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Conserved domains on  [gi|12854491|dbj|BAB30047|]
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unnamed protein product [Mus musculus]

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
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-257 6.10e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 6.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  43 LRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAV 122
Cdd:COG0666  49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 123 ECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKK 202
Cdd:COG0666 129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12854491 203 GADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 257
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-257 6.10e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 6.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  43 LRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAV 122
Cdd:COG0666  49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 123 ECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKK 202
Cdd:COG0666 129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12854491 203 GADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 257
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-234 4.03e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.95  E-value: 4.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKAVECQ 125
Cdd:PHA03100  39 LYLAKEARNIDVVK-ILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  126 QESCATV--LLLHGADPNLVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLL 185
Cdd:PHA03100 118 SNSYSIVeyLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLH 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 12854491  186 LAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQ 234
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-144 1.46e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491    51 LHKAATIGNEQKLKDYLErKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENqCKINVQDsENRTPLIKAVECQQESCA 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 12854491   131 TVLLLHGADPNLVD 144
Cdd:pfam12796  78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-202 6.24e-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: 50.40  E-value: 6.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  83 TPLHLACANGYTNIVSLLIENQCkiNVQD--------SENRTPLIKAVE-------CQ-QESCATVLLLHGADPNLVDVY 146
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGA--DVVSpratgtffRPGPKNLIYYGEhplsfaaCVgNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12854491 147 SNTALHYAVCGQNISLA----NKLLQYKANLEA------KNKDGHTPLLLAVAENNENMVKFLLKK 202
Cdd:cd22192 169 GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-208 4.69e-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: 47.77  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491    49 KKLHKAATIGNEQKLKDYL-ERKKYNVNGRDKRSRTPL-HLACANGYTNIVSLLIENQCKINVQDSenrtplikavecqq 126
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLeEPKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGDT-------------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   127 escatvlLLHGADPNLVDVYSNTALH---YAVCGQNISLANKllQYKANLEAknkdGHTPLLLAVAENNENMVKFLLKKG 203
Cdd:TIGR00870  85 -------LLHAISLEYVDAVEAILLHllaAFRKSGPLELAND--QYTSEFTP----GITALHLAAHRQNYEIVKLLLERG 151


                  ....*
gi 12854491   204 ADVNA 208
Cdd:TIGR00870 152 ASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 179-208 1.65e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 1.65e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 12854491    179 DGHTPLLLAVAENNENMVKFLLKKGADVNA 208
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-257 6.10e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 6.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  43 LRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAV 122
Cdd:COG0666  49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 123 ECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKK 202
Cdd:COG0666 129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12854491 203 GADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 257
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-249 1.44e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 1.44e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCA 130
Cdd:COG0666  91 LHAAARNGDLEIVK-LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 131 TVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASD 210
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 12854491 211 KNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTA 249
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-257 6.08e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.07  E-value: 6.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  43 LRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAV 122
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 123 ECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKK 202
Cdd:COG0666  96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12854491 203 GADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 257
Cdd:COG0666 176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-217 2.00e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 2.00e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCA 130
Cdd:COG0666 124 LHLAAYNGNLEIVK-LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 131 TVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASD 210
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                ....*..
gi 12854491 211 KNHRTAI 217
Cdd:COG0666 283 LDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-257 6.45e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 6.45e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  62 KLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHGADPN 141
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 142 LVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIAL 221
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 12854491 222 IVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 257
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-234 4.03e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.95  E-value: 4.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKAVECQ 125
Cdd:PHA03100  39 LYLAKEARNIDVVK-ILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  126 QESCATV--LLLHGADPNLVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLL 185
Cdd:PHA03100 118 SNSYSIVeyLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLH 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 12854491  186 LAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQ 234
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-210 3.57e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.07  E-value: 3.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   54 AATIGNEQKLKDYLeRKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVL 133
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12854491  134 --LLHGADPNLvdvySNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASD 210
Cdd:PLN03192 611 yhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA03095 PHA03095
ankyrin-like protein; Provisional
 87-249 4.16e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.45  E-value: 4.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   87 LACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATV---LLLHGADPNLVDVYSNTALHYAVCGQN-ISL 162
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  163 ANKLLQYKANLEAKNKDGHTPL--LLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI---VEPtSSVKLLLQQDT 237
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrnANV-ELLRLLIDAGA 178

                        170
                 ....*....|..
gi 12854491  238 DLAHKDIYGFTA 249
Cdd:PHA03095 179 DVYAVDDRFRSL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 73-222 7.22e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.71  E-value: 7.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   73 NVNGRDKRSRTPLHLACAN--GYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATV------------------ 132
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvny 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  133 LLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNA---- 208
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiiet 257

                        170
                 ....*....|....*...
gi 12854491  209 ----SDKNHRTAIMIALI 222
Cdd:PHA03100 258 llyfKDKDLNTITKIKML 275
PHA03095 PHA03095
ankyrin-like protein; Provisional
 73-253 7.32e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 7.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   73 NVNGRDKRSRTPLHLACANG---YTNIVSLLIENQCKINVQDSENRTPLIKAVECQQ-ESCATVLLLHGADPNLVDVYSN 148
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  149 TALHYAVCGQNI--SLANKLLQYKANLEAKNKDGHTPLLLAVAENNEN--MVKFLLKKGADVNASDKNHRTAI-MIALIV 223
Cdd:PHA03095 119 TPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLhHHLQSF 198

                        170       180       190
                 ....*....|....*....|....*....|.
gi 12854491  224 EPTSSV-KLLLQQDTDLAHKDIYGFTAEEYA 253
Cdd:PHA03095 199 KPRARIvRELIRAGCDPAATDMLGNTPLHSM 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-144 1.46e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491    51 LHKAATIGNEQKLKDYLErKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENqCKINVQDsENRTPLIKAVECQQESCA 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 12854491   131 TVLLLHGADPNLVD 144
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-177 1.61e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491    85 LHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHgADPNLVDvYSNTALHYAVCGQNISLAN 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 12854491   165 KLLQYKANLEAKN 177
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 19-239 1.39e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   19 HSSEVPiSLAKTAPPNLSIGGGYRLRD-KHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACA-NGYTNI 96
Cdd:PHA02876 279 HASQAP-SLSRLVPKLLERGADVNAKNiKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDI 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   97 VSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANK-LLQYKANLEA 175
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNS 437

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12854491  176 KNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNASDKNHRTAIMIALivEPTSSVKLLLQQDTDL 239
Cdd:PHA02876 438 KNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 51-220 1.54e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   51 LHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGY-TNIVSLLIENQCKINVQDSENRTPLIKAVECQQESC 129
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKD 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  130 ATVLLLH-GADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENM-VKFLLKKGADVN 207
Cdd:PHA02876 357 IVITLLElGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436

                        170
                 ....*....|...
gi 12854491  208 ASDKNHRTAIMIA 220
Cdd:PHA02876 437 SKNKDLSTPLHYA 449
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 50-254 1.67e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   50 KLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPL----------- 118
Cdd:PHA02876 147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLecavdsknidt 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  119 IKAV----------------ECQQESCATVLLLH--GADPNLVDVYSNTALHYAVCGQNIS-LANKLLQYKANLEAKNKD 179
Cdd:PHA02876 227 IKAIidnrsninkndlsllkAIRNEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK 306

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12854491  180 GHTPLLLaVAEN---NENmVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKL-LLQQDTDLAHKDIYGFTAEEYAS 254
Cdd:PHA02876 307 GETPLYL-MAKNgydTEN-IRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAA 383
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-243 1.34e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   151 LHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKgADVNASDkNHRTAIMIALIVEPTSSVK 230
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 12854491   231 LLLQQDTDLAHKD 243
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 51-250 1.77e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   51 LHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCA 130
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  131 TVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNas 209
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN-- 229

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 12854491  210 dknhrtaIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAE 250
Cdd:PHA02875 230 -------IMFMIEGEECTILDMICNMCTNLESEAIDALIAD 263
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-273 1.12e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.44  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   66 YLERKKYNVNGRDKRSRTPLH--LACANGYTNIVSLLIENQCKINVQDSENRTPL-IKAVECQ-QESCATVLLLHGADPN 141
Cdd:PHA03095 137 LLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKpRARIVRELIRAGCDPA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  142 LVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMI 219
Cdd:PHA03095 217 ATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 12854491  220 ALIVEPTSSVKLLLQQDTDLahkdiygftAEEYASFNGFTMYHHITANNENKKK 273
Cdd:PHA03095 297 MVRNNNGRAVRAALAKNPSA---------ETVAATLNTASVAGGDIPSDATRLC 341
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-221 4.96e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   39 GGYRLRDKHLKKLHKAATIgnEQKLKDYLERKKYNVNGRDKRS-RTPLHLACANGYTNIVSLLIENQCKINVQDSENRTP 117
Cdd:PHA02878 127 NIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  118 LIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCG-QNISLANKLLQYKANLEAKNK-DGHTPLLLAVaeNNENM 195
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERK 282

                        170       180
                 ....*....|....*....|....*.
gi 12854491  196 VKFLLKKGADVNASDKNHRTAIMIAL 221
Cdd:PHA02878 283 LKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 100-256 5.89e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 5.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  100 LIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANK-----LLQYKANLE 174
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLLEYGANVN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  175 AKNKDGHTPLLLAVAE--NNENMVKFLLKKGADVNASDKNHRTAIMIALI------------------VEPTSSVKLLLQ 234
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvdINAKNRVNYLLS 180

                        170       180
                 ....*....|....*....|..
gi 12854491  235 QDTDLAHKDIYGFTAEEYASFN 256
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYN 202
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 83-248 5.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 5.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   83 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHGADP---------------------- 140
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  141 -NLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMI 219
Cdd:PHA02874 117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                        170       180
                 ....*....|....*....|....*....
gi 12854491  220 ALIVEPTSSVKLLLQQDTDLAHKDIYGFT 248
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 72-256 7.77e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 7.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   72 YNVNGRDKRSRTPLHLAC-ANGYTNIVSLLIENQCKINVQDSENRTPL-IKAVECQQESCATVLLLHGADPNLVDVYSNT 149
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYIT 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  150 ALHYA-VCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI-VEPTS 227
Cdd:PHA02876 344 PLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYM 423

                        170       180
                 ....*....|....*....|....*....
gi 12854491  228 SVKLLLQQDTDLAHKDIYGFTAEEYASFN 256
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKK 452
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-233 1.78e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   55 ATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLL 134
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  135 LHGADPNlvDVY---SNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDK 211
Cdd:PHA02875  89 DLGKFAD--DVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166

                        170       180
                 ....*....|....*....|..
gi 12854491  212 NHRTAIMIALIVEPTSSVKLLL 233
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLL 188
PHA03095 PHA03095
ankyrin-like protein; Provisional
 62-202 6.15e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 6.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   62 KLKDYLERKKYNVNGRDKRSRTPLHLACAN--GYTNIVSLLIENQCKINVQDSENRTPLIKAVecQQESCATV----LLL 135
Cdd:PHA03095 168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMA--TGSSCKRSlvlpLLI 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12854491  136 HGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKK 202
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 88-253 2.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   88 ACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLL 167
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  168 QYKANL-EAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYG 246
Cdd:PHA02875  89 DLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168


                 ....*..
gi 12854491  247 FTAEEYA 253
Cdd:PHA02875 169 CTPLIIA 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-221 8.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 8.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   35 LSIGGGYRLRDKHLKK-LHKAATIGNEQKLKDYLERKKyNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSE 113
Cdd:PHA02874 111 LDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  114 NRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCgQNISlANKLLQYKANLEAKNKDGHTPLLLAVAEN-N 192
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRS-AIELLINNASINDQDIDGSTPLHHAINPPcD 267

                        170       180
                 ....*....|....*....|....*....
gi 12854491  193 ENMVKFLLKKGADVNASDKNHRTAIMIAL 221
Cdd:PHA02874 268 IDIIDILLYHKADISIKDNKGENPIDTAF 296
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 51-254 2.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   51 LHKAATIGNEQKLKDYLERKkYNVNGRDKRSRTPLHLACAN------------------GYT-------------NIVSL 99
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRG-HNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvFYTlvaikdafnnrnvEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  100 LIENQCKiNVQDSENRTPLIKAVECQQESCATVLLL-HGADPNLVDVYS-NTALHYAVCGQNISLANKLLQYKANLEAKN 177
Cdd:PHA02878 120 ILTNRYK-NIQTIDLVYIDKKSKDDIIEAEITKLLLsYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPD 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12854491  178 KDGHTPLLLAVAENNENMVKFLLKKGADVNasdknhrtaimialiveptssvklllqqdtdlaHKDIYGFTAEEYAS 254
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLENGASTD---------------------------------ARDKCGNTPLHISV 242
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 95-253 4.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 4.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   95 NIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLE 174
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12854491  175 AKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIAlIVEPTSSVKLLLQQDTdLAHKDIYGFTAEEYA 253
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-IIHNRSAIELLINNAS-INDQDIDGSTPLHHA 261
Ank_5 pfam13857
Ankyrin repeats (many copies);
66-121 6.24e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 6.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 12854491    66 YLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKA 121
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 130-201 7.96e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 7.96e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12854491  130 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLK 201
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
180-233 1.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 12854491   180 GHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLL 233
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-202 6.24e-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: 50.40  E-value: 6.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  83 TPLHLACANGYTNIVSLLIENQCkiNVQD--------SENRTPLIKAVE-------CQ-QESCATVLLLHGADPNLVDVY 146
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGA--DVVSpratgtffRPGPKNLIYYGEhplsfaaCVgNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12854491 147 SNTALHYAVCGQNISLA----NKLLQYKANLEA------KNKDGHTPLLLAVAENNENMVKFLLKK 202
Cdd:cd22192 169 GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 75-136 9.21e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 9.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12854491   75 NGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLLH 136
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
148-200 1.31e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12854491   148 NTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLL 200
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 130-240 1.58e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 130 ATVLLLHGAdPNLV------DVYSN-TALHYAVCGQNISLANKLLQYKANLEA---------KNKD-----GHTPLLLAV 188
Cdd:cd22192  66 AAVVLMEAA-PELVnepmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAA 144

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 12854491 189 AENNENMVKFLLKKGADVNASDKNHRTAIMIaliveptssvkLLLQQDTDLA 240
Cdd:cd22192 145 CVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNKTFA 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-134 2.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 2.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12854491    82 RTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLL 134
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-211 3.60e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 3.60e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 12854491   179 DGHTPLLLAVAE-NNENMVKFLLKKGADVNASDK 211
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-208 4.69e-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: 47.77  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491    49 KKLHKAATIGNEQKLKDYL-ERKKYNVNGRDKRSRTPL-HLACANGYTNIVSLLIENQCKINVQDSenrtplikavecqq 126
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLeEPKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGDT-------------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   127 escatvlLLHGADPNLVDVYSNTALH---YAVCGQNISLANKllQYKANLEAknkdGHTPLLLAVAENNENMVKFLLKKG 203
Cdd:TIGR00870  85 -------LLHAISLEYVDAVEAILLHllaAFRKSGPLELAND--QYTSEFTP----GITALHLAAHRQNYEIVKLLLERG 151


                  ....*
gi 12854491   204 ADVNA 208
Cdd:TIGR00870 152 ASVPA 156
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 5.81e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 5.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 12854491    51 LHKAATIGNEQKLKDYLErKKYNVNGRDKRSRTPLHLACANGYTNIVSLLI 101
Cdd:pfam13637   5 LHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 73-269 1.15e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.37  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   73 NVNGRDKRSRTPLHLACAN-----GYTNIVSLLIENQCKINVQDSENRTPLIKAVECQQESCATVLLL---HGADPNLVD 144
Cdd:PHA02798  63 NVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmieNGADTTLLD 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  145 VYSNTALHYAV---CGQNISLANKLLQYKANLEA-KNKDGHTPLLLAVAEN----NENMVKFLLKKGADVNASDKNHRTA 216
Cdd:PHA02798 143 KDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKSHKKK 222

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 12854491  217 IMIALIVeptssvkllLQQDTDLAHKDIYGF-----TAEEYASFNGFTMYHHITANNE 269
Cdd:PHA02798 223 FMEYLNS---------LLYDNKRFKKNILDFifsyiDINQVDELGFNPLYYSVSHNNR 271
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 149-206 1.19e-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: 46.16  E-value: 1.19e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12854491 149 TALHYAVCGQNISLANKLLQYKANL--EAKNKD---GHTPLLLAVAENNENMVKFLLKKGADV 206
Cdd:cd22192  53 TALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 179-208 1.65e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 1.65e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 12854491    179 DGHTPLLLAVAENNENMVKFLLKKGADVNA 208
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-187 1.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 12854491   133 LLLHG-ADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLA 187
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-167 4.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 12854491   114 NRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLL 167
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 57-241 5.27e-05

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: 44.49  E-value: 5.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  57 IGNEQKLKDYLERKKYNvngRDKRSRTPLHLACAN---GYTNIVSLLIENQckinvQDSENRTPLIKAvecqqescatvl 133
Cdd:cd21882   5 LGLLECLRWYLTDSAYQ---RGATGKTCLHKAALNlndGVNEAIMLLLEAA-----PDSGNPKELVNA------------ 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491 134 llhgadPNLVDVY-SNTALHYAVCGQNISLANKLLQYKANLEAK------NKDGHT-------PLLLAVAENNENMVKFL 199
Cdd:cd21882  65 ------PCTDEFYqGQTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLL 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 12854491 200 LKKGAD---VNASDKNHRTaIMIALIVEPTSSVK----------LLLQQDTDLAH 241
Cdd:cd21882 139 LENGAQpaaLEAQDSLGNT-VLHALVLQADNTPEnsafvcqmynLLLSYGAHLDP 192
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-208 6.87e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 6.87e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 12854491   179 DGHTPLLLAVAENNENMVKFLLKKGADVNA 208
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
100-154 1.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 12854491   100 LIEN-QCKINVQDSENRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHYA 154
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 93-195 1.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   93 YTNIVSLLIENQCKINVQ--DSENR--TPLIKAVECQQESCATVLLLHGADpnlVDVYSN----TALHYAVCGQNISLAN 164
Cdd:PHA02884  45 YTDIIDAILKLGADPEAPfpLSENSktNPLIYAIDCDNDDAAKLLIRYGAD---VNRYAEeakiTPLYISVLHGCLKCLE 121

                         90       100       110
                 ....*....|....*....|....*....|.
gi 12854491  165 KLLQYKANLEAKNKDGHTPLLLAVAENNENM 195
Cdd:PHA02884 122 ILLSYGADINIQTNDMVTPIELALMICNNFL 152
PHA02946 PHA02946
ankyin-like protein; Provisional
 108-211 2.47e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.96  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  108 NVQDSENRTPLIKAVECQQESCATVLLLHGADPNLVDVYSNTALHY--AVCGQNISLANKLLQYKANL-EAKNKDGHTPl 184
Cdd:PHA02946  66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKInNSVDEEGCGP- 144

                         90       100
                 ....*....|....*....|....*..
gi 12854491  185 LLAVAENNENMVKFLLKKGADVNASDK 211
Cdd:PHA02946 145 LLACTDPSERVFKKIMSIGFEARIVDK 171
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-109 4.54e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 4.54e-04
                          10        20
                  ....*....|....*....|....*...
gi 12854491    82 RTPLHLACANGYTNIVSLLIENQCKINV 109
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-111 5.39e-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: 36.88  E-value: 5.39e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 12854491    82 RTPLHLACA-NGYTNIVSLLIENQCKINVQD 111
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
166-220 6.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 12854491   166 LLQYK-ANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIA 220
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 82-109 1.22e-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: 35.64  E-value: 1.22e-03
                           10        20
                   ....*....|....*....|....*...
gi 12854491     82 RTPLHLACANGYTNIVSLLIENQCKINV 109
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 77-204 1.61e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   77 RDKRSRTPLHLACANGytNIVSLLIENqckiNVQDSENRTpLIKAVECQQESCATV---------------LLLHGADPN 141
Cdd:PHA02736  13 PDIEGENILHYLCRNG--GVTDLLAFK----NAISDENRY-LVLEYNRHGKQCVHIvsnpdkadpqeklklLMEWGADIN 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12854491  142 LVD-VYSNTALHYAVCGQNISLANKLL-QYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGA 204
Cdd:PHA02736  86 GKErVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 139-220 5.21e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.34  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  139 DPNLVDVYSNTALHYAVCGQNISlANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIM 218
Cdd:PTZ00322  75 DPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153


                 ..
gi 12854491  219 IA 220
Cdd:PTZ00322 154 LA 155
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 159-222 8.41e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 8.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12854491  159 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI 222
Cdd:PLN03192 537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600
PHA02798 PHA02798
ankyrin-like protein; Provisional
 94-248 9.51e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.12  E-value: 9.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491   94 TNIVSLLIENQCKINVQDSENRTPLikavecqqescATVLllhgadPNLVDVYSntalhyavcgqNISLANKLLQYKANL 173
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL-----------CTIL------SNIKDYKH-----------MLDIVKILIENGADI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12854491  174 EAKNKDGHTPLLLAVAE---NNENMVKFLLKKGADVNASDKNHRTAIMIALIVE---PTSSVKLLLQQDTDL-AHKDIYG 246
Cdd:PHA02798 103 NKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDInTHNNKEK 182


                 ..
gi 12854491  247 FT 248
Cdd:PHA02798 183 YD 184
 
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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