NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958776210|ref|XP_038965787|]
View 

inversin isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
349-582 1.17e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 349 MWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVI 428
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 429 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 508
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776210 509 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 582
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-240 2.81e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  19 HAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 179 DVEGKIPLHWAANHKDASAVHtvrcILDAAptESLLNWQDYEGRTPLHFAVADGNLTVVDVL 240
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVK----LLLEA--GADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-300 2.48e-11

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 2.48e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776210 225 LHFAVADGNLTVVDVLTSYEsCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGtvpSDSQGATPLHYAAQSN 300
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSG 72
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 575-601 1.97e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.97e-04
                          10        20
                  ....*....|....*....|....*..
gi 1958776210 575 AIQDIAAFKIQAVYKGYKVRKAFRDRK 601
Cdd:cd23767     6 QRMNRAATLIQALWRGYKVRKELKKKK 32
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
349-582 1.17e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 349 MWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVI 428
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 429 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 508
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776210 509 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 582
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-240 2.81e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  19 HAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 179 DVEGKIPLHWAANHKDASAVHtvrcILDAAptESLLNWQDYEGRTPLHFAVADGNLTVVDVL 240
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVK----LLLEA--GADLNAKDKDGLTALLLAAAAGAALIVKLL 271
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 358-576 1.22e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.89  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 358 DVLRTMLslKSDIDINMADKYGGTALHAAALSGHVST-----VKLLLDNDAQVDATDVMKHTPLFRA--CEMGHRDVIQT 430
Cdd:PHA03100   49 DVVKILL--DNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 431 LIKGGARVDLVDQDGHSLLHWAALGGNAD--VCQILIENKINPNVQDYagrtplqcaayggyINCmavLMENNADPNIQD 508
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR--------------VNY---LLSYGVPINIKD 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776210 509 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEerYTPLDYALLGERHEVIQFMLEHGAlSIAAI 576
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG--DTPLHIAILNNNKEIFKLLLNNGP-SIKTI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
416-508 1.39e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 416 LFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIEnKINPNVQDYaGRTPLQCAAYGGYINCMA 495
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958776210 496 VLMENNADPNIQD 508
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-262 4.84e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.02  E-value: 4.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  62 DCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGE 141
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 142 VdtQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKdasavhtvRCILDAAPTESLLNWQDYEG 221
Cdd:PHA02874  185 V--KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--------RSAIELLINNASINDQDIDG 254

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958776210 222 RTPLHFAVA-DGNLTVVDVLTsYESCNITSYDNLFRTPLHWA 262
Cdd:PHA02874  255 STPLHHAINpPCDIDIIDILL-YHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-179 1.49e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  85 LHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDtqdkNKQTALHWSAYYNNPEH 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1958776210 165 AKLLIKHDSNIGIPD 179
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-300 2.48e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 2.48e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776210 225 LHFAVADGNLTVVDVLTSYEsCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGtvpSDSQGATPLHYAAQSN 300
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSG 72
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 166-294 6.57e-09

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: 58.87  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 166 KLLIKHDSNIGIPDVEGKIPLHWAA--NHKDASAVhtvrcILDAAPTesLLNW----QDYEGRTPLHFAVADGNLTVVDV 239
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAAlyDNLEAAVV-----LMEAAPE--LVNEpmtsDLYQGETALHIAVVNQNLNLVRE 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776210 240 LTSYESCNIT----------SYDNLF---RTPLHWAALLGHAQIVHLLLERNKSgTVPSDSQGATPLH 294
Cdd:cd22192   108 LIARGADVVSpratgtffrpGPKNLIyygEHPLSFAACVGNEEIVRLLIEHGAD-IRAQDSLGNTVLH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 239-301 9.87e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 9.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776210 239 VLTSYESCNITSYDNlfRTPLHWAALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYAAQSNF 301
Cdd:PTZ00322  101 LLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGF 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 372-519 1.45e-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: 48.09  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 372 INMA---DKYGG-TALHAAALSGHVSTVKLLLDNDAQV---DATDVM------------KHTPLFRACeMGHRDVIQTLI 432
Cdd:cd22192    78 VNEPmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVvspRATGTFfrpgpknliyygEHPLSFAAC-VGNEEIVRLLI 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 433 KGGArvDLVDQD--GHSLLHWAALGGNAD-VCQI--LI---ENKINP----NVQDYAGRTPLQCAAYGGYINCMAVLMEN 500
Cdd:cd22192   157 EHGA--DIRAQDslGNTVLHILVLQPNKTfACQMydLIlsyDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234

                         170
                  ....*....|....*....
gi 1958776210 501 nadpniqdkegRTALHWSC 519
Cdd:cd22192   235 -----------RRHIQWTY 242
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 575-601 1.97e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.97e-04
                          10        20
                  ....*....|....*....|....*..
gi 1958776210 575 AIQDIAAFKIQAVYKGYKVRKAFRDRK 601
Cdd:cd23767     6 QRMNRAATLIQALWRGYKVRKELKKKK 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 150-294 4.21e-04

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: 43.53  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 150 QTALHWSAYYNNP-EHAKLLIKHDSNIgipdVEGKIPLHWAA-NHKDAsaVHTVRCILDAAPTES----LLNWQD----Y 219
Cdd:TIGR00870  53 RSALFVAAIENENlELTELLLNLSCRG----AVGDTLLHAISlEYVDA--VEAILLHLLAAFRKSgpleLANDQYtsefT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 220 EGRTPLHFAVADGNLTVVDVL------TSYES----CNITSYDNLF---RTPLHWAALLGHAQIVHLLLErNKSGTVPSD 286
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLlergasVPARAcgdfFVKSQGVDSFyhgESPLNAAACLGSPSIVALLSE-DPADILTAD 205


                  ....*...
gi 1958776210 287 SQGATPLH 294
Cdd:TIGR00870 206 SLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 1.29e-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: 36.41  E-value: 1.29e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958776210   48 GRTPLMYCVLADRLDCADALLKAGADVNK 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 444-473 2.75e-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: 2.75e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958776210  444 DGHSLLHWAALGGNADVCQILIENKINPNV 473
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 209-388 2.97e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 209 PTESLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLfrtpLHwAALLGHAQIV-----HLLLERNKSGTV 283
Cdd:TIGR00870  40 PKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGDTL----LH-AISLEYVDAVeaillHLLAAFRKSGPL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 284 P--------SDSQGATPLHYAAQ-SNFAVLHY---HGPDVPHHCavsnkvflqeTVKVFLTHPSVrdDSDLEGRTSFMWA 351
Cdd:TIGR00870 115 ElandqytsEFTPGITALHLAAHrQNYEIVKLlleRGASVPARA----------CGDFFVKSQGV--DSFYHGESPLNAA 182

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958776210 352 AGKGSDDVLRtmLSLKSDIDINMADKYGGTALHAAAL 388
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADILTADSLGNTLLHLLVM 217
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
349-582 1.17e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 349 MWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVI 428
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 429 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 508
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958776210 509 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 582
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
357-616 2.67e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 2.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 357 DDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGA 436
Cdd:COG0666    32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 437 RVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALH 516
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 517 WSCNNGYLDAIKLLLDFAAFPNQMenNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAFKIQAVYKGYKVRKA 596
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAK--DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                         250       260
                  ....*....|....*....|
gi 1958776210 597 FRDRKNLLMKHEQLRKDAAA 616
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
364-570 2.38e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 2.38e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 364 LSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQ 443
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 444 DGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGY 523
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958776210 524 LDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQFMLEHGA 570
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGE--TPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
247-515 4.78e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 4.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 247 NITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTVPSDSQGATPLHYAAQSNFAvlhyhgpdvphhcavsnkvflqET 326
Cdd:COG0666    45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL----------------------EI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 327 VKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVD 406
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL--EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 407 ATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAA 486
Cdd:COG0666   181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260

                         250       260
                  ....*....|....*....|....*....
gi 1958776210 487 YGGYINCMAVLMENNADPNIQDKEGRTAL 515
Cdd:COG0666   261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-240 2.81e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  19 HAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 179 DVEGKIPLHWAANHKDASAVHtvrcILDAAptESLLNWQDYEGRTPLHFAVADGNLTVVDVL 240
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVK----LLLEA--GADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-279 2.68e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 2.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  19 HAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE--AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 179 DVEGKIPLHWAANHKDasaVHTVRCILDAaptESLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYEScNITSYDNLFRTP 258
Cdd:COG0666   183 DNDGETPLHLAAENGH---LEIVKLLLEA---GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA-DLNAKDKDGLTA 255

                         250       260
                  ....*....|....*....|.
gi 1958776210 259 LHWAALLGHAQIVHLLLERNK 279
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-302 1.84e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  33 LIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDL 112
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 113 EEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANH 192
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 193 KDasaVHTVRCILDAAPTeslLNWQDYEGRTPLHFAVADGNLTVVDVLTSYEScNITSYDNLFRTPLHWAALLGHAQIVH 272
Cdd:COG0666   164 GN---LEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVK 236

                         250       260       270
                  ....*....|....*....|....*....|
gi 1958776210 273 LLLERNKSGTvPSDSQGATPLHYAAQSNFA 302
Cdd:COG0666   237 LLLEAGADLN-AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
96-482 4.27e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 4.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  96 FMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNI 175
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 176 GIPDVEGKIPLHWAANHKDASAvhtVRCILDAAPTeslLNWQDYEGRTPLHFAVADGNLTVVDVLTSYEScNITSYDNLF 255
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEI---VKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 256 RTPLHWAALLGHAQIVHLLLERnksgtvpsdsqGAtplhyaaqsnfavlhyhgpdvphhcavsnkvflqetvkvflthps 335
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLLLEA-----------GA--------------------------------------------- 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 336 vrddsdlegrtsfmwaagkgsddvlrtmlslksdiDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTP 415
Cdd:COG0666   178 -----------------------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776210 416 LFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPL 482
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 358-576 1.22e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.89  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 358 DVLRTMLslKSDIDINMADKYGGTALHAAALSGHVST-----VKLLLDNDAQVDATDVMKHTPLFRA--CEMGHRDVIQT 430
Cdd:PHA03100   49 DVVKILL--DNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 431 LIKGGARVDLVDQDGHSLLHWAALGGNAD--VCQILIENKINPNVQDYagrtplqcaayggyINCmavLMENNADPNIQD 508
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR--------------VNY---LLSYGVPINIKD 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776210 509 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEerYTPLDYALLGERHEVIQFMLEHGAlSIAAI 576
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG--DTPLHIAILNNNKEIFKLLLNNGP-SIKTI 254
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-300 1.47e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  64 ADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPgeVD 143
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD--IN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 144 TQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDasaVHTVRCILDA-APteslLNWQDYEGR 222
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN---LEIVKLLLEAgAD----VNAQDNDGN 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776210 223 TPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTVPsDSQGATPLHYAAQSN 300
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENG 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
395-570 3.20e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 3.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 395 VKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQ 474
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 475 DYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMenNEERYTPLDYAL 554
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTPLHLAA 161

                         170
                  ....*....|....*.
gi 1958776210 555 LGERHEVIQFMLEHGA 570
Cdd:COG0666   162 ANGNLEIVKLLLEAGA 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
416-508 1.39e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 416 LFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIEnKINPNVQDYaGRTPLQCAAYGGYINCMA 495
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958776210 496 VLMENNADPNIQD 508
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
449-540 1.66e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 1.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 449 LHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMEnNADPNIQDkEGRTALHWSCNNGYLDAIK 528
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1958776210 529 LLLDFAAFPNQM 540
Cdd:pfam12796  79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-186 4.06e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  19 HAAAVNGDKGALQRLIvGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666   125 HLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMApgEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA--DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                  ....*...
gi 1958776210 179 DVEGKIPL 186
Cdd:COG0666   282 LLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-262 4.84e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.02  E-value: 4.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  62 DCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGE 141
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 142 VdtQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKdasavhtvRCILDAAPTESLLNWQDYEG 221
Cdd:PHA02874  185 V--KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--------RSAIELLINNASINDQDIDG 254

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958776210 222 RTPLHFAVA-DGNLTVVDVLTsYESCNITSYDNLFRTPLHWA 262
Cdd:PHA02874  255 STPLHHAINpPCDIDIIDILL-YHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
383-475 1.13e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 383 LHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKgGARVDLVDqDGHSLLHWAALGGNADVCQ 462
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958776210 463 ILIENKINPNVQD 475
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-278 2.18e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 2.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  32 RLIVGNSALKDKEDQFGRTPLMYCVL-ADRLDCADALLKAGADVNKTDHSRRTALH--LAAQKGNYRFMKLLLTRRANWM 108
Cdd:PHA03095   67 RLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVN 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 109 QKDLEEMTPLH--LSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKL--LIKHDSNIGIPDVEGKI 184
Cdd:PHA03095  147 ALDLYGMTPLAvlLKSRNANVELLRLLID--AGADVYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNT 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 185 PLHWAANHKDASAVHTVRCILDAAPteslLNWQDYEGRTPLHFAVADGNLTVVDVLTSY-ESCNITSYDNlfRTPLHWAA 263
Cdd:PHA03095  225 PLHSMATGSSCKRSLVLPLLIAGIS----INARNRYGQTPLHYAAVFNNPRACRRLIALgADINAVSSDG--NTPLSLMV 298

                         250
                  ....*....|....*
gi 1958776210 264 LLGHAQIVHLLLERN 278
Cdd:PHA03095  299 RNNNGRAVRAALAKN 313
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 59-438 3.32e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 85.50  E-value: 3.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  59 DRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfma 138
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID--- 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 139 pgevDTQDKNKQTALHWSAYYNNPEHAKLLIkHDSNIGIP--DVEGKIPLHWAANHKDASavhtvRCILDAAPTESLLNW 216
Cdd:PHA02876  233 ----NRSNINKNDLSLLKAIRNEDLETSLLL-YDAGFSVNsiDDCKNTPLHHASQAPSLS-----RLVPKLLERGADVNA 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 217 QDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLFRTPLHWAALLG-HAQIVHLLLERNkSGTVPSDSQGATPLHY 295
Cdd:PHA02876  303 KNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELG-ANVNARDYCDKTPIHY 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 296 AAQSNFAV----LHYHGPDVPhhcAVSNKVFLQETVKVFLTHPsvrddsdlegrtsfmwaagkgsddvlrtMLSLKSDID 371
Cdd:PHA02876  382 AAVRNNVViintLLDYGADIE---ALSQKIGTALHFALCGTNP----------------------------YMSVKTLID 430

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 372 ----INMADKYGGTALHAAALSG-HVSTVKLLLDNDAQVDATDVMKHTPLFRAceMGHRDVIQTLIKGGARV 438
Cdd:PHA02876  431 rganVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
482-570 3.60e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 482 LQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFpnqmENNEERYTPLDYALLGERHEV 561
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEI 76


                  ....*....
gi 1958776210 562 IQFMLEHGA 570
Cdd:pfam12796  77 VKLLLEKGA 85
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 214-570 1.30e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.57  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 214 LNWQDYEGRTPLHFAVADGNLTVVDVLTSYES-CNITSYDNLfrTPLHWAALLGHAQIVHLLLErNKSGTVPSDSQGATP 292
Cdd:PHA02876  171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdVNIIALDDL--SVLECAVDSKNIDTIKAIID-NRSNINKNDLSLLKA 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 293 LHYAAQSNFAVLHYHGPDV---------PHHCAVSNKVfLQETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSD-DVLRT 362
Cdd:PHA02876  248 IRNEDLETSLLLYDAGFSVnsiddckntPLHHASQAPS-LSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 363 MLSLKSDIdiNMADKYGGTALH-AAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLV 441
Cdd:PHA02876  327 LIMLGADV--NAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 442 DQDGHSLLHWAALGGNAdvcqilienkinpnvqdyagrtplqcaayggYINcMAVLMENNADPNIQDKEGRTALHWSC-N 520
Cdd:PHA02876  405 SQKIGTALHFALCGTNP-------------------------------YMS-VKTLIDRGANVNSKNKDLSTPLHYACkK 452

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958776210 521 NGYLDAIKLLLDFAAFPNQMeNNEERYtPLDYALlgERHEVIQFMLEHGA 570
Cdd:PHA02876  453 NCKLDVIEMLLDNGADVNAI-NIQNQY-PLLIAL--EYHGIVNILLHYGA 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-179 1.49e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  85 LHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDtqdkNKQTALHWSAYYNNPEH 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1958776210 165 AKLLIKHDSNIGIPD 179
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 32-263 3.38e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.61  E-value: 3.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  32 RLIVGNSALKDKEDQFGRTPLMYCV---LADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGN-YRFMKLLLTRRANW 107
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 108 MQKDLEEMTPLH--LSTRHRSPKCLALLLKFMApgEVDTQDKNKQTALHwsAYYN----NPEHAKLLIKHDSNIGIPDVE 181
Cdd:PHA03095  111 NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGA--DVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 182 GKIPLHWAAN--HKDASAVHT-VRCILDAAPTESLlnwqdyeGRTPLHFAVADG---NLTVVDVLTSYESCNITsyDNLF 255
Cdd:PHA03095  187 FRSLLHHHLQsfKPRARIVRElIRAGCDPAATDML-------GNTPLHSMATGSsckRSLVLPLLIAGISINAR--NRYG 257


                  ....*...
gi 1958776210 256 RTPLHWAA 263
Cdd:PHA03095  258 QTPLHYAA 265
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-443 8.97e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 8.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 120 LSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKdasavh 199
Cdd:PHA03100    6 VLTKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIK------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 200 tvrcildaaptesllnwqdyegrtplhfAVADGNLTVVDVLTSYEScNITSYDNLFRTPLHWAA--LLGHAQIVHLLLER 277
Cdd:PHA03100   80 ----------------------------YNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAIskKSNSYSIVEYLLDN 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 278 NKSgTVPSDSQGATPLHYAAQSNfavlhyhgpdvphhcavSNKVflqETVKVFLTHpsvrdDSDLEGRTSFmwaagkgsd 357
Cdd:PHA03100  131 GAN-VNIKNSDGENLLHLYLESN-----------------KIDL---KILKLLIDK-----GVDINAKNRV--------- 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 358 DVLrtmlsLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGAR 437
Cdd:PHA03100  176 NYL-----LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                  ....*.
gi 1958776210 438 VDLVDQ 443
Cdd:PHA03100  251 IKTIIE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
 358-517 9.71e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 9.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 358 DVLRTMLSLKSDIdiNMADKYGGTALHAAaLSG---HVSTVKLLLDNDAQVDATDVMKHTPL-----FRACEMghrDVIQ 429
Cdd:PHA03095   98 DVIKLLIKAGADV--NAKDKVGRTPLHVY-LSGfniNPKVIRLLLRKGADVNALDLYGMTPLavllkSRNANV---ELLR 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 430 TLIKGGARVDLVDQDGHSLLHWAALG--GNADVCQILIENKINPNVQDYAGRTPLQCAAYGGyiNCMAVLM----ENNAD 503
Cdd:PHA03095  172 LLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS--SCKRSLVlpllIAGIS 249

                         170
                  ....*....|....
gi 1958776210 504 PNIQDKEGRTALHW 517
Cdd:PHA03095  250 INARNRYGQTPLHY 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 392-570 1.68e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 392 VSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAA-----LGGNADVCQILIE 466
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 467 NKINPNVQDYAGRTPLQCAAYG--GYINCMAVLMENNADPNIQDKEGRTALHW--SCNNGYLDAIKLLLDFAAFPNQMEN 542
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDKGVDINAKNR 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958776210 543 --------------NEERYTPLDYALLGERHEVIQFMLEHGA 570
Cdd:PHA03100  175 vnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGA 216
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 383-551 1.97e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 383 LHAAALSGHVSTVKLLLDNDAQVDatDVM---KHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNAD 459
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFAD--DVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 460 VCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGR-TALHWSCNNGYLDAIKLLLDFAAFPN 538
Cdd:PHA02875  150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229

                         170
                  ....*....|....
gi 1958776210 539 QMENNE-ERYTPLD 551
Cdd:PHA02875  230 IMFMIEgEECTILD 243
PHA03095 PHA03095
ankyrin-like protein; Provisional
 366-570 4.28e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 366 LKSDIDINMADKYGGTALHAAALSGH---VSTVKLLLDNDAQVDATDVMKHTPLFraCEMGH---RDVIQTLIKGGARVD 439
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLH--LYLYNattLDVIKLLIKAGADVN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 440 LVDQDGHSLLHwAALGG---NADVCQILIENKINPNVQDYAGRTPLqcAAYGGYINC----MAVLMENNADPNIQDKEGR 512
Cdd:PHA03095  112 AKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDRFR 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 513 TALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGE--RHEVIQFMLEHGA 570
Cdd:PHA03095  189 SLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGI 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 257-554 5.22e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 257 TPLHWAALLGHAQIVHLLLernKSGtvpsdsqgatplhyaaqsnfAVLHYHGPDVPHHCAVSNKVFLQETVKVFLTH--- 333
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFI---KHG--------------------ADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvd 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 334 PSVRDDSDLEgrtsfmwaagkgsDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKH 413
Cdd:PHA02874   94 TSILPIPCIE-------------KDMIKTIL--DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 414 TPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYggYINC 493
Cdd:PHA02874  159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRS 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 494 MAVLMENNADPNIQDKEGRTALHWSCNNG-YLDAIKLLLDFAAFPNQMENNEEryTPLDYAL 554
Cdd:PHA02874  237 AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGE--NPIDTAF 296
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 372-579 7.71e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 7.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 372 INMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMG-----------------------HRDVI 428
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGahdiikllidngvdtsilpipciEKDMI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 429 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 508
Cdd:PHA02874  108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776210 509 KEGRTALHWSCNNGYLDAIKLLLDFAAfpNQMENNEERYTPLDYALLGERhEVIQFMLEHGALSiaaIQDI 579
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGFTPLHNAIIHNR-SAIELLINNASIN---DQDI 252
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 211-470 1.18e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 211 ESLLNWQDYEGRTPLHFAVADGNLTVVDVLTsYESCNITSYDNLFRTPLHWAALLGHAQ-----IVHLLLERNKSGTVPs 285
Cdd:PHA03100   25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAP- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 286 DSQGATPLHYAAqsnfavlhyhgpdvphhcavSNKVFLQETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDD--VLRTM 363
Cdd:PHA03100  103 DNNGITPLLYAI--------------------SKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 364 LslKSDIDINMADKyggtalhaaalsghvstVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQ 443
Cdd:PHA03100  163 I--DKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223

                         250       260
                  ....*....|....*....|....*..
gi 1958776210 444 DGHSLLHWAALGGNADVCQILIENKIN 470
Cdd:PHA03100  224 YGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-146 1.79e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  52 LMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQkdLEEMTPLHLSTRHRSPKCLA 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....*
gi 1958776210 132 LLLKFMApgEVDTQD 146
Cdd:pfam12796  79 LLLEKGA--DINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-111 2.65e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  19 HAAAVNGDKGALQRLIVGNSAlKDKEDQFGRTPLMYCVLADRLDCADALLKaGADVNKTDHsRRTALHLAAQKGNYRFMK 98
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958776210  99 LLLTRRANWMQKD 111
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 252-531 2.83e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 252 DNLFRTPLHwaaLLGH------AQIVHLLLERNKSGTVPsDSQGATPLHYAAQSN-----FAVLHYHGPDVPHHCAVSNK 320
Cdd:PHA03095   44 GEYGKTPLH---LYLHyssekvKDIVRLLLEAGADVNAP-ERCGFTPLHLYLYNAttldvIKLLIKAGADVNAKDKVGRT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 321 VfLQetvkVFLTHPSVRDDsdlegrtsfmwaagkgsddVLRTMLSLKsdIDINMADKYGGTALHAAALSGHVS--TVKLL 398
Cdd:PHA03095  120 P-LH----VYLSGFNINPK-------------------VIRLLLRKG--ADVNALDLYGMTPLAVLLKSRNANveLLRLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 399 LDNDAQVDATDVMKHTPL------FRACEmghrDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQI--LIENKIN 470
Cdd:PHA03095  174 IDAGADVYAVDDRFRSLLhhhlqsFKPRA----RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGIS 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776210 471 PNVQDYAGRTPLQCAAYggYINCMAV--LMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 531
Cdd:PHA03095  250 INARNRYGQTPLHYAAV--FNNPRACrrLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
313-409 6.55e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 6.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 313 HHCAVSNKVflqETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSLksdIDINMADkYGGTALHAAALSGHV 392
Cdd:pfam12796   2 HLAAKNGNL---ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1958776210 393 STVKLLLDNDAQVDATD 409
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-201 8.72e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 8.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  17 QVHAAAVNGDKGALQRLIVGNSALKDKeDQFGRTPLMycVLADRLDCADALLK----AGADVNKTDHSRRTALHLAAQ-- 90
Cdd:PHA03095  122 HVYLSGFNINPKVIRLLLRKGADVNAL-DLYGMTPLA--VLLKSRNANVELLRllidAGADVYAVDDRFRSLLHHHLQsf 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  91 KGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLaLLLKFMAPG-EVDTQDKNKQTALHWSAYYNNPEHAKLLI 169
Cdd:PHA03095  199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRS-LVLPLLIAGiSINARNRYGQTPLHYAAVFNNPRACRRLI 277

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958776210 170 KHDSNIGIPDVEGKIPLHWAANHKDASAVHTV 201
Cdd:PHA03095  278 ALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 215-473 9.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 9.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 215 NWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLfRTPLHWAALLGHAQIVHLLLERNKSGTVPSDSQGATPLH 294
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLH 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 295 YAaqsnfavlhyhgpdvphhcAVSNKVflqetvkvflthpsvrddsdlegrtsfmwaagkgsdDVLRTMLSLKSDIDINM 374
Cdd:PHA02875  108 LA-------------------TILKKL------------------------------------DIMKLLIARGADPDIPN 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 375 ADKYggTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGH-SLLHWAA 453
Cdd:PHA02875  133 TDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAI 210

                         250       260
                  ....*....|....*....|
gi 1958776210 454 LGGNADVCQILIENKINPNV 473
Cdd:PHA02875  211 ENNKIDIVRLFIKRGADCNI 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-252 3.37e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 153 LHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDasaVHTVRCILDAAPTESllnwqDYEGRTPLHFAVADG 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH---LEIVKLLLEHADVNL-----KDNGRTALHYAARSG 72

                          90       100
                  ....*....|....*....|
gi 1958776210 233 NLTVVDVLTSYEsCNITSYD 252
Cdd:pfam12796  73 HLEIVKLLLEKG-ADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 395-555 3.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 395 VKLLLDNDAQVDATDVMK-HTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNV 473
Cdd:PHA02878  150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 474 QDYAGRTPLQCA-AYGGYINCMAVLMENNADPNIQDK-EGRTALHWSCNNGylDAIKLLLDFAAFPNQMenNEERYTPLD 551
Cdd:PHA02878  230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSL--NSYKLTPLS 305


                  ....
gi 1958776210 552 YALL 555
Cdd:PHA02878  306 SAVK 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-278 6.73e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 6.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 186 LHWAANHKDASAVHT-VRCILDAaptesllNWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDnlfRTPLHWAAL 264
Cdd:pfam12796   1 LHLAAKNGNLELVKLlLENGADA-------NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG---RTALHYAAR 70

                          90
                  ....*....|....
gi 1958776210 265 LGHAQIVHLLLERN 278
Cdd:pfam12796  71 SGHLEIVKLLLEKG 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 325-520 1.91e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 325 ETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDIDiNMADKYGGTALHAAALSGHVSTVKLLLDNDAQ 404
Cdd:PHA02875   49 EAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 405 VDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNvqdYAGRTP--- 481
Cdd:PHA02875  128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGcva 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958776210 482 LQCAAY-GGYINCMAVLMENNADPNIQ---DKEGRTALHWSCN 520
Cdd:PHA02875  205 ALCYAIeNNKIDIVRLFIKRGADCNIMfmiEGEECTILDMICN 247
Ank_2 pfam12796
Ankyrin repeats (3 copies);
225-300 2.48e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 2.48e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776210 225 LHFAVADGNLTVVDVLTSYEsCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGtvpSDSQGATPLHYAAQSN 300
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSG 72
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-229 4.28e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  67 LLKAGADVNKTD-HSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMApgEVDTQ 145
Cdd:PHA02878  153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA--STDAR 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 146 DKNKQTALHWS-AYYNNPEHAKLLIKHDSNIGIPD-VEGKIPLHWAANHKDasavhTVRCILDAAPTESLLNWqdyEGRT 223
Cdd:PHA02878  231 DKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER-----KLKLLLEYGADINSLNS---YKLT 302


                  ....*.
gi 1958776210 224 PLHFAV 229
Cdd:PHA02878  303 PLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 49-212 6.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 6.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  49 RTPLMYC-----VLADRLDCADALLKAGADVNKTDHSRRTALHLAAQK--GNYRFMKLLLTRRANWMQKDLEEMTPLHLS 121
Cdd:PHA03100   69 STPLHYLsnikyNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 122 TRHRSPKC------------------LALLLKFMAPgeVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGK 183
Cdd:PHA03100  149 LESNKIDLkilkllidkgvdinaknrVNYLLSYGVP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958776210 184 IPLHWAA--NHKDasavhTVRCILDAAPTES 212
Cdd:PHA03100  227 TPLHIAIlnNNKE-----IFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 224-515 7.57e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 7.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 224 PLHFAVADGNLTVVDVLTSyESCNITSYDNLFRTPLHWAALLGHAQ-IVHLLLERNKSGtvpsdsqgatpLHYAAQSNFA 302
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLT-RGHNVNQPDHRDLTPLHIICKEPNKLgMKEMIRSINKCS-----------VFYTLVAIKD 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 303 VLHYHgpDVphhcavsnkvflqETVKVFLT--HPSVRDDSDLEGRTsfmwaagKGSDDVLRTM---LSLKSDIDINMADK 377
Cdd:PHA02878  108 AFNNR--NV-------------EIFKIILTnrYKNIQTIDLVYIDK-------KSKDDIIEAEitkLLLSYGADINMKDR 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 378 YGG-TALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWA-ALG 455
Cdd:PHA02878  166 HKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYC 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776210 456 GNADVCQILIENKINPNVQDYA-GRTPLQCAAYGGYIncMAVLMENNADPNIQDKEGRTAL 515
Cdd:PHA02878  246 KDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304
PHA02798 PHA02798
ankyrin-like protein; Provisional
 392-551 9.16e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 64.47  E-value: 9.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 392 VSTVKLLLdndAQVDATDVMKHTPLFRacEMGHR-----DVIQTLIKGGARVDLVDQDGHS-----LLHWAALGGNADVC 461
Cdd:PHA02798   18 LSTVKLLI---KSCNPNEIVNEYSIFQ--KYLQRdspstDIVKLFINLGANVNGLDNEYSTplctiLSNIKDYKHMLDIV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 462 QILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVL---MENNADPNIQDKEGRTALH---WSCNNGYLDAIKLLLDFAA 535
Cdd:PHA02798   93 KILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmIENGADTTLLDKDGFTMLQvylQSNHHIDIEIIKLLLEKGV 172

                         170
                  ....*....|....*.
gi 1958776210 536 FPNQMeNNEERYTPLD 551
Cdd:PHA02798  173 DINTH-NNKEKYDTLH 187
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 16-175 2.16e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  16 SQVHAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYR 95
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  96 FMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMApgEVDTQDKNKQTALHWSAYYNN-PEHAKLLIKH--D 172
Cdd:PHA02875  150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA--NIDYFGKNGCVAALCYAIENNkIDIVRLFIKRgaD 227


                  ...
gi 1958776210 173 SNI 175
Cdd:PHA02875  228 CNI 230
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 312-503 6.29e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 6.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 312 PHHCAVSNKVFLQETVKVF------LTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDIDInmADKYGGTALHA 385
Cdd:PLN03192  487 QEDNVVILKNFLQHHKELHdlnvgdLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDI--GDSKGRTPLHI 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 386 AALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDlvDQDGHSLLHWAALGGNADVCQILI 465
Cdd:PLN03192  565 AASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELL 642

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958776210 466 ENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNAD 503
Cdd:PLN03192  643 KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 61-388 1.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  61 LDCADALLKAGADVNKTDHSRRTA-------LHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHrsPKCLAll 133
Cdd:PHA02878   10 TDNYETILKYIEYIDHTENYSTSAslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKE--PNKLG-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 134 LKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLI--KHDSNIGIPDVEGKiplhwAANHKDASAVHTVRCILDAAPTE 211
Cdd:PHA02878   86 MKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILtnRYKNIQTIDLVYID-----KKSKDDIIEAEITKLLLSYGADI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 212 SLLNwqDYEGRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLLeRNKSGTVPSDSQGAT 291
Cdd:PHA02878  161 NMKD--RHKGNTALHYATENKDQRLTELLLSY-GANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 292 PLHYAAQSnfaVLHYhgpdvphhcavsnkvflqETVKVFLTH-PSVRDDSDLEGRTSFMWAAgkGSDDVLRTMLSLKSdi 370
Cdd:PHA02878  237 PLHISVGY---CKDY------------------DILKLLLEHgVDVNAKSYILGLTALHSSI--KSERKLKLLLEYGA-- 291

                         330
                  ....*....|....*...
gi 1958776210 371 DINMADKYGGTALHAAAL 388
Cdd:PHA02878  292 DINSLNSYKLTPLSSAVK 309
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 448-531 2.03e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 448 LLHWAAlGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAI 527
Cdd:PTZ00322   86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ....
gi 1958776210 528 KLLL 531
Cdd:PTZ00322  165 QLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 496-568 2.46e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 2.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776210 496 VLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQFMLEH 568
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK--TPLELAEENGFREVVQLLSRH 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 34-280 2.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.68  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  34 IVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQ-----KGNYRFMKLLLTRRANWM 108
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 109 QKDLEEMTPLH--LSTRHRSPKCLALLLKFMApgevDTQDKNK--QTALHWSAYYNNPEH--AKLLIKHDSNIgipdveg 182
Cdd:PHA03100  101 APDNNGITPLLyaISKKSNSYSIVEYLLDNGA----NVNIKNSdgENLLHLYLESNKIDLkiLKLLIDKGVDI------- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 183 kiplhwaaNHKDasavhTVRCILDAApteSLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWA 262
Cdd:PHA03100  170 --------NAKN-----RVNYLLSYG---VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIA 232

                         250
                  ....*....|....*...
gi 1958776210 263 ALLGHAQIVHLLLERNKS 280
Cdd:PHA03100  233 ILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 382-570 3.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 382 ALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNA-DV 460
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVkAV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 461 CQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNqM 540
Cdd:PHA02875   85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD-I 163

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958776210 541 ENNEErYTPLDYALLGERHEVIQFMLEHGA 570
Cdd:PHA02875  164 EDCCG-CTPLIIAMAKGDIAICKMLLDSGA 192
Ank_4 pfam13637
Ankyrin repeats (many copies);
445-497 5.94e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.94e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958776210 445 GHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVL 497
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 166-294 6.57e-09

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: 58.87  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 166 KLLIKHDSNIGIPDVEGKIPLHWAA--NHKDASAVhtvrcILDAAPTesLLNW----QDYEGRTPLHFAVADGNLTVVDV 239
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAAlyDNLEAAVV-----LMEAAPE--LVNEpmtsDLYQGETALHIAVVNQNLNLVRE 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776210 240 LTSYESCNIT----------SYDNLF---RTPLHWAALLGHAQIVHLLLERNKSgTVPSDSQGATPLH 294
Cdd:cd22192   108 LIARGADVVSpratgtffrpGPKNLIyygEHPLSFAACVGNEEIVRLLIEHGAD-IRAQDSLGNTVLH 174
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-248 8.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 8.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  48 GRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTrrANWMQKDL---EEMTPLHLSTRH 124
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--LGKFADDVfykDGMTPLHLATIL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 125 RSPKCLALLLKFMAPGEVDTQDKNkqTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDasaVHTVRCI 204
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD---IAICKML 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958776210 205 LDAAPTesllnwQDYEGRTP----LHFAVADGNLTVVDVLTSYES-CNI 248
Cdd:PHA02875  188 LDSGAN------IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAdCNI 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
379-432 8.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 8.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776210 379 GGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLI 432
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 357-580 1.03e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 357 DDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGA 436
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 437 RV---DL--------VDQDGHSLLHWAALGGNA-DVCQ------------------ILIENKINPNVQDYAGRTPLQCAA 486
Cdd:PHA02876  236 NInknDLsllkairnEDLETSLLLYDAGFSVNSiDDCKntplhhasqapslsrlvpKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 487 YGGY-INCMAVLMENNADPNIQDKEGRTALHWSCN-NGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQF 564
Cdd:PHA02876  316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDK--TPIHYAAVRNNVVIINT 393

                         250
                  ....*....|....*.
gi 1958776210 565 MLEHGALSIAAIQDIA 580
Cdd:PHA02876  394 LLDYGADIEALSQKIG 409
Ank_4 pfam13637
Ankyrin repeats (many copies);
48-101 1.45e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776210  48 GRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLL 101
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
478-531 1.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776210 478 GRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 531
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-189 2.01e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 2.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  18 VHAAAVNGDKGALQRLIVGNSALKDKEDQfGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFM 97
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  98 KLLLTRRANWMQKDLEEMTPLHLSTRH-RSpkCLALLLKfmaPGEVDTQDKNKQTALHWSAYYN-NPEHAKLLIKHDSNI 175
Cdd:PHA02874  207 KLLIDHGNHIMNKCKNGFTPLHNAIIHnRS--AIELLIN---NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281

                         170
                  ....*....|....
gi 1958776210 176 GIPDVEGKIPLHWA 189
Cdd:PHA02874  282 SIKDNKGENPIDTA 295
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 452-538 5.51e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 5.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 452 AALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 531
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611


                  ....*..
gi 1958776210 532 DFAAFPN 538
Cdd:PLN03192  612 HFASISD 618
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 191-499 8.68e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 8.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 191 NHKDASAVHTVRCILDAAPTESLLNWQ------DYEGRTPLHFAVADGnltvvdvltsYESCNITsydnlfrtplhwaaL 264
Cdd:PLN03192  522 DPNMASNLLTVASTGNAALLEELLKAKldpdigDSKGRTPLHIAASKG----------YEDCVLV--------------L 577

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 265 LGHAQIVHLllernksgtvpSDSQGATPLHYAAQSNfavlHYHGPDVPHHCAVsnkvflqetvkvfLTHPSVRDDSdleg 344
Cdd:PLN03192  578 LKHACNVHI-----------RDANGNTALWNAISAK----HHKIFRILYHFAS-------------ISDPHAAGDL---- 625

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 345 rtsFMWAAGKGSDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDAT---DVMKHTPLFRAC- 420
Cdd:PLN03192  626 ---LCTAAKRNDLTAMKELL--KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAntdDDFSPTELRELLq 700

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 421 --EMGHRDVIqtlikggarVDLVDQDgHSLLHWAALGGNADVCQILIENKINPNVQDYAG----RTPLQCAAYGGYINCM 494
Cdd:PLN03192  701 krELGHSITI---------VDSVPAD-EPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGhpllRNERCCNEAGKLINLP 770


                  ....*
gi 1958776210 495 AVLME 499
Cdd:PLN03192  771 PSLEE 775
Ank_4 pfam13637
Ankyrin repeats (many copies);
344-399 8.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 8.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776210 344 GRTSFMWAAGKGSDDVLRTMLSLKsdIDINMADKYGGTALHAAALSGHVSTVKLLL 399
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG--ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-433 2.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  24 NGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTr 103
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 104 raNWMQKDLEEMTPLHLSTRHRSPKCLAlllkfmapgEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGK 183
Cdd:PHA02874   90 --NGVDTSILPIPCIEKDMIKTILDCGI---------DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 184 IPLHWAANHkdaSAVHTVRCILDAApteSLLNWQDYEGRTplhfavadgnltvvdvltsyescnitsydnlfrtPLHWAA 263
Cdd:PHA02874  159 YPIHIAIKH---NFFDIIKLLLEKG---AYANVKDNNGES----------------------------------PLHNAA 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 264 LLGHAQIVHLLLErNKSGTVPSDSQGATPLHYAAQSNFAVlhyhgpdvphhcavsnkvflqetVKVFLTHPSVrDDSDLE 343
Cdd:PHA02874  199 EYGDYACIKLLID-HGNHIMNKCKNGFTPLHNAIIHNRSA-----------------------IELLINNASI-NDQDID 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 344 GRTSFMWAAGKGSD-DVLRTMLSLKSDIDINmaDKYGGTALHAA-ALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACE 421
Cdd:PHA02874  254 GSTPLHHAINPPCDiDIIDILLYHKADISIK--DNKGENPIDTAfKYINKDPVIKDIIANAVLIKEADKLKDSDFLEHIE 331

                         410
                  ....*....|..
gi 1958776210 422 MGHRDVIQTLIK 433
Cdd:PHA02874  332 IKDNKEFSDFIK 343
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 356-433 4.66e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 4.66e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776210 356 SDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIK 433
Cdd:PTZ00322   92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 387-464 8.30e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 8.30e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776210 387 ALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQIL 464
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
414-465 1.20e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 414 TPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILI 465
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 21-236 2.57e-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: 50.40  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  21 AAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGAD-VNKTDHSR----RTALHLAAQKGNYR 95
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAVVNQNLN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  96 FMKLLLTRRAnwmqkdlEEMTPLHLSTR-HRSPKClalLLKFmapGEvdtqdknkqTALHWSAYYNNPEHAKLLIKHDSN 174
Cdd:cd22192   104 LVRELIARGA-------DVVSPRATGTFfRPGPKN---LIYY---GE---------HPLSFAACVGNEEIVRLLIEHGAD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776210 175 IGIPDVEGKIPLH---WAANHKDASAVHTVRCILDA----APTESLLNwqdYEGRTPLHFAVADGNLTV 236
Cdd:cd22192   162 IRAQDSLGNTVLHilvLQPNKTFACQMYDLILSYDKeddlQPLDLVPN---NQGLTPFKLAAKEGNIVM 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 309-570 6.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 6.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 309 PDVPHHCAVSNKVFlqETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHaaal 388
Cdd:PHA02878   37 PFIPLHQAVEARNL--DVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFN---- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 389 SGHVSTVKLLLdndaqVDATDVMKHTPLFRACEMGHRDVIQT-----LIKGGARVDLVDQD-GHSLLHWAALGGNADVCQ 462
Cdd:PHA02878  111 NRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKDDIIEAeitklLLSYGADINMKDRHkGNTALHYATENKDQRLTE 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 463 ILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCnnGYLdaikllldfaafpnqmen 542
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYC------------------ 245

                         250       260
                  ....*....|....*....|....*...
gi 1958776210 543 neerytpLDYallgerhEVIQFMLEHGA 570
Cdd:PHA02878  246 -------KDY-------DILKLLLEHGV 259
Ank_5 pfam13857
Ankyrin repeats (many copies);
464-516 9.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 9.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776210 464 LIENK-INPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALH 516
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 239-301 9.87e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 9.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776210 239 VLTSYESCNITSYDNlfRTPLHWAALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYAAQSNF 301
Cdd:PTZ00322  101 LLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGF 160
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 40-204 1.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  40 LKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLH 119
Cdd:PHA02878  160 INMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 120 LST-RHRSPKCLALLLKFMAPGEVDTQDKNkQTALHWSayYNNPEHAKLLIKHDSNIGIPDVEGKIPLhwaanhkdASAV 198
Cdd:PHA02878  240 ISVgYCKDYDILKLLLEHGVDVNAKSYILG-LTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPL--------SSAV 308


                  ....*.
gi 1958776210 199 HTVRCI 204
Cdd:PHA02878  309 KQYLCI 314
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 372-519 1.45e-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: 48.09  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 372 INMA---DKYGG-TALHAAALSGHVSTVKLLLDNDAQV---DATDVM------------KHTPLFRACeMGHRDVIQTLI 432
Cdd:cd22192    78 VNEPmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVvspRATGTFfrpgpknliyygEHPLSFAAC-VGNEEIVRLLI 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 433 KGGArvDLVDQD--GHSLLHWAALGGNAD-VCQI--LI---ENKINP----NVQDYAGRTPLQCAAYGGYINCMAVLMEN 500
Cdd:cd22192   157 EHGA--DIRAQDslGNTVLHILVLQPNKTfACQMydLIlsyDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234

                         170
                  ....*....|....*....
gi 1958776210 501 nadpniqdkegRTALHWSC 519
Cdd:cd22192   235 -----------RRHIQWTY 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 222-422 1.50e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 222 RTPLHFAVADGNLTVVDVLTSYEscniTSYDNLF----RTPLHWAALLGHAQIVHLLLERNKSGTVPSDSQgATPLHYAA 297
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLG----KFADDVFykdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPLHLAV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 298 QSNfavlhyhgpDVphhcavsnkvflqETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSlkSDIDINMADK 377
Cdd:PHA02875  144 MMG---------DI-------------KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD--SGANIDYFGK 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958776210 378 YGGTALHAAALSGH-VSTVKLLLDNDAQVD-ATDVM--KHTPLFRACEM 422
Cdd:PHA02875  200 NGCVAALCYAIENNkIDIVRLFIKRGADCNiMFMIEgeECTILDMICNM 248
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 351-482 1.94e-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: 47.70  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 351 AAGKGSDDVLRTMLsLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDND---AQVDATDVM--KHTPLFRACEMGHR 425
Cdd:cd22192    24 AAKENDVQAIKKLL-KCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLyqGETALHIAVVNQNL 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776210 426 DVIQTLIKGGARVDLVDQDG-------HSLLHW-------AALGGNADVCQILIENKINPNVQDYAGRTPL 482
Cdd:cd22192   103 NLVRELIARGADVVSPRATGtffrpgpKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 428-498 2.14e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 2.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776210 428 IQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLM 498
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
434-485 2.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 434 GGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCA 485
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
501-553 3.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958776210 501 NADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYA 553
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN--LKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-120 3.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958776210  67 LLKAG-ADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHL 120
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 411-570 4.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 411 MKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGY 490
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 491 INCMAVLMENNADPN-IQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQmeNNEERYTPLDYALLGERHEVIQFMLEHG 569
Cdd:PHA02875   81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI--PNTDKFSPLHLAVMMGDIKGIELLIDHK 158


                  .
gi 1958776210 570 A 570
Cdd:PHA02875  159 A 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
511-566 4.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 4.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776210 511 GRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFML 566
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
221-275 5.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 5.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958776210 221 GRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLL 275
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-153 5.18e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  13 SLASQVHAAAVNGDKgALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQK- 91
Cdd:PHA02878  167 KGNTALHYATENKDQ-RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYc 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776210  92 GNYRFMKLLLTRRANW-MQKDLEEMTPLHLSTrhRSPKCLALLLKFMApgEVDTQDKNKQTAL 153
Cdd:PHA02878  246 KDYDILKLLLEHGVDVnAKSYILGLTALHSSI--KSERKLKLLLEYGA--DINSLNSYKLTPL 304
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 215-275 6.20e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 6.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776210 215 NWQDYEGRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLL 275
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-134 1.08e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776210  81 RRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLL 134
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
139-189 1.67e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958776210 139 PGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWA 189
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 575-601 1.97e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.97e-04
                          10        20
                  ....*....|....*....|....*..
gi 1958776210 575 AIQDIAAFKIQAVYKGYKVRKAFRDRK 601
Cdd:cd23767     6 QRMNRAATLIQALWRGYKVRKELKKKK 32
Ank_2 pfam12796
Ankyrin repeats (3 copies);
515-571 2.78e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 2.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776210 515 LHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQFMLEHGAL 571
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR--TALHLAAKNGHLEIVKLLLEHADV 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
256-306 2.78e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958776210 256 RTPLHWAALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYAAQ-SNFAVLHY 306
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASnGNVEVLKL 52
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 150-294 4.21e-04

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: 43.53  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 150 QTALHWSAYYNNP-EHAKLLIKHDSNIgipdVEGKIPLHWAA-NHKDAsaVHTVRCILDAAPTES----LLNWQD----Y 219
Cdd:TIGR00870  53 RSALFVAAIENENlELTELLLNLSCRG----AVGDTLLHAISlEYVDA--VEAILLHLLAAFRKSgpleLANDQYtsefT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 220 EGRTPLHFAVADGNLTVVDVL------TSYES----CNITSYDNLF---RTPLHWAALLGHAQIVHLLLErNKSGTVPSD 286
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLlergasVPARAcgdfFVKSQGVDSFyhgESPLNAAACLGSPSIVALLSE-DPADILTAD 205


                  ....*...
gi 1958776210 287 SQGATPLH 294
Cdd:TIGR00870 206 SLGNTLLH 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 378-409 8.92e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 8.92e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958776210 378 YGGTALHAAALS-GHVSTVKLLLDNDAQVDATD 409
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-76 1.29e-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: 36.41  E-value: 1.29e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958776210   48 GRTPLMYCVLADRLDCADALLKAGADVNK 76
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-79 1.46e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.46e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958776210  48 GRTPLMYCVL-ADRLDCADALLKAGADVNKTDH 79
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
33-88 1.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776210  33 LIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLA 88
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-106 1.92e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776210  30 LQRLIVGNSALkDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRAN 106
Cdd:PHA03095  240 VLPLLIAGISI-NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPS 315
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 55-135 2.38e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  55 CVLADRLDCADA--LLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLAL 132
Cdd:PTZ00322   87 CQLAASGDAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 1958776210 133 LLK 135
Cdd:PTZ00322  167 LSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
243-296 2.73e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 2.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958776210 243 YESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYA 296
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 444-473 2.75e-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: 2.75e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958776210  444 DGHSLLHWAALGGNADVCQILIENKINPNV 473
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 321-512 2.94e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.56  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 321 VFLQETVKvFLTHPSVRDDSDleGRTSFMWAA---GKGSDDVLRTML-------SLKSDIDINMADKY--GGTALHAAAL 388
Cdd:cd22196    27 EYLMRTKK-RLTDSEFKDPET--GKTCLLKAMlnlHNGQNDTISLLLdiaektgNLKEFVNAAYTDSYykGQTALHIAIE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 389 SGHVSTVKLLLDNDAQVDAT---DVMKHT-----------PLFRACEMGHRDVIQTLIKG---GARVDLVDQDGHSLLHw 451
Cdd:cd22196   104 RRNMHLVELLVQNGADVHARasgEFFKKKkggpgfyfgelPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLH- 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776210 452 aALGGNADVCQ------------ILIE-NKINPNVQ-----DYAGRTPLQCAAYGGYINCMAVLMENnadpNIQDKEGR 512
Cdd:cd22196   183 -ALVEVADNTPentkfvtkmyneILILgAKIRPLLKleeitNKKGLTPLKLAAKTGKIGIFAYILGR----EIKEPECR 256
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 209-388 2.97e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 209 PTESLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLfrtpLHwAALLGHAQIV-----HLLLERNKSGTV 283
Cdd:TIGR00870  40 PKKLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGDTL----LH-AISLEYVDAVeaillHLLAAFRKSGPL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 284 P--------SDSQGATPLHYAAQ-SNFAVLHY---HGPDVPHHCavsnkvflqeTVKVFLTHPSVrdDSDLEGRTSFMWA 351
Cdd:TIGR00870 115 ElandqytsEFTPGITALHLAAHrQNYEIVKLlleRGASVPARA----------CGDFFVKSQGV--DSFYHGESPLNAA 182

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958776210 352 AGKGSDDVLRtmLSLKSDIDINMADKYGGTALHAAAL 388
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADILTADSLGNTLLHLLVM 217
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 358-519 3.41e-03

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: 40.63  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 358 DVLRTMLSLKSDIDINMADKY--GGTALHAAALSGHVSTVKLLLDNDAQVDAT---DVMKHTPL-----------FRACe 421
Cdd:cd21882    50 EAAPDSGNPKELVNAPCTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPGnlfyfgelplsLAAC- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 422 MGHRDVIQTLIKGGARV-DLVDQD--GHSLLHWAALGGN------ADVCQ-----ILIENKINPNVQ-----DYAGRTPL 482
Cdd:cd21882   129 TNQEEIVRLLLENGAQPaALEAQDslGNTVLHALVLQADntpensAFVCQmynllLSYGAHLDPTQQleeipNHQGLTPL 208

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958776210 483 QCAAYGGYINCMAVLMENNADPNIQDKEgRTALHWSC 519
Cdd:cd21882   209 KLAAVEGKIVMFQHILQREFSGPYQPLS-RKFTEWTY 244
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 50-123 3.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 3.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776210  50 TPLMYCVLADRLDCADALLKAGADVNK-TDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTR 123
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 427-603 3.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 427 VIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNI 506
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 507 QDkegrTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGER-HEVIQFMLEHGAlsiaaiqDIAAFKIQ 585
Cdd:PHA02876  240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSlSRLVPKLLERGA-------DVNAKNIK 306

                         170
                  ....*....|....*...
gi 1958776210 586 AVYKGYKVRKAFRDRKNL 603
Cdd:PHA02876  307 GETPLYLMAKNGYDTENI 324
Ank_5 pfam13857
Ankyrin repeats (many copies);
369-416 4.65e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 4.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958776210 369 DIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPL 416
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 510-538 5.07e-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: 34.87  E-value: 5.07e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958776210  510 EGRTALHWSCNNGYLDAIKLLLDFAAFPN 538
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 182-294 5.56e-03

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: 39.86  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210 182 GKIPLHWAANHKDASAVHTVRCILDAAPT----ESLLNWQD----YEGRTPLHFAVADGNLTVVDVLTSY-ESCNITSYD 252
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDsgnpKELVNAPCtdefYQGQTALHIAIENRNLNLVRLLVENgADVSARATG 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958776210 253 NLFRT-----------PLHWAALLGHAQIVHLLLER--NKSGTVPSDSQGATPLH 294
Cdd:cd21882   106 RFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENgaQPAALEAQDSLGNTVLH 160
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 444-475 5.67e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 5.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958776210 444 DGHSLLHWAAL-GGNADVCQILIENKINPNVQD 475
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 62-161 6.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  62 DCADALLKAGADVN----KTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLE-EMTPLHLSTRHRSPKCLALLLKF 136
Cdd:PHA02884   47 DIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSY 126

                          90       100
                  ....*....|....*....|....*
gi 1958776210 137 MAPGEVDTQDKNKQTALHWSAYYNN 161
Cdd:PHA02884  127 GADINIQTNDMVTPIELALMICNNF 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 444-473 6.68e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 6.68e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958776210 444 DGHSLLHWAALGGNADVCQILIENKINPNV 473
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 478-509 6.71e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 6.71e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958776210 478 GRTPLQCAAY-GGYINCMAVLMENNADPNIQDK 509
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 65-198 7.03e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776210  65 DALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPL--HLSTRHRspKCLALLLKFMAPgev 142
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnAISAKHH--KIFRILYHFASI--- 616

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776210 143 dtqdKNKQTA---LHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDASAV 198
Cdd:PLN03192  617 ----SDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMV 671
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 478-506 8.79e-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: 34.10  E-value: 8.79e-03
                           10        20
                   ....*....|....*....|....*....
gi 1958776210  478 GRTPLQCAAYGGYINCMAVLMENNADPNI 506
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH