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Conserved domains on  [gi|70887531|gb|EAO00287|]
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6-phosphofructo-2-kinase/fructose-2,6-biphosphatase, putative [Trypanosoma cruzi]

Protein Classification

shikimate kinase; dephospho-CoA kinase( domain architecture ID 1056707)

shikimate kinase catalyzes the specific phosphorylation of the 3-hydroxylgroup of shikimic acid using ATP as a cosubstrate; dephospho-CoA kinase catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NK super family cl17190
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 499-714 1.63e-67

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


The actual alignment was detected with superfamily member pfam01591:

Pssm-ID: 450170  Cd Length: 223  Bit Score: 225.68  E-value: 1.63e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    499 PLVVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVFNAGNYRRRLlgVEGTSDAGFYDPNNANGKQMREKMAEFACEDLVE 578
Cdd:pfam01591   13 KTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSA--VKAYSNYEFFRPDNPEAMKIREQCALAALKDVLA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    579 FISRHRIAVGVFDATNTTKARREHLVEFFNK-AFKqrhmesrVMFIESICNDDTIITENILRAKCDNDDFKNVgDTSKVI 657
Cdd:pfam01591   91 YLNEESGQVAIFDATNTTRERRKNILDFAEEnGLK-------VFFLESICNDPEIIARNIKLVKFSSPDYKGK-PPEEAI 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 70887531    658 ASFRSRISEYEKVYEPLDRADD--LSFIRIIDVKRHVVMKNIPCGLASSIAFFLMNLHP 714
Cdd:pfam01591  163 DDFMKRLECYEKQYEPLDDEHDedLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHV 221
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 294-838 1.52e-40

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


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 160.06  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   294 DVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAaanrhssvchylmnviqrlmltqeqkkpqiQ 373
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA------------------------------E 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   374 RNNDAESVESTEKNVQRNTSFGvsstnnsmmqsthltsalrestcslptpslpldseigneqqnehgllssflTCLPPDm 453
Cdd:PTZ00322  157 ENGFREVVQLLSRHSQCHFELG---------------------------------------------------ANAKPD- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   454 iSLMRSRSALSANPIEAPlHEDESEFEEQGTLSnfssyttisgtvpLVVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVF 533
Cdd:PTZ00322  185 -SFTGKPPSLEDSPISSH-HPDFSAVPQPMMGS-------------LIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   534 NAGNYRRRLlgveGTSDAGFYDPNNAngKQMREKMAEFACEDLVEFISRHRiAVGVFDATNTTKARREHLvefFNKAFKQ 613
Cdd:PTZ00322  250 IHQAYRRRL----ERRGGAVSSPTGA--AEVEFRIAKAIAHDMTTFICKTD-GVAVLDGTNTTHARRMAL---LRAIRET 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   614 RHM-ESRVMFIESICNDDTIITENILRAKcdnddFKNVGDTSKVIASFRSRISEYEKVYEPLDRAD--DLSFIRIIDVKR 690
Cdd:PTZ00322  320 GLIrMTRVVFVEVVNNNSETIRRNVLRAK-----EMFPGAPEDFVDRYYEVIEQLEAVYKSLNPVTdcDLTYIRIEDTQT 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   691 HvVMKNIPCGLASSIAFFLMNLHPVAHPIYISLPGETEGEKNHMYGGDEHLTPLGNKFALALkrfilerhFPHMIVLHGT 770
Cdd:PTZ00322  395 F-SLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLTERGRAYSRAL--------FEYFQKEIST 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887531   771 nhSVLNTLKPLAQSLQEDSGDGADKVEEEENSAFSGITCQEELLCP---LPGLDSINYGLFSGRTVQWVRK 838
Cdd:PTZ00322  466 --TSFTVMSSCAKRCTETVHYFAEESILQQSTASAASSQSPSLNCRvlyFPTLDDINHGDCEGQLLSDVRR 534
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
220-354 3.65e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  220 ALPLLQVPAQDTNADSVIKKQNIAALICVLERQKFALQRQLKEIRKELSAQNIFSLVRASNASQLQYLLENKIcDVNKRD 299
Cdd:COG0666   39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARD 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 70887531  300 YNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYL 354
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 499-714 1.63e-67

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 225.68  E-value: 1.63e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    499 PLVVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVFNAGNYRRRLlgVEGTSDAGFYDPNNANGKQMREKMAEFACEDLVE 578
Cdd:pfam01591   13 KTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSA--VKAYSNYEFFRPDNPEAMKIREQCALAALKDVLA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    579 FISRHRIAVGVFDATNTTKARREHLVEFFNK-AFKqrhmesrVMFIESICNDDTIITENILRAKCDNDDFKNVgDTSKVI 657
Cdd:pfam01591   91 YLNEESGQVAIFDATNTTRERRKNILDFAEEnGLK-------VFFLESICNDPEIIARNIKLVKFSSPDYKGK-PPEEAI 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 70887531    658 ASFRSRISEYEKVYEPLDRADD--LSFIRIIDVKRHVVMKNIPCGLASSIAFFLMNLHP 714
Cdd:pfam01591  163 DDFMKRLECYEKQYEPLDDEHDedLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHV 221
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 294-838 1.52e-40

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 160.06  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   294 DVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAaanrhssvchylmnviqrlmltqeqkkpqiQ 373
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA------------------------------E 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   374 RNNDAESVESTEKNVQRNTSFGvsstnnsmmqsthltsalrestcslptpslpldseigneqqnehgllssflTCLPPDm 453
Cdd:PTZ00322  157 ENGFREVVQLLSRHSQCHFELG---------------------------------------------------ANAKPD- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   454 iSLMRSRSALSANPIEAPlHEDESEFEEQGTLSnfssyttisgtvpLVVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVF 533
Cdd:PTZ00322  185 -SFTGKPPSLEDSPISSH-HPDFSAVPQPMMGS-------------LIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   534 NAGNYRRRLlgveGTSDAGFYDPNNAngKQMREKMAEFACEDLVEFISRHRiAVGVFDATNTTKARREHLvefFNKAFKQ 613
Cdd:PTZ00322  250 IHQAYRRRL----ERRGGAVSSPTGA--AEVEFRIAKAIAHDMTTFICKTD-GVAVLDGTNTTHARRMAL---LRAIRET 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   614 RHM-ESRVMFIESICNDDTIITENILRAKcdnddFKNVGDTSKVIASFRSRISEYEKVYEPLDRAD--DLSFIRIIDVKR 690
Cdd:PTZ00322  320 GLIrMTRVVFVEVVNNNSETIRRNVLRAK-----EMFPGAPEDFVDRYYEVIEQLEAVYKSLNPVTdcDLTYIRIEDTQT 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   691 HvVMKNIPCGLASSIAFFLMNLHPVAHPIYISLPGETEGEKNHMYGGDEHLTPLGNKFALALkrfilerhFPHMIVLHGT 770
Cdd:PTZ00322  395 F-SLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLTERGRAYSRAL--------FEYFQKEIST 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887531   771 nhSVLNTLKPLAQSLQEDSGDGADKVEEEENSAFSGITCQEELLCP---LPGLDSINYGLFSGRTVQWVRK 838
Cdd:PTZ00322  466 --TSFTVMSSCAKRCTETVHYFAEESILQQSTASAASSQSPSLNCRvlyFPTLDDINHGDCEGQLLSDVRR 534
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-356 1.03e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  276 VRASNASQLQYLLENKIcDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYLM 355
Cdd:COG0666  128 AYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206


                 .
gi 70887531  356 N 356
Cdd:COG0666  207 E 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
220-354 3.65e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  220 ALPLLQVPAQDTNADSVIKKQNIAALICVLERQKFALQRQLKEIRKELSAQNIFSLVRASNASQLQYLLENKIcDVNKRD 299
Cdd:COG0666   39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARD 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 70887531  300 YNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYL 354
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-356 6.28e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 6.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    276 VRASNASQLQYLLENKiCDVNKRDYNGCTPLHVAALEGNEVIVRVLISFgADLMAVDNtGRTPLDWAAANRHSSVCHYLM 355
Cdd:pfam12796    5 AKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81


                   .
gi 70887531    356 N 356
Cdd:pfam12796   82 E 82
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 301-328 1.44e-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: 42.57  E-value: 1.44e-05
                            10        20
                    ....*....|....*....|....*...
gi 70887531     301 NGCTPLHVAALEGNEVIVRVLISFGADL 328
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
COG4639 COG4639
Predicted kinase [General function prediction only];
500-609 2.91e-05

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 45.21  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  500 LVVcMVGLPGRGKSFIAQRISRylnwkgvPCRVFNAGNYRRRLLGVEgtsdagfyDPNNANGkqmrekmaefACEDLVEF 579
Cdd:COG4639    4 LVV-LIGLPGSGKSTFARRLFA-------PTEVVSSDDIRALLGGDE--------NDQSAWG----------DVFQLAHE 57

                         90       100       110
                 ....*....|....*....|....*....|...
gi 70887531  580 ISRHRIAVG---VFDATNTTKARREHLVEFFNK 609
Cdd:COG4639   58 IARARLRAGrltVVDATNLQREARRRLLALARA 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 300-339 3.22e-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: 3.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 70887531  300 YNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPL 339
Cdd:cd22192  134 YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 501-553 6.91e-03

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 38.23  E-value: 6.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 70887531  501 VVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVFNAGNYRRRLlgvegTSDAGF 553
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGL-----NKDLGF 48
 
Name Accession Description Interval E-value
6PF2K pfam01591
6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2, ...
 499-714 1.63e-67

6-phosphofructo-2-kinase; This enzyme occurs as a bifunctional enzyme with fructose-2,6-bisphosphatase. The bifunctional enzyme catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. This enzyme contains a P-loop motif.


Pssm-ID: 396253  Cd Length: 223  Bit Score: 225.68  E-value: 1.63e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    499 PLVVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVFNAGNYRRRLlgVEGTSDAGFYDPNNANGKQMREKMAEFACEDLVE 578
Cdd:pfam01591   13 KTMIVMVGLPARGKTYISKKLTRYLNWLGVPTKVFNVGEYRRSA--VKAYSNYEFFRPDNPEAMKIREQCALAALKDVLA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    579 FISRHRIAVGVFDATNTTKARREHLVEFFNK-AFKqrhmesrVMFIESICNDDTIITENILRAKCDNDDFKNVgDTSKVI 657
Cdd:pfam01591   91 YLNEESGQVAIFDATNTTRERRKNILDFAEEnGLK-------VFFLESICNDPEIIARNIKLVKFSSPDYKGK-PPEEAI 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 70887531    658 ASFRSRISEYEKVYEPLDRADD--LSFIRIIDVKRHVVMKNIPCGLASSIAFFLMNLHP 714
Cdd:pfam01591  163 DDFMKRLECYEKQYEPLDDEHDedLSYIKMINVGQSIVVNNVQGYLQSRIVYYLMNIHV 221
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 294-838 1.52e-40

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 160.06  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   294 DVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAaanrhssvchylmnviqrlmltqeqkkpqiQ 373
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA------------------------------E 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   374 RNNDAESVESTEKNVQRNTSFGvsstnnsmmqsthltsalrestcslptpslpldseigneqqnehgllssflTCLPPDm 453
Cdd:PTZ00322  157 ENGFREVVQLLSRHSQCHFELG---------------------------------------------------ANAKPD- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   454 iSLMRSRSALSANPIEAPlHEDESEFEEQGTLSnfssyttisgtvpLVVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVF 533
Cdd:PTZ00322  185 -SFTGKPPSLEDSPISSH-HPDFSAVPQPMMGS-------------LIVIMVGLPGRGKTYVARQIQRYFQWNGLQSRIF 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   534 NAGNYRRRLlgveGTSDAGFYDPNNAngKQMREKMAEFACEDLVEFISRHRiAVGVFDATNTTKARREHLvefFNKAFKQ 613
Cdd:PTZ00322  250 IHQAYRRRL----ERRGGAVSSPTGA--AEVEFRIAKAIAHDMTTFICKTD-GVAVLDGTNTTHARRMAL---LRAIRET 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   614 RHM-ESRVMFIESICNDDTIITENILRAKcdnddFKNVGDTSKVIASFRSRISEYEKVYEPLDRAD--DLSFIRIIDVKR 690
Cdd:PTZ00322  320 GLIrMTRVVFVEVVNNNSETIRRNVLRAK-----EMFPGAPEDFVDRYYEVIEQLEAVYKSLNPVTdcDLTYIRIEDTQT 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   691 HvVMKNIPCGLASSIAFFLMNLHPVAHPIYISLPGETEGEKNHMYGGDEHLTPLGNKFALALkrfilerhFPHMIVLHGT 770
Cdd:PTZ00322  395 F-SLNNISGWMPSRLAYMLHNLNPTPMNLYLTRAGEYVDLLSGRIGGNSRLTERGRAYSRAL--------FEYFQKEIST 465

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70887531   771 nhSVLNTLKPLAQSLQEDSGDGADKVEEEENSAFSGITCQEELLCP---LPGLDSINYGLFSGRTVQWVRK 838
Cdd:PTZ00322  466 --TSFTVMSSCAKRCTETVHYFAEESILQQSTASAASSQSPSLNCRvlyFPTLDDINHGDCEGQLLSDVRR 534
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-356 1.03e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  276 VRASNASQLQYLLENKIcDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYLM 355
Cdd:COG0666  128 AYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206


                 .
gi 70887531  356 N 356
Cdd:COG0666  207 E 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
220-354 3.65e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  220 ALPLLQVPAQDTNADSVIKKQNIAALICVLERQKFALQRQLKEIRKELSAQNIFSLVRASNASQLQYLLENKIcDVNKRD 299
Cdd:COG0666   39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARD 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 70887531  300 YNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYL 354
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-354 2.12e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 2.12e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887531  276 VRASNASQLQYLLENKiCDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYL 354
Cdd:COG0666  161 AANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-356 6.28e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 6.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    276 VRASNASQLQYLLENKiCDVNKRDYNGCTPLHVAALEGNEVIVRVLISFgADLMAVDNtGRTPLDWAAANRHSSVCHYLM 355
Cdd:pfam12796    5 AKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81


                   .
gi 70887531    356 N 356
Cdd:pfam12796   82 E 82
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
230-354 7.93e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 7.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  230 DTNADSVIKKQNIAALICVLERQKFALQRQLKEIRKELSAQNIFSLVRASNASQLQYLLENKICDVNKRDYNGCTPLHVA 309
Cdd:COG0666   15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 70887531  310 ALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYL 354
Cdd:COG0666   95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
Ank_5 pfam13857
Ankyrin repeats (many copies);
287-342 3.13e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 3.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 70887531    287 LLENKICDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWA 342
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
304-354 4.72e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 4.72e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 70887531    304 TPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYL 354
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 281-405 7.84e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 7.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   281 ASQLQYLLENKIcDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSsvchylmnviqR 360
Cdd:PHA03095  237 RSLVLPLLIAGI-SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG-----------R 304

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 70887531   361 LMLTQEQKKPqiqrnnDAESVESTEKNVQRNTSFGVSSTNNSMMQ 405
Cdd:PHA03095  305 AVRAALAKNP------SAETVAATLNTASVAGGDIPSDATRLCVA 343
Ank_2 pfam12796
Ankyrin repeats (3 copies);
306-359 7.67e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 7.67e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 70887531    306 LHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYLMNVIQ 359
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
284-347 4.29e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 4.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 70887531  284 LQYLLENKIcDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRH 347
Cdd:COG0666  202 VKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264
PHA03095 PHA03095
ankyrin-like protein; Provisional
 287-339 9.06e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 9.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 70887531   287 LLENKIcDVNKRDYNGCTPLHVAALEGNEV-IVRVLISFGADLMAVDNTGRTPL 339
Cdd:PHA03095   69 LLEAGA-DVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPL 121
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 301-333 1.18e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 1.18e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 70887531    301 NGCTPLHVAALE-GNEVIVRVLISFGADLMAVDN 333
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 286-347 3.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 3.16e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70887531   286 YLLENKiCDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRH 347
Cdd:PHA03100  177 YLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
284-332 4.24e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 4.24e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 70887531    284 LQYLLENkiCDVNKRDyNGCTPLHVAALEGNEVIVRVLISFGADLMAVD 332
Cdd:pfam12796   46 VKLLLEH--ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-322 4.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 70887531    272 IFSLVRASNASQLQYLLENKIcDVNKRDYNGCTPLHVAALEGNEVIVRVLI 322
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 294-340 6.43e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 6.43e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 70887531   294 DVNKRDYNGCTPLHV--AALEGNEVIVRVLISFGADLMAVDNTGRTPLD 340
Cdd:PHA03095  109 DVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA03095 PHA03095
ankyrin-like protein; Provisional
 280-340 8.92e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 8.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 70887531   280 NASQLQYLLENKIcDVNKRDYNGCTPLHV------AALEgnevIVRVLISFGADLMAVDNTGRTPLD 340
Cdd:PHA03095  131 NPKVIRLLLRKGA-DVNALDLYGMTPLAVllksrnANVE----LLRLLIDAGADVYAVDDRFRSLLH 192
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 301-328 1.44e-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: 42.57  E-value: 1.44e-05
                            10        20
                    ....*....|....*....|....*...
gi 70887531     301 NGCTPLHVAALEGNEVIVRVLISFGADL 328
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
COG4639 COG4639
Predicted kinase [General function prediction only];
500-609 2.91e-05

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 45.21  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531  500 LVVcMVGLPGRGKSFIAQRISRylnwkgvPCRVFNAGNYRRRLLGVEgtsdagfyDPNNANGkqmrekmaefACEDLVEF 579
Cdd:COG4639    4 LVV-LIGLPGSGKSTFARRLFA-------PTEVVSSDDIRALLGGDE--------NDQSAWG----------DVFQLAHE 57

                         90       100       110
                 ....*....|....*....|....*....|...
gi 70887531  580 ISRHRIAVG---VFDATNTTKARREHLVEFFNK 609
Cdd:COG4639   58 IARARLRAGrltVVDATNLQREARRRLLALARA 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 294-343 1.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 70887531   294 DVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAA 343
Cdd:PHA02874  149 DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 501-608 1.52e-04

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 43.07  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531    501 VVCMVGLPGRGKSFIAQRISRYLnwkgvPCRVFNAGNYRRRLLGvEGTSDAGFYDPNNANGKQMREKMAEFACedlvefi 580
Cdd:pfam13671    1 LILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFG-EGRPSISYYTDATDRTYERLHELARIAL------- 67

                           90       100
                   ....*....|....*....|....*...
gi 70887531    581 sRHRIAVgVFDATNTTKARREHLVEFFN 608
Cdd:pfam13671   68 -RAGRPV-ILDATNLRRDERARLLALAR 93
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 301-328 2.24e-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: 39.16  E-value: 2.24e-04
                           10        20
                   ....*....|....*....|....*...
gi 70887531    301 NGCTPLHVAALEGNEVIVRVLISFGADL 328
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 294-350 6.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 6.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 70887531   294 DVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWA--AANRHSSV 350
Cdd:PHA02876  367 NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlcGTNPYMSV 425
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 269-350 8.88e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   269 AQNIFSLVRASNASQLQYLLENKIcDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHS 348
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKL-DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHH 604


                  ..
gi 70887531   349 SV 350
Cdd:PLN03192  605 KI 606
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 272-334 1.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887531   272 IFSLVRASNASQLQYLLeNKICDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNT 334
Cdd:PHA03100  196 LHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 285-342 1.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 70887531   285 QYLLENKIcDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWA 342
Cdd:PHA02876  162 EMLLEGGA-DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA 218
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 300-339 3.22e-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: 3.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 70887531  300 YNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPL 339
Cdd:cd22192  134 YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 272-355 4.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70887531   272 IFSLVRASNASQLQYLLENKICDVNKRDYNgCTPLHVAALEG-----NEVIVRVLISFGADLMAVDNTGRTPLDWAAANR 346
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNN-STPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117


                  ....*....
gi 70887531   347 hssVCHYLM 355
Cdd:PHA03100  118 ---SNSYSI 123
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 294-355 5.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 5.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70887531   294 DVNKRDYN-GCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSVCHYLM 355
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 499-553 6.01e-03

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 38.45  E-value: 6.01e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 70887531    499 PLVVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVFNAGNYRRRLlgvegTSDAGF 553
Cdd:pfam01583    2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGL-----NKDLGF 51
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 501-553 6.91e-03

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 38.23  E-value: 6.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 70887531  501 VVCMVGLPGRGKSFIAQRISRYLNWKGVPCRVFNAGNYRRRLlgvegTSDAGF 553
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGL-----NKDLGF 48
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 276-343 7.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 7.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 70887531   276 VRASNASQLQYLLENKICDVNKRDYNGCTPLHVAALEGNEVI-VRVLISFGADLMAVDNTGRTPLDWAA 343
Cdd:PHA02876  281 SQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQAS 349
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 279-350 8.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 8.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 70887531   279 SNASQLQYLLENKICDVNKRDYNGCTPLHVAALEGNEVIVRVLISFGADLMAVDNTGRTPLDWAAANRHSSV 350
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI 238
 
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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