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Conserved domains on  [gi|23346511|ref|NP_694729|]
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protein phosphatase 1 regulatory inhibitor subunit 16B [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins 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

Gene Ontology:  GO:0005515
PubMed:  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];
71-321 6.47e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 6.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 151 KILVQYGADLLAVNSDGNMPYdlcedeptldvietcmayqgitqekineMRAApEQKMISDIHCMIAAGQDLDWIDGQGA 230
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPL----------------------------HLAA-ANGNLEIVKLLLEAGADVNARDNDGE 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 231 TLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVL 310
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                       250
                ....*....|.
gi 23346511 311 LLELKHKHDVI 321
Cdd:COG0666 268 VKLLLLALLLL 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-321 6.47e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 6.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 151 KILVQYGADLLAVNSDGNMPYdlcedeptldvietcmayqgitqekineMRAApEQKMISDIHCMIAAGQDLDWIDGQGA 230
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPL----------------------------HLAA-ANGNLEIVKLLLEAGADVNARDNDGE 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 231 TLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVL 310
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                       250
                ....*....|.
gi 23346511 311 LLELKHKHDVI 321
Cdd:COG0666 268 VKLLLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-164 1.09e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511    72 LLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHgANVNAKDNElWTPLHAAATCGHINLVK 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 23346511   152 ILVQYGADLLAVN 164
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 71-301 1.01e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   71 ALLEASLRNDAEEVRYFLKNKV---SPDLCnedGLTALHQC-CIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAAT--C 144
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGAdvnAPERC---GFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfN 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  145 GHINLVKILVQYGADLLAVNSDGNMPYD--LCEDEPTLDVIETCMAYQGITQEKINEMRAAPEQKMISD------IHCMI 216
Cdd:PHA03095 130 INPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFkprariVRELI 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  217 AAGQDLDWIDGQGATLLHIAGANGYLRAAEL--LLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSM 294
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289


                 ....*..
gi 23346511  295 DEMPIDL 301
Cdd:PHA03095 290 GNTPLSL 296
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 67-170 3.48e-06

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: 50.01  E-value: 3.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  67 EASVALLEASlrndaeevryflknkvsPDLCNE-------DGLTALHQCCIDNFEEIVKLLLSHGANVNA---------- 129
Cdd:cd22192  65 EAAVVLMEAA-----------------PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 23346511 130 -KDNELW---TPLHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:cd22192 128 gPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 100-129 1.34e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.34e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 23346511    100 DGLTALHQCCIDNFEEIVKLLLSHGANVNA 129
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-178 7.78e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511    67 EASVALLEASLRndaEEVRYFLKNkvSPDLCNE-DGLTALHQCCIDNFEEIVKLLLSHGANVNAKDN------------- 132
Cdd:TIGR00870  98 EAILLHLLAAFR---KSGPLELAN--DQYTSEFtPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsf 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 23346511   133 ---ELwtPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEP 178
Cdd:TIGR00870 173 yhgES--PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-321 6.47e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 6.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 151 KILVQYGADLLAVNSDGNMPYdlcedeptldvietcmayqgitqekineMRAApEQKMISDIHCMIAAGQDLDWIDGQGA 230
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPL----------------------------HLAA-ANGNLEIVKLLLEAGADVNARDNDGE 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 231 TLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVL 310
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                       250
                ....*....|.
gi 23346511 311 LLELKHKHDVI 321
Cdd:COG0666 268 VKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-315 1.55e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 1.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLV 150
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 151 KILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETcmayqgitqekinemraapeqkmisdihcMIAAGQDLDWIDGQGA 230
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL-----------------------------LLEAGADVNAQDNDGN 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511 231 TLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMPIDLCEEEEFKVL 310
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234


                ....*
gi 23346511 311 LLELK 315
Cdd:COG0666 235 VKLLL 239
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-164 1.09e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511    72 LLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHgANVNAKDNElWTPLHAAATCGHINLVK 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 23346511   152 ILVQYGADLLAVN 164
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 71-301 1.01e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   71 ALLEASLRNDAEEVRYFLKNKV---SPDLCnedGLTALHQC-CIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAAT--C 144
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGAdvnAPERC---GFTPLHLYlYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfN 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  145 GHINLVKILVQYGADLLAVNSDGNMPYD--LCEDEPTLDVIETCMAYQGITQEKINEMRAAPEQKMISD------IHCMI 216
Cdd:PHA03095 130 INPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFkprariVRELI 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  217 AAGQDLDWIDGQGATLLHIAGANGYLRAAEL--LLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSM 294
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289


                 ....*..
gi 23346511  295 DEMPIDL 301
Cdd:PHA03095 290 GNTPLSL 296
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-259 6.81e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 6.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   105 LHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGadllavnsDGNMpydlcedeptldvie 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------DVNL--------------- 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23346511   185 tcmayqgitqekinemraapeqkmisdihcmiaagqdldwiDGQGATLLHIAGANGYLRAAELLLDHGVRVDVKD 259
Cdd:pfam12796  58 -----------------------------------------KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-311 1.61e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   84 VRYFLKNKVSPDLCNEDGLTALHQCCIDNFE-----EIVKLLLSHGANVNAKDNELWTPLHAAATC--GHINLVKILVQY 156
Cdd:PHA03100  51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  157 GADLLAVNSDGNMP--YDLCEDEPTLDVIETcmayqgitqekinemraapeqkmisdihcMIAAGQDLDWIDgqgatllh 234
Cdd:PHA03100 131 GANVNIKNSDGENLlhLYLESNKIDLKILKL-----------------------------LIDKGVDINAKN-------- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  235 iagangylrAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMP----IDLCEEEEFKVL 310
Cdd:PHA03100 174 ---------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPlhiaILNNNKEIFKLL 244


                 .
gi 23346511  311 L 311
Cdd:PHA03100 245 L 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
200-291 1.44e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   200 MRAApEQKMISDIHCMIAAGQDLDWIDGQGATLLHIAGANGYLRAAELLLDHgVRVDVKDwDGWEPLHAAAFWGQMPMAE 279
Cdd:pfam12796   2 HLAA-KNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 23346511   280 LLVSHGASLSAR 291
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-170 4.18e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 4.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   78 RNDAEEVRYFLKNKVSPDLCNEDGLTALHQ----CCIDNfeEIVKLLLSHGANVNAKDN-EL---------------WTP 137
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLylesNKIDL--KILKLLIDKGVDINAKNRvNYllsygvpinikdvygFTP 195

                         90       100       110
                 ....*....|....*....|....*....|...
gi 23346511  138 LHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
Ank_4 pfam13637
Ankyrin repeats (many copies);
101-154 7.17e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 7.17e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23346511   101 GLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILV 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 8-376 9.95e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 9.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511    8 LTELQLLEKVPTLERLRAAQKRRAQQLKKWAQYEQDLlHRKRKHERKRSTGGRRKKVSFEASVaLLEASLRNDA--EEVr 85
Cdd:PLN03192 468 LSQLLRLKTSTLIEAMQTRQEDNVVILKNFLQHHKEL-HDLNVGDLLGDNGGEHDDPNMASNL-LTVASTGNAAllEEL- 544

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   86 yfLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGAdllavns 165
Cdd:PLN03192 545 --LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS------- 615

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  166 dgnmpydlcedeptldvietcmayqgitqekinemraapeqkmISDIHCmiaagqdldwidgqGATLLHIAGANGYLRAA 245
Cdd:PLN03192 616 -------------------------------------------ISDPHA--------------AGDLLCTAAKRNDLTAM 638

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  246 ELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEM-PIDLCEEEEFKvlllELKHKHDV---- 320
Cdd:PLN03192 639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFsPTELRELLQKR----ELGHSITIvdsv 714

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 23346511  321 --IMKSQLRHKSSLSRRTSSAGSRGKVVRRASLsdrtnlyrkeYEGEAILWQQRSAAE 376
Cdd:PLN03192 715 paDEPDLGRDGGSRPGRLQGTSSDNQCRPRVSI----------YKGHPLLRNERCCNE 762
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 109-300 1.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  109 CIDNfeEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCM- 187
Cdd:PHA02874 101 CIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLe 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  188 --AYQGITQEKINE-MRAAPEQKMISDIHCMIAAGQDLDWIDGQGATLLHIAGAngYLRAAELLLDHGVRVDVKDWDGWE 264
Cdd:PHA02874 179 kgAYANVKDNNGESpLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGST 256

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 23346511  265 PLHAAAfwgQMP----MAELLVSHGASLSARTSMDEMPID 300
Cdd:PHA02874 257 PLHHAI---NPPcdidIIDILLYHKADISIKDNKGENPID 293
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-206 2.76e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.46  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  117 VKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQGITQEk 196
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE- 176

                         90
                 ....*....|
gi 23346511  197 iNEMRAAPEQ 206
Cdd:PTZ00322 177 -LGANAKPDS 185
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-314 4.00e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  116 IVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEPTLDVIETCMAYQG-ITQ 194
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSnINK 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  195 EKINEMRAAPEQKMISDIhCMIAAGQDLDWIDGQGATLLHIAGANGYL-RAAELLLDHGVRVDVKDWDGWEPLHAAAFWG 273
Cdd:PHA02876 240 NDLSLLKAIRNEDLETSL-LLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23346511  274 -QMPMAELLVSHGASLSARTSMDEMPI----DLCEEEEFKVLLLEL 314
Cdd:PHA02876 319 yDTENIRTLIMLGADVNAADRLYITPLhqasTLDRNKDIVITLLEL 364
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 70-286 4.64e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 4.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   70 VALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINL 149
Cdd:PHA02875   4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  150 VKILV---QYGADLLAvnSDGNMPYDLCEDEPTLDVIETCMAYQGITQ----EKINEMRAAPEQKMISDIHCMIAAGQDL 222
Cdd:PHA02875  84 VEELLdlgKFADDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDipntDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23346511  223 DWIDGQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMP-MAELLVSHGA 286
Cdd:PHA02875 162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGA 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 82-332 2.03e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 2.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   82 EEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAatCGHIN------LVKILVQ 155
Cdd:PHA02878  18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII--CKEPNklgmkeMIRSINK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  156 --YGADLLAVNSDGN---------MPYDLCEDEPTLDVIETC-MAYQGITQEKInemraapeqkmisdIHCMIAAGQDLD 223
Cdd:PHA02878  96 csVFYTLVAIKDAFNnrnveifkiILTNRYKNIQTIDLVYIDkKSKDDIIEAEI--------------TKLLLSYGADIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  224 WID-GQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMP--ID 300
Cdd:PHA02878 162 MKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPlhIS 241

                        250       260       270
                 ....*....|....*....|....*....|..
gi 23346511  301 LCEEEEFKVLLLELKHKHDVIMKSQLRHKSSL 332
Cdd:PHA02878 242 VGYCKDYDILKLLLEHGVDVNAKSYILGLTAL 273
PHA02798 PHA02798
ankyrin-like protein; Provisional
 115-267 2.82e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 62.54  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  115 EIVKLLLSHGANVNAKDNELWTPLHAAATC-----GHINLVKILVQYGADLLAVNSDGNMPydLCedeptldvietCMAY 189
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETP--LY-----------CLLS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  190 QGITQEKINemraapeqkmisdIHCMIAAGQDLDWIDGQGATLLHI---AGANGYLRAAELLLDHGVRVDV-KDWDGWEP 265
Cdd:PHA02798 119 NGYINNLEI-------------LLFMIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLLLEKGVDINThNNKEKYDT 185


                 ..
gi 23346511  266 LH 267
Cdd:PHA02798 186 LH 187
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 68-291 8.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 8.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   68 ASVALLEASLRNDAEEVRYFLKNKVS-PDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGH 146
Cdd:PHA02874   1 ASQDLRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  147 INLVKILVQYGADllavNSDGNMPydlCEDEPTLDVIETCMAYQGITQEKINE-MRAAPEQKMISDIHCMIAAGQDLDWI 225
Cdd:PHA02874  81 HDIIKLLIDNGVD----TSILPIP---CIEKDMIKTILDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGADVNIE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23346511  226 DGQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSAR 291
Cdd:PHA02874 154 DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
Ank_2 pfam12796
Ankyrin repeats (3 copies);
233-284 1.12e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 1.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23346511   233 LHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSH 284
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 1.22e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 1.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23346511   120 LLSHG-ANVNAKDNELWTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLC 174
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 115-288 3.42e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  115 EIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKI---LVQYGADLLAVNSDGNMPYDLC-EDEPTLDVIETcmayq 190
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKL----- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  191 gitqekinemraapeqkmisdihcMIAAGQDLDWIDGQGATLLHI--AGANGYLRAAELLLDHGVRVDVKDWDGWEPLHA 268
Cdd:PHA03095 103 ------------------------LIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158

                        170       180
                 ....*....|....*....|
gi 23346511  269 aafwgqmpmaeLLVSHGASL 288
Cdd:PHA03095 159 -----------LLKSRNANV 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 79-159 3.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   79 NDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGA 158
Cdd:PHA03100 170 NAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                 .
gi 23346511  159 D 159
Cdd:PHA03100 250 S 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
231-282 5.60e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.60e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23346511   231 TLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLV 282
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-170 1.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   78 RNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYG 157
Cdd:PHA02874 134 KGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213

                         90
                 ....*....|...
gi 23346511  158 ADLLAVNSDGNMP 170
Cdd:PHA02874 214 NHIMNKCKNGFTP 226
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 71-201 1.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNEL----WTPLHAaatcgh 146
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETLlyfkDKDLNT------ 268

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 23346511  147 INLVKILVQYGADLLAVNSD--GNMPYdLCEDEPTLDVIETCmayqgitQEKINEMR 201
Cdd:PHA03100 269 ITKIKMLKKSIMYMFLLDPGfyKNRKL-IENSKSLKDVINEC-------EKEIERMK 317
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 84-170 2.64e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 2.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   84 VRYFLKNKVSPDLCNEDGLTALHQC---CIDnfEEIVKLLLSHGANVNAKDNEL-WTPLHAAATCGHInlVKILVQYGAD 159
Cdd:PHA02878 217 VHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVNAKSYILgLTALHSSIKSERK--LKLLLEYGAD 292

                         90
                 ....*....|.
gi 23346511  160 LLAVNSDGNMP 170
Cdd:PHA02878 293 INSLNSYKLTP 303
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-132 2.81e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 2.81e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 23346511   100 DGLTALHQCCID-NFEEIVKLLLSHGANVNAKDN 132
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 98-299 3.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 3.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   98 NEDGLTALHQCCIDNFE-EIVKLLLSHGANVNAKDNELWTPLHAAATCG-HINLVKILVQYGADLLAvnsdgnmpYDLCE 175
Cdd:PHA02876 304 NIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNA--------RDYCD 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  176 DEPtldvietcmayqgitqekineMRAAPEQKMISDIHCMIAAGQDLDWIDGQGATLLHIA--GANGYLrAAELLLDHGV 253
Cdd:PHA02876 376 KTP---------------------IHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlcGTNPYM-SVKTLIDRGA 433

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 23346511  254 RVDVKDWDGWEPLHAAAFWGQMP-MAELLVSHGASLSARTSMDEMPI 299
Cdd:PHA02876 434 NVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPL 480
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 80-288 3.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   80 DAEEVRYFLKNKVSPDLCNEDGLTALHQC-CIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGA 158
Cdd:PHA02876 320 DTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  159 DLLAVNSD--GNMPYDLCEDEPTLDVietcmayqgitqekinemraapeqkmisdiHCMIAAGQDLDWIDGQGATLLHIA 236
Cdd:PHA02876 400 DIEALSQKigTALHFALCGTNPYMSV------------------------------KTLIDRGANVNSKNKDLSTPLHYA 449

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 23346511  237 -GANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAfwGQMPMAELLVSHGASL 288
Cdd:PHA02876 450 cKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 147-300 4.08e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  147 INLVKILVQYGADllaVNSDGnmPYDLCedeptldVIETCMAYQGITQEKInemraapeqkmisdIHCMIAAGQDLDWID 226
Cdd:PHA03095  27 VEEVRRLLAAGAD---VNFRG--EYGKT-------PLHLYLHYSSEKVKDI--------------VRLLLEAGADVNAPE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23346511  227 GQGATLLHIAGANGY-LRAAELLLDHGVRVDVKDWDGWEPLHA--AAFWGQMPMAELLVSHGASLSARTSMDEMPID 300
Cdd:PHA03095  81 RCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
71-121 2.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 23346511    71 ALLEASLRNDAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLL 121
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 67-170 3.48e-06

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: 50.01  E-value: 3.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  67 EASVALLEASlrndaeevryflknkvsPDLCNE-------DGLTALHQCCIDNFEEIVKLLLSHGANVNA---------- 129
Cdd:cd22192  65 EAAVVLMEAA-----------------PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrp 127

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 23346511 130 -KDNELW---TPLHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:cd22192 128 gPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 212-297 4.30e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 4.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  212 IHCMIAAGQDLDWIDGQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGA---SL 288
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQchfEL 177


                 ....*....
gi 23346511  289 SARTSMDEM 297
Cdd:PTZ00322 178 GANAKPDSF 186
PHA02946 PHA02946
ankyin-like protein; Provisional
 80-188 4.34e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 4.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   80 DAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGH--INLVKILVQYG 157
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 23346511  158 ADL-LAVNSDGNMPYDLCEDePTLDVIETCMA 188
Cdd:PHA02946 131 AKInNSVDEEGCGPLLACTD-PSERVFKKIMS 161
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 80-170 7.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   80 DAEEVRYFLKNKVSPDLCNEDGL-TALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAATCGHINLVKILVQYGA 158
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90
                 ....*....|..
gi 23346511  159 DLLAVNSDGNMP 170
Cdd:PHA02878 226 STDARDKCGNTP 237
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 135-164 9.56e-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: 42.66  E-value: 9.56e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 23346511   135 WTPLHAAAT-CGHINLVKILVQYGADLLAVN 164
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 100-129 1.34e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.34e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 23346511    100 DGLTALHQCCIDNFEEIVKLLLSHGANVNA 129
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 135-160 2.50e-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: 41.42  E-value: 2.50e-05
                           10        20
                   ....*....|....*....|....*.
gi 23346511    135 WTPLHAAATCGHINLVKILVQYGADL 160
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 80-170 2.86e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.21  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   80 DAEEVRYFLKNKVSPDLCNEDGLTALHQCCIDNF--EEIVKLLLSHGANVNAKDNELWTPLHA------------AATCG 145
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildPETDN 375

                         90       100
                 ....*....|....*....|....*..
gi 23346511  146 HINL--VKILVQYGADLLAVNSDGNMP 170
Cdd:PHA02716 376 DIRLdvIQCLISLGADITAVNCLGYTP 402
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-160 2.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   69 SVALLEASLRNDAEEVRYFL---KNKVSPDLCNEdglTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLH-AAATC 144
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLsygANVNIPDKTNN---SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYC 245

                         90
                 ....*....|....*.
gi 23346511  145 GHINLVKILVQYGADL 160
Cdd:PHA02878 246 KDYDILKLLLEHGVDV 261
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-129 3.23e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 3.23e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 23346511   100 DGLTALHQCCIDNFEEIVKLLLSHGANVNA 129
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 75-170 4.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   75 ASLRNDAEEVRYFLKNKVSPDLCNEDGLTALH-QCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAAA--TCgHINLVK 151
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHfALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACkkNC-KLDVIE 460

                         90
                 ....*....|....*....
gi 23346511  152 ILVQYGADLLAVNSDGNMP 170
Cdd:PHA02876 461 MLLDNGADVNAINIQNQYP 479
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 37-159 6.05e-05

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: 6.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  37 WAQY--EQDLLHRKRKHErkrstggrrkkvsfeasVALLEASLRNDAEEVRYFLKNKvSPDLCNEDGL--TALHQCCIDN 112
Cdd:cd22192   1 WAQMldELHLLQQKRISE-----------------SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGALgeTALHVAALYD 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 23346511 113 FEEIVKLLLSHGAN-VN-AKDNELW---TPLHAAATCGHINLVKILVQYGAD 159
Cdd:cd22192  63 NLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGAD 114
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 232-316 1.35e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  232 LLHIAgANGYLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLSARTSMDEMPIDLCEEEEFK-VL 310
Cdd:PTZ00322  86 LCQLA-ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFReVV 164


                 ....*.
gi 23346511  311 LLELKH 316
Cdd:PTZ00322 165 QLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
135-170 1.65e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.65e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 23346511   135 WTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMP 170
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
Ank_5 pfam13857
Ankyrin repeats (many copies);
215-269 1.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23346511   215 MIAAGQ-DLDWIDGQGATLLHIAGANGYLRAAELLLDHGVRVDVKDWDGWEPLHAA 269
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 135-162 1.84e-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: 38.78  E-value: 1.84e-04
                          10        20
                  ....*....|....*....|....*...
gi 23346511   135 WTPLHAAATCGHINLVKILVQYGADLLA 162
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 78-171 4.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511   78 RNDAEEVRYFLKnkvSPDLCNEDGLTALHQCCIDNF--EEIVKLLLSHGANVNAK--DNELwTPLHAAATCG---HINLV 150
Cdd:PHA02859  31 KDDIEGVKKWIK---FVNDCNDLYETPIFSCLEKDKvnVEILKFLIENGADVNFKtrDNNL-SALHHYLSFNknvEPEIL 106

                         90       100
                 ....*....|....*....|.
gi 23346511  151 KILVQYGADLLAVNSDGNMPY 171
Cdd:PHA02859 107 KILIDSGSSITEEDEDGKNLL 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 216-320 5.47e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511  216 IAAGQDLDWIDGQGATLLHIAGANG---YLRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQ-MPMAELLVSHGASLSAR 291
Cdd:PHA03095  34 LAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAK 113

                         90       100       110
                 ....*....|....*....|....*....|..
gi 23346511  292 TSMDEMPIDLC---EEEEFKVLLLELKHKHDV 320
Cdd:PHA03095 114 DKVGRTPLHVYlsgFNINPKVIRLLLRKGADV 145
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-141 5.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 5.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 23346511    92 VSPDLCNEDGLTALHQCCIDNFEEIVKLLLSHGANVNAKDNELWTPLHAA 141
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-178 7.78e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 7.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346511    67 EASVALLEASLRndaEEVRYFLKNkvSPDLCNE-DGLTALHQCCIDNFEEIVKLLLSHGANVNAKDN------------- 132
Cdd:TIGR00870  98 EAILLHLLAAFR---KSGPLELAN--DQYTSEFtPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsf 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 23346511   133 ---ELwtPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDLCEDEP 178
Cdd:TIGR00870 173 yhgES--PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 261-292 1.02e-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: 36.88  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 23346511   261 DGWEPLHAAA-FWGQMPMAELLVSHGASLSART 292
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 242-289 1.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 1.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 23346511  242 LRAAELLLDHGVRVDVKDWDGWEPLHAAAFWGQMPMAELLVSHGASLS 289
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 117-173 2.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 2.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 23346511  117 VKLLLSHGANVNAKDNEL-WTPLHAAATCGHINLVKILVQYGADLLAVNSDGNMPYDL 173
Cdd:PHA02884  86 AKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIEL 143
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 228-259 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. 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: 35.73  E-value: 2.72e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 23346511   228 QGATLLHIA-GANGYLRAAELLLDHGVRVDVKD 259
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
75-106 4.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 4.38e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 23346511    75 ASLRNDAEEVRYFLKNKVSPDLCNEDGLTALH 106
Cdd:pfam13857  23 AAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 114-168 8.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 8.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 23346511  114 EEIVKLLLSHGANVNAKDNELWTPLHAAAT-CG-HINLVKILVQYGADLLAVNSDGN 168
Cdd:PHA02859 103 PEILKILIDSGSSITEEDEDGKNLLHMYMCnFNvRINVIKLLIDSGVSFLNKDFDNN 159
 
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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