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Conserved domains on  [gi|2462572959|ref|XP_054197879|]
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ankyrin repeat domain-containing protein 36A isoform X60 [Homo sapiens]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-260 8.81e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 8.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462572959 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDL 260
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PTZ00108 super family cl36510
DNA topoisomerase 2-like protein; Provisional
 728-946 4.43e-05

DNA topoisomerase 2-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00108:

Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 47.73  E-value: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  728 DEEDSVSNIATEIKDGEKSGTVSS---QKQPALKATTDEKDSV-----SNIATEIKDGEKSGTVSSQKPPALTATSDEEG 799
Cdd:PTZ00108  1144 QEEVEEKEIAKEQRLKSKTKGKASklrKPKLKKKEKKKKKSSAdkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS 1223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  800 SVLSIARENKDGEKS------RTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIA 873
Cdd:PTZ00108  1224 DQEDDEEQKTKPKKSsvkrlkSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  874 RENKDGEKSRTVSSEKppGLKASSAEKDSVLNIARGKKD-----GEKTKRVSSRKKPSLEATS--DEKDSFSNITREKKD 946
Cdd:PTZ00108  1304 SPTKKKVKKRLEGSLA--ALKKKKKSEKKTARKKKSKTRvkqasASQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-260 8.81e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 8.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462572959 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDL 260
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-128 2.80e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462572959 116 LLLQNGANPNITD 128
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-223 1.22e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.81  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462572959 171 AVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 92-229 6.01e-06

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: 50.08  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  92 NLCDREDRTPLIK-AVQLRQEACATLLLQNGANPNItdffGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 160
Cdd:TIGR00870  46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 161 SKCEYQ----PLLFAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALIHAVTLGEKDIVILLLQHNID 222
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200


                  ....*..
gi 2462572959 223 VLSRDAF 229
Cdd:TIGR00870 201 ILTADSL 207
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 728-946 4.43e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 47.73  E-value: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  728 DEEDSVSNIATEIKDGEKSGTVSS---QKQPALKATTDEKDSV-----SNIATEIKDGEKSGTVSSQKPPALTATSDEEG 799
Cdd:PTZ00108  1144 QEEVEEKEIAKEQRLKSKTKGKASklrKPKLKKKEKKKKKSSAdkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS 1223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  800 SVLSIARENKDGEKS------RTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIA 873
Cdd:PTZ00108  1224 DQEDDEEQKTKPKKSsvkrlkSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  874 RENKDGEKSRTVSSEKppGLKASSAEKDSVLNIARGKKD-----GEKTKRVSSRKKPSLEATS--DEKDSFSNITREKKD 946
Cdd:PTZ00108  1304 SPTKKKVKKRLEGSLA--ALKKKKKSEKKTARKKKSKTRvkqasASQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 114-220 7.68e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.54  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 114 ATLLLQNGA-----NPNITDFF-GRTALHYAVYNEDTSMIEKLLSHGTNI------------EECSKCEY--QPLLFAVS 173
Cdd:cd22192    66 AAVVLMEAApelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYgeHPLSFAAC 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462572959 174 RRKVKMVEFLLKKKANVNAIDYLGRSALiHavtlgekdivILLLQHN 220
Cdd:cd22192   146 VGNEEIVRLLIEHGADIRAQDSLGNTVL-H----------ILVLQPN 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 131-159 1.01e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 1.01e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462572959  131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-260 8.81e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 8.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462572959 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDL 260
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
28-266 2.41e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 2.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  28 IKPYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:COG0666    17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 108 LRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:COG0666    97 NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462572959 188 ANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDLPINSNP 266
Cdd:COG0666   177 ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-233 7.87e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 7.87e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462572959 196 LGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIA 233
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-201 4.93e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 4.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 116 LLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDY 195
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                  ....*.
gi 2462572959 196 LGRSAL 201
Cdd:COG0666   284 DLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-252 3.48e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 3.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  45 LEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP 124
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 125 NITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHA 204
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2462572959 205 VTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEY 252
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
36-128 2.80e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrRCELNLCDrEDRTPLIKAVQLRQEACAT 115
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462572959 116 LLLQNGANPNITD 128
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-223 1.22e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.81  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLAC-----ATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ--L 108
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 109 RQEACATLLLQNGANPNITDFFGRTALHYAV-YNE-DTSMIEKLLSHGTNIEECSKCEY----------------QPLLF 170
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLeSNKiDLKILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHY 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462572959 171 AVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
135-227 1.62e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 135 LHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKkANVNAIDYlGRSALIHAVTLGEKDIVI 214
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462572959 215 LLLQHNIDVLSRD 227
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 44-249 4.42e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.02  E-value: 4.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGAN 123
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 124 PNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKvKMVEFLLkKKANVNAIDYLGRSALIH 203
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHH 260

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2462572959 204 AVTLG-EKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNR--VIFDLI 249
Cdd:PHA02874  261 AINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdpVIKDII 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
102-194 3.89e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 102 LIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGtNIEECSKcEYQPLLFAVSRRKVKMVE 181
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462572959 182 FLLKKKANVNAID 194
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 51-205 2.94e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.54  E-value: 2.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  51 LLLTY-YDANKRDR-KERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITD 128
Cdd:PHA02878  152 LLLSYgADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 129 FFGRTALHYAV-YNEDTSMIEKLLSHGTNIEECSKC-EYQPLLFAV-SRRKVKMvefLLKKKANVNAIDYLGRSALIHAV 205
Cdd:PHA02878  232 KCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIkSERKLKL---LLEYGADINSLNSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 100-264 5.55e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 5.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 100 TPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHY-----AVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSR 174
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 175 RK--VKMVEFLLKKKANVNAIDYLGRSaLIHAVTLG---EKDIVILLLQHNIDvlsrdafrkiagdyaIEAKNRVifDLI 249
Cdd:PHA03100  117 KSnsYSIVEYLLDNGANVNIKNSDGEN-LLHLYLESnkiDLKILKLLIDKGVD---------------INAKNRV--NYL 178

                         170
                  ....*....|....*
gi 2462572959 250 YEYerkryeDLPINS 264
Cdd:PHA03100  179 LSY------GVPINI 187
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 39-222 9.60e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 9.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  39 AVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSR-----------RCELN-------------LC 94
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHgaipdvkypdiESELHdaveegdvkaveeLL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  95 D----------REDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECsk 162
Cdd:PHA02875   89 DlgkfaddvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKacLDIEDC-- 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462572959 163 CEYQPLLFAVSRRKVKMVEFLLKKKANvnaIDYLGR----SALIHAVTLGEKDIVILLLQHNID 222
Cdd:PHA02875  167 CGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKngcvAALCYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-280 9.99e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 9.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  32 HLKRIHRAVLHGNL--------EKLKYLLLTYYDANKRDRKERTALHLacatgqpemvhlLVSRRCElnlcdredrtPLI 103
Cdd:PHA03095    6 SVDIIMEAALYDYLlnasnvtvEEVRRLLAAGADVNFRGEYGKTPLHL------------YLHYSSE----------KVK 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 104 KAVQLrqeacatlLLQNGANPNITDFFGRTALHYAVYNEDT-SMIEKLLSHGTNIEECSKCEYQPL--LFAVSRRKVKMV 180
Cdd:PHA03095   64 DIVRL--------LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVI 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 181 EFLLKKKANVNAIDYLGRSALihAVTLGEKDIvilllqhNIDVLsRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEdl 260
Cdd:PHA03095  136 RLLLRKGADVNALDLYGMTPL--AVLLKSRNA-------NVELL-RLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAR-- 203

                         250       260
                  ....*....|....*....|
gi 2462572959 261 pINSNPVSSQKQPALKATSG 280
Cdd:PHA03095  204 -IVRELIRAGCDPAATDMLG 222
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 32-252 5.96e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 5.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPL--------- 102
Cdd:PHA02876  145 YMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLecavdskni 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 103 --IKAV----------------QLRQEACAT--LLLQNGANPNITDFFGRTALHYAVYNEDTS-MIEKLLSHGTNIEECS 161
Cdd:PHA02876  225 dtIKAIidnrsninkndlsllkAIRNEDLETslLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKN 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 162 KCEYQPL-LFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGE-KDIVILLLQHNIDVLSRDAFRKIAGDYAIE 239
Cdd:PHA02876  305 IKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAV 384

                         250
                  ....*....|...
gi 2462572959 240 AKNRVIFDLIYEY 252
Cdd:PHA02876  385 RNNVVIINTLLDY 397
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-223 1.93e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.17  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKL-KYLLLTYYDANKRDRKERTALHLACATG-QPEMVHLLVSRRCELNLCDREDRTPLIKAVQL-RQEA 112
Cdd:PHA02876  277 LHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKD 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 113 CATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKM-VEFLLKKKANVN 191
Cdd:PHA02876  357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462572959 192 AIDYLGRSALIHAVTLGEK-DIVILLLQHNIDV 223
Cdd:PHA02876  437 SKNKDLSTPLHYACKKNCKlDVIEMLLDNGADV 469
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-193 2.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKE-RTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACA 114
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 115 TLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLL-FAVSRRKVKMVEFLLKKKANVNAI 193
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNIM 231
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-194 2.70e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 2.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  30 PYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACAT--GQPEMVHLLVSRRCELNLCDREDRTPLIKAVq 107
Cdd:PHA03100   71 PLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL- 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 108 lrqEACAT------LLLQNGANPN----------------ITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEY 165
Cdd:PHA03100  150 ---ESNKIdlkilkLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226

                         170       180
                  ....*....|....*....|....*....
gi 2462572959 166 QPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03100  227 TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
99-151 6.71e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 6.71e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462572959  99 RTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLL 151
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
32-85 1.63e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462572959  32 HLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLV 85
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 36-255 1.80e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACAT 115
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 116 LLLQNGANPNITDFFGRTALHYAV-YNEdtSMIEKLLSHGT-NIEECSKceYQPLLFAVSRR-KVKMVEFLLKKKANVNA 192
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIiHNR--SAIELLINNASiNDQDIDG--STPLHHAINPPcDIDIIDILLYHKADISI 283

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572959 193 IDYLGRSALIHAVTLGEKDIVILLLQHNIdVLSRDAFRKIAGDY--AIEAK-NRVIFDLIYEYERK 255
Cdd:PHA02874  284 KDNKGENPIDTAFKYINKDPVIKDIIANA-VLIKEADKLKDSDFleHIEIKdNKEFSDFIKECNEE 348
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-194 3.80e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  44 NLEKLKYLLLTYYDANKRDRKERTALHLACATGQP--EMVHLLVSRRCELNLCDREDRTPLIKAVQlrQEACATLLLQN- 120
Cdd:PHA03095  166 NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRSLVLPl 243

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462572959 121 ---GANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAID 194
Cdd:PHA03095  244 liaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 67-226 7.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 7.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  67 TALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANP---------------------- 124
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 125 -NITDFFGRTALHYAVYNEDTSMIEKLLSHG--TNIEECSKCeyQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSAL 201
Cdd:PHA02874  117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGadVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                         170       180
                  ....*....|....*....|....*
gi 2462572959 202 IHAVTLGEKDIVILLLQHNIDVLSR 226
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNK 219
Ank_4 pfam13637
Ankyrin repeats (many copies);
131-184 2.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.51e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462572959 131 GRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLL 184
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-259 8.30e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 8.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTY-YDANKRDRKERTALHlACATGQ---PEMVHLLVSRRCELNLCDREDRTPLikAVQLRQE 111
Cdd:PHA03095   87 LHLYLYNATTLDVIKLLIKAgADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 112 ACAT----LLLQNGANPNITDFFGRTALHY---------AVYNEDT----------------------------SMIEKL 150
Cdd:PHA03095  164 NANVellrLLIDAGADVYAVDDRFRSLLHHhlqsfkpraRIVRELIragcdpaatdmlgntplhsmatgssckrSLVLPL 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 151 LSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL--QHNIDVLSR-- 226
Cdd:PHA03095  244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALakNPSAETVAAtl 323

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2462572959 227 DAFRKIAGDYAIEAKNRVI--------FDLIYEYERKRYED 259
Cdd:PHA03095  324 NTASVAGGDIPSDATRLCVakvvlrgaFSLLPEPIRAYHAD 364
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-226 4.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 4.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 100 TPLIKAVQLRQEACATLLLQNGANPN-------------------------------ITDFF---GRTALHYAVYNEDTS 145
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDvkypdieselhdaveegdvkaveelldlgkfADDVFykdGMTPLHLATILKKLD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 146 MIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQH--NIDV 223
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDY 196


                  ...
gi 2462572959 224 LSR 226
Cdd:PHA02875  197 FGK 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
164-217 7.60e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 7.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462572959 164 EYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-192 1.20e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  43 GNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQ--N 120
Cdd:PLN03192  536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaS 615

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462572959 121 GANPNItdffGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNA 192
Cdd:PLN03192  616 ISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-105 1.95e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462572959  57 DANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKA 105
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 36-225 2.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 2.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSrrcELNLCDREDRTPLIK-AVQLRQEACA 114
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSVFYTLVAIKdAFNNRNVEIF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 115 TLLLQNG--ANPNITDFFGRTALHYAVYneDTSMIEKLLSHGTNIEECSK-CEYQPLLFAVSRRKVKMVEFLLKKKANVN 191
Cdd:PHA02878  118 KIILTNRykNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2462572959 192 AIDYLGRSALIHAVTLGEKDIVILLLQH--NIDVLS 225
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENgaSTDARD 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-118 2.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462572959  65 ERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLL 118
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 72-223 2.89e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  72 ACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSmIEKLL 151
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRIL 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462572959 152 SHGTNIEEcSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDV 223
Cdd:PLN03192  611 YHFASISD-PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 92-229 6.01e-06

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: 50.08  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  92 NLCDREDRTPLIK-AVQLRQEACATLLLQNGANPNItdffGRTALHYAVyNEDTSMIEKLLSH-------GTNIE---EC 160
Cdd:TIGR00870  46 NCPDRLGRSALFVaAIENENLELTELLLNLSCRGAV----GDTLLHAIS-LEYVDAVEAILLHllaafrkSGPLElanDQ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 161 SKCEYQ----PLLFAVSRRKVKMVEFLLKKKANVNA------------IDYL--GRSALIHAVTLGEKDIVILLLQHNID 222
Cdd:TIGR00870 121 YTSEFTpgitALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALLSEDPAD 200


                  ....*..
gi 2462572959 223 VLSRDAF 229
Cdd:TIGR00870 201 ILTADSL 207
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 98-229 2.07e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  98 DRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKV 177
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462572959 178 KMVEFLLKKKANVNAIDYLGRSALIHAVTLGEK-DIVILLLQH--NIDVLSRDAF 229
Cdd:PHA02875   82 KAVEELLDLGKFADDVFYKDGMTPLHLATILKKlDIMKLLIARgaDPDIPNTDKF 136
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-154 3.36e-05

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: 47.77  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  67 TALHLACATGQPEMVHLLVSR------RCELNLCDREDRTPLIKAVQLR--------QEACATLLLQNGANPNITDFFGR 132
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERgasvpaRACGDFFVKSQGVDSFYHGESPlnaaaclgSPSIVALLSEDPADILTADSLGN 209

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462572959 133 TALHYAVYNED---------TSMIEKLLSHG 154
Cdd:TIGR00870 210 TLLHLLVMENEfkaeyeelsCQMYNFALSLL 240
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 728-946 4.43e-05

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 47.73  E-value: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  728 DEEDSVSNIATEIKDGEKSGTVSS---QKQPALKATTDEKDSV-----SNIATEIKDGEKSGTVSSQKPPALTATSDEEG 799
Cdd:PTZ00108  1144 QEEVEEKEIAKEQRLKSKTKGKASklrKPKLKKKEKKKKKSSAdkskkASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGS 1223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  800 SVLSIARENKDGEKS------RTVSSRKKPALKATSDEKDSFSNITRGKKDGEISRKVSSQKPPTLKGTSDEEDSVLGIA 873
Cdd:PTZ00108  1224 DQEDDEEQKTKPKKSsvkrlkSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPS 1303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  874 RENKDGEKSRTVSSEKppGLKASSAEKDSVLNIARGKKD-----GEKTKRVSSRKKPSLEATS--DEKDSFSNITREKKD 946
Cdd:PTZ00108  1304 SPTKKKVKKRLEGSLA--ALKKKKKSEKKTARKKKSKTRvkqasASQSSRLLRRPRKKKSDSSseDDDDSEVDDSEDEDD 1381
Ank_5 pfam13857
Ankyrin repeats (many copies);
83-138 7.54e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 7.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572959  83 LLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYA 138
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 114-220 7.68e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.54  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 114 ATLLLQNGA-----NPNITDFF-GRTALHYAVYNEDTSMIEKLLSHGTNI------------EECSKCEY--QPLLFAVS 173
Cdd:cd22192    66 AAVVLMEAApelvnEPMTSDLYqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYgeHPLSFAAC 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462572959 174 RRKVKMVEFLLKKKANVNAIDYLGRSALiHavtlgekdivILLLQHN 220
Cdd:cd22192   146 VGNEEIVRLLIEHGADIRAQDSLGNTVL-H----------ILVLQPN 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 139-222 9.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 9.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 139 VYNEDTSMIEKLLSHGTNIEECSKCE-YQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLL 217
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNCINISVDEtTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88


                  ....*
gi 2462572959 218 QHNID 222
Cdd:PHA02874   89 DNGVD 93
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 51-107 1.00e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462572959  51 LLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQ 107
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 131-159 1.01e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 1.01e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462572959  131 GRTALHYAVYNEDTSMIEKLLSHGTNIEE 159
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-171 1.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572959 117 LLQNG-ANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFA 171
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 36-187 2.56e-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: 45.00  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  36 IHRAVLHGNLEKLKYLLltyyDANKRDRKE---------RTALHLACATGQPEMVHLLVSRRCELN------LCDREDRT 100
Cdd:cd22192    55 LHVAALYDNLEAAVVLM----EAAPELVNEpmtsdlyqgETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPK 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 101 --------PLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTS----MIEKLLSHGTNIEECS------K 162
Cdd:cd22192   131 nliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDLQPldlvpnN 210

                         170       180
                  ....*....|....*....|....*
gi 2462572959 163 CEYQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd22192   211 QGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 90-229 2.89e-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: 44.62  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  90 ELNLCD--REDRTPLIKAVQLRQ-EACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNI--EECSKCE 164
Cdd:cd22192     7 ELHLLQqkRISESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 165 YQ---PLLFAVSRRKVKMVEFLLKKKANVN--------------AIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRD 227
Cdd:cd22192    87 YQgetALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166


                  ..
gi 2462572959 228 AF 229
Cdd:cd22192   167 SL 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 168-254 4.19e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 4.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959 168 LLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFD 247
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608


                  ....*..
gi 2462572959 248 LIYEYER 254
Cdd:PLN03192  609 ILYHFAS 615
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 64-187 7.72e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572959  64 KERTALHLACATGQPEMVHLLVSRRCELNL--CDREDRT-----------PLIKAVQLRQEACATLLLQNGANP---NIT 127
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSAraTGRFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQ 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572959 128 DFFGRTALHYAVYNED---------TSMIEKLLSHGTNIEECSKCE-------YQPLLFAVSRRKVKMVEFLLKKK 187
Cdd:cd21882   152 DSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDPTQQLEeipnhqgLTPLKLAAVEGKIVMFQHILQRE 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 66-96 8.86e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 8.86e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462572959  66 RTALHLACA-TGQPEMVHLLVSRRCELNLCDR 96
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 66-93 1.16e-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: 37.18  E-value: 1.16e-03
                           10        20
                   ....*....|....*....|....*...
gi 2462572959   66 RTALHLACATGQPEMVHLLVSRRCELNL 93
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 131-162 1.91e-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: 36.50  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462572959 131 GRTALHYAVYNE-DTSMIEKLLSHGTNIEECSK 162
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 66-92 5.23e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 5.23e-03
                          10        20
                  ....*....|....*....|....*..
gi 2462572959  66 RTALHLACATGQPEMVHLLVSRRCELN 92
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 99-128 6.66e-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: 6.66e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462572959  99 RTPLIKAV-QLRQEACATLLLQNGANPNITD 128
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 130-157 7.68e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.68e-03
                          10        20
                  ....*....|....*....|....*...
gi 2462572959 130 FGRTALHYAVYNEDTSMIEKLLSHGTNI 157
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
 
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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