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Conserved domains on  [gi|113197611|gb|AAI20888|]
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Ankmy1 protein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4642 super family cl34799
Uncharacterized conserved protein [Function unknown];
4-88 1.26e-20

Uncharacterized conserved protein [Function unknown];


The actual alignment was detected with superfamily member COG4642:

Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 92.71  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGS 82
Cdd:COG4642  184 GQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADgDRYEGEFKNGKRHGQGTMTYADGS 263


                 ....*.
gi 113197611  83 QDVGLW 88
Cdd:COG4642  264 VYEGEW 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
496-731 4.39e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 4.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 496 ITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVslpgEEG-VKITELLLHV 573
Cdd:COG0666  103 VKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA----ANGnLEIVKLLLEA 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 574 ITNVDAKAADedyvykggkadllpsslklnnepgppksfysthtfipeegGRTALHVACEREDnkkcaRDIVRLLLSHRA 653
Cdd:COG0666  176 GADVNARDND----------------------------------------GETPLHLAAENGH-----LEIVKLLLEAGA 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113197611 654 NPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDLVYEQQRSVENKIALIDRLISYGADVL 731
Cdd:COG0666  211 DVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
zf-MYND pfam01753
MYND finger;
844-884 3.94e-10

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.50  E-value: 3.94e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 113197611  844 CYQCGRSiGVRLSPCPRCYGILTCSKYCKTKAWiEFHKKDC 884
Cdd:pfam01753   1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-320 4.12e-10

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 4.12e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 113197611 276 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:COG0666  144 ADVnaQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
 277-368 1.81e-09

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 277 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMCFLQYYPC-----KSFHPNI--AERTLLQESPKS 349
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEifkllLNNGPSIktIIETLLYFKDKD 265

                         90
                 ....*....|....*....
gi 113197611 350 LVTpKISFLLADANIDYLY 368
Cdd:PHA03100 266 LNT-ITKIKMLKKSIMYMF 283
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
4-88 1.26e-20

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 92.71  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGS 82
Cdd:COG4642  184 GQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADgDRYEGEFKNGKRHGQGTMTYADGS 263


                 ....*.
gi 113197611  83 QDVGLW 88
Cdd:COG4642  264 VYEGEW 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
496-731 4.39e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 4.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 496 ITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVslpgEEG-VKITELLLHV 573
Cdd:COG0666  103 VKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA----ANGnLEIVKLLLEA 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 574 ITNVDAKAADedyvykggkadllpsslklnnepgppksfysthtfipeegGRTALHVACEREDnkkcaRDIVRLLLSHRA 653
Cdd:COG0666  176 GADVNARDND----------------------------------------GETPLHLAAENGH-----LEIVKLLLEAGA 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113197611 654 NPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDLVYEQQRSVENKIALIDRLISYGADVL 731
Cdd:COG0666  211 DVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 499-740 8.15e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 8.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 499 LLRRGADPNLCQVP-MQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpQLQSltPLHIAVslpgEEG-VKITELLLHVITN 576
Cdd:PHA02875  21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP-DIES--ELHDAV----EEGdVKAVEELLDLGKF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 577 VDakaadeDYVYKGGKADLLPSSLKLNNEPGPPKSFYSTHTFIPEEGGRTALHVACEREDNKkcardIVRLLLSHRANPN 656
Cdd:PHA02875  94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 657 VL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDlvyeqqrsvENKIALIDRLISYGADVlNPVT 735
Cdd:PHA02875 163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGADC-NIMF 232


                 ....*
gi 113197611 736 LVQGD 740
Cdd:PHA02875 233 MIEGE 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
624-689 2.90e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 2.90e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113197611  624 GRTALHVACEREDNkkcarDIVRLLLSHrANPNVLWSGHSPLSLAIASGNDLVVKELLSQGADPNL 689
Cdd:pfam12796  30 GRTALHLAAKNGHL-----EIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
zf-MYND pfam01753
MYND finger;
844-884 3.94e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.50  E-value: 3.94e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 113197611  844 CYQCGRSiGVRLSPCPRCYGILTCSKYCKTKAWiEFHKKDC 884
Cdd:pfam01753   1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-320 4.12e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 4.12e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 113197611 276 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:COG0666  144 ADVnaQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 277-368 1.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 277 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMCFLQYYPC-----KSFHPNI--AERTLLQESPKS 349
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEifkllLNNGPSIktIIETLLYFKDKD 265

                         90
                 ....*....|....*....
gi 113197611 350 LVTpKISFLLADANIDYLY 368
Cdd:PHA03100 266 LNT-ITKIKMLKKSIMYMF 283
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1-88 2.21e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 61.39  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   1 MKLGYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYG-TMHTKTMLFQGLYKEDQRFGPGIETYP 79
Cdd:PLN03185  42 MRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSWIQGLQEGPGKYTWA 121


                 ....*....
gi 113197611  80 DGSQDVGLW 88
Cdd:PLN03185 122 NGNVYLGDM 130
Ank_4 pfam13637
Ankyrin repeats (many copies);
283-320 8.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 8.80e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 113197611  283 GYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-344 1.34e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611  254 IMKAEEGDYNWIFGILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFgADVNKRsDEGITPLsmcflqYYPCKSF 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTAL------HYAARSG 72

                          90
                  ....*....|.
gi 113197611  334 HPNIAeRTLLQ 344
Cdd:pfam12796  73 HLEIV-KLLLE 82
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 16-38 3.15e-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: 3.15e-05
                          10        20
                  ....*....|....*....|...
gi 113197611   16 YHGQFYRDHFHGLGTYTWPDGSS 38
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 282-311 1.30e-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: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 113197611   282 KGYTVLAAAAMHSHLDIVNLLLDFGADVNK 311
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 624-728 1.63e-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: 45.26  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 624 GRTALHVACEREdNKKCardiVRLLLSHRAN--------------PNVLWSGHSPLSLAIASGNDLVVKELLSQGADP-N 688
Cdd:cd21882   73 GQTALHIAIENR-NLNL----VRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 113197611 689 LPLTKGLGTAlcVVCDLVYEQQRSVENK---IALIDRLISYGA 728
Cdd:cd21882  148 LEAQDSLGNT--VLHALVLQADNTPENSafvCQMYNLLLSYGA 188
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
16-35 2.28e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 38.86  E-value: 2.28e-04
                           10        20
                   ....*....|....*....|
gi 113197611    16 YHGQFYRDHFHGLGTYTWPD 35
Cdd:smart00698   3 YEGEWRNGKRHGRGVYTYAN 22
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 624-657 4.65e-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: 4.65e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 113197611   624 GRTALHVACEREDnkkcaRDIVRLLLSHRANPNV 657
Cdd:smart00248   2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 265-323 1.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 265 IFGILRDNLACADVADSKGYTVLAAAAMHSH-LDIVNLLLDFGADVNKRSDEGITPLSMC 323
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVY 124
 
Name Accession Description Interval E-value
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
4-88 1.26e-20

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 92.71  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGS 82
Cdd:COG4642  184 GQGTLTYANGDVYEGEFKNGQRHGQGTYTYADGDRYEGEFKNGKRHGQGTLTYADgDRYEGEFKNGKRHGQGTMTYADGS 263


                 ....*.
gi 113197611  83 QDVGLW 88
Cdd:COG4642  264 VYEGEW 269
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
4-88 1.59e-18

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 86.55  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGS 82
Cdd:COG4642  138 GGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADGDRYEGEFKNGKRHGQGTLTYANgDVYEGEFKNGQRHGQGTYTYADGD 217


                 ....*.
gi 113197611  83 QDVGLW 88
Cdd:COG4642  218 RYEGEF 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
496-731 4.39e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 4.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 496 ITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVslpgEEG-VKITELLLHV 573
Cdd:COG0666  103 VKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN---DGNTPLHLAA----ANGnLEIVKLLLEA 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 574 ITNVDAKAADedyvykggkadllpsslklnnepgppksfysthtfipeegGRTALHVACEREDnkkcaRDIVRLLLSHRA 653
Cdd:COG0666  176 GADVNARDND----------------------------------------GETPLHLAAENGH-----LEIVKLLLEAGA 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113197611 654 NPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDLVYEQQRSVENKIALIDRLISYGADVL 731
Cdd:COG0666  211 DVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
4-88 5.60e-18

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 85.01  E-value: 5.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGS 82
Cdd:COG4642  161 GQGTLTYADGDRYEGEFKNGKRHGQGTLTYANGDVYEGEFKNGQRHGQGTYTYADgDRYEGEFKNGKRHGQGTLTYADGD 240


                 ....*.
gi 113197611  83 QDVGLW 88
Cdd:COG4642  241 RYEGEF 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
515-732 6.27e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.39  E-value: 6.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 515 ALFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVSlpgEEGVKITELLLhvitnvdAKAADedyvykggkad 594
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDK---DGETPLHLAAY---NGNLEIVKLLL-------EAGAD----------- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 595 llpsslkLNnepgppksfysthtfIPEEGGRTALHVACEREDnkkcaRDIVRLLLSHRANPNVL-WSGHSPLSLAIASGN 673
Cdd:COG0666  146 -------VN---------------AQDNDGNTPLHLAAANGN-----LEIVKLLLEAGADVNARdNDGETPLHLAAENGH 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 113197611 674 DLVVKELLSQGADPNLPLTKGlGTALCVVCDlvyeqqrsvENKIALIDRLISYGADVLN 732
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDG-KTALDLAAE---------NGNLEIVKLLLEAGADLNA 247
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 499-740 8.15e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 8.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 499 LLRRGADPNLCQVP-MQALFLAVKAGDVEGVRLLLMSGAQTDIQFPpQLQSltPLHIAVslpgEEG-VKITELLLHVITN 576
Cdd:PHA02875  21 LLDIGINPNFEIYDgISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP-DIES--ELHDAV----EEGdVKAVEELLDLGKF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 577 VDakaadeDYVYKGGKADLLPSSLKLNNEPGPPKSFYSTHTFIPEEGGRTALHVACEREDNKkcardIVRLLLSHRANPN 656
Cdd:PHA02875  94 AD------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK-----GIELLIDHKACLD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 657 VL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLGTALCVVCDlvyeqqrsvENKIALIDRLISYGADVlNPVT 735
Cdd:PHA02875 163 IEdCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIE---------NNKIDIVRLFIKRGADC-NIMF 232


                 ....*
gi 113197611 736 LVQGD 740
Cdd:PHA02875 233 MIEGE 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
622-752 5.09e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 5.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 622 EGGRTALHVACEREDnkkcaRDIVRLLLSHRANPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGLgTALC 700
Cdd:COG0666   85 DGGNTLLHAAARNGD-----LEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN-TPLH 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 113197611 701 VVCDlvyeqqrsvENKIALIDRLISYGADVLNPvtlVQGDRTAVGTAVDYGY 752
Cdd:COG0666  159 LAAA---------NGNLEIVKLLLEAGADVNAR---DNDGETPLHLAAENGH 198
COG4642 COG4642
Uncharacterized conserved protein [Function unknown];
4-88 2.76e-11

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443680 [Multi-domain]  Cd Length: 271  Bit Score: 64.98  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTKT-MLFQGLYKEDQRFGPGIETYPDGS 82
Cdd:COG4642  115 GGGVLEGDDGGGYGGGTADGGRGGGGIYTFPNGDVYEGEFKNGKPHGQGTLTYADgDRYEGEFKNGKRHGQGTLTYANGD 194


                 ....*.
gi 113197611  83 QDVGLW 88
Cdd:COG4642  195 VYEGEF 200
Ank_2 pfam12796
Ankyrin repeats (3 copies);
624-689 2.90e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 2.90e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113197611  624 GRTALHVACEREDNkkcarDIVRLLLSHrANPNVLWSGHSPLSLAIASGNDLVVKELLSQGADPNL 689
Cdd:pfam12796  30 GRTALHLAAKNGHL-----EIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 432-726 3.40e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 432 LYSVDTNfESTKCLRNytINVSRDIMEKSAQAYSSLPQHPCFPYKGTVRKMaqSMVErrnrwmtitLLLRRGADPN---- 507
Cdd:PHA03100   1 LYSYIVL-TKSRIIKV--KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNI--DVVK---------ILLDNGADINsstk 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 508 --LCQVPMQALFLAVKAGDVEGVRLLLMSGAQTDIqfpPQLQSLTPLHIAVSLPGEEgVKITELLLHVITNVDAKAADED 585
Cdd:PHA03100  67 nnSTPLHYLSNIKYNLTDVKEIVKLLLEYGANVNA---PDNNGITPLLYAISKKSNS-YSIVEYLLDNGANVNIKNSDGE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 586 ----YVYKGGKADLLPSSLKLN-----NEPGPPKSF--YSTHTFIPEEGGRTALHVACEReDNKkcarDIVRLLLSHRAN 654
Cdd:PHA03100 143 nllhLYLESNKIDLKILKLLIDkgvdiNAKNRVNYLlsYGVPINIKDVYGFTPLHYAVYN-NNP----EFVKYLLDLGAN 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113197611 655 PNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLpltkglgtalcVVCDLVYEQQR--SVENKIALIDRLISY 726
Cdd:PHA03100 218 PNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT-----------IIETLLYFKDKdlNTITKIKMLKKSIMY 281
zf-MYND pfam01753
MYND finger;
844-884 3.94e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.50  E-value: 3.94e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 113197611  844 CYQCGRSiGVRLSPCPRCYGILTCSKYCKTKAWiEFHKKDC 884
Cdd:pfam01753   1 CAVCGKE-ALKLLRCSRCKSVYYCSKECQKADW-PYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-320 4.12e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.89  E-value: 4.12e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 113197611 276 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:COG0666  144 ADVnaQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
277-320 1.26e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 1.26e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 113197611 277 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:COG0666  114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 277-368 1.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 277 DVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMCFLQYYPC-----KSFHPNI--AERTLLQESPKS 349
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEifkllLNNGPSIktIIETLLYFKDKD 265

                         90
                 ....*....|....*....
gi 113197611 350 LVTpKISFLLADANIDYLY 368
Cdd:PHA03100 266 LNT-ITKIKMLKKSIMYMF 283
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 1-88 2.21e-09

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 61.39  E-value: 2.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   1 MKLGYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYG-TMHTKTMLFQGLYKEDQRFGPGIETYP 79
Cdd:PLN03185  42 MRHGNGKISWPSGATYEGEFSGGYMHGSGTYTGTDGTTYKGRWRLNLKHGLGyQRYPNGDVFEGSWIQGLQEGPGKYTWA 121


                 ....*....
gi 113197611  80 DGSQDVGLW 88
Cdd:PLN03185 122 NGNVYLGDM 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-322 2.76e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 2.76e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 113197611 276 ADV--ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSM 322
Cdd:COG0666  177 ADVnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
516-657 4.90e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 4.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611  516 LFLAVKAGDVEGVRLLLMSGAQTDIQFPpqlQSLTPLHIAVSLPGEEGVKIteLLLHVITNVDakaadedyvykggkadl 595
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK---NGRTALHLAAKNGHLEIVKL--LLEHADVNLK----------------- 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113197611  596 lpsslklnnepgppksfysthtfipeEGGRTALHVACErednkKCARDIVRLLLSHRANPNV 657
Cdd:pfam12796  59 --------------------------DNGRTALHYAAR-----SGHLEIVKLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-320 2.48e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 2.48e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113197611 253 MIMKAEEGDYNWIFGILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
643-730 2.54e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 643 DIVRLLLSHRANPNVL-WSGHSPLSLAIASGNDLVVKELLSQGADPNLPLTKGlGTALCVVCDlvyeqqrsvENKIALID 721
Cdd:COG0666   68 LVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAY---------NGNLEIVK 137


                 ....*....
gi 113197611 722 RLISYGADV 730
Cdd:COG0666  138 LLLEAGADV 146
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 4-88 5.36e-07

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 53.68  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGT-MHTKTMLFQGLYKEDQRFGPGIETYPDGS 82
Cdd:PLN03185  22 GPGKYLWSDGCMYEGEWRRGMRHGNGKISWPSGATYEGEFSGGYMHGSGTyTGTDGTTYKGRWRLNLKHGLGYQRYPNGD 101


                 ....*.
gi 113197611  83 QDVGLW 88
Cdd:PLN03185 102 VFEGSW 107
Ank_4 pfam13637
Ankyrin repeats (many copies);
283-320 8.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 8.80e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 113197611  283 GYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 624-657 2.65e-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: 2.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 113197611  624 GRTALHVACEREDNKkcarDIVRLLLSHRANPNV 657
Cdd:pfam00023   2 GNTPLHLAAGRRGNL----EIVKLLLSKGADVNA 31
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 4-57 3.72e-06

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 50.99  E-value: 3.72e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTFYLSQREGYGTMHTK 57
Cdd:PLN03185 137 GKGTLTWVSGDSYEGQWLDGMMHGFGVYTWSDGGCYVGTWTRGLKDGKGVFYPA 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
495-580 4.16e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611  495 TITLLLRRGADPNLC-QVPMQALFLAVKAGDVEGVRLLLmSGAQTDIqfppQLQSLTPLHIAVSLPGEEGVKiteLLLHV 573
Cdd:pfam12796  12 LVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLL-EHADVNL----KDNGRTALHYAARSGHLEIVK---LLLEK 83


                  ....*..
gi 113197611  574 ITNVDAK 580
Cdd:pfam12796  84 GADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
628-730 9.73e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 9.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611  628 LHVACEREDNkkcarDIVRLLLSHRANPNVLWS-GHSPLSLAIASGNDLVVKELLSQgADPNLPlTKGLgTALCVVCdlv 706
Cdd:pfam12796   1 LHLAAKNGNL-----ELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGR-TALHYAA--- 69

                          90       100
                  ....*....|....*....|....
gi 113197611  707 yeqqrsVENKIALIDRLISYGADV 730
Cdd:pfam12796  70 ------RSGHLEIVKLLLEKGADI 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-344 1.34e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611  254 IMKAEEGDYNWIFGILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFgADVNKRsDEGITPLsmcflqYYPCKSF 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTAL------HYAARSG 72

                          90
                  ....*....|.
gi 113197611  334 HPNIAeRTLLQ 344
Cdd:pfam12796  73 HLEIV-KLLLE 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 511-688 1.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 511 VPMQALFLAVKAGDVEGVRLLLMSGAQTDiqfPPQLQSLTPLHIAVSLPGEEGVK-----------------ITELLLH- 572
Cdd:PHA02878  36 IPFIPLHQAVEARNLDVVKSLLTRGHNVN---QPDHRDLTPLHIICKEPNKLGMKemirsinkcsvfytlvaIKDAFNNr 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 573 -------VITNVDAKAADEDYVY--KGGKADLLPSSL-KLNNEPGPPKSFYSTHTfipeegGRTALHVACEREDnkkcaR 642
Cdd:PHA02878 113 nveifkiILTNRYKNIQTIDLVYidKKSKDDIIEAEItKLLLSYGADINMKDRHK------GNTALHYATENKD-----Q 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 113197611 643 DIVRLLLSHRANPNVLWSG-HSPLSLAIASGNDLVVKELLSQGADPN 688
Cdd:PHA02878 182 RLTELLLSYGANVNIPDKTnNSPLHHAVKHYNKPIVHILLENGASTD 228
MORN pfam02493
MORN repeat; The MORN (Membrane Occupation and Recognition Nexus) repeat is found in multiple ...
 16-38 3.15e-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: 3.15e-05
                          10        20
                  ....*....|....*....|...
gi 113197611   16 YHGQFYRDHFHGLGTYTWPDGSS 38
Cdd:pfam02493   1 YEGEWKNGKRHGKGVYTWPDGDR 23
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 282-314 4.34e-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: 4.34e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 113197611  282 KGYTVL-AAAAMHSHLDIVNLLLDFGADVNKRSD 314
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 524-703 6.84e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 524 DVEGVRLLLMSGAQTDIQFPPQLQslTPLHIAVSLPGEegvKITELLLhvitnvdAKAADEDYVYKGGKADLLpSSLKLN 603
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGN--TALHYATENKDQ---RLTELLL-------SYGANVNIPDKTNNSPLH-HAVKHY 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 604 NEPGPPKSF-YSTHTFIPEEGGRTALHVACEREDNKkcarDIVRLLLSHRANPNVLWS--GHSPLSLAIASGNdlVVKEL 680
Cdd:PHA02878 213 NKPIVHILLeNGASTDARDKCGNTPLHISVGYCKDY----DILKLLLEHGVDVNAKSYilGLTALHSSIKSER--KLKLL 286

                        170       180       190
                 ....*....|....*....|....*....|
gi 113197611 681 LSQGADPNL-------PLTKGLGTALCVVC 703
Cdd:PHA02878 287 LEYGADINSlnsykltPLSSAVKQYLCINI 316
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 282-311 1.30e-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: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 113197611   282 KGYTVLAAAAMHSHLDIVNLLLDFGADVNK 311
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 624-728 1.63e-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: 45.26  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 624 GRTALHVACEREdNKKCardiVRLLLSHRAN--------------PNVLWSGHSPLSLAIASGNDLVVKELLSQGADP-N 688
Cdd:cd21882   73 GQTALHIAIENR-NLNL----VRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaA 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 113197611 689 LPLTKGLGTAlcVVCDLVYEQQRSVENK---IALIDRLISYGA 728
Cdd:cd21882  148 LEAQDSLGNT--VLHALVLQADNTPENSafvCQMYNLLLSYGA 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-312 1.75e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.25  E-value: 1.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 113197611  273 LACADV-ADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKR 312
Cdd:pfam12796  50 LEHADVnLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
MORN smart00698
Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases;
16-35 2.28e-04

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


Pssm-ID: 197832 [Multi-domain]  Cd Length: 22  Bit Score: 38.86  E-value: 2.28e-04
                           10        20
                   ....*....|....*....|
gi 113197611    16 YHGQFYRDHFHGLGTYTWPD 35
Cdd:smart00698   3 YEGEWRNGKRHGRGVYTYAN 22
Ank_5 pfam13857
Ankyrin repeats (many copies);
280-323 2.62e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 113197611  280 DSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLSMC 323
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03185 PLN03185
phosphatidylinositol phosphate kinase; Provisional
 4-90 3.94e-04

phosphatidylinositol phosphate kinase; Provisional


Pssm-ID: 215619 [Multi-domain]  Cd Length: 765  Bit Score: 44.05  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611   4 GYGEFSWPTGEAYHGQFYRDHFHGLGTYTWPDGSSFTGTfYLSqregyGTMHtktmlfqglykedqrfGPGIETYPDGSQ 83
Cdd:PLN03185 114 GPGKYTWANGNVYLGDMKGGKMSGKGTLTWVSGDSYEGQ-WLD-----GMMH----------------GFGVYTWSDGGC 171


                 ....*..
gi 113197611  84 DVGLWFR 90
Cdd:PLN03185 172 YVGTWTR 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 624-657 4.65e-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: 4.65e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 113197611   624 GRTALHVACEREDnkkcaRDIVRLLLSHRANPNV 657
Cdd:smart00248   2 GRTPLHLAAENGN-----LEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 282-311 1.17e-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: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 113197611  282 KGYTVLAAAAMHSHLDIVNLLLDFGADVNK 311
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 265-323 1.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 1.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 265 IFGILRDNLACADVADSKGYTVLAAAAMHSH-LDIVNLLLDFGADVNKRSDEGITPLSMC 323
Cdd:PHA03095  65 IVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVY 124
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 285-328 1.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 113197611 285 TVLAAAAMHSHL---DIVNLLLDFGADVNKRSDEGITPLSMCFLQYY 328
Cdd:PHA02878 266 YILGLTALHSSIkseRKLKLLLEYGADINSLNSYKLTPLSSAVKQYL 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
 276-327 3.49e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 3.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 113197611 276 ADVADSKGY-----TVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLsMCFLQY 327
Cdd:PHA03095  38 ADVNFRGEYgktplHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPL-HLYLYN 93
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 268-398 3.77e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611 268 ILRDNLACADVADSKGYTVLAAAAMHSHLDIVNLLLDFGADVNKRSDEGITPLsmcflqyypcksfhpNIAERTLLQESP 347
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL---------------ELAEENGFREVV 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 113197611 348 KSLVTPKISFLLADANidylydvGMPiaggDEL--KTSSLDDSLASMQTPESS 398
Cdd:PTZ00322 165 QLLSRHSQCHFELGAN-------AKP----DSFtgKPPSLEDSPISSHHPDFS 206
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 661-689 4.36e-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: 4.36e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 113197611  661 GHSPLSLAIASGNDL-VVKELLSQGADPNL 689
Cdd:pfam00023   2 GNTPLHLAAGRRGNLeIVKLLLSKGADVNA 31
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 661-689 4.51e-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: 4.51e-03
                           10        20
                   ....*....|....*....|....*....
gi 113197611   661 GHSPLSLAIASGNDLVVKELLSQGADPNL 689
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 268-320 5.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 5.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 113197611 268 ILRDNLACADVADSKGYTVLAAAAMHS--HLDIVNLLLDFGADVNKRSDEGITPL 320
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLL 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
665-757 6.58e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.63  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113197611  665 LSLAIASGNDLVVKELLSQGADPNLPLTKGLgTALCVVCdlvyeqqrsVENKIALIDRLISYGAdvlnpVTLVQGDRTAV 744
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAA---------KNGHLEIVKLLLEHAD-----VNLKDNGRTAL 65

                          90
                  ....*....|...
gi 113197611  745 GTAVDYGYFKFFQ 757
Cdd:pfam12796  66 HYAARSGHLEIVK 78
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 661-688 6.83e-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: 6.83e-03
                          10        20
                  ....*....|....*....|....*...
gi 113197611  661 GHSPLSLAIASGNDLVVKELLSQGADPN 688
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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