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Conserved domains on  [gi|288558803|sp|Q495B1|]
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RecName: Full=Ankyrin repeat and death domain-containing protein 1A

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-381 3.53e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 3.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 106 ILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVALDHVDKLGRTAFHRAAEHGQLDALDFLVGSGCDH 185
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 186 NVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYA 265
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 266 ALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLI 345
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 288558803 346 AGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIKADR 381
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-118 2.94e-13

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   19 LHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHeAAVDEEDavgaltearlcFGMNALLLS 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-----------NGRTALHYA 68

                          90       100
                  ....*....|....*....|
gi 288558803   99 AWFGHLRILQILVNSGAKIH 118
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADIN 88
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 426-494 4.34e-03

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


:

Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 36.11  E-value: 4.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 426 REWKKLAYSWEFTEAHVDAIEQQwtGTRSYQEHGHRMLLIWlhgVATAGENPSK-ALFEGLVAIGRRDLA 494
Cdd:cd01670   11 RDWKKLARKLGLSEGDIDQIEED--NRDDLKEQAYQMLERW---REREGDEATLgRLIQALREIGRRDLA 75
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-381 3.53e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 3.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 106 ILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVALDHVDKLGRTAFHRAAEHGQLDALDFLVGSGCDH 185
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 186 NVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYA 265
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 266 ALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLI 345
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 288558803 346 AGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIKADR 381
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-392 9.80e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 121.67  E-value: 9.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 110 LVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVA-LDHVDKLGRTAFHRAAEHGQ-LDALDFLVGSGCDHNV 187
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGAdVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 188 KDKEGNTALH--LAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHsAAGGSH---PDCVQLLLRAGSTVNALTQKNLSCL 262
Cdd:PHA03095 113 KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRnanVELLRLLIDAGADVYAVDDRFRSLL 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 263 HYAALS--GSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPA--LVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQD 338
Cdd:PHA03095 192 HHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPR 271

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 339 IADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIKA-----------DRFYRWEKDHPSD 392
Cdd:PHA03095 272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKnpsaetvaatlNTASVAGGDIPSD 336
Ank_2 pfam12796
Ankyrin repeats (3 copies);
163-253 1.16e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  163 FHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDiGLDLEEQNaEGLTALHSAAGGSHPDCVQ 242
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 288558803  243 LLLRAGSTVNA 253
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-118 2.94e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   19 LHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHeAAVDEEDavgaltearlcFGMNALLLS 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-----------NGRTALHYA 68

                          90       100
                  ....*....|....*....|
gi 288558803   99 AWFGHLRILQILVNSGAKIH 118
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADIN 88
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 22-184 2.31e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  22 AARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHEAAVDEEDAVG--ALTEArlcfgmnallLSA 99
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGntALWNA----------ISA 601

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 100 wfGHLRILQILVnsgakiHCESKD----GLTLLHCAAQKGHVPVLAFIMEDLEDValDHVDKLGRTAFHRAAEHGQLDAL 175
Cdd:PLN03192 602 --KHHKIFRILY------HFASISdphaAGDLLCTAAKRNDLTAMKELLKQGLNV--DSEDHQGATALQVAMAEDHVDMV 671


                 ....*....
gi 288558803 176 DFLVGSGCD 184
Cdd:PLN03192 672 RLLIMNGAD 680
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 165-332 1.58e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 165 RAAEHGQLDALDFLVGS-GCDHNVKDKEGNTALHLAAGRGHMAVLQRLVD-----IGLDLEEQNAEGLTALHSAAGGSHP 238
Cdd:cd22192   23 LAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 239 DCVQLLLRAGSTVNA---------LTQKNL-----SCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFP 304
Cdd:cd22192  103 NLVRELIARGADVVSpratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNK 182

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 288558803 305 ALV----RLLINSDSDVNAV------DNRQQTPLHLAA 332
Cdd:cd22192  183 TFAcqmyDLILSYDKEDDLQpldlvpNNQGLTPFKLAA 220
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-179 4.24e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  19 LHEAARQNNVGRMQELIG-RRVNTRARNHVGRVALHWAAGAGHEQAVRLLLE---------------------HEAAVDE 76
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelvnepmtsdlyqgetalHIAVVNQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  77 -EDAVGALTE-------ARLC-------------FGMNALLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHC----A 131
Cdd:cd22192  101 nLNLVRELIArgadvvsPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqP 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 288558803 132 AQKGHVPVLAFIM---EDLEDVALDHV-DKLGRTAFHRAAEHGQLDALDFLV 179
Cdd:cd22192  181 NKTFACQMYDLILsydKEDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 16-200 2.15e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   16 ERQLHEAARQNNVgrmQELIGRRVNTRARNHVGRVALHwAAGAGHEQAVRLLLEHEAAVDEEDAVGALTEA----RLCFG 91
Cdd:TIGR00870  53 RSALFVAAIENEN---LELTELLLNLSCRGAVGDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPLELANDqytsEFTPG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   92 MNALLLSAWFGHLRILQILVNSGAKIHCESkdgltllHCAA--QKGHVPVLAFimedledvaldhvdklGRTAFHRAAEH 169
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA-------CGDFfvKSQGVDSFYH----------------GESPLNAAACL 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 288558803  170 GQLDALDFLVGSGCDHNVKDKEGNTALHLAA 200
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 290-319 3.03e-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: 3.03e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 288558803   290 QGASPLHLAVRHNFPALVRLLINSDSDVNA 319
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 426-494 4.34e-03

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 36.11  E-value: 4.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 426 REWKKLAYSWEFTEAHVDAIEQQwtGTRSYQEHGHRMLLIWlhgVATAGENPSK-ALFEGLVAIGRRDLA 494
Cdd:cd01670   11 RDWKKLARKLGLSEGDIDQIEED--NRDDLKEQAYQMLERW---REREGDEATLgRLIQALREIGRRDLA 75
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-381 3.53e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.11  E-value: 3.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 106 ILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVALDHVDKLGRTAFHRAAEHGQLDALDFLVGSGCDH 185
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 186 NVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYA 265
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 266 ALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLI 345
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 288558803 346 AGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIKADR 381
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
86-361 8.47e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 8.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  86 ARLCFGMNALLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVALDhvDKLGRTAFHR 165
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK--DDGGNTLLHA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 166 AAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLL 245
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 246 RAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQ 325
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 288558803 326 TPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTAL 361
Cdd:COG0666  254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-295 1.91e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   3 EELAWETDGLLPLERQLHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHEAAVDEEDAvga 82
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD--- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  83 ltearlcFGMNALLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDValDHVDKLGRTA 162
Cdd:COG0666   86 -------GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDNDGNTP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 163 FHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQ 242
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 288558803 243 LLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPL 295
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-392 9.80e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 121.67  E-value: 9.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 110 LVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVA-LDHVDKLGRTAFHRAAEHGQ-LDALDFLVGSGCDHNV 187
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGAdVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 188 KDKEGNTALH--LAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHsAAGGSH---PDCVQLLLRAGSTVNALTQKNLSCL 262
Cdd:PHA03095 113 KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRnanVELLRLLIDAGADVYAVDDRFRSLL 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 263 HYAALS--GSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPA--LVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQD 338
Cdd:PHA03095 192 HHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPR 271

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 339 IADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIKA-----------DRFYRWEKDHPSD 392
Cdd:PHA03095 272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKnpsaetvaatlNTASVAGGDIPSD 336
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 102-366 6.73e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 95.03  E-value: 6.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 102 GHLRILQILVNSGAKI-HCESKDGLTLLhCAAQKGHVPVLAFIMEDLEDVALDHVDKLGRtafhraaehgqlDALDFLVG 180
Cdd:PHA02874  46 GDAKIVELFIKHGADInHINTKIPHPLL-TAIKIGAHDIIKLLIDNGVDTSILPIPCIEK------------DMIKTILD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 181 SGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLS 260
Cdd:PHA02874 113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 261 CLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPAlVRLLINSDSdVNAVDNRQQTPLHLAAEHAW-QDI 339
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSA-IELLINNAS-INDQDIDGSTPLHHAINPPCdIDI 270

                        250       260
                 ....*....|....*....|....*..
gi 288558803 340 ADMLLIAGVDLNLRDKQGKTALAVAVR 366
Cdd:PHA02874 271 IDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
163-253 1.16e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  163 FHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDiGLDLEEQNaEGLTALHSAAGGSHPDCVQ 242
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 288558803  243 LLLRAGSTVNA 253
Cdd:pfam12796  79 LLLEKGADINV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 17-376 3.52e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 87.81  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  17 RQLHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEH---------------EAAVDEE--DA 79
Cdd:PHA02876 147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgadvniialddlsvlECAVDSKniDT 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  80 VGALTEARLCFGMNAL-LLSAWFGH-LRILQILVNSGAKIHCESKDGLTLLHCAAQkghVPVLAFIMEDLEDVALDHVDK 157
Cdd:PHA02876 227 IKAIIDNRSNINKNDLsLLKAIRNEdLETSLLLYDAGFSVNSIDDCKNTPLHHASQ---APSLSRLVPKLLERGADVNAK 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 158 --LGRTAFHRAAEHG-QLDALDFLVGSGCDHNVKDKEGNTALHLAA--GRGHMAVLQrLVDIGLDLEEQNAEGLTALHSA 232
Cdd:PHA02876 304 niKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStlDRNKDIVIT-LLELGANVNARDYCDKTPIHYA 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 233 AGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYAaLSGSEDVSRV--LIHAGGCANVVDHQGASPLHLAVRHNF-PALVRL 309
Cdd:PHA02876 383 AVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNCkLDVIEM 461

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288558803 310 LINSDSDVNAVDNRQQTPLHLAAEhaWQDIADMLLIAGVDlnLRDKQgktALAVAVRSNHVSLVDMI 376
Cdd:PHA02876 462 LLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHYGAE--LRDSR---VLHKSLNDNMFSFRYII 521
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 181-378 3.63e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 181 SGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSH-----PDCVQLLLRAGSTVNALT 255
Cdd:PHA03100  24 EDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 256 QKNLSCLHYAALSGSEDVSRV--LIHAGGCANVVDHQGASPLHLAVRHNFPAL------------------VRLLINSDS 315
Cdd:PHA03100 104 NNGITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGV 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288558803 316 DVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIK 378
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 148-351 7.56e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.87  E-value: 7.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 148 EDVALDHVDKLGRTAFHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGrgHMAVLQRLVDI-------GLDLEE 220
Cdd:PHA03100  24 EDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSN--IKYNLTDVKEIvkllleyGANVNA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 221 QNAEGLTALHSAAGGS--HPDCVQLLLRAGSTVNALTQKNLSCLHYAALSGSED--VSRVLIHAG--------------- 281
Cdd:PHA03100 102 PDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGvdinaknrvnyllsy 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288558803 282 GC-ANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLN 351
Cdd:PHA03100 182 GVpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-189 1.02e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   95 LLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFImedLEDVALDHVDKlGRTAFHRAAEHGQLDA 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL---LEHADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 288558803  175 LDFLVGSGCDHNVKD 189
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
262-354 1.12e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  262 LHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDsDVNAVDNrQQTPLHLAAEHAWQDIAD 341
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 288558803  342 MLLIAGVDLNLRD 354
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 113-377 1.71e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.34  E-value: 1.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 113 SGAKIHC----ESKDGLTLLHCAAQKGHVPVLAFIMEDLEDValDHVDKLGRTAFHRAAEHGQLDALDFLVGSGCDHNVK 188
Cdd:PHA02876 130 SGNDIHYdkinESIEYMKLIKERIQQDELLIAEMLLEGGADV--NAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 189 DKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSaaggSHPDCVQLLLRAGSTVNALTQKNLSCLHYAALS 268
Cdd:PHA02876 208 ALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRN----EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQA 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 269 GSedVSRV---LIHAGGCANVVDHQGASPLHLAVRHNFPAL-VRLLINSDSDVNAVDNRQQTPLHLAAE-HAWQDIADML 343
Cdd:PHA02876 284 PS--LSRLvpkLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITL 361

                        250       260       270
                 ....*....|....*....|....*....|....
gi 288558803 344 LIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMII 377
Cdd:PHA02876 362 LELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
Ank_2 pfam12796
Ankyrin repeats (3 copies);
295-380 4.00e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 4.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  295 LHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIAdMLLIAGVDLNLRDkQGKTALAVAVRSNHVSLVD 374
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*.
gi 288558803  375 MIIKAD 380
Cdd:pfam12796  79 LLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-321 1.44e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  229 LHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIhAGGCANVVDHqGASPLHLAVRHNFPALVR 308
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 288558803  309 LLINSDSDVNAVD 321
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 241-390 3.83e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.53  E-value: 3.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 241 VQLLLRAGSTVNALTQKNL-SCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNA 319
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288558803 320 VDNRQQTPLHLAAEHAWQ-DIADMLLIAGVDLNLRDK-QGKTALAVAVRSNHVSLVDMIIKAD-RFYRWEKDHP 390
Cdd:PHA02878 230 RDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADiNSLNSYKLTP 303
PHA03095 PHA03095
ankyrin-like protein; Provisional
 8-322 5.35e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 5.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   8 ETDGLLPLerqlHEAARQNNVGRMQE-LIGRRVNTRARNHVGRVALHwaagagheqavrllleheaavdeedavgalteA 86
Cdd:PHA03095  80 ERCGFTPL----HLYLYNATTLDVIKlLIKAGADVNAKDKVGRTPLH--------------------------------V 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  87 RLCfGMNAlllsawfgHLRILQILVNSGAKIHCESKDGLTLLHCaaqkghvpvlaFImedledvaldhvdklgrtAFHRA 166
Cdd:PHA03095 124 YLS-GFNI--------NPKVIRLLLRKGADVNALDLYGMTPLAV-----------LL------------------KSRNA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 167 aehgQLDALDFLVGSGCDHNVKDKEGNTALH--LAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGShpDC---- 240
Cdd:PHA03095 166 ----NVELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS--SCkrsl 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 241 VQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAV 320
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319


                 ..
gi 288558803 321 DN 322
Cdd:PHA03095 320 AA 321
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 104-288 1.44e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 104 LRILQILVNSGAKIHCESKDGLTLLHCAAQK--GHVPvlafIMEDLEDVALD--HVDKLGRTAFHRAAE--HGQLDALDF 177
Cdd:PHA03100  86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYS----IVEYLLDNGANvnIKNSDGENLLHLYLEsnKIDLKILKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 178 LVGSGCDHNVKDKegntalhlaagrghmavLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQK 257
Cdd:PHA03100 162 LIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224

                        170       180       190
                 ....*....|....*....|....*....|.
gi 288558803 258 NLSCLHYAALSGSEDVSRVLIHAGGCANVVD 288
Cdd:PHA03100 225 GDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 141-361 1.66e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 73.36  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 141 AFIMEDLEDVALDHVDKLGRTAFHRAAEHGqLDALDFLVGSGCDHNVKDKEGNtaLHLAAGRGHMAVLQRLVDIGLDLEE 220
Cdd:PLN03192 477 STLIEAMQTRQEDNVVILKNFLQHHKELHD-LNVGDLLGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDI 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 221 QNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHaggCANVVD-HQGASPLHLAV 299
Cdd:PLN03192 554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH---FASISDpHAAGDLLCTAA 630

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 300 RHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDL---NLRDKQGKTAL 361
Cdd:PLN03192 631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 239-377 2.04e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 239 DCVQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVN 318
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 288558803 319 AVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHvSLVDMII 377
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-118 2.94e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   19 LHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHeAAVDEEDavgaltearlcFGMNALLLS 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-----------NGRTALHYA 68

                          90       100
                  ....*....|....*....|
gi 288558803   99 AWFGHLRILQILVNSGAKIH 118
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADIN 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 101-320 8.97e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.02  E-value: 8.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 101 FGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIME--DLEDVALDHVdklgRTAFHRAAEHGQLDALDFL 178
Cdd:PHA02875  12 FGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKhgAIPDVKYPDI----ESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 179 VGSGCDHN-VKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQK 257
Cdd:PHA02875  88 LDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288558803 258 NLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQG-ASPLHLAVRHNFPALVRLLINSDSDVNAV 320
Cdd:PHA02875 168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-222 1.77e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  128 LHCAAQKGHVPVLAFIMEdlEDVALDHVDKLGRTAFHRAAEHGQLDALDFLVgSGCDHNVKDkEGNTALHLAAGRGHMAV 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 288558803  208 LQRLVDIGLDLEEQN 222
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 19-267 2.43e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  19 LHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHEAAVDEEDAVGALTEArlCFGMNA---- 94
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDA--FNNRNVeifk 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  95 LLLSAWFGHLR-------------------ILQILVNSGAKIHCESKDGL-TLLHCAAQKGHVPVLAFIMedLEDVALDH 154
Cdd:PHA02878 119 IILTNRYKNIQtidlvyidkkskddiieaeITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL--SYGANVNI 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 155 VDKLGRTAFHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGR-GHMAVLQRLVDIGLDLEEQNA-EGLTALHSA 232
Cdd:PHA02878 197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSS 276

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 288558803 233 AggSHPDCVQLLLRAGSTVNALTQKNLSCLHYAAL 267
Cdd:PHA02878 277 I--KSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 225-366 3.92e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 225 GLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRH--N 302
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYckD 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 303 FpALVRLLINSDSDVNAVDN-RQQTPLHLAAEHawQDIADMLLIAGVDLNLRDKQGKTALAVAVR 366
Cdd:PHA02878 248 Y-DILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 160-378 4.00e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 160 RTAFHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPD 239
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 240 CVQLLLRAGSTVN-ALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVN 318
Cdd:PHA02875  83 AVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288558803 319 AVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGK-TALAVAVRSNHVSLVDMIIK 378
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
159-212 2.84e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 2.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 288558803  159 GRTAFHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLV 212
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
192-245 4.19e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 4.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 288558803  192 GNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLL 245
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 22-184 2.31e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 2.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  22 AARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHEAAVDEEDAVG--ALTEArlcfgmnallLSA 99
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGntALWNA----------ISA 601

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 100 wfGHLRILQILVnsgakiHCESKD----GLTLLHCAAQKGHVPVLAFIMEDLEDValDHVDKLGRTAFHRAAEHGQLDAL 175
Cdd:PLN03192 602 --KHHKIFRILY------HFASISdphaAGDLLCTAAKRNDLTAMKELLKQGLNV--DSEDHQGATALQVAMAEDHVDMV 671


                 ....*....
gi 288558803 176 DFLVGSGCD 184
Cdd:PLN03192 672 RLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-179 4.70e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 288558803  124 GLTLLHCAAQKGHVPVLAFIMEDLEDValDHVDKLGRTAFHRAAEHGQLDALDFLV 179
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADI--NAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 186-377 5.20e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 186 NVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTqknLSCLHya 265
Cdd:PHA02874  29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP---IPCIE-- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 266 alsgsEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLI 345
Cdd:PHA02874 104 -----KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178

                        170       180       190
                 ....*....|....*....|....*....|..
gi 288558803 346 AGVDLNLRDKQGKTALAVAVRSNHVSLVDMII 377
Cdd:PHA02874 179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-138 6.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 6.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  10 DGLLPLerqlHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHEAAVDEEDavgaltearlC 89
Cdd:PHA02875 101 DGMTPL----HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED----------C 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 288558803  90 FGMNALLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHVP 138
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI 215
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 165-332 1.58e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 165 RAAEHGQLDALDFLVGS-GCDHNVKDKEGNTALHLAAGRGHMAVLQRLVD-----IGLDLEEQNAEGLTALHSAAGGSHP 238
Cdd:cd22192   23 LAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 239 DCVQLLLRAGSTVNA---------LTQKNL-----SCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFP 304
Cdd:cd22192  103 NLVRELIARGADVVSpratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNK 182

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 288558803 305 ALV----RLLINSDSDVNAV------DNRQQTPLHLAA 332
Cdd:cd22192  183 TFAcqmyDLILSYDKEDDLQpldlvpNNQGLTPFKLAA 220
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 271-378 2.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 271 EDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVD- 349
Cdd:PHA02874  15 EAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDt 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 288558803 350 ----------------------LNLRDKQGKTALAVAVRSNHVSLVDMIIK 378
Cdd:PHA02874  95 silpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFE 145
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 307-378 2.40e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 288558803 307 VRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIK 378
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 266-344 3.39e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 3.39e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288558803 266 ALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLL 344
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 95-253 3.59e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.95  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  95 LLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHvpvlafimEDLEDVALDHV------DKLGRTAFHRA-- 166
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGY--------EDCVLVLLKHAcnvhirDANGNTALWNAis 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 167 AEHGQLdaldFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLR 246
Cdd:PLN03192 601 AKHHKI----FRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676


                 ....*..
gi 288558803 247 AGSTVNA 253
Cdd:PLN03192 677 NGADVDK 683
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 91-287 3.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  91 GMNALLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMeDLEDVALDHVDKLGRTAFHRAAEHG 170
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL-DLGKFADDVFYKDGMTPLHLATILK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 171 QLDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGST 250
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 288558803 251 VNALTQK-NLSCLHYAALSGSEDVSRVLIHAGGCANVV 287
Cdd:PHA02875 194 IDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-179 4.24e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  19 LHEAARQNNVGRMQELIG-RRVNTRARNHVGRVALHWAAGAGHEQAVRLLLE---------------------HEAAVDE 76
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelvnepmtsdlyqgetalHIAVVNQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  77 -EDAVGALTE-------ARLC-------------FGMNALLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHC----A 131
Cdd:cd22192  101 nLNLVRELIArgadvvsPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqP 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 288558803 132 AQKGHVPVLAFIM---EDLEDVALDHV-DKLGRTAFHRAAEHGQLDALDFLV 179
Cdd:cd22192  181 NKTFACQMYDLILsydKEDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_5 pfam13857
Ankyrin repeats (many copies);
309-364 5.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 5.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 288558803  309 LLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVA 364
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
258-311 1.50e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 288558803  258 NLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLI 311
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
326-377 1.99e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 288558803  326 TPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMII 377
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
146-199 2.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 288558803  146 DLEDVALDHVDKLGRTAFHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLA 199
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
183-232 3.31e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 3.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 288558803  183 CDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSA 232
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 108-186 6.18e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 108 QILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVALdhVDKLGRTAFHRAAEHGQLDALDFLVG-SGCDHN 186
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL--LDKDGKTPLELAEENGFREVVQLLSRhSQCHFE 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
 307-379 8.62e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 8.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288558803 307 VRLLINSDSDVNAVDNRQQTPLHL---AAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHV-SLVDMIIKA 379
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 224-378 9.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 9.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 224 EGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGgcanvVDhqgASPLHLAVRHNf 303
Cdd:PHA02874  34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-----VD---TSILPIPCIEK- 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 304 pALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIK 378
Cdd:PHA02874 105 -DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 104-227 1.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 104 LRILQILVNSGAKIHCESKD-GLTLLH--CAAQKGHVPVLAFIMEDlEDVALDHVDKLGRTAFHRAAEHG--QLDALDFL 178
Cdd:PHA02859  66 VEILKFLIENGADVNFKTRDnNLSALHhyLSFNKNVEPEILKILID-SGSSITEEDEDGKNLLHMYMCNFnvRINVIKLL 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 288558803 179 VGSGCDHNVKDKEGNTALH-LAAGRGHMAVLQRLVDIGLDLEEQNAEGLT 227
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYN 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-78 1.00e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   19 LHEAARQNNVGRMQELIgRRVNTRARNHvGRVALHWAAGAGHEQAVRLLLEHEAAVDEED 78
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 122-255 1.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 122 KDGLTLLHCAAQKGHVPVLAFIMEDLEDVALDHVDKLgrTAFHRAAEHGQLDALDFLVGSGCDHNVKDKEGNTALHLAAG 201
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 202 RGHMAVLQRLVDIGLDLEEQNAEG-LTALHSAAGGSHPDCVQLLLRAGSTVNALT 255
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-111 1.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288558803   51 ALHWAAGAGHEQAVRLLLEHEAAVDEEDAvgaltearlcFGMNALLLSAWFGHLRILQILV 111
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDG----------NGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 241-359 1.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 241 VQLLLRAGSTVNALTQ-KNLSCLHYAaLSGSEDVS----RVLIHAGGCANVVDHQGASPLHL-----AVRHNfpaLVRLL 310
Cdd:PHA02859  69 LKFLIENGADVNFKTRdNNLSALHHY-LSFNKNVEpeilKILIDSGSSITEEDEDGKNLLHMymcnfNVRIN---VIKLL 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 288558803 311 INSDSDVNAVDNRQQTPLH-LAAEHAWQDIADMLLIAGVDLNLRDKQGKT 359
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYN 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 178-246 1.64e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 1.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288558803 178 LVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLR 246
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02917 PHA02917
ankyrin-like protein; Provisional
 316-377 1.69e-05

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 47.69  E-value: 1.69e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288558803 316 DVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAV-RSNHVSLVDMII 377
Cdd:PHA02917 444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLL 506
PHA02798 PHA02798
ankyrin-like protein; Provisional
 104-322 2.47e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 104 LRILQILVNSGAKIHCESKDGLTLLHCAAQKGHV---PVLAFIMEDLEDVALdhVDKLGRTAFH---RAAEHGQLDALDF 177
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTL--LDKDGFTMLQvylQSNHHIDIEIIKL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 178 LVGSGCDHNV-KDKEGNTALHL----AAGRGHMAVLQRLVDIGLDLEEQNA-------EGLTALHSAAGGSHPDCVQLLL 245
Cdd:PHA02798 167 LLEKGVDINThNNKEKYDTLHCyfkyNIDRIDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIF 246

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288558803 246 rAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDN 322
Cdd:PHA02798 247 -SYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISY 322
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 305-369 2.75e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.78  E-value: 2.75e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 305 ALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNH 369
Cdd:PLN03192 539 ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 36-199 3.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  36 GRRVNTRARNhvGRVALHWAAGAGHEQAVRLLLEHEAAVDEEDAVGaltearlCFGMNALLLSAWFghlRILQILVNSGA 115
Cdd:PHA02874 114 GIDVNIKDAE--LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG-------CYPIHIAIKHNFF---DIIKLLLEKGA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 116 KIHCESKDGLTLLHCAAQKGHVPVLAFIMEDLEDVALDHvdKLGRTAFHRAAEHGQlDALDFLVGSGcDHNVKDKEGNTA 195
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC--KNGFTPLHNAIIHNR-SAIELLINNA-SINDQDIDGSTP 257


                 ....
gi 288558803 196 LHLA 199
Cdd:PHA02874 258 LHHA 261
PHA02791 PHA02791
ankyrin-like protein; Provisional
 288-380 5.08e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 45.03  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 288 DHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNrqQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRS 367
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                         90
                 ....*....|...
gi 288558803 368 NHVSLVDMIIKAD 380
Cdd:PHA02791 105 GNMQTVKLFVKKN 117
PHA02946 PHA02946
ankyin-like protein; Provisional
 178-367 6.98e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 178 LVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRLVDIGLDLEEQNAEGLTALHSAAGGSHP--DCVQLLLRAGSTVNALT 255
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKINNSV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 256 QKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFP--ALVRLLINSDSDVNAVDNRQQTPLHLAAE 333
Cdd:PHA02946 138 DEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPkaSTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 288558803 334 HAWQ--DIADMLLiAGVDLNLRDKQGKTALAVAVRS 367
Cdd:PHA02946 218 KTVKnvDIINLLL-PSTDVNKQNKFGDSPLTLLIKT 252
PHA02798 PHA02798
ankyrin-like protein; Provisional
 172-388 8.32e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 8.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 172 LDALDFLVGSGCDHNVKDKEGNTALHLAAGRGHMAVLQRL---VDIGLDLEEQNAEGLTALHSAAGGSHP---DCVQLLL 245
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 246 RAGSTVNALT------------QKNLSCLhyaalsgSEDVSRVLIHAGGCANVVDHQGASPLH------LAVRHNFPALV 307
Cdd:PHA02798 169 EKGVDINTHNnkekydtlhcyfKYNIDRI-------DADILKLFVDNGFIINKENKSHKKKFMeylnslLYDNKRFKKNI 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 308 RLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLVDMIIKAD------- 380
Cdd:PHA02798 242 LDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKpnkntis 321


                 ....*....
gi 288558803 381 -RFYRWEKD 388
Cdd:PHA02798 322 yTYYKLRKH 330
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-142 8.99e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 8.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 288558803   91 GMNALLLSAWFGHLRILQILVNSGAKIHCESKDGLTLLHCAAQKGHVPVLAF 142
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 19-75 9.49e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 9.49e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 288558803  19 LHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHEAAVD 75
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682
PHA02741 PHA02741
hypothetical protein; Provisional
 124-258 1.05e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.11  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 124 GLTLLHCAAQKGHVPVLA----FIMEDLEDVALDHVDKLGRTAFHRAAEHGQ----LDALDFLVGSGCDHNVKDK-EGNT 194
Cdd:PHA02741  21 GENFFHEAARCGCFDIIArftpFIRGDCHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMlEGDT 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 195 ALHLAAGRGHMAVLQRLV-DIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKN 258
Cdd:PHA02741 101 ALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSRGFSNEN 165
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 241-320 1.23e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 241 VQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLI-----NSDS 315
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177


                 ....*
gi 288558803 316 DVNAV 320
Cdd:PTZ00322 178 GANAK 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
277-331 1.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 288558803  277 LIHAGGCA-NVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLA 331
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
225-278 1.62e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 288558803  225 GLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYAALSGSEDVSRVLI 278
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
19-68 3.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 3.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 288558803   19 LHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLL 68
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 258-329 4.61e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 4.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288558803 258 NLSCLH-YAALSG-SEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLH 329
Cdd:PHA02946  37 NYHILHaYCGIKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 260-381 5.00e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 260 SCLHYAALSGSEDVSRVLIHAG-GCANVVD----HQGASPLHLAVRHNFPALVRLLINSDSDVNA--------VDNRQ-- 324
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMEAApELVNEPMtsdlYQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffRPGPKnl 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288558803 325 ----QTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTALAVAVRSNHVSLV----DMIIKADR 381
Cdd:cd22192  133 iyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDK 197
Ank_4 pfam13637
Ankyrin repeats (many copies);
293-344 8.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 8.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 288558803  293 SPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQDIADMLL 344
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 19-199 1.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  19 LHEAARQNNVGRMQELIGRRVNTRARNHVGRVALHWAAGAGHEQAVRLLLEHeaavdeedavGALTEARLCFGMNALLLS 98
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK----------GAYANVKDNNGESPLHNA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803  99 AWFGHLRILQILVNSGAKIHCESKDGLTLLHCAA--QKGHVPVLafimedLEDVALDHVDKLGRTAFHRAAEHG-QLDAL 175
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIihNRSAIELL------INNASINDQDIDGSTPLHHAINPPcDIDII 271

                        170       180
                 ....*....|....*....|....
gi 288558803 176 DFLVGSGCDHNVKDKEGNTALHLA 199
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPIDTA 295
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 16-200 2.15e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   16 ERQLHEAARQNNVgrmQELIGRRVNTRARNHVGRVALHwAAGAGHEQAVRLLLEHEAAVDEEDAVGALTEA----RLCFG 91
Cdd:TIGR00870  53 RSALFVAAIENEN---LELTELLLNLSCRGAVGDTLLH-AISLEYVDAVEAILLHLLAAFRKSGPLELANDqytsEFTPG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803   92 MNALLLSAWFGHLRILQILVNSGAKIHCESkdgltllHCAA--QKGHVPVLAFimedledvaldhvdklGRTAFHRAAEH 169
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA-------CGDFfvKSQGVDSFYH----------------GESPLNAAACL 185

                         170       180       190
                  ....*....|....*....|....*....|.
gi 288558803  170 GQLDALDFLVGSGCDHNVKDKEGNTALHLAA 200
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLV 216
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 291-319 2.62e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 2.62e-03
                          10        20
                  ....*....|....*....|....*....
gi 288558803  291 GASPLHLAVRHNFPALVRLLINSDSDVNA 319
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02917 PHA02917
ankyrin-like protein; Provisional
 285-344 2.96e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 40.37  E-value: 2.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288558803 285 NVVDHQGASPLHLAVRHNFPALVRLLINSDSDVNAVDNRQQTPLHLAAEHAWQ-DIADMLL 344
Cdd:PHA02917 446 NMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNiELLKMLL 506
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 290-319 3.03e-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: 3.03e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 288558803   290 QGASPLHLAVRHNFPALVRLLINSDSDVNA 319
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 426-494 4.34e-03

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 36.11  E-value: 4.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 426 REWKKLAYSWEFTEAHVDAIEQQwtGTRSYQEHGHRMLLIWlhgVATAGENPSK-ALFEGLVAIGRRDLA 494
Cdd:cd01670   11 RDWKKLARKLGLSEGDIDQIEED--NRDDLKEQAYQMLERW---REREGDEATLgRLIQALREIGRRDLA 75
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 325-355 4.65e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 4.65e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 288558803  325 QTPLHLAAEHA-WQDIADMLLIAGVDLNLRDK 355
Cdd:pfam00023   3 NTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 264-361 4.86e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 4.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 264 YAALSGSEDVSRVLIHAGGCANVVDHQGASPLHLAVRHNFPAL--VRLLINSDSDVNAVDNRQQTPL-----HLAAEHAW 336
Cdd:PHA02798   9 YITFSDNVKLSTVKLLIKSCNPNEIVNEYSIFQKYLQRDSPSTdiVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHM 88

                         90       100
                 ....*....|....*....|....*
gi 288558803 337 QDIADMLLIAGVDLNLRDKQGKTAL 361
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPL 113
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 290-322 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: 34.57  E-value: 5.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 288558803  290 QGASPLHLAV-RHNFPALVRLLINSDSDVNAVDN 322
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 156-232 5.35e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 37.87  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 156 DKLGRTAFHRAAEHGQLDA---LDFLVGSGCDHNVKD-KEGNTALHLAAGRGHMAVLQRLV-DIGLDLEEQNAEGLTALH 230
Cdd:PHA02743  54 DHHGRQCTHMVAWYDRANAvmkIELLVNMGADINARElGTGNTLLHIAASTKNYELAEWLCrQLGVNLGAINYQHETAYH 133


                 ..
gi 288558803 231 SA 232
Cdd:PHA02743 134 IA 135
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 224-255 6.43e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 6.43e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 288558803  224 EGLTALHSAAG-GSHPDCVQLLLRAGSTVNALT 255
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-222 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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 6.83e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 288558803  191 EGNTALHLAAGR-GHMAVLQRLVDIGLDLEEQN 222
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 208-376 7.30e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 7.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 208 LQRLVDIGLDLEEQNAEGLTALHSAAGGSHPDCVQLLLRAGSTVNALTQKNLSCLHYaaLSGSED--VSRV--LIHAGG- 282
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDevIERInlLVQYGAk 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288558803 283 CANVVDHQGASPLhLAVRHNFPALVRLLINSDSDVNAVDN--RQQTPLHLAAEHAWQDIADMLLIAGVDLNLRDKQGKTA 360
Cdd:PHA02946 133 INNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211

                        170
                 ....*....|....*.
gi 288558803 361 LAVaVRSNHVSLVDMI 376
Cdd:PHA02946 212 LHI-VCSKTVKNVDII 226
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-78 8.91e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 8.91e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 288558803   48 GRVALHWAAG-AGHEQAVRLLLEHEAAVDEED 78
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
 
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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