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Conserved domains on  [gi|755497895|ref|XP_011237482|]
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uncharacterized protein LOC70981 isoform X2 [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];
64-289 1.24e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  64 DNDLHMAACAGDLPFVRLYFTLGKYEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWED 143
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 144 KIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVH 223
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755497895 224 AVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYAIEGDRDVRTMLLELRKRNRA 289
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-289 1.24e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  64 DNDLHMAACAGDLPFVRLYFTLGKYEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWED 143
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 144 KIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVH 223
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755497895 224 AVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYAIEGDRDVRTMLLELRKRNRA 289
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 89-268 9.82e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.86  E-value: 9.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  89 EVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALH 168
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 169 YAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRlKMAQFLVRmEASVHAVDSQRRNSLMYAVR--CDSPVmVN 246
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINppCDIDI-ID 272

                        170       180
                 ....*....|....*....|....*.
gi 755497895 247 LILQQGVDINLKDLFGW----TALRY 268
Cdd:PHA02874 273 ILLYHKADISIKDNKGEnpidTAFKY 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-189 7.48e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 7.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  101 MHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEhHANLHIKDSmGNTALHYAVYSGNLATAA 180
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*....
gi 755497895  181 RLLQYGADI 189
Cdd:pfam12796  79 LLLEKGADI 87
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-217 4.12e-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: 48.47  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 100 AMHFACFYGHLELVIYLWRRGCEIN---VC------DNHNIT-----PLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNT 165
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADVVsprATgtffrpGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755497895 166 ALHYAVYSGNLATAAR----LLQYGADIEE------RTKDNLTPLLLALRENRLKMAQFLVR 217
Cdd:cd22192  172 VLHILVLQPNKTFACQmydlILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 123-293 4.48e-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: 45.46  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  123 INVCDNHNITPLMKAVQSWEDKIVCFLLEHHANlhiKDSMGNTALHYAV--YSGNLATAARL------------LQYGAD 188
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISleYVDAVEAILLHllaafrksgpleLANDQY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  189 IEERTKDnLTPLLLALRENRLKMAQFLVRMEASVHA-------VDSQRRNSLMY------AVRC-DSPVMVNLILQQGVD 254
Cdd:TIGR00870 122 TSEFTPG-ITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYHgesplnAAAClGSPSIVALLSEDPAD 200

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 755497895  255 INLKDLFGWTALRYAIegdrdvrtMLLELRKRNRAFQSS 293
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV--------MENEFKAEYEELSCQ 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 162-191 1.88e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.88e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 755497895   162 MGNTALHYAVYSGNLATAARLLQYGADIEE 191
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-289 1.24e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 1.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  64 DNDLHMAACAGDLPFVRLYFTLGKYEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWED 143
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 144 KIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVH 223
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755497895 224 AVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYAIEGDRDVRTMLLELRKRNRA 289
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-307 2.07e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 2.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  65 NDLHMAACAGDLPFVRLYFTLGKYEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDK 144
Cdd:COG0666   22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 145 IVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHA 224
Cdd:COG0666  102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 225 VDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYAIE-GDRDVRTMLLELRKRNRAFQSSENSSIRLINK 303
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEnGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261


                 ....
gi 755497895 304 ADAE 307
Cdd:COG0666  262 AGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
67-266 2.88e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 2.88e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  67 LHMAACAGDLPFVRLYFTLGKyEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIV 146
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 147 CFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVD 226
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755497895 227 SQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTAL 266
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-282 2.03e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 2.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  89 EVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALH 168
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 169 YAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLI 248
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755497895 249 LQQGVDINLKDLFGWTALRYAIE-GDRDVRTMLLE 282
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAEnGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-282 7.05e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 7.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 110 LELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADI 189
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 190 EERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYA 269
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170
                 ....*....|....
gi 755497895 270 IE-GDRDVRTMLLE 282
Cdd:COG0666  161 AAnGNLEIVKLLLE 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 89-268 9.82e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.86  E-value: 9.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  89 EVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALH 168
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 169 YAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRlKMAQFLVRmEASVHAVDSQRRNSLMYAVR--CDSPVmVN 246
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINppCDIDI-ID 272

                        170       180
                 ....*....|....*....|....*.
gi 755497895 247 LILQQGVDINLKDLFGW----TALRY 268
Cdd:PHA02874 273 ILLYHKADISIKDNKGEnpidTAFKY 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-189 7.48e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 7.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  101 MHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEhHANLHIKDSmGNTALHYAVYSGNLATAA 180
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*....
gi 755497895  181 RLLQYGADI 189
Cdd:pfam12796  79 LLLEKGADI 87
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-279 9.85e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.08  E-value: 9.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  75 DLPFVRLYFTLGKyEVNHRDRENRN-AMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHH 153
Cdd:PHA02878 146 EAEITKLLLSYGA-DINMKDRHKGNtALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 154 ANLHIKDSMGNTALHYAV-YSGNLATAARLLQYGADIE-ERTKDNLTPLLLALR-ENRLKMaqfLVRMEASVHAVDSQRR 230
Cdd:PHA02878 225 ASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKsERKLKL---LLEYGADINSLNSYKL 301

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755497895 231 NSLMYAVR------CDSPVMVNLILQQGVDINLKDLFGWTALRYAIEGDRDVRTM 279
Cdd:PHA02878 302 TPLSSAVKqylcinIGRILISNICLLKRIKPDIKNSEGFIDNMDCITSNKRLNQI 356
Ank_2 pfam12796
Ankyrin repeats (3 copies);
67-160 3.11e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 3.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895   67 LHMAACAGDLPFVRLYFTLGkYEVNHRDRENRNAMHFACFYGHLELVIYLWRRgCEINVCDNHNiTPLMKAVQSWEDKIV 146
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 755497895  147 CFLLEHHANLHIKD 160
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 111-270 4.22e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 4.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 111 ELVIYLWRRGCEINVCDNHNITPLM-----KAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVY--SGNLATAARLL 183
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 184 QYGADIEERTKDNLTPLLLALRENR--LKMAQFLVRMEASVHAVDS---------------QRRNS-LMYAVRCDSPVMV 245
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvnyllsygvpinikdVYGFTpLHYAVYNNNPEFV 208

                        170       180
                 ....*....|....*....|....*
gi 755497895 246 NLILQQGVDINLKDLFGWTALRYAI 270
Cdd:PHA03100 209 KYLLDLGANPNLVNKYGDTPLHIAI 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
167-259 1.79e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  167 LHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASvhAVDSQRRNSLMYAVRCDSPVMVN 246
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 755497895  247 LILQQGVDINLKD 259
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 110-270 3.74e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 3.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 110 LELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHY-----AVYSGNLATAARLLQ 184
Cdd:PHA03100  15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 185 YGADIEERTKDNLTPLLLALRE--NRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRC---DSPVM--------------- 244
Cdd:PHA03100  95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkiDLKILkllidkgvdinaknr 174

                        170       180
                 ....*....|....*....|....*.
gi 755497895 245 VNLILQQGVDINLKDLFGWTALRYAI 270
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAV 200
Ank_2 pfam12796
Ankyrin repeats (3 copies);
134-226 1.64e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  134 LMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYgADIEERTkDNLTPLLLALRENRLKMAQ 213
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 755497895  214 FLVRMEASVHAVD 226
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 108-228 4.34e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 4.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 108 GHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWED--KIVCFLLEHHANLHIKDS----------------MGNTALHY 169
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHY 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755497895 170 AVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVDSQ 228
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 55-220 5.54e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 5.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  55 AYLDMAYfPD--NDLHMAACAGDLPFVRLYFTLGKYEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNIT 132
Cdd:PHA02875  59 AIPDVKY-PDieSELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFS 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 133 PLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKD-NLTPLLLALRENRLKM 211
Cdd:PHA02875 138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDI 217


                 ....*....
gi 755497895 212 AQFLVRMEA 220
Cdd:PHA02875 218 VRLFIKRGA 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 79-207 9.63e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 9.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  79 VRLYFTLGKYEVNhRDRENRNAMHFACFYGHL--ELVIYLWRRGCEINVCDNHNITPL--MKAVQSWEDKIVCFLLEHHA 154
Cdd:PHA03095 170 LRLLIDAGADVYA-VDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGI 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755497895 155 NLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALREN 207
Cdd:PHA03095 249 SINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN 301
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-282 1.09e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  97 NRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNL 176
Cdd:PHA02875   2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 177 ATAARLLQYGADIEERT-KDNLTPLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLILQQGVDI 255
Cdd:PHA02875  82 KAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                        170       180
                 ....*....|....*....|....*...
gi 755497895 256 NLKDLFGWTALRYAI-EGDRDVRTMLLE 282
Cdd:PHA02875 162 DIEDCCGCTPLIIAMaKGDIAICKMLLD 189
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-298 1.97e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 116 LWRRGCEINVCDNHNITPLMKAVQSWEDK-IVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTK 194
Cdd:PHA02876 327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 195 DNLTPLLLAL-RENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCD-SPVMVNLILQQGVDINLKDLFGWTALRYAIEG 272
Cdd:PHA02876 407 KIGTALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY 486

                        170       180
                 ....*....|....*....|....*....
gi 755497895 273 DRDVRTML---LELRKrNRAFQSSENSSI 298
Cdd:PHA02876 487 HGIVNILLhygAELRD-SRVLHKSLNDNM 514
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-281 2.04e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 116 LWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIeerTKD 195
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKN 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 196 NLTpLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDS-PVMVNLILQQGVDINLKDLFGWTALRYAIEGDR 274
Cdd:PHA02876 241 DLS-LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319

                        170
                 ....*....|
gi 755497895 275 D---VRTMLL 281
Cdd:PHA02876 320 DtenIRTLIM 329
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 108-287 3.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 3.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 108 GHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFL-----------------------LEHHANLHIKDSMGN 164
Cdd:PHA02874  46 GDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGIDVNIKDAELK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 165 TALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVM 244
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 755497895 245 VNLILQQGVDINLKDLFGWTALRYAIEGDRDVRTMLLELRKRN 287
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASIN 248
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-268 3.54e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 3.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 110 LELVIYLWRRGCEINVCDNHNITPL---MKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLL-QY 185
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 186 GADIEERTKDNLTPLLLALR--ENRLKMAQFLVRMEASVHAVDSQRRNSL---MYAVRCDsPVMVNLILQQGVDINLKDL 260
Cdd:PHA03095 107 GADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNAN-VELLRLLIDAGADVYAVDD 185


                 ....*...
gi 755497895 261 FGWTALRY 268
Cdd:PHA03095 186 RFRSLLHH 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
 67-286 1.13e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  67 LHMAACAGD-LPFVRLYFTLGKYeVNHRDRENRNAMHfACFYG---HLELVIYLWRRGCEINVCDNHNITPLMKAVQS-- 140
Cdd:PHA03095  87 LHLYLYNATtLDVIKLLIKAGAD-VNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSrn 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 141 WEDKIVCFLLEHHANLHIKDSMGNTALHY-AVYSGNLATAAR-LLQYGADIEERTKDNLTPLLLAL---RENRLKMAQFL 215
Cdd:PHA03095 165 ANVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIVReLIRAGCDPAATDMLGNTPLHSMAtgsSCKRSLVLPLL 244

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755497895 216 VRmEASVHAVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYAIEgDRDVRTMLLELRKR 286
Cdd:PHA03095 245 IA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR-NNNGRAVRAALAKN 313
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-255 1.19e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  52 EDPAYLdmayfpdndlhMAACAGDLPFVRLYFTLGKyEVNHRDRENRNAMHFACFYG-HLELVIYLWRRGCEINVCDNHN 130
Cdd:PHA02876 308 ETPLYL-----------MAKNGYDTENIRTLIMLGA-DVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCD 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 131 ITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAAR-LLQYGADIEERTKDNLTPLLLALREN-R 208
Cdd:PHA02876 376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNSKNKDLSTPLHYACKKNcK 455

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755497895 209 LKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSpvMVNLILQQGVDI 255
Cdd:PHA02876 456 LDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAEL 500
Ank_4 pfam13637
Ankyrin repeats (many copies);
163-216 1.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.76e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755497895  163 GNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLV 216
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 101-282 2.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 101 MHFACFYGHLELVIYLWRRGCEINVCDNHNITPL-----------MKAV------------------------------- 138
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLhiickepnklgMKEMirsinkcsvfytlvaikdafnnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 139 ----------------------QSWEDKIVCFLLEHHANLHIKD-SMGNTALHYAVYSGNLATAARLLQYGADIEERTKD 195
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskdDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 196 NLTPLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAV-RCDSPVMVNLILQQGVDINLKD-LFGWTALRYAIEgD 273
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIK-S 279


                 ....*....
gi 755497895 274 RDVRTMLLE 282
Cdd:PHA02878 280 ERKLKLLLE 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 94-226 2.95e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 2.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  94 DRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVcFLLEHHAnlHIKDS-MGNTALHYAVY 172
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF-RILYHFA--SISDPhAAGDLLCTAAK 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755497895 173 SGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVD 226
Cdd:PLN03192 632 RNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 116-271 4.56e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 116 LWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKD 195
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755497895 196 NLtpLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLILQQGVDI---NLKDLFGWTALRYAIE 271
Cdd:PLN03192 624 DL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTELRELLQ 700
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 132-282 4.61e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 132 TPLMKAVQSWEDKIVCFLLEhhANLHIKDSM---GNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENR 208
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLD--LGKFADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755497895 209 LKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFG-WTALRYAIEGDR-DVRTMLLE 282
Cdd:PHA02875 148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKiDIVRLFIK 223
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-269 1.88e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  86 GKYEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCD-----------------------------NHNITPLMK 136
Cdd:PHA02876 167 GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDLSLLK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 137 AVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLAT-AARLLQYGADIEERTKDNLTPL-LLALRENRLKMAQF 214
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRT 326

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755497895 215 LVRMEASVHAVDSQRRNSLMYAVRCD-SPVMVNLILQQGVDINLKDLFGWTALRYA 269
Cdd:PHA02876 327 LIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYA 382
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-134 7.47e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 7.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755497895   89 EVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPL 134
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 144-266 1.28e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.83  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 144 KIVCFLLEHHANLHIKDSMGNTAL-----HYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRE---NRLKMAQFL 215
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFM 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755497895 216 VRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLI---LQQGVDINL-KDLFGWTAL 266
Cdd:PHA02798 132 IENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIkllLEKGVDINThNNKEKYDTL 186
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-217 4.12e-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: 48.47  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 100 AMHFACFYGHLELVIYLWRRGCEIN---VC------DNHNIT-----PLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNT 165
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADVVsprATgtffrpGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755497895 166 ALHYAVYSGNLATAAR----LLQYGADIEE------RTKDNLTPLLLALRENRLKMAQFLVR 217
Cdd:cd22192  172 VLHILVLQPNKTFACQmydlILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 149-227 4.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 4.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755497895 149 LLEHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVDS 227
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
Ank_5 pfam13857
Ankyrin repeats (many copies);
220-269 4.54e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 4.54e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755497895  220 ASVHAVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYA 269
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
149-203 7.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755497895  149 LLEH-HANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLA 203
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
67-116 7.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 7.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755497895   67 LHMAACAGDLPFVRLYFTLGKyEVNHRDRENRNAMHFACFYGHLELVIYL 116
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 171-284 1.15e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 171 VYSGNLATAARLLQYGAD-IEERTKDNLTPLLLALRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLIL 249
Cdd:PHA02874   9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755497895 250 QQGVD-----------------------INLKDLFGWTALRYAIE-GDRDVRTMLLELR 284
Cdd:PHA02874  89 DNGVDtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKkGDLESIKMLFEYG 147
Ank_2 pfam12796
Ankyrin repeats (3 copies);
233-273 1.26e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 1.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755497895  233 LMYAVRCDSPVMVNLILQQGVDINLKDLFGWTALRYAIEGD 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG 41
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 123-293 4.48e-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: 45.46  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  123 INVCDNHNITPLMKAVQSWEDKIVCFLLEHHANlhiKDSMGNTALHYAV--YSGNLATAARL------------LQYGAD 188
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLNLSC---RGAVGDTLLHAISleYVDAVEAILLHllaafrksgpleLANDQY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  189 IEERTKDnLTPLLLALRENRLKMAQFLVRMEASVHA-------VDSQRRNSLMY------AVRC-DSPVMVNLILQQGVD 254
Cdd:TIGR00870 122 TSEFTPG-ITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYHgesplnAAAClGSPSIVALLSEDPAD 200

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 755497895  255 INLKDLFGWTALRYAIegdrdvrtMLLELRKRNRAFQSS 293
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV--------MENEFKAEYEELSCQ 231
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 183-334 5.49e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 183 LQYGADIEERtkdnltplllaLRENRLKMAQFLVRMEASVHAVDSQRRNSLMYAVRCDSPVMVNLILQQGVDINLKDLFG 262
Cdd:PHA02876 143 IEYMKLIKER-----------IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDD 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755497895 263 WTALRYAIEgDRDVRTMLLELRKRNRafqssenssirlINKADAEVTSPTANETLgikrrpmdQTQIVMLDS 334
Cdd:PHA02876 212 LSVLECAVD-SKNIDTIKAIIDNRSN------------INKNDLSLLKAIRNEDL--------ETSLLLYDA 262
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 53-157 6.32e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  53 DPAYLDMAYFpdnDLHMAACAGDLPFVRLYFTLGKyEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNIT 132
Cdd:PTZ00322  75 DPVVAHMLTV---ELCQLAASGDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                         90       100
                 ....*....|....*....|....*
gi 755497895 133 PLMKAVQSWEDKIVCFLLEHHANLH 157
Cdd:PTZ00322 151 PLELAEENGFREVVQLLSRHSQCHF 175
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 163-194 7.76e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 7.76e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 755497895  163 GNTALHYAVYS-GNLATAARLLQYGADIEERTK 194
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
132-183 8.18e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 8.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755497895  132 TPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYSGNLATAARLL 183
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 122-266 9.15e-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: 44.23  E-value: 9.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 122 EINVCDNHNIT--PLMKA-----VQSWEDKIVCflleHHANLHIKDSMGNTALHYAVYSGNLATAARLLQYGADI--EER 192
Cdd:cd22192    7 ELHLLQQKRISesPLLLAakendVQAIKKLLKC----PSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 193 TKD---NLTPLLLALRENRLKMAQFLVRMEASVH------AVDSQRRNSLMY--------AVRCDSPVMVNLILQQGVDI 255
Cdd:cd22192   83 TSDlyqGETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADI 162

                        170
                 ....*....|.
gi 755497895 256 NLKDLFGWTAL 266
Cdd:cd22192  163 RAQDSLGNTVL 173
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 88-161 1.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 1.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755497895  88 YEVNHRDRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHNITPLMKAVQSWEDKIVCFLLEHHANLHIKDS 161
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 162-191 1.88e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.88e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 755497895   162 MGNTALHYAVYSGNLATAARLLQYGADIEE 191
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
118-170 3.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 3.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755497895  118 RRGCEINVCDNHNITPLMKAV--QSWEdkIVCFLLEHHANLHIKDSMGNTALHYA 170
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAkyGALE--IVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 96-230 7.58e-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: 41.40  E-value: 7.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  96 ENRNAMHFACFYGHLELVIYLWRRGCEINVCDN--------HNIT-----PLMKA--VQSWEdkIVCFLLEHHAN---LH 157
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspGNLFyfgelPLSLAacTNQEE--IVRLLLENGAQpaaLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 158 IKDSMGNTALHYAVYSGNLATAAR---------LLQYGA------DIEERT-KDNLTPLLLALRENRLKMAQFLVRMEAS 221
Cdd:cd21882  150 AQDSLGNTVLHALVLQADNTPENSafvcqmynlLLSYGAhldptqQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQREFS 229


                 ....*....
gi 755497895 222 VHAVDSQRR 230
Cdd:cd21882  230 GPYQPLSRK 238
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 96-125 9.16e-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: 36.08  E-value: 9.16e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 755497895   96 ENRNAMHFACFYGHLELVIYLWRRGCEINV 125
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 77-219 1.24e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  77 PFVRLYFTLGKYEvnhrdreNRNAMHFACFYGHLELVIYLWRRGCEINVC---------DNHNI-----TPLMKAVQSWE 142
Cdd:cd22194  128 RFINAEYTEEAYE-------GQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkYKHEGfyfgeTPLALAACTNQ 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 143 DKIVCFLLEH-HANLHIKDSMGNTALHYAV-----YSGNLATAARLLQY------GADIEE-RTKDNLTPLLLALRENRL 209
Cdd:cd22194  201 PEIVQLLMEKeSTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMillkseNKNLETiRNNEGLTPLQLAAKMGKA 280

                        170
                 ....*....|
gi 755497895 210 KMAQFLVRME 219
Cdd:cd22194  281 EILKYILSRE 290
PHA02791 PHA02791
ankyrin-like protein; Provisional
 94-186 2.49e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895  94 DRENRNAMHFACFYGHLELVIYLWRRGCEINVCDNHniTPLMKAVQSWEDKIVCFLLEHHANLHIKDSMGNTALHYAVYS 173
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                         90       100
                 ....*....|....*....|
gi 755497895 174 GNLATAA-------RLLQYG 186
Cdd:PHA02791 105 GNMQTVKlfvkknwRLMFYG 124
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 163-189 3.23e-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: 34.54  E-value: 3.23e-03
                          10        20
                  ....*....|....*....|....*..
gi 755497895  163 GNTALHYAVYSGNLATAARLLQYGADI 189
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 132-219 6.02e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 38.62  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755497895 132 TPLMKAVQSWEDKIVCFLLEHH---ANLHIKDSMGNTALHYAV----------------YSGNLATAARLLQYGADIEER 192
Cdd:cd22193  125 LPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLHALVtvadntkentkfvtrmYDMILIRGAKLCPTVELEEIR 204

                         90       100
                 ....*....|....*....|....*..
gi 755497895 193 TKDNLTPLLLALRENRLKMAQFLVRME 219
Cdd:cd22193  205 NNDGLTPLQLAAKMGKIEILKYILQRE 231
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 128-205 7.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 7.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755497895 128 NHNITPLMKAVQSWEDKIVCFLLEHHANLH-IKDSMGNTALHYAVYSGNLATAARLLQYGADIEERTKDNLTPLLLALR 205
Cdd:PHA02884  68 NSKTNPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
 
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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