|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
270-560 |
5.02e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.53 E-value: 5.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 270 IVHLLLERNKSGTVPSDSQGATPLHYAAQSNFAETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLrtMLSLKSDID 349
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVA--LLLLAAGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 350 INMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHW 429
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 430 AALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 509
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958776206 510 DFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 560
Cdd:COG0666 240 EAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
19-240 |
8.14e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 8.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 19 HAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776206 179 DVEGKIPLHWAANHKDASAVHtvrcILDAAptESLLNWQDYEGRTPLHFAVADGNLTVVDVL 240
Cdd:COG0666 216 DNDGKTALDLAAENGNLEIVK----LLLEA--GADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
336-554 |
2.02e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 100.89 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 336 DVLRTMLslKSDIDINMADKYGGTALHAAALSGHVST-----VKLLLDNDAQVDATDVMKHTPLFRA--CEMGHRDVIQT 408
Cdd:PHA03100 49 DVVKILL--DNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 409 LIKGGARVDLVDQDGHSLLHWAALGGNAD--VCQILIENKINPNVQDYagrtplqcaayggyINCmavLMENNADPNIQD 486
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR--------------VNY---LLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776206 487 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEerYTPLDYALLGERHEVIQFMLEHGAlSIAAI 554
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG--DTPLHIAILNNNKEIFKLLLNNGP-SIKTI 254
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
394-486 |
3.29e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.63 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 394 LFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIEnKINPNVQDYaGRTPLQCAAYGGYINCMA 473
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1958776206 474 VLMENNADPNIQD 486
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
62-262 |
3.34e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 91.18 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 62 DCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGE 141
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 142 VdtQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKdasavhtvRCILDAAPTESLLNWQDYEG 221
Cdd:PHA02874 185 V--KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--------RSAIELLINNASINDQDIDG 254
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958776206 222 RTPLHFAVA-DGNLTVVDVLTsYESCNITSYDNLFRTPLHWA 262
Cdd:PHA02874 255 STPLHHAINpPCDIDIIDILL-YHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
85-179 |
6.50e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 85 LHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDtqdkNKQTALHWSAYYNNPEH 164
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1958776206 165 AKLLIKHDSNIGIPD 179
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
166-294 |
9.67e-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: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 166 KLLIKHDSNIGIPDVEGKIPLHWAA--NHKDASAVhtvrcILDAAPTesLLNW----QDYEGRTPLHFAVADGNLTVVDV 239
Cdd:cd22192 35 KLLKCPSCDLFQRGALGETALHVAAlyDNLEAAVV-----LMEAAPE--LVNEpmtsDLYQGETALHIAVVNQNLNLVRE 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776206 240 LTSYESCNIT----------SYDNLF---RTPLHWAALLGHAQIVHLLLERNKSgTVPSDSQGATPLH 294
Cdd:cd22192 108 LIARGADVVSpratgtffrpGPKNLIyygEHPLSFAACVGNEEIVRLLIEHGAD-IRAQDSLGNTVLH 174
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
291-497 |
1.09e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 55.79 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 291 TPLHYAAQSNFAETVKVFLTHPSVrddsDLE-----GRTSFMWAAGKGSDDVLRTMLSLKSDIdINMA---DKYGG-TAL 361
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSC----DLFqrgalGETALHVAALYDNLEAAVVLMEAAPEL-VNEPmtsDLYQGeTAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 362 HAAALSGHVSTVKLLLDNDAQV---DATDVM------------KHTPLFRACeMGHRDVIQTLIKGGArvDLVDQD--GH 424
Cdd:cd22192 94 HIAVVNQNLNLVRELIARGADVvspRATGTFfrpgpknliyygEHPLSFAAC-VGNEEIVRLLIEHGA--DIRAQDslGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 425 SLLHWAALGGNAD-VCQI--LI---ENKINP----NVQDYAGRTPLQCAAYGGYINCMAVLMENnadpniqdkegRTALH 494
Cdd:cd22192 171 TVLHILVLQPNKTfACQMydLIlsyDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239
|
...
gi 1958776206 495 WSC 497
Cdd:cd22192 240 WTY 242
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
221-275 |
1.19e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958776206 221 GRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLL 275
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
735-760 |
5.64e-05 |
|
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: 40.99 E-value: 5.64e-05
10 20
....*....|....*....|....*.
gi 1958776206 735 RKELFRRKNKAAAVIQRAWRSYQLRK 760
Cdd:cd23767 1 EEEELQRMNRAATLIQALWRGYKVRK 26
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
215-312 |
6.40e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 215 NWQDYEGRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLlernkSGTVPSDSQG---AT 291
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLL-----SRHSQCHFELganAK 182
|
90 100
....*....|....*....|.
gi 1958776206 292 PLHYAAQSNFAETVKVFLTHP 312
Cdd:PTZ00322 183 PDSFTGKPPSLEDSPISSHHP 203
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
595-688 |
3.05e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.62 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 595 KKREEENKRKEAEQK--GQPDTDPPRPQVLPCPPSPQNEPSRQSAAPSKQPPAShtvQSPDPEQGRPAGQCPGRASHRdc 672
Cdd:NF033838 396 KKAEEEAKRKAAEEDkvKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPAD---QQAEEDYARRSEEEYNRLTQQ-- 470
|
90
....*....|....*.
gi 1958776206 673 ssdlQGTASRKPSESP 688
Cdd:NF033838 471 ----QPPKTEKPAQPS 482
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
48-76 |
3.18e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.18e-04
10 20
....*....|....*....|....*....
gi 1958776206 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 ... |
422-451 |
6.72e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 6.72e-04
10 20 30
....*....|....*....|....*....|
gi 1958776206 422 DGHSLLHWAALGGNADVCQILIENKINPNV 451
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
553-579 |
6.78e-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: 37.91 E-value: 6.78e-04
10 20
....*....|....*....|....*..
gi 1958776206 553 AIQDIAAFKIQAVYKGYKVRKAFRDRK 579
Cdd:cd23767 6 QRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
150-366 |
9.07e-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: 43.15 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 150 QTALHWSAYYNNP-EHAKLLIKHDSNIgipdVEGKIPLHWAA-NHKDAsavhtvrcildaapTESLLNW--QDYEGRTPL 225
Cdd:TIGR00870 53 RSALFVAAIENENlELTELLLNLSCRG----AVGDTLLHAISlEYVDA--------------VEAILLHllAAFRKSGPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 226 HFAVadgnltvvDVLTSYESCNITsydnlfrtPLHWAALLGHAQIVHLLLERnksgtvpsdsqGATpLHYAAQSNFaetv 305
Cdd:TIGR00870 115 ELAN--------DQYTSEFTPGIT--------ALHLAAHRQNYEIVKLLLER-----------GAS-VPARACGDF---- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776206 306 kvFLTHPSVrdDSDLEGRTSFMWAAGKGSDDVLRtmLSLKSDIDINMADKYGGTALHAAAL 366
Cdd:TIGR00870 163 --FVKSQGV--DSFYHGESPLNAAACLGSPSIVA--LLSEDPADILTADSLGNTLLHLLVM 217
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
591-685 |
1.49e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 591 DAAAKKREEENKRKEAEQKGQPDTDPPRPQvlpcPPSPQNEPSRQSAAPSKQPPASHTVQSP-DPEQGRPAGQCPGRASH 669
Cdd:PHA03307 325 SSSSTSSSSESSRGAAVSPGPSPSRSPSPS----RPPPPADPSSPRKRPRPSRAPSSPAASAgRPTRRRARAAVAGRARR 400
|
90
....*....|....*.
gi 1958776206 670 RDCSSdlQGTASRKPS 685
Cdd:PHA03307 401 RDATG--RFPAGRPRP 414
|
|
| FAM217 |
pfam15344 |
FAM217 family; This family of proteins is found in eukaryotes. Proteins in this family are ... |
617-720 |
2.28e-03 |
|
FAM217 family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 329 and 507 amino acids in length. There is a conserved YPDFLP sequence motif.
Pssm-ID: 464662 Cd Length: 234 Bit Score: 40.48 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 617 PRPQVLPCPPSPQNEPSRQSAAPSKQPpashtvQSPDPEQGRPAGQCPGRASHRDCSsdlqgtaSRKPSESPREHCRGAS 696
Cdd:pfam15344 114 ARPPTAPGTPGALKSPGSSKLIASALP------SKKLPHQEGLSKSGPSRKKEKHCE-------EHHPSYAFETHPRPSD 180
|
90 100
....*....|....*....|....
gi 1958776206 697 AGVHPRSCEDGDSYRHQGTSSAEK 720
Cdd:pfam15344 181 VLSSSRLCSQKQSASKWRVRSEEK 204
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
256-280 |
5.84e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 5.84e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
270-560 |
5.02e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.53 E-value: 5.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 270 IVHLLLERNKSGTVPSDSQGATPLHYAAQSNFAETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLrtMLSLKSDID 349
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVA--LLLLAAGAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 350 INMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHW 429
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 430 AALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 509
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958776206 510 DFAAFPNqmENNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAF 560
Cdd:COG0666 240 EAGADLN--AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
335-594 |
2.79e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 167.82 E-value: 2.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 335 DDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGA 414
Cdd:COG0666 32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 415 RVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALH 494
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 495 WSCNNGYLDAIKLLLDFAAFPNQMenNEERYTPLDYALLGERHEVIQFMLEHGALSIAAIQDIAAFKIQAVYKGYKVRKA 574
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAK--DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
|
250 260
....*....|....*....|
gi 1958776206 575 FRDRKNLLMKHEQLRKDAAA 594
Cdd:COG0666 270 LLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
247-493 |
2.75e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 156.27 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 247 NITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTVPSDSQGATPLHYAAQSNFAETVKVFLTHPSVRDDSDLEGRTSF 326
Cdd:COG0666 45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 327 MWAAGKGSDDVLRtMLsLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVI 406
Cdd:COG0666 125 HLAAYNGNLEIVK-LL-LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 407 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 486
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 1958776206 487 KEGRTAL 493
Cdd:COG0666 283 LDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
19-240 |
8.14e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 8.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 19 HAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE--AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776206 179 DVEGKIPLHWAANHKDASAVHtvrcILDAAptESLLNWQDYEGRTPLHFAVADGNLTVVDVL 240
Cdd:COG0666 216 DNDGKTALDLAAENGNLEIVK----LLLEA--GADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
33-324 |
4.85e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 129.69 E-value: 4.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 33 LIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDL 112
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 113 EEMTPLHLSTRHRSPKCLALLLKfmAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANH 192
Cdd:COG0666 86 GGNTLLHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 193 KDasaVHTVRCILDAAPTeslLNWQDYEGRTPLHFAVADGNLTVVDVLTSYEScNITSYDNLFRTPLHWAALLGHAQIVH 272
Cdd:COG0666 164 GN---LEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958776206 273 LLLERNKSGTvPSDSQGATPLHYAAQSNFAETVKVFLTHPSVRDDSDLEGRT 324
Cdd:COG0666 237 LLLEAGADLN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
64-355 |
7.59e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 123.14 E-value: 7.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 64 ADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPgeVD 143
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD--IN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 144 TQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDasaVHTVRCILDA-APteslLNWQDYEGR 222
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN---LEIVKLLLEAgAD----VNAQDNDGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 223 TPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTVPsDSQGATPLHYAAQSNFA 302
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1958776206 303 ETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDIDINMADK 355
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
336-554 |
2.02e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 100.89 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 336 DVLRTMLslKSDIDINMADKYGGTALHAAALSGHVST-----VKLLLDNDAQVDATDVMKHTPLFRA--CEMGHRDVIQT 408
Cdd:PHA03100 49 DVVKILL--DNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 409 LIKGGARVDLVDQDGHSLLHWAALGGNAD--VCQILIENKINPNVQDYagrtplqcaayggyINCmavLMENNADPNIQD 486
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR--------------VNY---LLSYGVPINIKD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776206 487 KEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEerYTPLDYALLGERHEVIQFMLEHGAlSIAAI 554
Cdd:PHA03100 190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG--DTPLHIAILNNNKEIFKLLLNNGP-SIKTI 254
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
19-186 |
3.10e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.10 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 19 HAAAVNGDKGALQRLIvGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMK 98
Cdd:COG0666 125 HLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 99 LLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMApgEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIP 178
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA--DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
|
....*...
gi 1958776206 179 DVEGKIPL 186
Cdd:COG0666 282 LLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
394-486 |
3.29e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.63 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 394 LFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIEnKINPNVQDYaGRTPLQCAAYGGYINCMA 473
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1958776206 474 VLMENNADPNIQD 486
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
427-518 |
4.36e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 427 LHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMEnNADPNIQDkEGRTALHWSCNNGYLDAIK 506
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|..
gi 1958776206 507 LLLDFAAFPNQM 518
Cdd:pfam12796 79 LLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
361-453 |
3.30e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.94 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 361 LHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKgGARVDLVDqDGHSLLHWAALGGNADVCQ 440
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1958776206 441 ILIENKINPNVQD 453
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
62-262 |
3.34e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 91.18 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 62 DCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGE 141
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 142 VdtQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKdasavhtvRCILDAAPTESLLNWQDYEG 221
Cdd:PHA02874 185 V--KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--------RSAIELLINNASINDQDIDG 254
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958776206 222 RTPLHFAVA-DGNLTVVDVLTsYESCNITSYDNLFRTPLHWA 262
Cdd:PHA02874 255 STPLHHAINpPCDIDIIDILL-YHKADISIKDNKGENPIDTA 295
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
214-548 |
3.50e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 92.82 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 214 LNWQDYEGRTPLHFAVADGNLTVVDVLTSYES-CNITSYD-------------------------NLFRTPLHWAALLGH 267
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdVNIIALDdlsvlecavdsknidtikaiidnrsNINKNDLSLLKAIRN 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 268 AQIVHLLLERNKSGTVPS-DSQGATPLHYAAQS-NFAETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSD-DVLRTMLSL 344
Cdd:PHA02876 251 EDLETSLLLYDAGFSVNSiDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIML 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 345 KSDIdiNMADKYGGTALH-AAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDG 423
Cdd:PHA02876 331 GADV--NAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 424 HSLLHWAALGGNAdvcqilienkinpnvqdyagrtplqcaayggYINcMAVLMENNADPNIQDKEGRTALHWSC-NNGYL 502
Cdd:PHA02876 409 GTALHFALCGTNP-------------------------------YMS-VKTLIDRGANVNSKNKDLSTPLHYACkKNCKL 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958776206 503 DAIKLLLDFAAFPNQMeNNEERYtPLDYALlgERHEVIQFMLEHGA 548
Cdd:PHA02876 457 DVIEMLLDNGADVNAI-NIQNQY-PLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
59-416 |
1.04e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 91.28 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 59 DRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKfma 138
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID--- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 139 pgevDTQDKNKQTALHWSAYYNNPEHAKLLIkHDSNIGIP--DVEGKIPLHWAANHKDASavhtvRCILDAAPTESLLNW 216
Cdd:PHA02876 233 ----NRSNINKNDLSLLKAIRNEDLETSLLL-YDAGFSVNsiDDCKNTPLHHASQAPSLS-----RLVPKLLERGADVNA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 217 QDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLFRTPLHWAALLG-HAQIVHLLLERNkSGTVPSDSQGATPLHY 295
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELG-ANVNARDYCDKTPIHY 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 296 AAQSNFAETVKVFLTHpsvrdDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDID----INMADKYGGTALHAAALSG-HV 370
Cdd:PHA02876 382 AAVRNNVVIINTLLDY-----GADIEALSQKIGTALHFALCGTNPYMSVKTLIDrganVNSKNKDLSTPLHYACKKNcKL 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1958776206 371 STVKLLLDNDAQVDATDVMKHTPLFRAceMGHRDVIQTLIKGGARV 416
Cdd:PHA02876 457 DVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL 500
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
460-548 |
1.48e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 460 LQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFpnqmENNEERYTPLDYALLGERHEV 539
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEI 76
|
....*....
gi 1958776206 540 IQFMLEHGA 548
Cdd:pfam12796 77 VKLLLEKGA 85
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
293-387 |
1.49e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 81.32 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 293 LHYAAQSNFAETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSLksdIDINMADkYGGTALHAAALSGHVST 372
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKD-NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1958776206 373 VKLLLDNDAQVDATD 387
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
85-179 |
6.50e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.39 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 85 LHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDtqdkNKQTALHWSAYYNNPEH 164
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1958776206 165 AKLLIKHDSNIGIPD 179
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
252-495 |
2.16e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 86.23 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 252 DNLFRTPLHwaaLLGH------AQIVHLLLERNKSGTVPsDSQGATPLHYAAQsnFAETVkvflthpsvrddsdlegrts 325
Cdd:PHA03095 44 GEYGKTPLH---LYLHyssekvKDIVRLLLEAGADVNAP-ERCGFTPLHLYLY--NATTL-------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 326 fmwaagkgsdDVLRTMLSLKSDIdiNMADKYGGTALHAAaLSG---HVSTVKLLLDNDAQVDATDVMKHTPL-----FRA 397
Cdd:PHA03095 98 ----------DVIKLLIKAGADV--NAKDKVGRTPLHVY-LSGfniNPKVIRLLLRKGADVNALDLYGMTPLavllkSRN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 398 CEMghrDVIQTLIKGGARVDLVDQDGHSLLHWAALG--GNADVCQILIENKINPNVQDYAGRTPLQCAAYGGyiNCMAVL 475
Cdd:PHA03095 165 ANV---ELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS--SCKRSL 239
|
250 260
....*....|....*....|....
gi 1958776206 476 M----ENNADPNIQDKEGRTALHW 495
Cdd:PHA03095 240 VlpllIAGISINARNRYGQTPLHY 263
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
32-263 |
4.02e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.08 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 32 RLIVGNSALKDKEDQFGRTPLMYCV---LADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGN-YRFMKLLLTRRANW 107
Cdd:PHA03095 31 RRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 108 MQKDLEEMTPLH--LSTRHRSPKCLALLLKFMApgEVDTQDKNKQTALHwsAYYN----NPEHAKLLIKHDSNIGIPDVE 181
Cdd:PHA03095 111 NAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGA--DVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 182 GKIPLHWAAN--HKDASAVHT-VRCILDAAPTESLlnwqdyeGRTPLHFAVADG---NLTVVDVLTSYESCNITsyDNLF 255
Cdd:PHA03095 187 FRSLLHHHLQsfKPRARIVRElIRAGCDPAATDML-------GNTPLHSMATGSsckRSLVLPLLIAGISINAR--NRYG 257
|
....*...
gi 1958776206 256 RTPLHWAA 263
Cdd:PHA03095 258 QTPLHYAA 265
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
120-421 |
4.16e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 84.72 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 120 LSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKdasavh 199
Cdd:PHA03100 6 VLTKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIK------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 200 tvrcildaaptesllnwqdyegrtplhfAVADGNLTVVDVLTSYEScNITSYDNLFRTPLHWAA--LLGHAQIVHLLLER 277
Cdd:PHA03100 80 ----------------------------YNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAIskKSNSYSIVEYLLDN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 278 NKSgTVPSDSQGATPLHYAAQSNFAET--VKVFLTHpsvrdDSDLEGRTSFmwaagkgsdDVLrtmlsLKSDIDINMADK 355
Cdd:PHA03100 131 GAN-VNIKNSDGENLLHLYLESNKIDLkiLKLLIDK-----GVDINAKNRV---------NYL-----LSYGVPINIKDV 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776206 356 YGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQ 421
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
211-448 |
5.26e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 81.25 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 211 ESLLNWQDYEGRTPLHFAVADGNLTVVDVLTsYESCNITSYDNLFRTPLHWAALLGHAQ-----IVHLLLERNKSGTVPs 285
Cdd:PHA03100 25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAP- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 286 DSQGATPLHYAAQ--SNFAETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDD--VLRTMLslKSDIDINMADKyggtal 361
Cdd:PHA03100 103 DNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLI--DKGVDINAKNR------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 362 haaalsghvstVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQI 441
Cdd:PHA03100 175 -----------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
|
....*..
gi 1958776206 442 LIENKIN 448
Cdd:PHA03100 244 LLNNGPS 250
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
215-451 |
4.11e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.49 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 215 NWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLfRTPLHWAALLGHAQIVHLLLERNKSGTVPSDSQGATPLH 294
Cdd:PHA02875 29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 295 YAAQSNfaetvKVflthpsvrddsdlegrtsfmwaagkgsdDVLRTMLSLKSDIDINMADKYggTALHAAALSGHVSTVK 374
Cdd:PHA02875 108 LATILK-----KL----------------------------DIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGIE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776206 375 LLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGH-SLLHWAALGGNADVCQILIENKINPNV 451
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
225-311 |
5.27e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.30 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 225 LHFAVADGNLTVVDVLTSYEsCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGtvpSDSQGATPLHYAAQSNFAET 304
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEI 76
|
....*..
gi 1958776206 305 VKVFLTH 311
Cdd:pfam12796 77 VKLLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
344-548 |
8.98e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.76 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 344 LKSDIDINMADKYGGTALHAAALSGH---VSTVKLLLDNDAQVDATDVMKHTPLFraCEMGH---RDVIQTLIKGGARVD 417
Cdd:PHA03095 34 LAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLH--LYLYNattLDVIKLLIKAGADVN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 418 LVDQDGHSLLHwAALGG---NADVCQILIENKINPNVQDYAGRTPLqcAAYGGYINC----MAVLMENNADPNIQDKEGR 490
Cdd:PHA03095 112 AKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVYAVDDRFR 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 491 TALHWSCNNGYLDAIKLLLDFAAFPNQMENNEERYTPLDYALLGE--RHEVIQFMLEHGA 548
Cdd:PHA03095 189 SLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGI 248
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
52-146 |
9.83e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.53 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 52 LMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQkdLEEMTPLHLSTRHRSPKCLA 131
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78
|
90
....*....|....*
gi 1958776206 132 LLLKFMApgEVDTQD 146
Cdd:pfam12796 79 LLLEKGA--DINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
19-111 |
1.17e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 19 HAAAVNGDKGALQRLIVGNSAlKDKEDQFGRTPLMYCVLADRLDCADALLKaGADVNKTDHsRRTALHLAAQKGNYRFMK 98
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1958776206 99 LLLTRRANWMQKD 111
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
370-548 |
2.76e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.86 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 370 VSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAA-----LGGNADVCQILIE 444
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 445 NKINPNVQDYAGRTPLQCAAYG--GYINCMAVLMENNADPNIQDKEGRTALHW--SCNNGYLDAIKLLLDFAAFPNQMEN 520
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLylESNKIDLKILKLLIDKGVDINAKNR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1958776206 521 --------------NEERYTPLDYALLGERHEVIQFMLEHGA 548
Cdd:PHA03100 175 vnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGA 216
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
361-529 |
3.17e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 75.80 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 361 LHAAALSGHVSTVKLLLDNDAQVDatDVM---KHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNAD 437
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFAD--DVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 438 VCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGR-TALHWSCNNGYLDAIKLLLDFAAFPN 516
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
|
170
....*....|....
gi 1958776206 517 QMENNE-ERYTPLD 529
Cdd:PHA02875 230 IMFMIEgEECTILD 243
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
257-532 |
3.51e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.77 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 257 TPLHWAALLGHAQIVHLLLernKSGTVPS--DSQGATPLHYAAQSNFAETVKVFLTH---PSVRDDSDLEgrtsfmwaag 331
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFI---KHGADINhiNTKIPHPLLTAIKIGAHDIIKLLIDNgvdTSILPIPCIE---------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 332 kgsDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIK 411
Cdd:PHA02874 104 ---KDMIKTIL--DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 412 GGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYggYINCMAVLMENNADPNIQDKEGRT 491
Cdd:PHA02874 179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGST 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1958776206 492 ALHWSCNNG-YLDAIKLLLDFAAFPNQMENNEEryTPLDYAL 532
Cdd:PHA02874 257 PLHHAINPPcDIDIIDILLYHKADISIKDNKGE--NPIDTAF 296
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
350-557 |
5.47e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.00 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 350 INMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMG-----------------------HRDVI 406
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGahdiikllidngvdtsilpipciEKDMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 407 QTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQD 486
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776206 487 KEGRTALHWSCNNGYLDAIKLLLDFAAfpNQMENNEERYTPLDYALLGERhEVIQFMLEHGALSiaaIQDI 557
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGFTPLHNAIIHNR-SAIELLINNASIN---DQDI 252
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
224-493 |
6.59e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 75.30 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 224 PLHFAVADGNLTVVDVLTSyESCNITSYDNLFRTPLHWAALLGHAQ-IVHLLLERNKSGTVPSDSQGATPLHYaaqsNFA 302
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLT-RGHNVNQPDHRDLTPLHIICKEPNKLgMKEMIRSINKCSVFYTLVAIKDAFNN----RNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 303 ETVKVFLT--HPSVRDDSDLEGRTsfmwaagKGSDDVLRTM---LSLKSDIDINMADKYGG-TALHAAALSGHVSTVKLL 376
Cdd:PHA02878 115 EIFKIILTnrYKNIQTIDLVYIDK-------KSKDDIIEAEitkLLLSYGADINMKDRHKGnTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 377 LDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWA-ALGGNADVCQILIENKINPNVQDYA 455
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYI 267
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958776206 456 -GRTPLQCAAYGGYIncMAVLMENNADPNIQDKEGRTAL 493
Cdd:PHA02878 268 lGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
166-460 |
7.68e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 75.06 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 166 KLLIKHDSNIGIPDVEGKIPLHWAANHKDASAVHTVRCILDAApteSLLNWQDYEGRTPLHFAVADGN-LTVVDVLTSYe 244
Cdd:PHA03095 31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAG---ADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 245 SCNITSYDNLFRTPLHwAALLG---HAQIVHLLLERNKSGTVpSDSQGATPLHyaaqsnfaetvkVFLTHPSVrddsdle 321
Cdd:PHA03095 107 GADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNA-LDLYGMTPLA------------VLLKSRNA------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 322 grtsfmwaagkgSDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVST--VKLLLDNDAQVDATDVMKHTPLFRACE 399
Cdd:PHA03095 166 ------------NVELLRLLI--DAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIRAGCDPAATDMLGNTPLHSMAT 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776206 400 MG--HRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPL 460
Cdd:PHA03095 232 GSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
153-252 |
1.53e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 153 LHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDasaVHTVRCILDAAPTESllnwqDYEGRTPLHFAVADG 232
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGH---LEIVKLLLEHADVNL-----KDNGRTALHYAARSG 72
|
90 100
....*....|....*....|
gi 1958776206 233 NLTVVDVLTSYEsCNITSYD 252
Cdd:pfam12796 73 HLEIVKLLLEKG-ADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
17-201 |
2.16e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 17 QVHAAAVNGDKGALQRLIVGNSALKDKeDQFGRTPLMycVLADRLDCADALLK----AGADVNKTDHSRRTALHLAAQ-- 90
Cdd:PHA03095 122 HVYLSGFNINPKVIRLLLRKGADVNAL-DLYGMTPLA--VLLKSRNANVELLRllidAGADVYAVDDRFRSLLHHHLQsf 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 91 KGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLaLLLKFMAPG-EVDTQDKNKQTALHWSAYYNNPEHAKLLI 169
Cdd:PHA03095 199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRS-LVLPLLIAGiSINARNRYGQTPLHYAAVFNNPRACRRLI 277
|
170 180 190
....*....|....*....|....*....|..
gi 1958776206 170 KHDSNIGIPDVEGKIPLHWAANHKDASAVHTV 201
Cdd:PHA03095 278 ALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
186-278 |
3.22e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 186 LHWAANHKDASAVHT-VRCILDAaptesllNWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDnlfRTPLHWAAL 264
Cdd:pfam12796 1 LHLAAKNGNLELVKLlLENGADA-------NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG---RTALHYAAR 70
|
90
....*....|....
gi 1958776206 265 LGHAQIVHLLLERN 278
Cdd:pfam12796 71 SGHLEIVKLLLEKG 84
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
92-477 |
6.28e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.92 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 92 GNYRFMKLLLTRRANWMQKDLEE-MTPLHLSTRHRSPKCLALLLKFMApgEVDTQDKNKQTALHWSAYYNNPEHAKLLIK 170
Cdd:PHA02874 12 GDIEAIEKIIKNKGNCINISVDEtTTPLIDAIRSGDAKIVELFIKHGA--DINHINTKIPHPLLTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 171 H--DSNI-GIPDVEGKiplhwaanhkdasavhTVRCILDAAPTeslLNWQDYEGRTPLHFAVADGNLTVVDVLTSYES-C 246
Cdd:PHA02874 90 NgvDTSIlPIPCIEKD----------------MIKTILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGAdV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 247 NItsydnlfrtplhwaallghaqivhlllernksgtvpSDSQGATPLHYAAQSNFAETVKVFLThpsvrddsdlegrtsf 326
Cdd:PHA02874 151 NI------------------------------------EDDNGCYPIHIAIKHNFFDIIKLLLE---------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 327 mwaagKGSddvlrtmlslksdiDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACeMGHRDVI 406
Cdd:PHA02874 179 -----KGA--------------YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAI 238
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958776206 407 QTLIKgGARVDLVDQDGHSLLHWA-ALGGNADVCQILIENKINPNVQDYAGRTPLQCAAygGYINCMAVLME 477
Cdd:PHA02874 239 ELLIN-NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAF--KYINKDPVIKD 307
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
61-366 |
7.83e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 68.75 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 61 LDCADALLKAGADVNKTDHSRRTA-------LHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHrsPKCLAll 133
Cdd:PHA02878 10 TDNYETILKYIEYIDHTENYSTSAslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKE--PNKLG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 134 LKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLI--KHDSNIGIPDVEGKiplhwAANHKDASAVHTVRCILDAAPTE 211
Cdd:PHA02878 86 MKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILtnRYKNIQTIDLVYID-----KKSKDDIIEAEITKLLLSYGADI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 212 SLLNwqDYEGRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLLeRNKSGTVPSDSQGAT 291
Cdd:PHA02878 161 NMKD--RHKGNTALHYATENKDQRLTELLLSY-GANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNT 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776206 292 PLHYAAQSNFA-ETVKVFLTH-PSVRDDSDLEGRTSFMWAAgkGSDDVLRTMLSLKSdiDINMADKYGGTALHAAAL 366
Cdd:PHA02878 237 PLHISVGYCKDyDILKLLLEHgVDVNAKSYILGLTALHSSI--KSERKLKLLLEYGA--DINSLNSYKLTPLSSAVK 309
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
49-212 |
9.99e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.69 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 49 RTPLMYC-----VLADRLDCADALLKAGADVNKTDHSRRTALHLAAQK--GNYRFMKLLLTRRANWMQKDLEEMTPLHLS 121
Cdd:PHA03100 69 STPLHYLsnikyNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 122 TRHRSPKC------------------LALLLKFMAPgeVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGK 183
Cdd:PHA03100 149 LESNKIDLkilkllidkgvdinaknrVNYLLSYGVP--INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
|
170 180 190
....*....|....*....|....*....|.
gi 1958776206 184 IPLHWAA--NHKDasavhTVRCILDAAPTES 212
Cdd:PHA03100 227 TPLHIAIlnNNKE-----IFKLLLNNGPSIK 252
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
370-529 |
1.50e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 64.47 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 370 VSTVKLLLdndAQVDATDVMKHTPLFRacEMGHR-----DVIQTLIKGGARVDLVDQDGHS-----LLHWAALGGNADVC 439
Cdd:PHA02798 18 LSTVKLLI---KSCNPNEIVNEYSIFQ--KYLQRdspstDIVKLFINLGANVNGLDNEYSTplctiLSNIKDYKHMLDIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 440 QILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVL---MENNADPNIQDKEGRTALH---WSCNNGYLDAIKLLLDFAA 513
Cdd:PHA02798 93 KILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmIENGADTTLLDKDGFTMLQvylQSNHHIDIEIIKLLLEKGV 172
|
170
....*....|....*.
gi 1958776206 514 FPNQMeNNEERYTPLD 529
Cdd:PHA02798 173 DINTH-NNKEKYDTLH 187
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
262-477 |
1.61e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.89 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 262 AALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYAAQSNFAETVKVFLTHPSVRDDSDLEGRTSfMW------------- 328
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDI-GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA-LWnaisakhhkifri 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 329 -------------------AAGKGSDDVLRTMLslKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDAT--- 386
Cdd:PLN03192 610 lyhfasisdphaagdllctAAKRNDLTAMKELL--KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAntd 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 387 DVMKHTPLFRAC---EMGHRDVIqtlikggarVDLVDQDgHSLLHWAALGGNADVCQILIENKINPNVQDYAG----RTP 459
Cdd:PLN03192 688 DDFSPTELRELLqkrELGHSITI---------VDSVPAD-EPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGhpllRNE 757
|
250
....*....|....*...
gi 1958776206 460 LQCAAYGGYINCMAVLME 477
Cdd:PLN03192 758 RCCNEAGKLINLPPSLEE 775
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
16-175 |
3.46e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.09 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 16 SQVHAAAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYR 95
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 96 FMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMApgEVDTQDKNKQTALHWSAYYNN-PEHAKLLIKH--D 172
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA--NIDYFGKNGCVAALCYAIENNkIDIVRLFIKRgaD 227
|
...
gi 1958776206 173 SNI 175
Cdd:PHA02875 228 CNI 230
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
423-475 |
1.05e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.05e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958776206 423 GHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVL 475
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
357-410 |
1.41e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 1.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958776206 357 GGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLI 410
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
48-101 |
2.47e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.47e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958776206 48 GRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLL 101
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
456-509 |
3.06e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 3.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958776206 456 GRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 509
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
316-481 |
3.34e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 60.65 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 316 DDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDIDInmADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLF 395
Cdd:PLN03192 519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDI--GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 396 RACEMGHRDVIQTLIKGGARVDlvDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVL 475
Cdd:PLN03192 597 NAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
|
....*.
gi 1958776206 476 MENNAD 481
Cdd:PLN03192 675 IMNGAD 680
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
34-280 |
4.29e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 59.68 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 34 IVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQ-----KGNYRFMKLLLTRRANWM 108
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 109 QKDLEEMTPLH--LSTRHRSPKCLALLLKFMApgevDTQDKNK--QTALHWSAYYNNPEH--AKLLIKHDSNIgipdveg 182
Cdd:PHA03100 101 APDNNGITPLLyaISKKSNSYSIVEYLLDNGA----NVNIKNSdgENLLHLYLESNKIDLkiLKLLIDKGVDI------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 183 kiplhwaaNHKDasavhTVRCILDAApteSLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWA 262
Cdd:PHA03100 170 --------NAKN-----RVNYLLSYG---VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIA 232
|
250
....*....|....*...
gi 1958776206 263 ALLGHAQIVHLLLERNKS 280
Cdd:PHA03100 233 ILNNNKEIFKLLLNNGPS 250
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
426-509 |
4.72e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.91 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 426 LLHWAAlGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAI 505
Cdd:PTZ00322 86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
|
....
gi 1958776206 506 KLLL 509
Cdd:PTZ00322 165 QLLS 168
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
360-548 |
5.67e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.23 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 360 ALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNA-DV 438
Cdd:PHA02875 5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVkAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 439 CQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNqM 518
Cdd:PHA02875 85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD-I 163
|
170 180 190
....*....|....*....|....*....|
gi 1958776206 519 ENNEErYTPLDYALLGERHEVIQFMLEHGA 548
Cdd:PHA02875 164 EDCCG-CTPLIIAMAKGDIAICKMLLDSGA 192
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
474-546 |
5.84e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.91 E-value: 5.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776206 474 VLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQFMLEH 546
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK--TPLELAEENGFREVVQLLSRH 170
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
335-558 |
6.95e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 59.69 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 335 DDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGA 414
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 415 RV---DL--------VDQDGHSLLHWAALGGNA-DVCQ------------------ILIENKINPNVQDYAGRTPLQCAA 464
Cdd:PHA02876 236 NInknDLsllkairnEDLETSLLLYDAGFSVNSiDDCKntplhhasqapslsrlvpKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 465 YGGY-INCMAVLMENNADPNIQDKEGRTALHWSCN-NGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQF 542
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDK--TPIHYAAVRNNVVIINT 393
|
250
....*....|....*.
gi 1958776206 543 MLEHGALSIAAIQDIA 558
Cdd:PHA02876 394 LLDYGADIEALSQKIG 409
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
222-400 |
8.87e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.46 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 222 RTPLHFAVADGNLTVVDVLTSYEscniTSYDNLF----RTPLHWAALLGHAQIVHLLLERNKSGTVPSDSQgATPLHYAA 297
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLG----KFADDVFykdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPLHLAV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 298 QSNFAETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSlkSDIDINMADKYGGTALHAAALSGH-VSTVKLL 376
Cdd:PHA02875 144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD--SGANIDYFGKNGCVAALCYAIENNkIDIVRLF 221
|
170 180
....*....|....*....|....*..
gi 1958776206 377 LDNDAQVD-ATDVM--KHTPLFRACEM 400
Cdd:PHA02875 222 IKRGADCNiMFMIEgeECTILDMICNM 248
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
166-294 |
9.67e-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: 9.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 166 KLLIKHDSNIGIPDVEGKIPLHWAA--NHKDASAVhtvrcILDAAPTesLLNW----QDYEGRTPLHFAVADGNLTVVDV 239
Cdd:cd22192 35 KLLKCPSCDLFQRGALGETALHVAAlyDNLEAAVV-----LMEAAPE--LVNEpmtsDLYQGETALHIAVVNQNLNLVRE 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776206 240 LTSYESCNIT----------SYDNLF---RTPLHWAALLGHAQIVHLLLERNKSgTVPSDSQGATPLH 294
Cdd:cd22192 108 LIARGADVVSpratgtffrpGPKNLIyygEHPLSFAACVGNEEIVRLLIEHGAD-IRAQDSLGNTVLH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
322-377 |
1.29e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.89 E-value: 1.29e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776206 322 GRTSFMWAAGKGSDDVLRTMLSLKsdIDINMADKYGGTALHAAALSGHVSTVKLLL 377
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKG--ADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
48-248 |
1.30e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.08 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 48 GRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTrrANWMQKDL---EEMTPLHLSTRH 124
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--LGKFADDVfykDGMTPLHLATIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 125 RSPKCLALLLKFMAPGEVDTQDKNkqTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDasaVHTVRCI 204
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD---IAICKML 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1958776206 205 LDAAPTesllnwQDYEGRTP----LHFAVADGNLTVVDVLTSYES-CNI 248
Cdd:PHA02875 188 LDSGAN------IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAdCNI 230
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
18-189 |
1.61e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.05 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 18 VHAAAVNGDKGALQRLIVGNSALKDKEDQfGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFM 97
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 98 KLLLTRRANWMQKDLEEMTPLHLSTRH-RSpkCLALLLKfmaPGEVDTQDKNKQTALHWSAYYN-NPEHAKLLIKHDSNI 175
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAIIHnRS--AIELLIN---NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281
|
170
....*....|....
gi 1958776206 176 GIPDVEGKIPLHWA 189
Cdd:PHA02874 282 SIKDNKGENPIDTA 295
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
430-516 |
6.97e-08 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 430 AALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCNNGYLDAIKLLL 509
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
....*..
gi 1958776206 510 DFAAFPN 516
Cdd:PLN03192 612 HFASISD 618
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
291-497 |
1.09e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 55.79 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 291 TPLHYAAQSNFAETVKVFLTHPSVrddsDLE-----GRTSFMWAAGKGSDDVLRTMLSLKSDIdINMA---DKYGG-TAL 361
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSC----DLFqrgalGETALHVAALYDNLEAAVVLMEAAPEL-VNEPmtsDLYQGeTAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 362 HAAALSGHVSTVKLLLDNDAQV---DATDVM------------KHTPLFRACeMGHRDVIQTLIKGGArvDLVDQD--GH 424
Cdd:cd22192 94 HIAVVNQNLNLVRELIARGADVvspRATGTFfrpgpknliyygEHPLSFAAC-VGNEEIVRLLIEHGA--DIRAQDslGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 425 SLLHWAALGGNAD-VCQI--LI---ENKINP----NVQDYAGRTPLQCAAYGGYINCMAVLMENnadpniqdkegRTALH 494
Cdd:cd22192 171 TVLHILVLQPNKTfACQMydLIlsyDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239
|
...
gi 1958776206 495 WSC 497
Cdd:cd22192 240 WTY 242
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
239-323 |
1.29e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.29 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 239 VLTSYESCNITSYDNlfRTPLHWAALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYAAQSNFAETVKVFLTHPsvRDDS 318
Cdd:PTZ00322 101 LLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQLLSRHS--QCHF 175
|
....*
gi 1958776206 319 DLEGR 323
Cdd:PTZ00322 176 ELGAN 180
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
292-548 |
2.06e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.50 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 292 PLHYAAQSNFAETVKVFLTHPSVRDDSDLEGRTSFMWAAGKGSDDVLRTMLSLKSDIDINMADKYGGTALHaaalSGHVS 371
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFN----NRNVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 372 TVKLLLdndaqVDATDVMKHTPLFRACEMGHRDVIQT-----LIKGGARVDLVDQD-GHSLLHWAALGGNADVCQILIEN 445
Cdd:PHA02878 116 IFKIIL-----TNRYKNIQTIDLVYIDKKSKDDIIEAeitklLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 446 KINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALHWSCnnGYLdaikllldfaafpnqmenneery 525
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYC----------------------- 245
|
250 260
....*....|....*....|...
gi 1958776206 526 tpLDYallgerhEVIQFMLEHGA 548
Cdd:PHA02878 246 --KDY-------DILKLLLEHGV 259
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
392-443 |
2.69e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.04 E-value: 2.69e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958776206 392 TPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILI 443
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
334-411 |
1.00e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 1.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776206 334 SDDVLRTMLSLKSDIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIK 411
Cdd:PTZ00322 92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
442-494 |
1.53e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 1.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958776206 442 LIENK-INPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNIQDKEGRTALH 494
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
365-442 |
1.78e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 1.78e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958776206 365 ALSGHVSTVKLLLDNDAQVDATDVMKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQIL 442
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
21-236 |
3.57e-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: 50.78 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 21 AAVNGDKGALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGAD-VNKTDHSR----RTALHLAAQKGNYR 95
Cdd:cd22192 24 AAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAVVNQNLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 96 FMKLLLTRRAnwmqkdlEEMTPLHLSTR-HRSPKClalLLKFmapGEvdtqdknkqTALHWSAYYNNPEHAKLLIKHDSN 174
Cdd:cd22192 104 LVRELIARGA-------DVVSPRATGTFfRPGPKN---LIYY---GE---------HPLSFAACVGNEEIVRLLIEHGAD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776206 175 IGIPDVEGKIPLH---WAANHKDASAVHTVRCILDA----APTESLLNwqdYEGRTPLHFAVADGNLTV 236
Cdd:cd22192 162 IRAQDSLGNTVLHilvLQPNKTFACQMYDLILSYDKeddlQPLDLVPN---NQGLTPFKLAAKEGNIVM 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
256-309 |
5.06e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 5.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958776206 256 RTPLHWAALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYAAQSNFAETVKVFL 309
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
479-531 |
5.64e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 5.64e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1958776206 479 NADPNIQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYA 531
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN--LKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
67-120 |
6.10e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 6.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958776206 67 LLKAG-ADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHL 120
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
412-463 |
6.73e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 6.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1958776206 412 GGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCA 463
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
489-544 |
9.58e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 9.58e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776206 489 GRTALHWSCNNGYLDAIKLLLDFAAFPNqmENNEERYTPLDYALLGERHEVIQFML 544
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
40-204 |
9.72e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.11 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 40 LKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLH 119
Cdd:PHA02878 160 INMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 120 LST-RHRSPKCLALLLKFMAPGEVDTQDKNkQTALHWSayYNNPEHAKLLIKHDSNIGIPDVEGKIPLhwaanhkdASAV 198
Cdd:PHA02878 240 ISVgYCKDYDILKLLLEHGVDVNAKSYILG-LTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPL--------SSAV 308
|
....*.
gi 1958776206 199 HTVRCI 204
Cdd:PHA02878 309 KQYLCI 314
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
221-275 |
1.19e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1958776206 221 GRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLL 275
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
81-134 |
3.05e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958776206 81 RRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLL 134
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
218-411 |
3.96e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 46.57 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 218 DYEGRTPLHFAVADGNLTVVDVLTsyescNITSYDNLFRT--PLHWAALLGHAQIVHLLLernKSGTVPS--DSQGATPL 293
Cdd:PHA02791 27 DVHGHSALYYAIADNNVRLVCTLL-----NAGALKNLLENefPLHQAATLEDTKIVKILL---FSGMDDSqfDDKGNTAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 294 HYAAQSNFAETVKVFLTHP-SVRDDSDLEGRTSFMWAAGKGSDDVLRTMLS-LKSDIDINMADkyggTALHAAALSGHVS 371
Cdd:PHA02791 99 YYAVDSGNMQTVKLFVKKNwRLMFYGKTGWKTSFYHAVMLNDVSIVSYFLSeIPSTFDLAILL----SCIHITIKNGHVD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958776206 372 TVKLLLDNDAQVDATDVMKHTPLFR-ACEMGHRDVIQTLIK 411
Cdd:PHA02791 175 MMILLLDYMTSTNTNNSLLFIPDIKlAIDNKDLEMLQALFK 215
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
139-189 |
4.06e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 4.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958776206 139 PGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWA 189
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
13-153 |
4.10e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 47.18 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 13 SLASQVHAAAVNGDKgALQRLIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLAAQK- 91
Cdd:PHA02878 167 KGNTALHYATENKDQ-RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYc 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958776206 92 GNYRFMKLLLTRRANW-MQKDLEEMTPLHLSTrhRSPKCLALLLKFMApgEVDTQDKNKQTAL 153
Cdd:PHA02878 246 KDYDILKLLLEHGVDVnAKSYILGLTALHSSI--KSERKLKLLLEYGA--DINSLNSYKLTPL 304
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
406-476 |
4.14e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 4.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776206 406 IQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLM 476
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
735-760 |
5.64e-05 |
|
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: 40.99 E-value: 5.64e-05
10 20
....*....|....*....|....*.
gi 1958776206 735 RKELFRRKNKAAAVIQRAWRSYQLRK 760
Cdd:cd23767 1 EEEELQRMNRAATLIQALWRGYKVRK 26
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
493-549 |
5.94e-05 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 42.41 E-value: 5.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958776206 493 LHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGERHEVIQFMLEHGAL 549
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGR--TALHLAAKNGHLEIVKLLLEHADV 55
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
215-312 |
6.40e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 215 NWQDYEGRTPLHFAVADGNLTVVDVLTSYeSCNITSYDNLFRTPLHWAALLGHAQIVHLLlernkSGTVPSDSQG---AT 291
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLL-----SRHSQCHFELganAK 182
|
90 100
....*....|....*....|.
gi 1958776206 292 PLHYAAQSNFAETVKVFLTHP 312
Cdd:PTZ00322 183 PDSFTGKPPSLEDSPISSHHP 203
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
389-548 |
6.48e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.52 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 389 MKHTPLFRACEMGHRDVIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGY 468
Cdd:PHA02875 1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 469 INCMAVLMENNADPN-IQDKEGRTALHWSCNNGYLDAIKLLLDFAAFPNQmeNNEERYTPLDYALLGERHEVIQFMLEHG 547
Cdd:PHA02875 81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI--PNTDKFSPLHLAVMMGDIKGIELLIDHK 158
|
.
gi 1958776206 548 A 548
Cdd:PHA02875 159 A 159
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
356-387 |
2.26e-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: 39.19 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|...
gi 1958776206 356 YGGTALHAAALS-GHVSTVKLLLDNDAQVDATD 387
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
595-688 |
3.05e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.62 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 595 KKREEENKRKEAEQK--GQPDTDPPRPQVLPCPPSPQNEPSRQSAAPSKQPPAShtvQSPDPEQGRPAGQCPGRASHRdc 672
Cdd:NF033838 396 KKAEEEAKRKAAEEDkvKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPAD---QQAEEDYARRSEEEYNRLTQQ-- 470
|
90
....*....|....*.
gi 1958776206 673 ssdlQGTASRKPSESP 688
Cdd:NF033838 471 ----QPPKTEKPAQPS 482
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
48-76 |
3.18e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.18e-04
10 20
....*....|....*....|....*....
gi 1958776206 48 GRTPLMYCVLADRLDCADALLKAGADVNK 76
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
48-79 |
3.81e-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: 38.42 E-value: 3.81e-04
10 20 30
....*....|....*....|....*....|...
gi 1958776206 48 GRTPLMYCVL-ADRLDCADALLKAGADVNKTDH 79
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
33-88 |
4.35e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 4.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776206 33 LIVGNSALKDKEDQFGRTPLMYCVLADRLDCADALLKAGADVNKTDHSRRTALHLA 88
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
422-451 |
6.72e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.57 E-value: 6.72e-04
10 20 30
....*....|....*....|....*....|
gi 1958776206 422 DGHSLLHWAALGGNADVCQILIENKINPNV 451
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
553-579 |
6.78e-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: 37.91 E-value: 6.78e-04
10 20
....*....|....*....|....*..
gi 1958776206 553 AIQDIAAFKIQAVYKGYKVRKAFRDRK 579
Cdd:cd23767 6 QRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
243-296 |
6.84e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 6.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958776206 243 YESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTVpSDSQGATPLHYA 296
Cdd:pfam13857 4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
150-366 |
9.07e-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: 43.15 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 150 QTALHWSAYYNNP-EHAKLLIKHDSNIgipdVEGKIPLHWAA-NHKDAsavhtvrcildaapTESLLNW--QDYEGRTPL 225
Cdd:TIGR00870 53 RSALFVAAIENENlELTELLLNLSCRG----AVGDTLLHAISlEYVDA--------------VEAILLHllAAFRKSGPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 226 HFAVadgnltvvDVLTSYESCNITsydnlfrtPLHWAALLGHAQIVHLLLERnksgtvpsdsqGATpLHYAAQSNFaetv 305
Cdd:TIGR00870 115 ELAN--------DQYTSEFTPGIT--------ALHLAAHRQNYEIVKLLLER-----------GAS-VPARACGDF---- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958776206 306 kvFLTHPSVrdDSDLEGRTSFMWAAGKGSDDVLRtmLSLKSDIDINMADKYGGTALHAAAL 366
Cdd:TIGR00870 163 --FVKSQGV--DSFYHGESPLNAAACLGSPSIVA--LLSEDPADILTADSLGNTLLHLLVM 217
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
488-516 |
1.30e-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: 36.80 E-value: 1.30e-03
10 20
....*....|....*....|....*....
gi 1958776206 488 EGRTALHWSCNNGYLDAIKLLLDFAAFPN 516
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
347-394 |
1.44e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1958776206 347 DIDINMADKYGGTALHAAALSGHVSTVKLLLDNDAQVDATDVMKHTPL 394
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
591-685 |
1.49e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 591 DAAAKKREEENKRKEAEQKGQPDTDPPRPQvlpcPPSPQNEPSRQSAAPSKQPPASHTVQSP-DPEQGRPAGQCPGRASH 669
Cdd:PHA03307 325 SSSSTSSSSESSRGAAVSPGPSPSRSPSPS----RPPPPADPSSPRKRPRPSRAPSSPAASAgRPTRRRARAAVAGRARR 400
|
90
....*....|....*.
gi 1958776206 670 RDCSSdlQGTASRKPS 685
Cdd:PHA03307 401 RDATG--RFPAGRPRP 414
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
422-453 |
1.62e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|...
gi 1958776206 422 DGHSLLHWAAL-GGNADVCQILIENKINPNVQD 453
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
422-451 |
1.83e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|
gi 1958776206 422 DGHSLLHWAALGGNADVCQILIENKINPNV 451
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
65-318 |
1.87e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 42.16 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 65 DALLKAGADVNKTDHSRRTALHLAAQKGNyrfmkllltrranwmqkdlEEmtplhlstrhrspkCLALLLKFMApgEVDT 144
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGY-------------------ED--------------CVLVLLKHAC--NVHI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 145 QDKNKQTALhWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIpLHWAANHKDASAVHT-VRCILDaapteslLNWQDYEGRT 223
Cdd:PLN03192 587 RDANGNTAL-WNAISAKHHKIFRILYHFASISDPHAAGDL-LCTAAKRNDLTAMKElLKQGLN-------VDSEDHQGAT 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 224 PLHFAVADGNLTVVDVL-TSYESCNITSYDNLFrTPLHWAALLGHAQIVHLLLERNKSGTVPSD---SQGATPLHYAAQS 299
Cdd:PLN03192 658 ALQVAMAEDHVDMVRLLiMNGADVDKANTDDDF-SPTELRELLQKRELGHSITIVDSVPADEPDlgrDGGSRPGRLQGTS 736
|
250 260
....*....|....*....|..
gi 1958776206 300 NFAET---VKVFLTHPSVRDDS 318
Cdd:PLN03192 737 SDNQCrprVSIYKGHPLLRNER 758
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
456-487 |
1.95e-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: 1.95e-03
10 20 30
....*....|....*....|....*....|...
gi 1958776206 456 GRTPLQCAAY-GGYINCMAVLMENNADPNIQDK 487
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| FAM217 |
pfam15344 |
FAM217 family; This family of proteins is found in eukaryotes. Proteins in this family are ... |
617-720 |
2.28e-03 |
|
FAM217 family; This family of proteins is found in eukaryotes. Proteins in this family are typically between 329 and 507 amino acids in length. There is a conserved YPDFLP sequence motif.
Pssm-ID: 464662 Cd Length: 234 Bit Score: 40.48 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 617 PRPQVLPCPPSPQNEPSRQSAAPSKQPpashtvQSPDPEQGRPAGQCPGRASHRDCSsdlqgtaSRKPSESPREHCRGAS 696
Cdd:pfam15344 114 ARPPTAPGTPGALKSPGSSKLIASALP------SKKLPHQEGLSKSGPSRKKEKHCE-------EHHPSYAFETHPRPSD 180
|
90 100
....*....|....*....|....
gi 1958776206 697 AGVHPRSCEDGDSYRHQGTSSAEK 720
Cdd:pfam15344 181 VLSSSRLCSQKQSASKWRVRSEEK 204
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
456-484 |
2.39e-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: 36.03 E-value: 2.39e-03
10 20
....*....|....*....|....*....
gi 1958776206 456 GRTPLQCAAYGGYINCMAVLMENNADPNI 484
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
47-76 |
3.47e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.70 E-value: 3.47e-03
10 20 30
....*....|....*....|....*....|
gi 1958776206 47 FGRTPLMYCVLADRLDCADALLKAGADVNK 76
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
405-581 |
3.68e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.82 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 405 VIQTLIKGGARVDLVDQDGHSLLHWAALGGNADVCQILIENKINPNVQDYAGRTPLQCAAYGGYINCMAVLMENNADPNI 484
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 485 QDkegrTALHWSCNNGYLDAIKLLLDFAAFPNQMENNEEryTPLDYALLGER-HEVIQFMLEHGAlsiaaiqDIAAFKIQ 563
Cdd:PHA02876 240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSlSRLVPKLLERGA-------DVNAKNIK 306
|
170
....*....|....*...
gi 1958776206 564 AVYKGYKVRKAFRDRKNL 581
Cdd:PHA02876 307 GETPLYLMAKNGYDTENI 324
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
359-385 |
4.10e-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: 4.10e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
148-175 |
4.43e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 4.43e-03
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
55-135 |
4.50e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.65 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 55 CVLADRLDCADA--LLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLAL 132
Cdd:PTZ00322 87 CQLAASGDAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
...
gi 1958776206 133 LLK 135
Cdd:PTZ00322 167 LSR 169
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
616-747 |
4.63e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 616 PPRPQVLPCPPSPQNEPSRQSA-APSKQPPASHTVQSPDPEQGRP-AGQCPGRASH-----RDCSSDLQGTASRKPSESP 688
Cdd:PHA03307 259 RPAPITLPTRIWEASGWNGPSSrPGPASSSSSPRERSPSPSPSSPgSGPAPSSPRAsssssSSRESSSSSTSSSSESSRG 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958776206 689 REHCRGASAGVHPRSCEDGDSYRhqGTSSAEKCREQRLLIIQRERSRKELFRRKNKAAA 747
Cdd:PHA03307 339 AAVSPGPSPSRSPSPSRPPPPAD--PSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVA 395
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
356-385 |
5.15e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 5.15e-03
10 20 30
....*....|....*....|....*....|
gi 1958776206 356 YGGTALHAAALSGHVSTVKLLLDNDAQVDA 385
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
336-497 |
5.24e-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: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 336 DVLRTMLSLKSDIDINMADKY--GGTALHAAALSGHVSTVKLLLDNDAQVDAT---DVMKHTPL-----------FRACe 399
Cdd:cd21882 50 EAAPDSGNPKELVNAPCTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPGnlfyfgelplsLAAC- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 400 MGHRDVIQTLIKGGARV-DLVDQD--GHSLLHWAALGGN------ADVCQ-----ILIENKINPNVQ-----DYAGRTPL 460
Cdd:cd21882 129 TNQEEIVRLLLENGAQPaALEAQDslGNTVLHALVLQADntpensAFVCQmynllLSYGAHLDPTQQleeipNHQGLTPL 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 1958776206 461 QCAAYGGYINCMAVLMENNADPNIQDKEgRTALHWSC 497
Cdd:cd21882 209 KLAAVEGKIVMFQHILQREFSGPYQPLS-RKFTEWTY 244
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
50-123 |
5.40e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 39.97 E-value: 5.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958776206 50 TPLMYCVLADRLDCADALLKAGADVNK-TDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTR 123
Cdd:PHA02884 72 NPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
256-280 |
5.84e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.26 E-value: 5.84e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
82-106 |
6.02e-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: 6.02e-03
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
316-364 |
6.03e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 6.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958776206 316 DDSDLEGRTSFMWAAGKGSDDVLRTMLslKSDIDINMADKYGGTALHAA 364
Cdd:pfam13857 10 NRLDGEGYTPLHVAAKYGALEIVRVLL--AYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
114-169 |
6.65e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.71 E-value: 6.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958776206 114 EMTPLHLSTRHRSPKCLALLLKFMAPgeVDTQDKNKQTALHWSAYYNNPEHAKLLI 169
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGAD--INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
213-262 |
7.27e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.40 E-value: 7.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1958776206 213 LLNWQDYEGRTPLHFAVADGNLTVVDVLTSYEsCNITSYDNLFRTPLHWA 262
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
182-294 |
8.24e-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: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 182 GKIPLHWAANHKDASAVHTVRCILDAAPT----ESLLNWQD----YEGRTPLHFAVADGNLTVVDVLTSY-ESCNITSYD 252
Cdd:cd21882 26 GKTCLHKAALNLNDGVNEAIMLLLEAAPDsgnpKELVNAPCtdefYQGQTALHIAIENRNLNLVRLLVENgADVSARATG 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1958776206 253 NLFRT-----------PLHWAALLGHAQIVHLLLER--NKSGTVPSDSQGATPLH 294
Cdd:cd21882 106 RFFRKspgnlfyfgelPLSLAACTNQEEIVRLLLENgaQPAALEAQDSLGNTVLH 160
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
256-278 |
8.84e-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: 8.84e-03
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
62-161 |
8.99e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 39.20 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 62 DCADALLKAGADVN----KTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLE-EMTPLHLSTRHRSPKCLALLLKF 136
Cdd:PHA02884 47 DIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSY 126
|
90 100
....*....|....*....|....*
gi 1958776206 137 MAPGEVDTQDKNKQTALHWSAYYNN 161
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNF 151
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
612-717 |
9.52e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 39.77 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958776206 612 PDTDPPRPQVLPCPPSPQNEPSRQSAAPSKQPPASHTVQSPDPEQGRPAGQCPGRASHRDCSSDLQGTASRKPSESPREH 691
Cdd:PHA03307 180 EETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPR 259
|
90 100 110
....*....|....*....|....*....|....
gi 1958776206 692 --------CRGASAGVHPRSCEDGDSYRHQGTSS 717
Cdd:PHA03307 260 papitlptRIWEASGWNGPSSRPGPASSSSSPRE 293
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
151-199 |
9.77e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.33 E-value: 9.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1958776206 151 TALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDASAVH 199
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| |
