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Conserved domains on  [gi|568909075|ref|XP_006529654|]
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ankyrin repeat and MYND domain-containing protein 1 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
33-184 3.95e-26

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 109.28  E-value: 3.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   33 TESQDSVKSYTFFRRSRPGDLGE----DEEESEGTV--GEQDLKGTYkqlvqgvqEWQDGCVYKGEFGLNMKLGYGEFSW 106
Cdd:COG4642   119 LEGDDGGGYGGGTADGGRGGGGIytfpNGDVYEGEFknGKPHGQGTL--------TYADGDRYEGEFKNGKRHGQGTLTY 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909075  107 PTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGSQDVGLW 184
Cdd:COG4642   191 ANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADgDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
592-827 5.33e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 5.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  592 ITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVslpgEEG-VKITELLLHV 669
Cdd:COG0666   103 VKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA----ANGnLEIVKLLLEA 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  670 ITNVDAKAADedyvykggkadllpsslklnnepgppksfysthtfipeegGRTALHVACEREDnkkcaRDIVRLLLSHRA 749
Cdd:COG0666   176 GADVNARDND----------------------------------------GETPLHLAAENGH-----LEIVKLLLEAGA 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909075  750 NPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDLVYEQQRSVENKIALIDRLISYGADVL 827
Cdd:COG0666   211 DVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
zf-MYND pfam01753
MYND finger;
940-980 4.24e-10

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 4.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568909075   940 CYQCGRSiGVRLSPCPRCYGILTCSKYCKTKAWiEFHKKDC 980
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-416 4.97e-10

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 4.97e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568909075  372 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:COG0666   144 ADVnaQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
 373-464 1.48e-09

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  373 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMCFLQYYPC-----KSFHPNI--AERTLLQESPKS 445
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEifkllLNNGPSIktIIETLLYFKDKD 265

                          90
                  ....*....|....*....
gi 568909075  446 LVTpKISFLLADANIDYLY 464
Cdd:PHA03100  266 LNT-ITKIKMLKKSIMYMF 283
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
33-184 3.95e-26

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 109.28  E-value: 3.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   33 TESQDSVKSYTFFRRSRPGDLGE----DEEESEGTV--GEQDLKGTYkqlvqgvqEWQDGCVYKGEFGLNMKLGYGEFSW 106
Cdd:COG4642   119 LEGDDGGGYGGGTADGGRGGGGIytfpNGDVYEGEFknGKPHGQGTL--------TYADGDRYEGEFKNGKRHGQGTLTY 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909075  107 PTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGSQDVGLW 184
Cdd:COG4642   191 ANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADgDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
592-827 5.33e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 5.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  592 ITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVslpgEEG-VKITELLLHV 669
Cdd:COG0666   103 VKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA----ANGnLEIVKLLLEA 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  670 ITNVDAKAADedyvykggkadllpsslklnnepgppksfysthtfipeegGRTALHVACEREDnkkcaRDIVRLLLSHRA 749
Cdd:COG0666   176 GADVNARDND----------------------------------------GETPLHLAAENGH-----LEIVKLLLEAGA 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909075  750 NPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDLVYEQQRSVENKIALIDRLISYGADVL 827
Cdd:COG0666   211 DVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 83-184 3.16e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 83.73  E-value: 3.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   83 WQDGCVYKGEFGLNMKLGYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYG-TMHTKTMLFQGLY 161
Cdd:PLN03185   28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107

                          90       100
                  ....*....|....*....|...
gi 568909075  162 KEDQRFGPGIETYPDGSQDVGLW 184
Cdd:PLN03185  108 IQGLQEGPGKYTWANGNVYLGDM 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 595-836 1.01e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  595 LLRRGADPNLCQVP-MQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpQLQSltPLHIAVslpgEEG-VKITELLLHVITN 672
Cdd:PHA02875   21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP-DIES--ELHDAV----EEGdVKAVEELLDLGKF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  673 VDakaadeDYVYKGGKADLLPSSLKLNNEPGPPKSFYSTHTFIPEEGGRTALHVACEREDNKkcardIVRLLLSHRANPN 752
Cdd:PHA02875   94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  753 VL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDlvyeqqrsvENKIALIDRLISYGADVlNPVT 831
Cdd:PHA02875  163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGADC-NIMF 232


                  ....*
gi 568909075  832 LVQGD 836
Cdd:PHA02875  233 MIEGE 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
720-785 3.40e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 3.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568909075   720 GRTALHVACEREDNkkcarDIVRLLLSHrANPNVLWSGHSPLSLAIASGNDLVVKELLSQGADPNL 785
Cdd:pfam12796   30 GRTALHLAAKNGHL-----EIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
zf-MYND pfam01753
MYND finger;
940-980 4.24e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 4.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568909075   940 CYQCGRSiGVRLSPCPRCYGILTCSKYCKTKAWiEFHKKDC 980
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-416 4.97e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 4.97e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568909075  372 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:COG0666   144 ADVnaQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 373-464 1.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  373 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMCFLQYYPC-----KSFHPNI--AERTLLQESPKS 445
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEifkllLNNGPSIktIIETLLYFKDKD 265

                          90
                  ....*....|....*....
gi 568909075  446 LVTpKISFLLADANIDYLY 464
Cdd:PHA03100  266 LNT-ITKIKMLKKSIMYMF 283
Ank_4 pfam13637
Ankyrin repeats (many copies);
379-416 8.52e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 8.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568909075   379 GYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
Ank_2 pfam12796
Ankyrin repeats (3 copies);
350-440 1.58e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   350 IMKAEEGDYNWIFGILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFgADVNKRsDEGITPLsmcflqYYPCKSF 429
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTAL------HYAARSG 72

                           90
                   ....*....|.
gi 568909075   430 HPNIAeRTLLQ 440
Cdd:pfam12796   73 HLEIV-KLLLE 82
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 112-134 3.66e-05

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: 41.24  E-value: 3.66e-05
                           10        20
                   ....*....|....*....|...
gi 568909075   112 YHGQFYRDHFHGLGTYTWPDGSS 134
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 720-824 1.32e-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: 46.03  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  720 GRTALHVACEREdNKKCardiVRLLLSHRAN--------------PNVLWSGHSPLSLAIASGNDLVVKELLSQGADP-N 784
Cdd:cd21882    73 GQTALHIAIENR-NLNL----VRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaA 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568909075  785 LPLTKGLGTAlcVVCDLVYEQQRSVENK---IALIDRLISYGA 824
Cdd:cd21882   148 LEAQDSLGNT--VLHALVLQADNTPENSafvCQMYNLLLSYGA 188
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 378-407 1.51e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.51e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 568909075    378 KGYTVLAAAAMHSHLDIVNLLLDFGADVNK 407
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
112-131 3.56e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 38.48  E-value: 3.56e-04
                            10        20
                    ....*....|....*....|
gi 568909075    112 YHGQFYRDHFHGLGTYTWPD 131
Cdd:smart00698    3 YEGEWRNGKRHGRGVYTYAN 22
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 720-753 5.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.42e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 568909075    720 GRTALHVACEREDnkkcaRDIVRLLLSHRANPNV 753
Cdd:smart00248    2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 381-424 1.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 1.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568909075  381 TVLAAAAMHSHL---DIVNLLLDFGADVNKRSDEGITPLSMCFLQYY 424
Cdd:PHA02878  266 YILGLTALHSSIkseRKLKLLLEYGADINSLNSYKLTPLSSAVKQYL 312
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
33-184 3.95e-26

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 109.28  E-value: 3.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   33 TESQDSVKSYTFFRRSRPGDLGE----DEEESEGTV--GEQDLKGTYkqlvqgvqEWQDGCVYKGEFGLNMKLGYGEFSW 106
Cdd:COG4642   119 LEGDDGGGYGGGTADGGRGGGGIytfpNGDVYEGEFknGKPHGQGTL--------TYADGDRYEGEFKNGKRHGQGTLTY 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909075  107 PTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGSQDVGLW 184
Cdd:COG4642   191 ANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADgDRYEGEFKNGKRHGQGTMTYADGSVYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
8-184 1.29e-22

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 98.88  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075    8 VTTDSQGSKTLSSRGLEGQNGRSLDTESQDSVKSYTFFRRSRPGDLGEDEEESEGTVGEQDLKGTYKQL-------VQGV 80
Cdd:COG4642    62 VAGGGGGEGGVTAAGGGGGGGGGKGDGGDGGGGEGGFGGGGGGGGGKKGGGGGGGGVLEGDDGGGYGGGtadggrgGGGI 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   81 QEWQDGCVYKGEFGLNMKLGYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQG 159
Cdd:COG4642   142 YTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADgDRYEG 221

                         170       180
                  ....*....|....*....|....*
gi 568909075  160 LYKEDQRFGPGIETYPDGSQDVGLW 184
Cdd:COG4642   222 EFKNGKRHGQGTLTYADGDRYEGEF 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
592-827 5.33e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 5.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  592 ITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVslpgEEG-VKITELLLHV 669
Cdd:COG0666   103 VKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA----ANGnLEIVKLLLEA 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  670 ITNVDAKAADedyvykggkadllpsslklnnepgppksfysthtfipeegGRTALHVACEREDnkkcaRDIVRLLLSHRA 749
Cdd:COG0666   176 GADVNARDND----------------------------------------GETPLHLAAENGH-----LEIVKLLLEAGA 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568909075  750 NPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDLVYEQQRSVENKIALIDRLISYGADVL 827
Cdd:COG0666   211 DVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
611-828 7.61e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.39  E-value: 7.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  611 ALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVSlpgEEGVKITELLLhvitnvdAKAADedyvykggkad 690
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDK---DGETPLHLAAY---NGNLEIVKLLL-------EAGAD----------- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  691 llpsslkLNnepgppksfysthtfIPEEGGRTALHVACEREDnkkcaRDIVRLLLSHRANPNVL-WSGHSPLSLAIASGN 769
Cdd:COG0666   146 -------VN---------------AQDNDGNTPLHLAAANGN-----LEIVKLLLEAGADVNARdNDGETPLHLAAENGH 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568909075  770 DLVVKELLSQGADPNLPLTKGlGTALCVVCDlvyeqqrsvENKIALIDRLISYGADVLN 828
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDG-KTALDLAAE---------NGNLEIVKLLLEAGADLNA 247
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 83-184 3.16e-16

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 83.73  E-value: 3.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   83 WQDGCVYKGEFGLNMKLGYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYG-TMHTKTMLFQGLY 161
Cdd:PLN03185   28 WSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSW 107

                          90       100
                  ....*....|....*....|...
gi 568909075  162 KEDQRFGPGIETYPDGSQDVGLW 184
Cdd:PLN03185  108 IQGLQEGPGKYTWANGNVYLGDM 130
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 595-836 1.01e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  595 LLRRGADPNLCQVP-MQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpQLQSltPLHIAVslpgEEG-VKITELLLHVITN 672
Cdd:PHA02875   21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP-DIES--ELHDAV----EEGdVKAVEELLDLGKF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  673 VDakaadeDYVYKGGKADLLPSSLKLNNEPGPPKSFYSTHTFIPEEGGRTALHVACEREDNKkcardIVRLLLSHRANPN 752
Cdd:PHA02875   94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  753 VL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDlvyeqqrsvENKIALIDRLISYGADVlNPVT 831
Cdd:PHA02875  163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGADC-NIMF 232


                  ....*
gi 568909075  832 LVQGD 836
Cdd:PHA02875  233 MIEGE 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
718-848 6.16e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 6.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  718 EGGRTALHVACEREDnkkcaRDIVRLLLSHRANPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLgTALC 796
Cdd:COG0666    85 DGGNTLLHAAARNGD-----LEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLH 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568909075  797 VVCDlvyeqqrsvENKIALIDRLISYGADVLNPvtlVQGDRTAVGTAVDYGY 848
Cdd:COG0666   159 LAAA---------NGNLEIVKLLLEAGADVNAR---DNDGETPLHLAAENGH 198
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 528-822 1.78e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  528 LYSVDTNfESTKCLRNytINVSRDIMEKSAQAYSSLPQHPCFPYKGTVRKMaqSMVErrnrwmtitLLLRRGADPN---- 603
Cdd:PHA03100    1 LYSYIVL-TKSRIIKV--KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNI--DVVK---------ILLDNGADINsstk 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  604 --LCQVPMQALFLAVKAGDVEGVRLLLMSGAQTDIQFPPQLqslTPLHIAVSLPGEEgVKITELLLHVITNVDAKAADED 681
Cdd:PHA03100   67 nnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGI---TPLLYAISKKSNS-YSIVEYLLDNGANVNIKNSDGE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  682 ----YVYKGGKADLLPSSLKLN-----NEPGPPKSF--YSTHTFIPEEGGRTALHVACEReDNKkcarDIVRLLLSHRAN 750
Cdd:PHA03100  143 nllhLYLESNKIDLKILKLLIDkgvdiNAKNRVNYLlsYGVPINIKDVYGFTPLHYAVYN-NNP----EFVKYLLDLGAN 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568909075  751 PNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLpltkglgtalcVVCDLVYEQQR--SVENKIALIDRLISY 822
Cdd:PHA03100  218 PNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT-----------IIETLLYFKDKdlNTITKIKMLKKSIMY 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
720-785 3.40e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 3.40e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568909075   720 GRTALHVACEREDNkkcarDIVRLLLSHrANPNVLWSGHSPLSLAIASGNDLVVKELLSQGADPNL 785
Cdd:pfam12796   30 GRTALHLAAKNGHL-----EIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
zf-MYND pfam01753
MYND finger;
940-980 4.24e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 4.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568909075   940 CYQCGRSiGVRLSPCPRCYGILTCSKYCKTKAWiEFHKKDC 980
Cdd:pfam01753    1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-416 4.97e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 4.97e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568909075  372 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:COG0666   144 ADVnaQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 373-464 1.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  373 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMCFLQYYPC-----KSFHPNI--AERTLLQESPKS 445
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEifkllLNNGPSIktIIETLLYFKDKD 265

                          90
                  ....*....|....*....
gi 568909075  446 LVTpKISFLLADANIDYLY 464
Cdd:PHA03100  266 LNT-ITKIKMLKKSIMYMF 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
373-416 1.52e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568909075  373 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 77-153 2.86e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 61.39  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   77 VQGVQE------WQDGCVYKGEFGLNMKLGYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTM 150
Cdd:PLN03185  108 IQGLQEgpgkytWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVF 187


                  ...
gi 568909075  151 HTK 153
Cdd:PLN03185  188 YPA 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
372-418 3.33e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 3.33e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568909075  372 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSM 418
Cdd:COG0666   177 ADVnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
612-753 5.75e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 5.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   612 LFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVSLPGEEGVKIteLLLHVITNVDakaadedyvykggkadl 691
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAAKNGHLEIVKL--LLEHADVNLK----------------- 58

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568909075   692 lpsslklnnepgppksfysthtfipeEGGRTALHVACErednkKCARDIVRLLLSHRANPNV 753
Cdd:pfam12796   59 --------------------------DNGRTALHYAAR-----SGHLEIVKLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
349-416 2.98e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 2.98e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568909075  349 MIMKAEEGDYNWIFGILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 85-184 5.56e-08

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 57.15  E-value: 5.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   85 DGCVYKGEFGLNMKLGYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGT-MHTKTMLFQGLYKE 163
Cdd:PLN03185    7 NGDFYSGSLLGNVPEGPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTyTGTDGTTYKGRWRL 86

                          90       100
                  ....*....|....*....|.
gi 568909075  164 DQRFGPGIETYPDGSQDVGLW 184
Cdd:PLN03185   87 NLKHGLGYQRYPNGDVFEGSW 107
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
739-826 3.06e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  739 DIVRLLLSHRANPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGlGTALCVVCDlvyeqqrsvENKIALID 817
Cdd:COG0666    68 LVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAY---------NGNLEIVK 137


                  ....*....
gi 568909075  818 RLISYGADV 826
Cdd:COG0666   138 LLLEAGADV 146
Ank_4 pfam13637
Ankyrin repeats (many copies);
379-416 8.52e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 8.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568909075   379 GYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 720-753 3.08e-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: 44.59  E-value: 3.08e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568909075   720 GRTALHVACEREDNKkcarDIVRLLLSHRANPNV 753
Cdd:pfam00023    2 GNTPLHLAAGRRGNL----EIVKLLLSKGADVNA 31
Ank_2 pfam12796
Ankyrin repeats (3 copies);
591-676 4.88e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 4.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   591 TITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLmSGAQTDIqfppQLQSLTPLHIAVSLPGEEGVKiteLLLHV 669
Cdd:pfam12796   12 LVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLL-EHADVNL----KDNGRTALHYAARSGHLEIVK---LLLEK 83


                   ....*..
gi 568909075   670 ITNVDAK 676
Cdd:pfam12796   84 GADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
724-826 1.14e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   724 LHVACEREDNkkcarDIVRLLLSHRANPNVLWS-GHSPLSLAIASGNDLVVKELLSQgADPNLPlTKGLgTALCVVCdlv 802
Cdd:pfam12796    1 LHLAAKNGNL-----ELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGR-TALHYAA--- 69

                           90       100
                   ....*....|....*....|....
gi 568909075   803 yeqqrsVENKIALIDRLISYGADV 826
Cdd:pfam12796   70 ------RSGHLEIVKLLLEKGADI 87
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 607-784 1.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  607 VPMQALFLAVKAGDVEGVRLLLMSGAQTDiqfPPQLQSLTPLHIAVSLPGEEGVK-----------------ITELLLH- 668
Cdd:PHA02878   36 IPFIPLHQAVEARNLDVVKSLLTRGHNVN---QPDHRDLTPLHIICKEPNKLGMKemirsinkcsvfytlvaIKDAFNNr 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  669 -------VITNVDAKAADEDYVY--KGGKADLLPSSL-KLNNEPGPPKSFYSTHTfipeegGRTALHVACEREDnkkcaR 738
Cdd:PHA02878  113 nveifkiILTNRYKNIQTIDLVYidKKSKDDIIEAEItKLLLSYGADINMKDRHK------GNTALHYATENKD-----Q 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 568909075  739 DIVRLLLSHRANPNVLWSG-HSPLSLAIASGNDLVVKELLSQGADPN 784
Cdd:PHA02878  182 RLTELLLSYGANVNIPDKTnNSPLHHAVKHYNKPIVHILLENGASTD 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
350-440 1.58e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   350 IMKAEEGDYNWIFGILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFgADVNKRsDEGITPLsmcflqYYPCKSF 429
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTAL------HYAARSG 72

                           90
                   ....*....|.
gi 568909075   430 HPNIAeRTLLQ 440
Cdd:pfam12796   73 HLEIV-KLLLE 82
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 112-134 3.66e-05

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: 41.24  E-value: 3.66e-05
                           10        20
                   ....*....|....*....|...
gi 568909075   112 YHGQFYRDHFHGLGTYTWPDGSS 134
Cdd:pfam02493    1 YEGEWKNGKRHGKGVYTWPDGDR 23
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 620-799 4.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  620 DVEGVRLLLMSGAQTDIQFPPQLQslTPLHIAVSLPGEegvKITELLLhvitnvdAKAADEDYVYKGGKADLLpSSLKLN 699
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGN--TALHYATENKDQ---RLTELLL-------SYGANVNIPDKTNNSPLH-HAVKHY 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  700 NEPGPPKSF-YSTHTFIPEEGGRTALHVACEREDNKkcarDIVRLLLSHRANPNVLWS--GHSPLSLAIASGNdlVVKEL 776
Cdd:PHA02878  213 NKPIVHILLeNGASTDARDKCGNTPLHISVGYCKDY----DILKLLLEHGVDVNAKSYilGLTALHSSIKSER--KLKLL 286

                         170       180       190
                  ....*....|....*....|....*....|
gi 568909075  777 LSQGADPNL-------PLTKGLGTALCVVC 799
Cdd:PHA02878  287 LEYGADINSlnsykltPLSSAVKQYLCINI 316
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 378-410 5.05e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 5.05e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568909075   378 KGYTVL-AAAAMHSHLDIVNLLLDFGADVNKRSD 410
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 720-824 1.32e-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: 46.03  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  720 GRTALHVACEREdNKKCardiVRLLLSHRAN--------------PNVLWSGHSPLSLAIASGNDLVVKELLSQGADP-N 784
Cdd:cd21882    73 GQTALHIAIENR-NLNL----VRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaA 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568909075  785 LPLTKGLGTAlcVVCDLVYEQQRSVENK---IALIDRLISYGA 824
Cdd:cd21882   148 LEAQDSLGNT--VLHALVLQADNTPENSafvCQMYNLLLSYGA 188
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 378-407 1.51e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.51e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 568909075    378 KGYTVLAAAAMHSHLDIVNLLLDFGADVNK 407
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
369-408 2.06e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.25  E-value: 2.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568909075   369 LACADV-ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKR 408
Cdd:pfam12796   50 LEHADVnLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_5 pfam13857
Ankyrin repeats (many copies);
376-419 2.22e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.22e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 568909075   376 DSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMC 419
Cdd:pfam13857   13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
112-131 3.56e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 38.48  E-value: 3.56e-04
                            10        20
                    ....*....|....*....|
gi 568909075    112 YHGQFYRDHFHGLGTYTWPD 131
Cdd:smart00698    3 YEGEWRNGKRHGRGVYTYAN 22
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 720-753 5.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.42e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 568909075    720 GRTALHVACEREDnkkcaRDIVRLLLSHRANPNV 753
Cdd:smart00248    2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 378-407 1.37e-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: 37.24  E-value: 1.37e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568909075   378 KGYTVLAAAAMHSHLDIVNLLLDFGADVNK 407
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 381-424 1.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 1.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 568909075  381 TVLAAAAMHSHL---DIVNLLLDFGADVNKRSDEGITPLSMCFLQYY 424
Cdd:PHA02878  266 YILGLTALHSSIkseRKLKLLLEYGADINSLNSYKLTPLSSAVKQYL 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
 361-419 1.71e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  361 IFGILRDNLACADVADSKGYTVLAAAAMHSH-LDIVNLLLDFGADVNKRSDEGITPLSMC 419
Cdd:PHA03095   65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVY 124
PHA03095 PHA03095
ankyrin-like protein; Provisional
 372-423 4.18e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 4.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568909075  372 ADVADSKGY-----TVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLsMCFLQY 423
Cdd:PHA03095   38 ADVNFRGEYgktplHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPL-HLYLYN 93
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 364-494 4.41e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075  364 ILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLsmcflqyypcksfhpNIAERTLLQESP 443
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL---------------ELAEENGFREVV 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568909075  444 KSLVTPKISFLLADANidylydvGMPiaggDEL--KTSSLDDSLASMQTPESS 494
Cdd:PTZ00322  165 QLLSRHSQCHFELGAN-------AKP----DSFtgKPPSLEDSPISSHHPDFS 206
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 364-416 4.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 4.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568909075  364 ILRDNLACADVADSKGYTVLAAAAMHS--HLDIVNLLLDFGADVNKRSDEGITPL 416
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLL 145
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 757-785 5.08e-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: 5.08e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568909075   757 GHSPLSLAIASGNDL-VVKELLSQGADPNL 785
Cdd:pfam00023    2 GNTPLHLAAGRRGNLeIVKLLLSKGADVNA 31
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 757-785 5.25e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 5.25e-03
                            10        20
                    ....*....|....*....|....*....
gi 568909075    757 GHSPLSLAIASGNDLVVKELLSQGADPNL 785
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
761-853 7.72e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.63  E-value: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568909075   761 LSLAIASGNDLVVKELLSQGADPNLPLTKGLgTALCVVCdlvyeqqrsVENKIALIDRLISYGAdvlnpVTLVQGDRTAV 840
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAA---------KNGHLEIVKLLLEHAD-----VNLKDNGRTAL 65

                           90
                   ....*....|...
gi 568909075   841 GTAVDYGYFKFFQ 853
Cdd:pfam12796   66 HYAARSGHLEIVK 78
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 757-784 7.95e-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: 34.93  E-value: 7.95e-03
                           10        20
                   ....*....|....*....|....*...
gi 568909075   757 GHSPLSLAIASGNDLVVKELLSQGADPN 784
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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