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Conserved domains on  [gi|1983575845|ref|NP_001380391|]
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ankyrin repeat and MYND domain-containing protein 1 isoform 10 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
576-826 9.52e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 9.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  576 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 654
Cdd:COG0666     88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  655 gEEG-VQIVELLLHAITDVDAKASDeddtykpgkldllpsslklsnepgppqayystdtalpeegGRTALHMACEREDDn 733
Cdd:COG0666    162 -ANGnLEIVKLLLEAGADVNARDND----------------------------------------GETPLHLAAENGHL- 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  734 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKL 812
Cdd:COG0666    200 ----EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275

                          250
                   ....*....|....
gi 1983575845  813 ALIDRLISHGADIL 826
Cdd:COG0666    276 LLLAAALLDLLTLL 289
COG4642 super family cl34799
Uncharacterized conserved protein [Function unknown];
52-158 8.68e-22

Uncharacterized conserved protein [Function unknown];


The actual alignment was detected with superfamily member COG4642:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 96.18  E-value: 8.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 129
Cdd:COG4642    139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218

                           90       100
                   ....*....|....*....|....*....
gi 1983575845  130 lFQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:COG4642    219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
318-391 8.23e-11

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 8.23e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845  318 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666     85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
zf-MYND pfam01753
MYND finger;
941-981 2.00e-09

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 53.58  E-value: 2.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1983575845  941 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWtEFHKKDC 981
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
576-826 9.52e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 9.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  576 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 654
Cdd:COG0666     88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  655 gEEG-VQIVELLLHAITDVDAKASDeddtykpgkldllpsslklsnepgppqayystdtalpeegGRTALHMACEREDDn 733
Cdd:COG0666    162 -ANGnLEIVKLLLEAGADVNARDND----------------------------------------GETPLHLAAENGHL- 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  734 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKL 812
Cdd:COG0666    200 ----EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275

                          250
                   ....*....|....
gi 1983575845  813 ALIDRLISHGADIL 826
Cdd:COG0666    276 LLLAAALLDLLTLL 289
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
52-158 8.68e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 96.18  E-value: 8.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 129
Cdd:COG4642    139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218

                           90       100
                   ....*....|....*....|....*....
gi 1983575845  130 lFQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:COG4642    219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 57-158 7.70e-18

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 88.74  E-value: 7.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   57 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 135
Cdd:PLN03185    28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107

                           90       100
                   ....*....|....*....|...
gi 1983575845  136 KADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185   108 IQGLQEGPGKYTWANGNVYLGDM 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 594-824 6.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 6.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  594 LLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEG-VQIVELLLHAITD 671
Cdd:PHA02875    21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKF 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  672 VDakasdeDDTYKPGKLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEREDDNkcardIVRLLLSHGANPN 751
Cdd:PHA02875    94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845  752 LL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 824
Cdd:PHA02875   163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
318-391 8.23e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 8.23e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845  318 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666     85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
719-784 4.07e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 4.07e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  719 GRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:pfam12796   30 GRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
zf-MYND pfam01753
MYND finger;
941-981 2.00e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 53.58  E-value: 2.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1983575845  941 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWtEFHKKDC 981
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
328-403 1.04e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 1.04e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 403
Cdd:pfam12796    5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 348-400 1.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1983575845  348 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 400
Cdd:PHA03100   186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 611-782 1.97e-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: 48.47  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  611 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdeddtykpgkl 688
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  689 dllpsslkLSNEPGPPQAYYstdtalpeegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 753
Cdd:cd22192     77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133

                          170       180
                   ....*....|....*....|....*....
gi 1983575845  754 WSGHSPLSLSIASGNELVVKELLTQGADP 782
Cdd:cd22192    134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 719-752 5.28e-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: 41.03  E-value: 5.28e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1983575845   719 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 752
Cdd:smart00248    2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 86-108 3.52e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 38.54  E-value: 3.52e-04
                           10        20
                   ....*....|....*....|...
gi 1983575845   86 YHGQFYRDHCHGLGTYMWPDGSS 108
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
85-105 9.10e-04

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.32  E-value: 9.10e-04
                            10        20
                    ....*....|....*....|.
gi 1983575845    85 SYHGQFYRDHCHGLGTYMWPD 105
Cdd:smart00698    2 RYEGEWRNGKRHGRGVYTYAN 22
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 353-382 3.57e-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: 36.03  E-value: 3.57e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1983575845   353 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 382
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
576-826 9.52e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 9.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  576 RMALSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalp 654
Cdd:COG0666     88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDgETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA--- 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  655 gEEG-VQIVELLLHAITDVDAKASDeddtykpgkldllpsslklsnepgppqayystdtalpeegGRTALHMACEREDDn 733
Cdd:COG0666    162 -ANGnLEIVKLLLEAGADVNARDND----------------------------------------GETPLHLAAENGHL- 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  734 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDLTYEHQRNMDSKL 812
Cdd:COG0666    200 ----EIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275

                          250
                   ....*....|....
gi 1983575845  813 ALIDRLISHGADIL 826
Cdd:COG0666    276 LLLAAALLDLLTLL 289
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
52-158 8.68e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 96.18  E-value: 8.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMK--TR 129
Cdd:COG4642    139 GGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYAdgDR 218

                           90       100
                   ....*....|....*....|....*....
gi 1983575845  130 lFQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:COG4642    219 -YEGEFKNGKRHGQGTLTYADGDRYEGEF 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
611-827 3.21e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 3.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  611 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAKASDeddtykpgkldl 690
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAY---NGNLEIVKLLLEAGADVNAQDND------------ 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  691 lpsslklsnepgppqayystdtalpeegGRTALHMACEREDdnkcaRDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 769
Cdd:COG0666    153 ----------------------------GNTPLHLAAANGN-----LEIVKLLLEAGADVNARdNDGETPLHLAAENGHL 199

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845  770 LVVKELLTQGADPNLPLTKGlGSALCVACdltyehqrnMDSKLALIDRLISHGADILK 827
Cdd:COG0666    200 EIVKLLLEAGADVNAKDNDG-KTALDLAA---------ENGNLEIVKLLLEAGADLNA 247
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
611-825 4.96e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 4.96e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  611 LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAlpgEEGVQIVELLLHAITDVDAKASDeddtykpgkldl 690
Cdd:COG0666     58 LLAAALAGDLLVALLLLAAGADINA---KDDGGNTLLHAAAR---NGDLEIVKLLLEAGADVNARDKD------------ 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  691 lpsslklsnepgppqayystdtalpeegGRTALHMACEREDDnkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNE 769
Cdd:COG0666    120 ----------------------------GETPLHLAAYNGNL-----EIVKLLLEAGADVNAQdNDGNTPLHLAAANGNL 166

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  770 LVVKELLTQGADPNLPLTKGlGSALCVACdltyehqrnMDSKLALIDRLISHGADI 825
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDG-ETPLHLAA---------ENGHLEIVKLLLEAGADV 212
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
52-158 3.01e-19

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 88.86  E-value: 3.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMymktrlf 131
Cdd:COG4642    185 QGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADGDRYEGEFKNGKRHGQGTM------- 257

                           90       100
                   ....*....|....*....|....*..
gi 1983575845  132 qglykadqrfgpgveTYPDGSQDVGLW 158
Cdd:COG4642    258 ---------------TYADGSVYEGEW 269
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 57-158 7.70e-18

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 88.74  E-value: 7.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   57 WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYG-TMYMKTRLFQGLY 135
Cdd:PLN03185    28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107

                           90       100
                   ....*....|....*....|...
gi 1983575845  136 KADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185   108 IQGLQEGPGKYTWANGNVYLGDM 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 594-824 6.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.86  E-value: 6.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  594 LLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAalpgEEG-VQIVELLLHAITD 671
Cdd:PHA02875    21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP---DIESELHDAV----EEGdVKAVEELLDLGKF 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  672 VDakasdeDDTYKPGKLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEREDDNkcardIVRLLLSHGANPN 751
Cdd:PHA02875    94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845  752 LL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKGLGSALCVACDltyehqrnmDSKLALIDRLISHGAD 824
Cdd:PHA02875   163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGAD 227
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
49-158 9.49e-12

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 66.52  E-value: 9.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   49 QLVQGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMKT 128
Cdd:COG4642     90 DGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYAD 169

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1983575845  129 -RLFQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:COG4642    170 gDRYEGEFKNGKRHGQGTLTYANGDVYEGEF 200
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 574-781 2.63e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 2.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  574 MRRMALSMIERRKRWRTIKLLLRRGADPN------LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQlstLTPL 647
Cdd:PHA03100    34 KPVLPLYLAKEARNIDVVKILLDNGADINsstknnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG---ITPL 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  648 HIAAALPGEEgVQIVELLLHAITDVDAKASDEDD------TYKPGKLDLLpsSLKLSNepgppQAY------------YS 709
Cdd:PHA03100   111 LYAISKKSNS-YSIVEYLLDNGANVNIKNSDGENllhlylESNKIDLKIL--KLLIDK-----GVDinaknrvnyllsYG 182

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983575845  710 TDTALPEEGGRTALHMACERedDNKcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGAD 781
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYN--NNP---EFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
318-391 8.23e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 8.23e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845  318 EQLSMEMILKAEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666     85 DGGNTLLHAAARNGDLE-IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
324-391 3.30e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 3.30e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845  324 MILKAEEGNHEWIcRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666    124 LHLAAYNGNLEIV-KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
719-784 4.07e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 4.07e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  719 GRTALHMACEREDdnkcaRDIVRLLLSHgANPNLLWSGHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:pfam12796   30 GRTALHLAAKNGH-----LEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
611-752 4.99e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 4.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  611 LFLAVKAGDVDGVRLLLEHGARTDICFPpqlSTLTPLHIAAAlpgEEGVQIVELLL-HAITDVDakasdeddtykpgkld 689
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAAK---NGHLEIVKLLLeHADVNLK---------------- 58

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1983575845  690 llpsslklsnepgppqayystdtalpeEGGRTALHMACEreddnKCARDIVRLLLSHGANPNL 752
Cdd:pfam12796   59 ---------------------------DNGRTALHYAAR-----SGHLEIVKLLLEKGADINV 89
zf-MYND pfam01753
MYND finger;
941-981 2.00e-09

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 53.58  E-value: 2.00e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1983575845  941 CYQCGRSiGVRLLPCPRCYGILTCSKYCKTKAWtEFHKKDC 981
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
328-393 2.30e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 2.30e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSM 393
Cdd:COG0666    161 AANGNLE-IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
590-675 2.92e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 2.92e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  590 TIKLLLRRGADPNLC-CVPMQVLFLAVKAGDVDGVRLLLEHGARTDicfppQLSTLTPLHIAAalpgEEG-VQIVELLLH 667
Cdd:pfam12796   12 LVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAA----RSGhLEIVKLLLE 82


                   ....*...
gi 1983575845  668 AITDVDAK 675
Cdd:pfam12796   83 KGADINVK 90
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 51-127 5.52e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 60.23  E-value: 5.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   51 VQGVQE------WQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTM 124
Cdd:PLN03185   108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187


                   ...
gi 1983575845  125 YMK 127
Cdd:PLN03185   188 YPA 190
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 59-158 8.67e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 59.46  E-value: 8.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   59 DGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTmYMKTR--LFQGLYK 136
Cdd:PLN03185     7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGT-YTGTDgtTYKGRWR 85

                           90       100
                   ....*....|....*....|..
gi 1983575845  137 ADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185    86 LNLKHGLGYQRYPNGDVFEGSW 107
PHA03095 PHA03095
ankyrin-like protein; Provisional
 587-784 2.74e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 2.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  587 RWRTIKLLLRRGADPNLCCV----PMQVlFLAVKAGDVDGVRLLLEHGArtDICfPPQLSTLTPLHIAAALPGEEgVQIV 662
Cdd:PHA03095    96 TLDVIKLLIKAGADVNAKDKvgrtPLHV-YLSGFNINPKVIRLLLRKGA--DVN-ALDLYGMTPLAVLLKSRNAN-VELL 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  663 ELLLHAITDVDAKaSDEDDTYkpgkLDLLPSSLKLSNEPGPPQAYYSTDTALPEEGGRTALHMACEReddNKCARDIVRL 742
Cdd:PHA03095   171 RLLIDAGADVYAV-DDRFRSL----LHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATG---SSCKRSLVLP 242

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1983575845  743 LLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:PHA03095   243 LLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
711-825 3.94e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.03  E-value: 3.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  711 DTALPEEGGRTALHMACEREDDnkcarDIVRLLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQGADPNLPLTKG 789
Cdd:COG0666     46 ALALADALGALLLLAAALAGDL-----LVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1983575845  790 lGSALCVACdltyehqrnMDSKLALIDRLISHGADI 825
Cdd:COG0666    121 -ETPLHLAA---------YNGNLEIVKLLLEAGADV 146
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 579-784 5.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 5.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  579 LSMIERRKRWRTIKLLLRRGA----DPNLCCVPMQV--LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAA 652
Cdd:PHA03100     1 LYSYIVLTKSRIIKVKNIKYIimedDLNDYSYKKPVlpLYLAKEARNIDVVKILLDNGADINS---STKNNSTPLHYLSN 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  653 LPG--EEGVQIVELLLHAITDVDAkasdeddTYKPGKLDLLPSSLKLSNepgppqaYYSTDTALPEEG---------GRT 721
Cdd:PHA03100    78 IKYnlTDVKEIVKLLLEYGANVNA-------PDNNGITPLLYAISKKSN-------SYSIVEYLLDNGanvniknsdGEN 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  722 ALHMACEREDDNKcarDIVRLLLSHGANPN------LLWS-----------GHSPLSLSIASGNELVVKELLTQGADPNL 784
Cdd:PHA03100   144 LLHLYLESNKIDL---KILKLLIDKGVDINaknrvnYLLSygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 623-798 6.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 6.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  623 VRLLLEHGARTDICFPPQLStlTPLHIAAALPGEEgvqIVELLLhaITDVDAKASDEDDTYKpgkldlLPSSLKLSNEPG 702
Cdd:PHA02878   150 TKLLLSYGADINMKDRHKGN--TALHYATENKDQR---LTELLL--SYGANVNIPDKTNNSP------LHHAVKHYNKPI 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  703 PPQAY-YSTDTALPEEGGRTALHMACEREDDnkcaRDIVRLLLSHGANPNLLWS--GHSPLSLSIASgnELVVKELLTQG 779
Cdd:PHA02878   217 VHILLeNGASTDARDKCGNTPLHISVGYCKD----YDILKLLLEHGVDVNAKSYilGLTALHSSIKS--ERKLKLLLEYG 290

                          170       180
                   ....*....|....*....|....*.
gi 1983575845  780 ADPNL-------PLTKGLGSALCVAC 798
Cdd:PHA02878   291 ADINSlnsykltPLSSAVKQYLCINI 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
328-403 1.04e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 1.04e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCgADVNKCsDEGLTAlsmcflLHYPAQS 403
Cdd:pfam12796    5 AKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTA------LHYAARS 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 719-752 1.09e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 1.09e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1983575845  719 GRTALHMACEREDDnkcaRDIVRLLLSHGANPNL 752
Cdd:pfam00023    2 GNTPLHLAAGRRGN----LEIVKLLLSKGADVNA 31
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
324-391 1.18e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.49  E-value: 1.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845  324 MILKAEEGNHEWICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666     57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 348-400 1.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1983575845  348 DVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMCFLLHYP 400
Cdd:PHA03100   186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
723-825 2.95e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  723 LHMACEREDdnkcaRDIVRLLLSHGANPNLLWS-GHSPLSLSIASGNELVVKELLTQgADPNLPlTKGLgSALCVACDLT 801
Cdd:pfam12796    1 LHLAAKNGN-----LELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGR-TALHYAARSG 72

                           90       100
                   ....*....|....*....|....
gi 1983575845  802 YehqrnmdskLALIDRLISHGADI 825
Cdd:pfam12796   73 H---------LEIVKLLLEKGADI 87
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 52-158 3.57e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 50.99  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845   52 QGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGT-MYMKTRL 130
Cdd:PLN03185    46 NGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGYQRYPNGDVFEGSWIQGLQEGPGKyTWANGNV 125

                           90       100
                   ....*....|....*....|....*...
gi 1983575845  131 FQGLYKADQRFGPGVETYPDGSQDVGLW 158
Cdd:PLN03185   126 YLGDMKGGKMSGKGTLTWVSGDSYEGQW 153
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 578-764 5.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 5.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  578 ALSMIERRKRWRTIKLLLRRGADPNlccVPMQV----LFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAAL 653
Cdd:PHA02878   171 ALHYATENKDQRLTELLLSYGANVN---IPDKTnnspLHHAVKHYNKPIVHILLENGASTDA---RDKCGNTPLHISVGY 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  654 PgeEGVQIVELLLHAITDVDAKasdeddtykpgkldllpSSLKlsnepgppqayystdtalpeegGRTALHMACEREddn 733
Cdd:PHA02878   245 C--KDYDILKLLLEHGVDVNAK-----------------SYIL----------------------GLTALHSSIKSE--- 280

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1983575845  734 kcarDIVRLLLSHGANPNLL-WSGHSPLSLSI 764
Cdd:PHA02878   281 ----RKLKLLLEYGADINSLnSYKLTPLSSAV 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 619-825 1.00e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  619 DVDGVRLLLEHGArtDICFPPQLSTlTPLHIAAALPGEEGVQIVELLLHAITDVDAKasdedDTYkpgkldllpsslkls 698
Cdd:PHA03095    26 TVEEVRRLLAAGA--DVNFRGEYGK-TPLHLYLHYSSEKVKDIVRLLLEAGADVNAP-----ERC--------------- 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  699 nepgppqayystdtalpeegGRTALHMACEreddNKCARDIVRLLLSHGANPNL-LWSGHSPLS--LSIASGNELVVKEL 775
Cdd:PHA03095    83 --------------------GFTPLHLYLY----NATTLDVIKLLIKAGADVNAkDKVGRTPLHvyLSGFNINPKVIRLL 138

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  776 LTQGADPNlpltkglgsalcvACDLtYEHQ------RNMDSKLALIDRLISHGADI 825
Cdd:PHA03095   139 LRKGADVN-------------ALDL-YGMTplavllKSRNANVELLRLLIDAGADV 180
Ank_2 pfam12796
Ankyrin repeats (3 copies);
328-381 1.22e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 1.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1983575845  328 AEEGNHEwICRILKDNFASADVADakGYTVLAAAATHCHNDIVNLLLDCGADVN 381
Cdd:pfam12796   38 AKNGHLE-IVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGADIN 88
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 611-782 1.97e-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: 48.47  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  611 LFLAVKAGDVDGVRLLLEHgARTDICfppQLSTL--TPLHIAAALpgeEGVQIVELLLHAITDvdakasdeddtykpgkl 688
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKC-PSCDLF---QRGALgeTALHVAALY---DNLEAAVVLMEAAPE----------------- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  689 dllpsslkLSNEPGPPQAYYstdtalpeegGRTALHMACEREDDNkcardIVRLLLSHGA---NP------------NLL 753
Cdd:cd22192     77 --------LVNEPMTSDLYQ----------GETALHIAVVNQNLN-----LVRELIARGAdvvSPratgtffrpgpkNLI 133

                          170       180
                   ....*....|....*....|....*....
gi 1983575845  754 WSGHSPLSLSIASGNELVVKELLTQGADP 782
Cdd:cd22192    134 YYGEHPLSFAACVGNEEIVRLLIEHGADI 162
PHA03095 PHA03095
ankyrin-like protein; Provisional
 591-782 4.93e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 4.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  591 IKLLLRRGADPN----LCCVPMQVLFLAVKAGDVDGVRLLLEHGARTDIcfpPQLSTLTPLHIAAALPGEEGVqiVELLL 666
Cdd:PHA03095    30 VRRLLAAGADVNfrgeYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCGFTPLHLYLYNATTLDV--IKLLI 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  667 HAITDVDAKasdedDTYkpgkldllpsslklsnepgppqayystdtalpeegGRTALHmACEReddNKCAR-DIVRLLLS 745
Cdd:PHA03095   105 KAGADVNAK-----DKV-----------------------------------GRTPLH-VYLS---GFNINpKVIRLLLR 140

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1983575845  746 HGANPN-LLWSGHSPLSLSIASGN---ELvVKELLTQGADP 782
Cdd:PHA03095   141 KGADVNaLDLYGMTPLAVLLKSRNanvEL-LRLLIDAGADV 180
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 719-752 5.28e-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: 41.03  E-value: 5.28e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1983575845   719 GRTALHMACEREDdnkcaRDIVRLLLSHGANPNL 752
Cdd:smart00248    2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
354-391 1.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.10e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1983575845  354 GYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
328-391 1.77e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.56  E-value: 1.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1983575845  328 AEEGNHEwICRILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:COG0666    194 AENGHLE-IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 86-108 3.52e-04

MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple copies in several proteins including junctophilins (See Takeshima et al. Mol. Cell 2000;6:11-22). A MORN-repeat protein has been identified in the parasite Toxoplasma gondiis a dynamic component of cell division apparatus in Toxoplasma gondii. It has been hypothesized to functions as a linker protein between certain membrane regions and the parasite's cytoskeleton.


Pssm-ID: 308220 [Multi-domain]  Cd Length: 23  Bit Score: 38.54  E-value: 3.52e-04
                           10        20
                   ....*....|....*....|...
gi 1983575845   86 YHGQFYRDHCHGLGTYMWPDGSS 108
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 579-753 3.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  579 LSMIERRKRWRTIKLLLRRGADPNLCCVP-MQVLFLAVKAGDVDGVRLLLEHGARTDI--CFppqlsTLTPLHIAAAlpg 655
Cdd:PHA02875   106 LHLATILKKLDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLDIedCC-----GCTPLIIAMA--- 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  656 EEGVQIVELLLHAITDVDakasdeddtykpgkldllpsslklsnepgppqaYYStdtalpEEGGRTALhmaCEREDDNKC 735
Cdd:PHA02875   178 KGDIAICKMLLDSGANID---------------------------------YFG------KNGCVAAL---CYAIENNKI 215

                          170
                   ....*....|....*...
gi 1983575845  736 arDIVRLLLSHGANPNLL 753
Cdd:PHA02875   216 --DIVRLFIKRGADCNIM 231
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 719-782 8.89e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 8.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845  719 GRTALHMACEREDDNkcardIVRLLLSHGAN--------------PNLLWSGHSPLSLSIASGNELVVKELLTQGADP 782
Cdd:cd21882     73 GQTALHIAIENRNLN-----LVRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQP 145
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
85-105 9.10e-04

Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 37.32  E-value: 9.10e-04
                            10        20
                    ....*....|....*....|.
gi 1983575845    85 SYHGQFYRDHCHGLGTYMWPD 105
Cdd:smart00698    2 RYEGEWRNGKRHGRGVYTYAN 22
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 353-385 1.32e-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: 37.27  E-value: 1.32e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1983575845  353 KGYTVL-AAAATHCHNDIVNLLLDCGADVNKCSD 385
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
358-391 1.94e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1983575845  358 LAAAATHCHNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
608-666 1.96e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.96e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1983575845  608 MQVLFLAVKAGDVDGVRLLLEHGA---RTDICFppqlstLTPLHIAAAlpgEEGVQIVELLL 666
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAdinAVDGNG------ETALHFAAS---NGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 719-751 2.12e-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: 36.47  E-value: 2.12e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1983575845  719 GRTALHMACEREDdnkcaRDIVRLLLSHGANPN 751
Cdd:pfam13606    2 GNTPLHLAARNGR-----LEIVKLLLENGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 589-779 2.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 2.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  589 RTIKLLLRRGADPNLCC--VPmQVLFLAVKAGDVDGVRLLLEHGARTDICFPPQLSTltplhiaaalpgeegvQIVELLL 666
Cdd:PHA02874    49 KIVELFIKHGADINHINtkIP-HPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEK----------------DMIKTIL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1983575845  667 HAITDVDAKASdEDDTY-----KPGKLDLLPSSLKlsnepgppqayYSTDTALPEEGGRTALHMACEREddnkcARDIVR 741
Cdd:PHA02874   112 DCGIDVNIKDA-ELKTFlhyaiKKGDLESIKMLFE-----------YGADVNIEDDNGCYPIHIAIKHN-----FFDIIK 174

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1983575845  742 LLLSHGANPNLL-WSGHSPLSLSIASGNELVVKELLTQG 779
Cdd:PHA02874   175 LLLEKGAYANVKdNNGESPLHNAAEYGDYACIKLLIDHG 213
Ank_4 pfam13637
Ankyrin repeats (many copies);
719-776 3.41e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1983575845  719 GRTALHMACEREDDnkcarDIVRLLLSHGANPNLLW-SGHSPLSLSIASGNELVVKELL 776
Cdd:pfam13637    1 ELTALHAAAASGHL-----ELLRLLLEKGADINAVDgNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 353-382 3.57e-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: 36.03  E-value: 3.57e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1983575845   353 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 382
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
339-394 3.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.62e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1983575845  339 ILKDNFASADVADAKGYTVLAAAATHCHNDIVNLLLDCGADVNKCSDEGLTALSMC 394
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 353-382 5.35e-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: 35.31  E-value: 5.35e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1983575845  353 KGYTVLAAAATHCHNDIVNLLLDCGADVNK 382
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 336-394 6.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 6.10e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1983575845  336 ICRILKDNFASADVADAKGYTVLaaaatHC---HN---DIVNLLLDCGADVNKCSDEGLTALSMC 394
Cdd:PHA03095    65 IVRLLLEAGADVNAPERCGFTPL-----HLylyNAttlDVIKLLIKAGADVNAKDKVGRTPLHVY 124
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 336-391 6.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 6.85e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1983575845  336 ICRILKDNFASADVADAKGYTVLAAAATHC--HNDIVNLLLDCGADVNKCSDEGLTAL 391
Cdd:PHA03100    88 IVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLL 145
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 645-675 9.81e-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: 9.81e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1983575845  645 TPLHIAAALPGeeGVQIVELLLHAITDVDAK 675
Cdd:pfam00023    4 TPLHLAAGRRG--NLEIVKLLLSKGADVNAR 32
 
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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