWERVGVEPS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  228 GRGFNSLTL--NEAGRPHNPLINAGAIMICSLLHplIELSD-RFDHVIKMYRKMAGGKRVGFSNSTYLSERQTADRNFAL 304
Cdd:TIGR03814  86 GDPFNSIVQleLEPGKPRNPFINAGAIAVTSLLP--GRTSDeKLERILEFVRKLAGNRSITIDEEVAQSERETGFRNRAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  305 GHYMKEKGAFptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGE 384
Cdd:TIGR03814 164 AYLLKSFGNL--ENDVEEVLDVYFKQCSIEMTCKDLARAGLFLANGGVNPLTGEQVISAEVAKRINALMLTCGLYDASGE 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 754347355  385 FAFQIGLPAKSGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYN 439
Cdd:TIGR03814 242 FAYRVGLPAKSGVGGGILAVVPGKMGIAVWSPALDEAGNSVAGQKALELLSEKLG 296
PRK00971 PRK00971
glutaminase; Provisional
 155-441 1.30e-109

glutaminase; Provisional


Pssm-ID: 234880  Cd Length: 307  Bit Score: 329.81  E-value: 1.30e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 155 KSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPSGRGFNSL 234
Cdd:PRK00971  20 GQGKVADYIPELAKVDPNKLGIAVCTVDGEVYSAGDADERFSIQSISKVFSLALALQHYGEEEVWQRVGKEPSGDPFNSL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 235 TLNEA--GRPHNPLINAGAIMICSLLhpLIELS-DRFDHVIKMYRKMAGGKRVGFSNSTYLSERQTADRNFALGHYMKEK 311
Cdd:PRK00971 100 VQLELeqGKPRNPMINAGAIVVTDLL--QGRLSeEPCERLLEFVRQLAGNPDILYDEVVASSELEHADRNAAIAYLMKSF 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 312 GAFPTgtNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEFAFQIGL 391
Cdd:PRK00971 178 GNIEN--DVETVLDTYFHQCALEMSCVDLARAGLFLANGGVSPHTGERVVSPRQARQVNALMLTCGMYDASGEFAYRVGL 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 754347355 392 PAKSGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGIEFCQRLIAKYNFH 441
Cdd:PRK00971 256 PAKSGVGGGILAVVPGEMAIAVWSPELDAKGNSLAGTAALERLSQRLGLS 305
PRK12356 PRK12356
glutaminase; Reviewed
 148-436 1.95e-84

glutaminase; Reviewed


Pssm-ID: 237073  Cd Length: 319  Bit Score: 265.68  E-value: 1.95e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 148 FDKVRANKSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPS 227
Cdd:PRK12356  18 YAQFKSDTGGKNADYIPALANVPSDLFGVAVVTTDGQVYSAGDSDYRFAIESISKVFTLALALEDVGPQAVREKIGADPT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 228 GRGFNSLT--LNEAGRPHNPLINAGAIMICSLLhPLIELSDRFDHVIKMYRKMAGgKRVGFSNSTYLSERQTADRNFALG 305
Cdd:PRK12356  98 GLPFNSVIaiELHGGKPLNPLVNAGAIATTSLV-PGANSDERWQRILDGQQRFAG-RELALSDEVYQSEQTTNFHNRAIA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 306 HYMKEKGAFptGTNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEF 385
Cdd:PRK12356 176 WLLYSYGRL--YCDPMEACDVYTRQCSTLVTARDLATMGATLAAGGVNPLTGKRVVDADNVPYILAEMTMEGLYERSGDW 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754347355 386 AFQIGLPAKSGVSGAMMVVVPNAMGIAIWSPPLDRFGNSVRGiefcQRLIA 436
Cdd:PRK12356 254 AYTVGLPGKSGVGGGILAVVPGKMGIAAFSPPLDSAGNSVRG----QKAVA 300
PRK12357 PRK12357
glutaminase; Reviewed
 155-428 8.79e-73

glutaminase; Reviewed


Pssm-ID: 237074  Cd Length: 326  Bit Score: 235.39  E-value: 8.79e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 155 KSGTVADYIPQLSRVSPNQFAVSVCTVDGQRFSMGESSTEFCLQSTCMPINYILALEEHGEERVHEHVGREPSGRGFNS- 233
Cdd:PRK12357  29 AEGRSASYIPALGEINVSQLGICIVKPDGTMIKSGDWEVPFTLQSISKVISFIAACLSRGISYVLERVDVEPTGDAFNSi 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 234 --LTLNEAGRPHNPLINAGAIMICSLLH---PLIELSDRFDHVIKMYrkmagGKRVGFSNSTYLSERQTADRNFALGHYM 308
Cdd:PRK12357 109 irLEIHKPGKPFNPMINAGAITVASLLPgtsVQEKLESLYVLIEKMI-----GKRPAINEEVFQSEWETAHRNRALAYYL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 309 KEKGAFPTgtNLMETLEFYFQLCSVEMTADSLSILAGTLANGGNCPITGESVVSSDAVKNALSVMYSCGMYDYSGEFAFQ 388
Cdd:PRK12357 184 KETGFLES--DVEETLEVYLKQCSIEVTTEDIALIGLILAHDGYHPIRKEQVIPKEVARLTKALMLTCGMYNASGKFAAF 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 754347355 389 IGLPAKSGVSGAMMVVVP----------NAMGIAIWSPPLDRFGNSVRGI 428
Cdd:PRK12357 262 VGLPAKSGVSGGIMTLVPpksrkdlpfqDGCGIGIYGPAIDEYGNSLPGI 311
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
464-564 7.25e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.32  E-value: 7.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 464 ARDDELVTLLF-AASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEvIDINVLDRWGGTPLDDA 542
Cdd:COG0666   82 AKDDGGNTLLHaAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA 160

                         90       100
                 ....*....|....*....|..
gi 754347355 543 IRENHPAVIALLRTHGGKQNAR 564
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNAR 182
EF-hand_14 pfam17959
EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.
 58-135 1.49e-18

EF-hand domain; This EF-hand domain is found at the N-terminus of the human glutaminase enzyme.


Pssm-ID: 465587  Cd Length: 90  Bit Score: 80.74  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355   58 QED-IFQSLAQNDAHHISKTDFLRALVSTGLLPDDPRLKEsmlLMQSVPEM--------------MDLATFKRCIAPNIL 122
Cdd:pfam17959   1 LEDlLFDLFRDEETDKLSVAKFLKALAATGIRKDDPRLAE---LMKNLKKAdqenseptdsetllLDRETFKKCIGSNIV 77

                          90
                  ....*....|...
gi 754347355  123 LIDRAFQGDLVIP 135
Cdd:pfam17959  78 LISKALKNQFVIP 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
464-564 2.04e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 2.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 464 ARDDELVTLL-FAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEViDINVLDRWGGTPLDDA 542
Cdd:COG0666  148 AQDNDGNTPLhLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLA 226

                         90       100
                 ....*....|....*....|..
gi 754347355 543 IRENHPAVIALLRTHGGKQNAR 564
Cdd:COG0666  227 AENGNLEIVKLLLEAGADLNAK 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
472-564 3.09e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355  472 LLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLscEVIDINVLDRwGGTPLDDAIRENHPAVI 551
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 754347355  552 ALLRTHGGKQNAR 564
Cdd:pfam12796  78 KLLLEKGADINVK 90
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 470-557 3.50e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.07  E-value: 3.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 470 VTLLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEViDINVLDRWGGTPLDDAIRENHPA 549
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 754347355 550 VIALLRTH 557
Cdd:PTZ00322 163 VVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
471-521 2.05e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 2.05e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 754347355  471 TLLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLL 521
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
464-569 1.78e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 464 ARDDELVT-LLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLScEVIDINVLDRWGGTPLDDA 542
Cdd:COG0666  181 ARDNDGETpLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGLTALLLA 259

                         90       100
                 ....*....|....*....|....*..
gi 754347355 543 IRENHPAVIALLRTHGGKQNARVVART 569
Cdd:COG0666  260 AAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_4 pfam13637
Ankyrin repeats (many copies);
501-554 1.65e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 754347355  501 GRTAIHLAASEGHLKVVEFLLsCEVIDINVLDRWGGTPLDDAIRENHPAVIALL 554
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 463-554 5.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 463 KARDDELVTLLFAAST---GDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGH--LKVVEFLLS--------CEV---- 525
Cdd:PHA03100 100 NAPDNNGITPLLYAISkksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDkgvdinakNRVnyll 179

                         90       100       110
                 ....*....|....*....|....*....|..
gi 754347355 526 ---IDINVLDRWGGTPLDDAIRENHPAVIALL 554
Cdd:PHA03100 180 sygVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 472-554 6.96e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 6.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 472 LLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLL--SCeviDINVLDRWGGTPLDDAIRENHPA 549
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLkhAC---NVHIRDANGNTALWNAISAKHHK 605


                 ....*
gi 754347355 550 VIALL 554
Cdd:PLN03192 606 IFRIL 610
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 472-564 7.72e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 7.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 472 LLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLL--SCEVIDINVLDRWGGTPLDDAIRENH-- 547
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImnGADVDKANTDDDFSPTELRELLQKRElg 705

                         90       100
                 ....*....|....*....|....*.
gi 754347355 548 ---------PAVIALLRTHGGKQNAR 564
Cdd:PLN03192 706 hsitivdsvPADEPDLGRDGGSRPGR 731
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 465-558 9.96e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 9.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 465 RDDELVTLL-FAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEVIdINVLDRWGGTPLDDAI 543
Cdd:PHA02874 120 KDAELKTFLhYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAA 198

                         90
                 ....*....|....*
gi 754347355 544 RENHPAVIALLRTHG 558
Cdd:PHA02874 199 EYGDYACIKLLIDHG 213
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 487-559 3.13e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 3.13e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754347355 487 LFLS-GVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEvIDINVLDRWGGTPLDDAIRENHPAVIALLRTHGG 559
Cdd:PHA03100 177 YLLSyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_5 pfam13857
Ankyrin repeats (many copies);
492-540 3.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 754347355  492 VNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEViDINVLDRWGGTPLD 540
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALD 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 500-533 7.83e-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. 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: 39.97  E-value: 7.83e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 754347355  500 DGRTAIHLAA-SEGHLKVVEFLLSCEViDINVLDR 533
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGA-DVNARDK 34
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-564 1.61e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.79  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 459 NKREKARDDELVTLLFAASTGDLSSVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLScEVIDINVLDRWGGTP 538
Cdd:COG0666   12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA-AGADINAKDDGGNTL 90

                         90       100
                 ....*....|....*....|....*.
gi 754347355 539 LDDAIRENHPAVIALLRTHGGKQNAR 564
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNAR 116
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 500-530 2.49e-04

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: 38.34  E-value: 2.49e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 754347355   500 DGRTAIHLAASEGHLKVVEFLLScEVIDINV 530
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD-KGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 459-556 3.53e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 459 NKREKARDDELVTLLFAASTGDLssVRRLFLSGVNLNEGDYDGRTAIH--LAASEGHLKVVEFLLScEVIDINVLDRWGG 536
Cdd:PHA03095  77 NAPERCGFTPLHLYLYNATTLDV--IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLR-KGADVNALDLYGM 153

                         90       100
                 ....*....|....*....|
gi 754347355 537 TPLDDAIReNHPAVIALLRT 556
Cdd:PHA03095 154 TPLAVLLK-SRNANVELLRL 172
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 500-530 6.79e-04

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: 37.24  E-value: 6.79e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 754347355  500 DGRTAIHLAASEGHLKVVEFLLSCEViDINV 530
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA-DINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 464-569 3.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 464 ARDDELVTLLFAASTGdlSSVRR-----LFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEViDINVLDRWGGTP 538
Cdd:PHA03095 217 ATDMLGNTPLHSMATG--SSCKRslvlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA-DINAVSSDGNTP 293

                         90       100       110
                 ....*....|....*....|....*....|..
gi 754347355 539 LDDAIR-ENHPAVIALLRTHggkQNARVVART 569
Cdd:PHA03095 294 LSLMVRnNNGRAVRAALAKN---PSAETVAAT 322
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 483-564 3.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 483 SVRRLFLSGVNLNEGDYDGRTAIHLAASEGHLKVVEFLLSCEViDINVLDRWGGTPLDDAIRENHPAVIALLRTHGGKQN 562
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184


                 ..
gi 754347355 563 AR 564
Cdd:PHA02874 185 VK 186
PHA03095 PHA03095
ankyrin-like protein; Provisional
 464-569 9.98e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 9.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754347355 464 ARDDELVTLL--FAASTGDLSSV-RRLFLSGVNLNEGDYDGRTAIHLAA---SEGHLKVVEFLLscEVIDINVLDRWGGT 537
Cdd:PHA03095 182 AVDDRFRSLLhhHLQSFKPRARIvRELIRAGCDPAATDMLGNTPLHSMAtgsSCKRSLVLPLLI--AGISINARNRYGQT 259

                         90       100       110
                 ....*....|....*....|....*....|...
gi 754347355 538 PLDDA-IRENHPAVIALLrthggKQNARVVART 569
Cdd:PHA03095 260 PLHYAaVFNNPRACRRLI-----ALGADINAVS 287
 
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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