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Conserved domains on  [gi|2041616053|emb|CAF3514305|]
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unnamed protein product [Didymodactylos carnosus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11430360)

ankyrin repeat (ANK) domain-containing protein mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-311 2.83e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 2.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 101 LNNFQNLPAITLAVREGDLRYVKELLNENMDLISKvDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRA 180
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 181 CYgdgtHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQ 260
Cdd:COG0666   161 AA----NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2041616053 261 ELSRHGDDAEERDNDGRTWIHYSVRKTEPLECLKSLLSPKTMLLRDTEGRT 311
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-378 5.73e-13

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 280 IHYSVRKtEPLECLKSLLSPKT-MLLRDTEGRTCLHVAAEQGSVLACRLIFDMGEKNsnktyiheVDNQKQTPLHIATKN 358
Cdd:pfam12796   1 LHLAAKN-GNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--------LKDNGRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 2041616053 359 GHARVLKELLDHGGDPQVRD 378
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 344-442 2.22e-04

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: 44.89  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 344 VDNQKQTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYALNRGLyfcRSVFEVYLRDKRGLMN---NSPRDS-- 418
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF---REVVQLLSRHSQCHFElgaNAKPDSft 187

                          90       100
                  ....*....|....*....|....*
gi 2041616053 419 -RPSTTRSFGNEASHDMFSNVaPSP 442
Cdd:PTZ00322  188 gKPPSLEDSPISSHHPDFSAV-PQP 211
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-311 2.83e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 2.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 101 LNNFQNLPAITLAVREGDLRYVKELLNENMDLISKvDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRA 180
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 181 CYgdgtHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQ 260
Cdd:COG0666   161 AA----NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2041616053 261 ELSRHGDDAEERDNDGRTWIHYSVRKTEPLECLKSLLSPKTMLLRDTEGRT 311
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 122-392 2.25e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 2.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 122 VKELLNENMDlISKVDSFGRDLLTYAVQFNQIN---ILKYLLEKQANVNTLANDGSTCLHraCYgdgtHCN---IDIVRL 195
Cdd:PHA03095   30 VRRLLAAGAD-VNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLH--LY----LYNattLDVIKL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 196 LLEYNADHAILDVHLRSPLHWSVLTENID--CLKLLIEYKANIHVKDVDGMTPAmwACHLDRFDHFQELSR----HGDDA 269
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNANVELLRllidAGADV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 270 EERDNDGRTWIHY---SVRKTEplECLKSLLSPK-TMLLRDTEGRTCLHVAAEQGSvlaCR--LIFDMGEKNSNktyIHE 343
Cdd:PHA03095  181 YAVDDRFRSLLHHhlqSFKPRA--RIVRELIRAGcDPAATDMLGNTPLHSMATGSS---CKrsLVLPLLIAGIS---INA 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2041616053 344 VDNQKQTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYALNRG 392
Cdd:PHA03095  253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-240 6.18e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 6.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 144 LTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRACYGDgthcNIDIVRLLLEynadHAILDV--HLRSPLHWSVLTE 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG----HLEIVKLLLE----HADVNLkdNGRTALHYAARSG 72

                          90
                  ....*....|....*....
gi 2041616053 222 NIDCLKLLIEYKANIHVKD 240
Cdd:pfam12796  73 HLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-378 5.73e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 280 IHYSVRKtEPLECLKSLLSPKT-MLLRDTEGRTCLHVAAEQGSVLACRLIFDMGEKNsnktyiheVDNQKQTPLHIATKN 358
Cdd:pfam12796   1 LHLAAKN-GNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--------LKDNGRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 2041616053 359 GHARVLKELLDHGGDPQVRD 378
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 113-368 1.62e-06

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: 52.01  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 113 AVREGDLRYVK-ELLNENMDLISKVDSFGRDLLTYAVQFNQINILKYLLEKQanvNTLANDGSTCLHRACYGDGTHCNiD 191
Cdd:TIGR00870  24 AAERGDLASVYrDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISLEYVDAVE-A 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 192 IVRLLL------------------EYNADHaildvhlrSPLHWSVLTENIDCLKLLIEYKANIHVKdvdgmtpamwaCHL 253
Cdd:TIGR00870 100 ILLHLLaafrksgplelandqytsEFTPGI--------TALHLAAHRQNYEIVKLLLERGASVPAR-----------ACG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 254 DRFdhfqelsrhgddaeeRDNDGRTWIHYSVRKTEPLECLKS-----LLS--PKTMLLRDTEGRTCLHVAAEQG------ 320
Cdd:TIGR00870 161 DFF---------------VKSQGVDSFYHGESPLNAAACLGSpsivaLLSedPADILTADSLGNTLLHLLVMENefkaey 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2041616053 321 SVLACR---LIFDMGEKNSNKTYIHEVDN-QKQTPLHIATKNGHARVLKELL 368
Cdd:TIGR00870 226 EELSCQmynFALSLLDKLRDSKELEVILNhQGLTPLKLAAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 347-374 6.24e-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: 40.65  E-value: 6.24e-05
                           10        20
                   ....*....|....*....|....*...
gi 2041616053  347 QKQTPLHIATKNGHARVLKELLDHGGDP 374
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 112-246 1.28e-04

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: 45.77  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 112 LAVREGDLRYVKELL-NENMDLISKvDSFGRDLLTYAVQFNQINILKYLLEkqaNVNTLAND--------GSTCLHRACY 182
Cdd:cd22192    23 LAAKENDVQAIKKLLkCPSCDLFQR-GALGETALHVAALYDNLEAAVVLME---AAPELVNEpmtsdlyqGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616053 183 GDgthcNIDIVRLLLEYNAD----HAILDVHLRS----------PLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTP 246
Cdd:cd22192    99 NQ----NLNLVRELIARGADvvspRATGTFFRPGpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 209-238 1.62e-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: 39.49  E-value: 1.62e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2041616053  209 HLRSPLHWSVLTENIDCLKLLIEYKANIHV 238
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 344-442 2.22e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 344 VDNQKQTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYALNRGLyfcRSVFEVYLRDKRGLMN---NSPRDS-- 418
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF---REVVQLLSRHSQCHFElgaNAKPDSft 187

                          90       100
                  ....*....|....*....|....*
gi 2041616053 419 -RPSTTRSFGNEASHDMFSNVaPSP 442
Cdd:PTZ00322  188 gKPPSLEDSPISSHHPDFSAV-PQP 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 310-392 2.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 310 RTCLHVAAEQGSVLACRLIFDMGeknsnkTYIHEVDNQK-QTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYA 388
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLG------KFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142


                  ....
gi 2041616053 389 LNRG 392
Cdd:PHA02875  143 VMMG 146
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 286-373 2.55e-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: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 286 KTEPLECLKSLL-SPKTMLL-RDTEGRTCLHVAAEQGSVLACRLIFDMGEKNSNKTYIHEVdNQKQTPLHIATKNGHARV 363
Cdd:cd22192    26 KENDVQAIKKLLkCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDL-YQGETALHIAVVNQNLNL 104

                          90
                  ....*....|
gi 2041616053 364 LKELLDHGGD 373
Cdd:cd22192   105 VRELIARGAD 114
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-311 2.83e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 2.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 101 LNNFQNLPAITLAVREGDLRYVKELLNENMDLISKvDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRA 180
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 181 CYgdgtHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQ 260
Cdd:COG0666   161 AA----NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2041616053 261 ELSRHGDDAEERDNDGRTWIHYSVRKTEPLECLKSLLSPKTMLLRDTEGRT 311
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-338 3.60e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053  98 KHSLNNFQNLPAITLAVREGDLRYVKELLNENMDLISKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCL 177
Cdd:COG0666    45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 178 HRACYgdgtHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFD 257
Cdd:COG0666   125 HLAAY----NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 258 HFQELSRHGDDAEERDNDGRTWIHYSVRKTEPLECLKSLLSPKTMLLRDTEGRTCLHVAAEQGSVLACRLIFDMGEKNSN 337
Cdd:COG0666   201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                  .
gi 2041616053 338 K 338
Cdd:COG0666   281 A 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-392 2.43e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 2.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 122 VKELLNENMDLISKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRACYGDgthcNIDIVRLLLEYNA 201
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAG----DLLVALLLLAAGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 202 DHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQELSRHGDDAEERDNDGRTWIH 281
Cdd:COG0666    79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 282 YSVRKtEPLECLKSLLSPKTML-LRDTEGRTCLHVAAEQGSVLACRLIFDMGEKNSNKtyihevDNQKQTPLHIATKNGH 360
Cdd:COG0666   159 LAAAN-GNLEIVKLLLEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK------DNDGKTALDLAAENGN 231

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2041616053 361 ARVLKELLDHGGDPQVRDVHGISSLDYALNRG 392
Cdd:COG0666   232 LEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
PHA03095 PHA03095
ankyrin-like protein; Provisional
 122-392 2.25e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 2.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 122 VKELLNENMDlISKVDSFGRDLLTYAVQFNQIN---ILKYLLEKQANVNTLANDGSTCLHraCYgdgtHCN---IDIVRL 195
Cdd:PHA03095   30 VRRLLAAGAD-VNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLH--LY----LYNattLDVIKL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 196 LLEYNADHAILDVHLRSPLHWSVLTENID--CLKLLIEYKANIHVKDVDGMTPAmwACHLDRFDHFQELSR----HGDDA 269
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNANVELLRllidAGADV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 270 EERDNDGRTWIHY---SVRKTEplECLKSLLSPK-TMLLRDTEGRTCLHVAAEQGSvlaCR--LIFDMGEKNSNktyIHE 343
Cdd:PHA03095  181 YAVDDRFRSLLHHhlqSFKPRA--RIVRELIRAGcDPAATDMLGNTPLHSMATGSS---CKrsLVLPLLIAGIS---INA 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2041616053 344 VDNQKQTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYALNRG 392
Cdd:PHA03095  253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-240 6.18e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 6.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 144 LTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRACYGDgthcNIDIVRLLLEynadHAILDV--HLRSPLHWSVLTE 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG----HLEIVKLLLE----HADVNLkdNGRTALHYAARSG 72

                          90
                  ....*....|....*....
gi 2041616053 222 NIDCLKLLIEYKANIHVKD 240
Cdd:pfam12796  73 HLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-207 2.73e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 112 LAVREGDLRYVKELLNENMDlISKVDSFGRDLLTYAVQFNQINILKYLLEKqANVNtLANDGSTCLHRACYgdgtHCNID 191
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAAR----SGHLE 75

                          90
                  ....*....|....*.
gi 2041616053 192 IVRLLLEYNADHAILD 207
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-273 3.92e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 3.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 177 LHRACYgdgtHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYkANIHVKDvDGMTPAMWACHLDRF 256
Cdd:pfam12796   1 LHLAAK----NGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 2041616053 257 DHFQELSRHGDDAEERD 273
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-378 5.73e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 280 IHYSVRKtEPLECLKSLLSPKT-MLLRDTEGRTCLHVAAEQGSVLACRLIFDMGEKNsnktyiheVDNQKQTPLHIATKN 358
Cdd:pfam12796   1 LHLAAKN-GNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--------LKDNGRTALHYAARS 71

                          90       100
                  ....*....|....*....|
gi 2041616053 359 GHARVLKELLDHGGDPQVRD 378
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 96-270 1.00e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053  96 VPKHSLNNFQNLPAITLAV-REGDLRYVKELLNENMDLISKVDSFGRDLLTYAVQ--FNQINILKYLLEKQANVNTLAND 172
Cdd:PHA03100   61 INSSTKNNSTPLHYLSNIKyNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 173 GSTCLH---RACYGD----------GTHCN-IDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHV 238
Cdd:PHA03100  141 GENLLHlylESNKIDlkilkllidkGVDINaKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2041616053 239 KDVDGMTPAMWACHLDRFDHFQELSRHGDDAE 270
Cdd:PHA03100  221 VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-389 2.77e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.99  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 113 AVREGDLRYVKELLNENMDlISKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLAndgSTCLhracygdgthcNIDI 192
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGAD-INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP---IPCI-----------EKDM 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 193 VRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQELSRHGDDAEER 272
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 273 DNDGRTWIHYSVRKTEpLECLKSLLSPKT-MLLRDTEGRTCLHVAAEQGSVLACRLIfdmgeknsNKTYIHEVDNQKQTP 351
Cdd:PHA02874  187 DNNGESPLHNAAEYGD-YACIKLLIDHGNhIMNKCKNGFTPLHNAIIHNRSAIELLI--------NNASINDQDIDGSTP 257

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2041616053 352 LHIATKNGHAR-VLKELLDHGGDPQVRDVHGISSLDYAL 389
Cdd:PHA02874  258 LHHAINPPCDIdIIDILLYHKADISIKDNKGENPIDTAF 296
Ank_2 pfam12796
Ankyrin repeats (3 copies);
214-298 2.52e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 214 LHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQELSRHGDdaEERDNDGRTWIHYSVRKtEPLECL 293
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARS-GHLEIV 77


                  ....*
gi 2041616053 294 KSLLS 298
Cdd:pfam12796  78 KLLLE 82
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 122-373 9.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 122 VKELLNENMDLISKVDSFGRDL----LTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHraCYGDGTHCNIDIVRLLL 197
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLhylsNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLL--YAISKKSNSYSIVEYLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 198 EYNADHAILDVHLRSPLHWSV--LTENIDCLKLLIEYKANIHVKDvdgmtpamwachldRFDHFQElsrHGDDAEERDND 275
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKN--------------RVNYLLS---YGVPINIKDVY 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 276 GRTWIHYSVRKTEPlECLKSLLspktmllrdtegrtclhvaaeqgsvlacrlifdmgEKNSNktyIHEVDNQKQTPLHIA 355
Cdd:PHA03100  192 GFTPLHYAVYNNNP-EFVKYLL-----------------------------------DLGAN---PNLVNKYGDTPLHIA 232

                         250
                  ....*....|....*...
gi 2041616053 356 TKNGHARVLKELLDHGGD 373
Cdd:PHA03100  233 ILNNNKEIFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-298 1.52e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 113 AVREGDLRYVKELLNENMDLISKvDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRAC-YGDgthcnID 191
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAeYGD-----YA 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 192 IVRLLLEYNADHAILDVHLRSPLHWSVLtENIDCLKLLIEyKANIHVKDVDGMTPAMWA----CHLDRFDhfqELSRHGD 267
Cdd:PHA02874  205 CIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLIN-NASINDQDIDGSTPLHHAinppCDIDIID---ILLYHKA 279

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2041616053 268 DAEERDNDGRTWIHYSVRKTEPLECLKSLLS 298
Cdd:PHA02874  280 DISIKDNKGENPIDTAFKYINKDPVIKDIIA 310
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 150-388 2.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.45  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 150 FNQINILKYLLEKQANVNTLANDGS-----TCLHRACygdgTHCNIDIVRLLLEYNADHAILDVHLRSPLH-----WSVL 219
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLNDYSykkpvLPLYLAK----EARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 220 TENIDCLKLLIEYKANIHVKDVDGMTPAMWA--CHLDRFDHFQELSRHGDDAEERDNDGRTWIHYSVRKTEP-LECLKSL 296
Cdd:PHA03100   83 TDVKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdLKILKLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 297 LSPKTmllrdtegrtclhvaaeqgsvlacrlifDMGEKN------SNKTYIHEVDNQKQTPLHIATKNGHARVLKELLDH 370
Cdd:PHA03100  163 IDKGV----------------------------DINAKNrvnyllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL 214

                         250
                  ....*....|....*...
gi 2041616053 371 GGDPQVRDVHGISSLDYA 388
Cdd:PHA03100  215 GANPNLVNKYGDTPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 36-357 4.98e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053  36 LHALHFLQQYYLVLQKRDKEQKPLQWTIERGLSPLTPFREAPDKFEW----QWISVDSNkVKQTvpkhslnNFQNLPAIT 111
Cdd:PHA02878    4 LYKSMYTDNYETILKYIEYIDHTENYSTSASLIPFIPLHQAVEARNLdvvkSLLTRGHN-VNQP-------DHRDLTPLH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 112 LAVREGDLRYVKELLNEnmdlISKVD-SFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTClhRACYGDGThcNI 190
Cdd:PHA02878   76 IICKEPNKLGMKEMIRS----INKCSvFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYID--KKSKDDII--EA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 191 DIVRLLLEYNADHAILDVH-LRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQELSRHGDDA 269
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 270 EERDNDGRTWIHYSVRKTEPLECLKSLL------SPKTMLLrdteGRTCLHVAAEQGSVLacRLIFDMGEKnsnktyIHE 343
Cdd:PHA02878  228 DARDKCGNTPLHISVGYCKDYDILKLLLehgvdvNAKSYIL----GLTALHSSIKSERKL--KLLLEYGAD------INS 295

                         330
                  ....*....|....
gi 2041616053 344 VDNQKQTPLHIATK 357
Cdd:PHA02878  296 LNSYKLTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 110-250 1.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 110 ITLAVREGDLRYVKELLNENMdlISKVDSFG-RDLLTYAVQFNQINILKYLLEkqanVNTLAND-----GSTCLHRACYG 183
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGA--IPDVKYPDiESELHDAVEEGDVKAVEELLD----LGKFADDvfykdGMTPLHLATIL 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2041616053 184 DgthcNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWA 250
Cdd:PHA02875  113 K----KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-197 3.83e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 3.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616053 140 GRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRACYgdgtHCNIDIVRLLL 197
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS----NGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
345-388 4.36e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 4.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2041616053 345 DNQKQTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYA 388
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
309-368 1.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 309 GRTCLHVAAEQGSVLACRLIFDmgeknsNKTYIHEVDNQKQTPLHIATKNGHARVLKELL 368
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE------KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 147-374 2.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 147 AVQFNQINILKYLLEKQANVNTLANDGSTCLHRACygdgTHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCL 226
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAM----KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 227 KLLIEykANIHVKDV---DGMTPAMWACHLDRFDHFQELSRHGDDAEerdndgrtwihysvrktepleclksllspktml 303
Cdd:PHA02875   85 EELLD--LGKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPD--------------------------------- 129

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2041616053 304 LRDTEGRTCLHVAAEQGSVLACRLIFDmgeknsNKTYIHEVDNQKQTPLHIATKNGHARVLKELLDHGGDP 374
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIKGIELLID------HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-168 4.51e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 4.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 109 AITLAVREGDLRYVKELLNENMdliSKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNT 168
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLEHAD---VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
173-230 1.24e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616053 173 GSTCLHRACYgdgtHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLI 230
Cdd:pfam13637   1 ELTALHAAAA----SGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 113-368 1.62e-06

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: 52.01  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 113 AVREGDLRYVK-ELLNENMDLISKVDSFGRDLLTYAVQFNQINILKYLLEKQanvNTLANDGSTCLHRACYGDGTHCNiD 191
Cdd:TIGR00870  24 AAERGDLASVYrDLEEPKKLNINCPDRLGRSALFVAAIENENLELTELLLNL---SCRGAVGDTLLHAISLEYVDAVE-A 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 192 IVRLLL------------------EYNADHaildvhlrSPLHWSVLTENIDCLKLLIEYKANIHVKdvdgmtpamwaCHL 253
Cdd:TIGR00870 100 ILLHLLaafrksgplelandqytsEFTPGI--------TALHLAAHRQNYEIVKLLLERGASVPAR-----------ACG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 254 DRFdhfqelsrhgddaeeRDNDGRTWIHYSVRKTEPLECLKS-----LLS--PKTMLLRDTEGRTCLHVAAEQG------ 320
Cdd:TIGR00870 161 DFF---------------VKSQGVDSFYHGESPLNAAACLGSpsivaLLSedPADILTADSLGNTLLHLLVMENefkaey 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2041616053 321 SVLACR---LIFDMGEKNSNKTYIHEVDN-QKQTPLHIATKNGHARVLKELL 368
Cdd:TIGR00870 226 EELSCQmynFALSLLDKLRDSKELEVILNhQGLTPLKLAAKEGRIVLFRLKL 277
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 114-466 6.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 6.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 114 VREGDLRYVKELLNENMDLISKvDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRACYGDGTHC----- 188
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAK-DIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTikaii 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 189 ------------------NIDIVRLLLEYNADHAI--LDVHLRSPLHWSVLTENIDCL-KLLIEYKANIHVKDVDGMTPa 247
Cdd:PHA02876  232 dnrsninkndlsllkairNEDLETSLLLYDAGFSVnsIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETP- 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 248 MWACHLDRFD--HFQELSRHGDDAEERDNDGRTWIHYSVRKTEPLECLKSLLS-PKTMLLRDTEGRTCLHVAAEQGSVLA 324
Cdd:PHA02876  311 LYLMAKNGYDteNIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLElGANVNARDYCDKTPIHYAAVRNNVVI 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 325 CRLIFDMGEK----------------------NSNKTYIHEVDNQK------QTPLHIATKNG-HARVLKELLDHGGDPQ 375
Cdd:PHA02876  391 INTLLDYGADiealsqkigtalhfalcgtnpyMSVKTLIDRGANVNsknkdlSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 376 VRDVHGISSLDYALN-RGLYFCRSVFEVYLRDKRGLmnnspRDSRPSTTRSFGNEASHDMFSNVAPSPPINGHANFIRRP 454
Cdd:PHA02876  471 AINIQNQYPLLIALEyHGIVNILLHYGAELRDSRVL-----HKSLNDNMFSFRYIIAHICIQDFIRHDIRNEVNPLKRVP 545

                         410
                  ....*....|..
gi 2041616053 455 TRATTDSVSFSQ 466
Cdd:PHA02876  546 TRFTSLRESFKE 557
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 152-353 6.36e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 49.91  E-value: 6.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 152 QINILKYLLEK-QANVNTLAND-GSTCLHraCYGDGTHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENI--DCLK 227
Cdd:PHA02716  154 DLDLIKYMVDVgIVNLNYVCKKtGYGILH--AYLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIK 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 228 LLIEYKANIHVKDVDGMTPAM-WACHLDRFDhfQELSR----HGDDAEERDNDGRTWIHYSVRKTEPLECLKSLLSPKTM 302
Cdd:PHA02716  232 KIIELGGDMDMKCVNGMSPIMtYIINIDNIN--PEITNiyieSLDGNKVKNIPMILHSYITLARNIDISVVYSFLQPGVK 309

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2041616053 303 L-LRDTEGRTCLH--VAAEQGSVLACRLIFDMGeknsnkTYIHEVDNQKQTPLH 353
Cdd:PHA02716  310 LhYKDSAGRTCLHqyILRHNISTDIIKLLHEYG------NDLNEPDNIGNTVLH 357
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-160 3.91e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2041616053 106 NLPAITLAVREGDLRYVKELLNENMDlISKVDSFGRDLLTYAVQFNQINILKYLL 160
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-260 4.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2041616053 211 RSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWAChldRFDHFQ 260
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA---SNGNVE 48
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 146-285 6.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 46.66  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 146 YAVQFNQINILKYLLEKQANVNTLAN-DGSTCLHraCYGDGTHCNIDIVRLLLEYNADH---------AILDVHLR---- 211
Cdd:PHA02989  117 YNSNINNCDMLRFLLSKGINVNDVKNsRGYNLLH--MYLESFSVKKDVIKILLSFGVNLfektslyglTPMNIYLRndid 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 212 --------------------SPLHWSVLTENID--------CLKLL--IEYKANIHVKDVDGMTPAMWACHLDRFDHFQE 261
Cdd:PHA02989  195 visikvikylikkgvnietnNNGSESVLESFLDnnkilskkEFKVLnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNY 274

                         170       180
                  ....*....|....*....|....
gi 2041616053 262 LSRHGDDAEERDNDGRTWIHYSVR 285
Cdd:PHA02989  275 LLKLGDDIYNVSKDGDTVLTYAIK 298
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 347-374 6.24e-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: 40.65  E-value: 6.24e-05
                           10        20
                   ....*....|....*....|....*...
gi 2041616053  347 QKQTPLHIATKNGHARVLKELLDHGGDP 374
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02795 PHA02795
ankyrin-like protein; Provisional
 133-232 8.18e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 8.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 133 ISKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHRAcygdgthcnIDIVRLLLEYNADHAILDVHLRS 212
Cdd:PHA02795  214 INQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVA---------VDRGSVIARRETHLKILEILLRE 284

                          90       100
                  ....*....|....*....|....*...
gi 2041616053 213 PLHWSVL--------TENIDCLKLLIEY 232
Cdd:PHA02795  285 PLSIDCIklailnntIENHDVIKLCIKY 312
PHA02792 PHA02792
ankyrin-like protein; Provisional
 111-235 1.07e-04

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 46.10  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 111 TLAVREGDLRYVKELLNENMDLISKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCLHrACYGDGTHCNI 190
Cdd:PHA02792  381 TLSIHESDVLSILKLCKPYIDDINKIDKHGRSILYYCIESHSVSLVEWLIDNGADINITTKYGSTCIG-ICVILAHACIP 459

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2041616053 191 DIVRLLLEynadhaILDVHL-RSPlhwsvlteNIDCLKLLIEYKAN 235
Cdd:PHA02792  460 EIAELYIK------ILEIILsKLP--------TIECIKKTVDYLSN 491
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 349-378 1.17e-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. 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: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2041616053 349 QTPLHIA-TKNGHARVLKELLDHGGDPQVRD 378
Cdd:pfam00023   3 NTPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 193-265 1.22e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2041616053 193 VRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDRFDHFQELSRH 265
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 112-246 1.28e-04

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: 45.77  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 112 LAVREGDLRYVKELL-NENMDLISKvDSFGRDLLTYAVQFNQINILKYLLEkqaNVNTLAND--------GSTCLHRACY 182
Cdd:cd22192    23 LAAKENDVQAIKKLLkCPSCDLFQR-GALGETALHVAALYDNLEAAVVLME---AAPELVNEpmtsdlyqGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616053 183 GDgthcNIDIVRLLLEYNAD----HAILDVHLRS----------PLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTP 246
Cdd:cd22192    99 NQ----NLNLVRELIARGADvvspRATGTFFRPGpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 99-297 1.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053  99 HSLNNFQNLPaITLAVREGDL-RYVKELLNENMDLISKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGSTCL 177
Cdd:PHA02876  267 NSIDDCKNTP-LHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 178 HRACYGDGthcNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWA-CHLDRF 256
Cdd:PHA02876  346 HQASTLDR---NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPY 422

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2041616053 257 DHFQELSRHGDDAEERDNDGRTWIHYSVRKTEPLECLKSLL 297
Cdd:PHA02876  423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLL 463
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 209-238 1.62e-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: 39.49  E-value: 1.62e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2041616053  209 HLRSPLHWSVLTENIDCLKLLIEYKANIHV 238
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 344-442 2.22e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 344 VDNQKQTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYALNRGLyfcRSVFEVYLRDKRGLMN---NSPRDS-- 418
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF---REVVQLLSRHSQCHFElgaNAKPDSft 187

                          90       100
                  ....*....|....*....|....*
gi 2041616053 419 -RPSTTRSFGNEASHDMFSNVaPSP 442
Cdd:PTZ00322  188 gKPPSLEDSPISSHHPDFSAV-PQP 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 310-392 2.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 310 RTCLHVAAEQGSVLACRLIFDMGeknsnkTYIHEVDNQK-QTPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYA 388
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLG------KFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142


                  ....
gi 2041616053 389 LNRG 392
Cdd:PHA02875  143 VMMG 146
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 88-198 4.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053  88 DSNKVKQTVPKHSLNNFQNLPAI--TLAVREGDLRYVKELLNENMDLISKVDSFGRDLLTYAVQFNQ---INILKYLLEK 162
Cdd:PHA02859   33 DIEGVKKWIKFVNDCNDLYETPIfsCLEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSFNKnvePEILKILIDS 112

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2041616053 163 QANVNTLANDGSTCLHRacYGDGTHCNIDIVRLLLE 198
Cdd:PHA02859  113 GSSITEEDEDGKNLLHM--YMCNFNVRINVIKLLID 146
Ank_5 pfam13857
Ankyrin repeats (many copies);
159-215 5.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 5.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2041616053 159 LLE-KQANVNTLANDGSTCLHRACYGDgthcNIDIVRLLLEYNADHAILDVHLRSPLH 215
Cdd:pfam13857   1 LLEhGPIDLNRLDGEGYTPLHVAAKYG----ALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 112-244 5.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 112 LAVREGDLRYVKELLNENMDLiSKVDSFGRDLLTYAVQFNQINILKYLLEKQANVNTLANDGstCLHRACYGDGTHcNID 191
Cdd:PHA02875  141 LAVMMGDIKGIELLIDHKACL-DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG--CVAALCYAIENN-KID 216

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2041616053 192 IVRLLLEYNADHAILdvhlrsplhWSVLTENIDCLKLLIEYKANIHVKDVDGM 244
Cdd:PHA02875  217 IVRLFIKRGADCNIM---------FMIEGEECTILDMICNMCTNLESEAIDAL 260
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 189-396 6.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 6.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 189 NIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTPAMWACHLDrfdhfqelsrHGDD 268
Cdd:PHA02874   47 DAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILD----------CGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 269 AEERDNDGRTWIHYSVRKTEpLECLKSLLSPKTmllrdtegrtclhvaaeqgsvlacrlifDMGEKNSNKTYihevdnqk 348
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGD-LESIKMLFEYGA----------------------------DVNIEDDNGCY-------- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2041616053 349 qtPLHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYALNRGLYFC 396
Cdd:PHA02874  160 --PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 172-207 6.88e-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. 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: 38.04  E-value: 6.88e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2041616053 172 DGSTCLHRACYGDGthcNIDIVRLLLEYNADHAILD 207
Cdd:pfam00023   1 DGNTPLHLAAGRRG---NLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-328 1.09e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 196 LLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIHVKDVDGMTpAMW----ACHLDRFD---HFQELSR---H 265
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT-ALWnaisAKHHKIFRilyHFASISDphaA 622

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616053 266 GD---DAEERDNdgrtwihysvrktepLECLKSLLspKTMLLRDTE---GRTCLHVAAEQGSVLACRLI 328
Cdd:PLN03192  623 GDllcTAAKRND---------------LTAMKELL--KQGLNVDSEdhqGATALQVAMAEDHVDMVRLL 674
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 113-230 1.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 113 AVREGDLRYVKELLnENMDLISKVDSFGRDLLTYAVQF-NQINILKYLLEKQANVNTLAN-DGSTCLHRACYGDgthcni 190
Cdd:PHA02878  208 AVKHYNKPIVHILL-ENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE------ 280

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2041616053 191 DIVRLLLEYNADHAILDVHLRSPLHWSVLTE-NIDCLKLLI 230
Cdd:PHA02878  281 RKLKLLLEYGADINSLNSYKLTPLSSAVKQYlCINIGRILI 321
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 159-237 1.65e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2041616053 159 LLEKQANVNTLANDGSTCLHRACygdgTHCNIDIVRLLLEYNADHAILDVHLRSPLHWSVLTENIDCLKLLIEYKANIH 237
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIAC----ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 286-373 2.55e-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: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2041616053 286 KTEPLECLKSLL-SPKTMLL-RDTEGRTCLHVAAEQGSVLACRLIFDMGEKNSNKTYIHEVdNQKQTPLHIATKNGHARV 363
Cdd:cd22192    26 KENDVQAIKKLLkCPSCDLFqRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDL-YQGETALHIAVVNQNLNL 104

                          90
                  ....*....|
gi 2041616053 364 LKELLDHGGD 373
Cdd:cd22192   105 VRELIARGAD 114
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 349-376 2.72e-03

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: 36.08  E-value: 2.72e-03
                          10        20
                  ....*....|....*....|....*...
gi 2041616053 349 QTPLHIATKNGHARVLKELLDHGGDPQV 376
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
352-396 3.33e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 3.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2041616053 352 LHIATKNGHARVLKELLDHGGDPQVRDVHGISSLDYALNRGLYFC 396
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI 45
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-202 4.26e-03

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: 35.64  E-value: 4.26e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2041616053  172 DGSTCLHRACYgdgtHCNIDIVRLLLEYNAD 202
Cdd:smart00248   1 DGRTPLHLAAE----NGNLEVVKLLLDKGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 211-240 8.89e-03

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: 34.57  E-value: 8.89e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2041616053 211 RSPLHWSVL-TENIDCLKLLIEYKANIHVKD 240
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-167 9.27e-03

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: 34.49  E-value: 9.27e-03
                           10        20
                   ....*....|....*....|....*...
gi 2041616053  140 GRDLLTYAVQFNQINILKYLLEKQANVN 167
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
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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