|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
35-271 |
4.41e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.98 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 35 IHDAVRAGDVKQLSDIVERGANVNEVDAlHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACL 114
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 115 QALIINGANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVD 194
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 203096504 195 YNGNLPVHLAAMEGHLHCFKFLLSRVNsavqALKAFNDNGENVLDLAHRFLKQNIVQFIQGAEYEGSHLDDQDDLAF 271
Cdd:COG0666 217 NDGKTALDLAAENGNLEIVKLLLEAGA----DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
69-161 |
2.39e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.08 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 69 LHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALIINGAnlATQDDRGCTPVHLAATHGHSFSLQ 148
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 203096504 149 VMLRSGVDPSVTD 161
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
22-235 |
1.03e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.22 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 22 ADSSSRNKVPFGSIH-----DAVRAGDVKQLsdiVERGANVNEVDaLHQFTPLHW--AAHSGSLECLHWLLWNGADATQT 94
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvylsgFNINPKVIRLL---LRKGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 95 TTRGWTAAHVAA--IRGQDACLQALIINGANLATQDDRGCTPVHLAATHGHSFSLQV--MLRSGVDPSVTDKREWRPVHY 170
Cdd:PHA03095 184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHY 263
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 203096504 171 AA-FHGRLGCLQLLvKWGCGIEDVDYNGNLPVHLAAMEGHLHCFKFLLSRVNSA---VQALKAFNDNGE 235
Cdd:PHA03095 264 AAvFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAetvAATLNTASVAGG 331
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
202-333 |
1.04e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.90 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 202 HLAAMEGHLHCFKFLLSRVNSAvqalKAFNDNGENVLdlahrflkqnivqfiqgaeyegshlddqddlafpgHVAAFKGD 281
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADA----NLQDKNGRTAL-----------------------------------HLAAKNGH 42
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 203096504 282 LEMLKKLIDDGVINLnerDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITN 333
Cdd:pfam12796 43 LEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
217-355 |
8.12e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 63.05 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 217 LSRVNSAVQALKAFNDNGENVLDLAHRFLKQNIVQFIQGAEYEGSHLDDQDDLAFPGHVAAFKGDLEMLKKLIDDGVINL 296
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 203096504 297 NERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLL 355
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
274-355 |
3.54e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.66 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 274 HVAAFKGDLEMLKKLIDDGViNLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVK 353
Cdd:PHA02874 129 HYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
..
gi 203096504 354 LL 355
Cdd:PHA02874 208 LL 209
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
67-220 |
3.94e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.16 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 67 TPLHWAAHSGSLECLHWLL-WNGADATQTTTRGWTAAHVAAIRGQDACLQALIING---ANLATQDD--RGCTPVHLAAT 140
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 141 HGHSFSLQVMLRSGVD---PSVTDK--REWR---------PVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAM 206
Cdd:cd22192 99 NQNLNLVRELIARGADvvsPRATGTffRPGPknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
|
170
....*....|....*...
gi 203096504 207 EGH--LHC--FKFLLSRV 220
Cdd:cd22192 179 QPNktFACqmYDLILSYD 196
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-510 |
3.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 337 ERPSDVAKRFAHLAAvkLLEGLQKyEIDDIEGDKNHISFFIRHGVEgstdAKDDLSLSESDkanarmraHKKIVELRQLL 416
Cdd:PRK03918 307 DELREIEKRLSRLEE--EINGIEE-RIKELEEKEERLEELKKKLKE----LEKRLEELEER--------HELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 417 EIAESNFKHLGGITEEDLKQKKELLESKKtiTELQEQLAYERLRREKLECQLDEYRVEVNQLKEALEKIQVPSAEAMEDD 496
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEH 449
|
170
....*....|....*...
gi 203096504 497 S----CEYSKEKRRMKKK 510
Cdd:PRK03918 450 RkellEEYTAELKRIEKE 467
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
302-331 |
4.04e-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: 4.04e-04
10 20 30
....*....|....*....|....*....|
gi 203096504 302 NGSTPMHKAAGQGHIDCLQWLVEMGADSNI 331
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
64-90 |
6.86e-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: 37.18 E-value: 6.86e-04
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
402-508 |
7.16e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 402 RMRAHKKIVELRQLLEIAEsnfkhlggitEEDLKQKKELLESKKTITELQEQLAYERLRREKLECQLDEYRVEVNQLKEA 481
Cdd:pfam20492 1 REEAEREKQELEERLKQYE----------EETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
|
90 100
....*....|....*....|....*..
gi 203096504 482 LEKIQVpSAEAMEDDSCEYSKEKRRMK 508
Cdd:pfam20492 71 AEMEAE-EKEQLEAELAEAQEEIARLE 96
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-486 |
4.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 407 KKIVELRQLLEIAESNFKHLggitEEDLKQ-KKELLESKKTITELQEQLAYERLRREKLECQLDEYRVEVNQLKEALEKI 485
Cdd:COG4372 45 EELEQLREELEQAREELEQL----EEELEQaRSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
.
gi 203096504 486 Q 486
Cdd:COG4372 121 Q 121
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
344-487 |
9.94e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.07 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 344 KRFAHLAA--------VKLLEGLQK--YEIDDI-EGDKNHISFFIrhgvEGSTDAKDDLSlsesDKANARMRahkKIVEL 412
Cdd:smart00787 123 KTFARLEAkkmwyewrMKLLEGLKEglDENLEGlKEDYKLLMKEL----ELLNSIKPKLR----DRKDALEE---ELRQL 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 203096504 413 RQLL-EIAESNFKHLGGITEEDLKQKKELLESKKTITELQEQLAYERLRREKLECQLDEYRVEVNQLKEALEKIQV 487
Cdd:smart00787 192 KQLEdELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
35-271 |
4.41e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.98 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 35 IHDAVRAGDVKQLSDIVERGANVNEVDAlHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACL 114
Cdd:COG0666 58 LLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 115 QALIINGANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVD 194
Cdd:COG0666 137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 203096504 195 YNGNLPVHLAAMEGHLHCFKFLLSRVNsavqALKAFNDNGENVLDLAHRFLKQNIVQFIQGAEYEGSHLDDQDDLAF 271
Cdd:COG0666 217 NDGKTALDLAAENGNLEIVKLLLEAGA----DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
47-371 |
6.30e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 113.13 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 47 LSDIVERGANVNEVDALHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALIINGANLAT 126
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 127 QDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAM 206
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 207 EGHLHCFKFLLSR---VNsavqalkAFNDNGENVLdlahrflkqnivqfiqgaeyegshlddqddlafpgHVAAFKGDLE 283
Cdd:COG0666 163 NGNLEIVKLLLEAgadVN-------ARDNDGETPL-----------------------------------HLAAENGHLE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 284 MLKKLIDDGViNLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLLEGLQKYEI 363
Cdd:COG0666 201 IVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
....*...
gi 203096504 364 DDIEGDKN 371
Cdd:COG0666 280 AALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
84-406 |
1.83e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 111.97 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 84 LLWNGADATQTTTRGWTAAHVAAIRGQDACLQALIINGANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKR 163
Cdd:COG0666 7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 164 EWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAMEGHLHCFKFLLSR---VNSAvqalkafNDNGENVLdl 240
Cdd:COG0666 87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgadVNAQ-------DNDGNTPL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 241 ahrflkqnivqfiqgaeyegshlddqddlafpgHVAAFKGDLEMLKKLIDDGViNLNERDENGSTPMHKAAGQGHIDCLQ 320
Cdd:COG0666 158 ---------------------------------HLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 321 WLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLLEGLQKYEIDDIEGDKNHISFFIRHGVEGSTDAKDDLSLSESDKAN 400
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*.
gi 203096504 401 ARMRAH 406
Cdd:COG0666 284 DLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
22-199 |
1.46e-22 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 97.72 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 22 ADSSSRNKVPFGSIHDAVRAGDVKQLSDIVERGANVNEVDAlHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTA 101
Cdd:COG0666 111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 102 AHVAAIRGQDACLQALIINGANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQ 181
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
|
170
....*....|....*...
gi 203096504 182 LLVKWGCGIEDVDYNGNL 199
Cdd:COG0666 270 LLLLALLLLAAALLDLLT 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
69-161 |
2.39e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.08 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 69 LHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALIINGAnlATQDDRGCTPVHLAATHGHSFSLQ 148
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 203096504 149 VMLRSGVDPSVTD 161
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
22-235 |
1.03e-14 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 76.22 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 22 ADSSSRNKVPFGSIH-----DAVRAGDVKQLsdiVERGANVNEVDaLHQFTPLHW--AAHSGSLECLHWLLWNGADATQT 94
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvylsgFNINPKVIRLL---LRKGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 95 TTRGWTAAHVAA--IRGQDACLQALIINGANLATQDDRGCTPVHLAATHGHSFSLQV--MLRSGVDPSVTDKREWRPVHY 170
Cdd:PHA03095 184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHY 263
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 203096504 171 AA-FHGRLGCLQLLvKWGCGIEDVDYNGNLPVHLAAMEGHLHCFKFLLSRVNSA---VQALKAFNDNGE 235
Cdd:PHA03095 264 AAvFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAetvAATLNTASVAGG 331
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
39-346 |
2.62e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.00 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 39 VRAGDVKQLSDIVERGANVNEVDALHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALI 118
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 119 INGAnlatqdDRGCTPVHLAATHghsfSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGN 198
Cdd:PHA02874 89 DNGV------DTSILPIPCIEKD----MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 199 LPVHLAAMEGHLHCFKFLLSrvNSAVQALKafNDNGENVLDLAHRFLKQNIVQFIQGaeyEGSHLDDQDDLAF-PGHVAA 277
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLE--KGAYANVK--DNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFtPLHNAI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 278 FKgDLEMLKKLIDDGVInlNERDENGSTPMHKAAGQG-HIDCLQWLVEMGADSNITNKAGERPSDVAKRF 346
Cdd:PHA02874 232 IH-NRSAIELLINNASI--NDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
132-355 |
7.59e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 73.55 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 132 CTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHG-RLGC----LQLLVKWGCGIEDVDYNGNLPVHLAAM 206
Cdd:PHA03100 36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKyNLTDvkeiVKLLLEYGANVNAPDNNGITPLLYAIS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 207 E--GHLHCFKFLLSRvNSAVQALkafNDNGENVLdlaHRFLKQNivqfiqgaeyegshlddqddlafpghvaafKGDLEM 284
Cdd:PHA03100 116 KksNSYSIVEYLLDN-GANVNIK---NSDGENLL---HLYLESN------------------------------KIDLKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 285 LKKLIDDGV---------------INLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHL 349
Cdd:PHA03100 159 LKLLIDKGVdinaknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
....*.
gi 203096504 350 AAVKLL 355
Cdd:PHA03100 239 EIFKLL 244
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
50-250 |
8.50e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 73.46 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 50 IVERGANVNEVDALHQfTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALIINGANLATQDD 129
Cdd:PHA02874 110 ILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 130 RGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRlGCLQLLVKwGCGIEDVDYNGNLPVHLAAmegH 209
Cdd:PHA02874 189 NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAI---N 263
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 203096504 210 LHCFKFLLSRV--NSAVQALKafNDNGENVLDLAHRFLKQNIV 250
Cdd:PHA02874 264 PPCDIDIIDILlyHKADISIK--DNKGENPIDTAFKYINKDPV 304
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
35-128 |
1.82e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 35 IHDAVRAGDVKQLSDIVERGANVNEVDALHQfTPLHWAAHSGSLECLHWLLwNGADAtQTTTRGWTAAHVAAIRGQDACL 114
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLL-EHADV-NLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 203096504 115 QALIINGANLATQD 128
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
136-219 |
2.01e-13 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 65.91 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 136 HLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKwgCGIEDVDYNGNLPVHLAAMEGHLHCFKF 215
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKL 79
|
....
gi 203096504 216 LLSR 219
Cdd:pfam12796 80 LLEK 83
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
138-363 |
2.31e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 69.51 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 138 AATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAMEGHLHCFKFLl 217
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 218 srvnsavqalkafndngenvldlahrflkqnivqfiqgaeYEGSHLDDQ----DDLAFpghvAAFKGDLEMLKKLIDDGv 293
Cdd:PLN03192 611 ----------------------------------------YHFASISDPhaagDLLCT----AAKRNDLTAMKELLKQG- 645
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 294 INLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADsnitnkagerpSDVAKRFAHLAAVKLLEGLQKYEI 363
Cdd:PLN03192 646 LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD-----------VDKANTDDDFSPTELRELLQKREL 704
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
35-187 |
2.58e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.48 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 35 IHDAVRAGDVKQLSDIVERGANVNEVDALHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACL 114
Cdd:PHA02875 72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 203096504 115 QALIINGANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKR-EWRPVHYAAFHGRLGCLQLLVKWG 187
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRG 225
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
202-333 |
1.04e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.90 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 202 HLAAMEGHLHCFKFLLSRVNSAvqalKAFNDNGENVLdlahrflkqnivqfiqgaeyegshlddqddlafpgHVAAFKGD 281
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADA----NLQDKNGRTAL-----------------------------------HLAAKNGH 42
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 203096504 282 LEMLKKLIDDGVINLnerDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITN 333
Cdd:pfam12796 43 LEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
37-204 |
1.47e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 66.53 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 37 DAVRAGDVKQLSDIVERGANVNEVDAlHQFTPLHWAAHSGSLECLHWLLWNGADAT--------------------QTTT 96
Cdd:PHA02874 41 DAIRSGDAKIVELFIKHGADINHINT-KIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpipciekdmiktildcgiDVNI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 97 RGW---TAAHVAAIRGQDACLQALIINGANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAF 173
Cdd:PHA02874 120 KDAelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
|
170 180 190
....*....|....*....|....*....|.
gi 203096504 174 HGRLGCLQLLVKWGCGIEDVDYNGNLPVHLA 204
Cdd:PHA02874 200 YGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
274-355 |
1.73e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.51 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 274 HVAAFKGDLEMLKKLIDDGViNLNERDENGSTPMHKAAGQGHIDCLQWLVEmGADSNITNKaGERPSDVAKRFAHLAAVK 353
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
|
..
gi 203096504 354 LL 355
Cdd:pfam12796 79 LL 80
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
41-233 |
2.30e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 65.84 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 41 AGDVKQLSDI-VERGANVNEVDAlHQFTPLHWAA--HSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQD--ACLQ 115
Cdd:PHA03100 82 LTDVKEIVKLlLEYGANVNAPDN-NGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 116 ALIINGANLATQDdrgctpvhlaathghsfSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDY 195
Cdd:PHA03100 161 LLIDKGVDINAKN-----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 203096504 196 NGNLPVHLAAMEGHLHCFKFLLSR---VNSAVQALKAFNDN 233
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLLLNNgpsIKTIIETLLYFKDK 264
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
169-253 |
4.28e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.36 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 169 HYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAMEGHLHCFKFLLSRVNSAVQalkafnDNGENVLDLAHRFLKQN 248
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK------DNGRTALHYAARSGHLE 75
|
....*
gi 203096504 249 IVQFI 253
Cdd:pfam12796 76 IVKLL 80
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
39-339 |
7.33e-11 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 64.28 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 39 VRAGDVKQLsdiVERGANVNEVDALHQfTPLHWAAHSGSLEC---LHWLLWNGADATQTTTRGWTAAH-------VAAIr 108
Cdd:PHA03095 25 VTVEEVRRL---LAAGADVNFRGEYGK-TPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylynatTLDV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 109 gqdacLQALIINGANLATQDDRGCTP--VHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVH-YAAFHG-RLGCLQLLV 184
Cdd:PHA03095 100 -----IKLLIKAGADVNAKDKVGRTPlhVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 185 KWGCGIEDVDYNGNLPVHlaameghlhcfKFLLS-RVNSAVqalkaFNDNGENVLDLAHRFLKQNIvqfiqgaeyegshl 263
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLH-----------HHLQSfKPRARI-----VRELIRAGCDPAATDMLGNT-------------- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 203096504 264 ddqddlafPGHVAAFKGDLEMLK--KLIDDGVInLNERDENGSTPMHKAAGQG-HIDCLQwLVEMGADSNITNKAGERP 339
Cdd:PHA03095 225 --------PLHSMATGSSCKRSLvlPLLIAGIS-INARNRYGQTPLHYAAVFNnPRACRR-LIALGADINAVSSDGNTP 293
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
217-355 |
8.12e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 63.05 E-value: 8.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 217 LSRVNSAVQALKAFNDNGENVLDLAHRFLKQNIVQFIQGAEYEGSHLDDQDDLAFPGHVAAFKGDLEMLKKLIDDGVINL 296
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 203096504 297 NERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLL 355
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
274-323 |
1.84e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 1.84e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 203096504 274 HVAAFKGDLEMLKKLIDDGViNLNERDENGSTPMHKAAGQGHIDCLQWLV 323
Cdd:pfam13637 6 HAAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
34-204 |
4.17e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 62.39 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 34 SIHDAVRAGDVKQLSDIVERGANVNEVDaLHQFTPLHWAAHSGSLECL-HWLLWNGADATQTTTRGWTAAHVAAIRGQDA 112
Cdd:PHA02876 243 SLLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDT 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 113 -CLQALIINGANLATQDDRGCTPVHLAATHGHSFSLQV-MLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGI 190
Cdd:PHA02876 322 eNIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
|
170
....*....|....
gi 203096504 191 EDVDYNGNLPVHLA 204
Cdd:PHA02876 402 EALSQKIGTALHFA 415
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
67-118 |
1.14e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 1.14e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 203096504 67 TPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALI 118
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
164-217 |
1.60e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 1.60e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 203096504 164 EWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAMEGHLHCFKFLL 217
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
288-343 |
1.12e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.19 E-value: 1.12e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 203096504 288 LIDDGVINLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVA 343
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
34-359 |
3.50e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 56.23 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 34 SIHDAVRAGDVKQLSDIVERGANVNEVDaLHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDAC 113
Cdd:PHA02876 148 LIKERIQQDELLIAEMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 114 LQALIINGANLATQDDRgctpvHLAATHGHSFSLQVML-RSGVDPSVTDKREWRPVHYAAFHGRLGCL-QLLVKWGCGIE 191
Cdd:PHA02876 227 IKAIIDNRSNINKNDLS-----LLKAIRNEDLETSLLLyDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 192 DVDYNGNLPVHLAAMEGH-LHCFKFLLSR---VNSA----------VQALKAFNDNGENVLDLA--------------HR 243
Cdd:PHA02876 302 AKNIKGETPLYLMAKNGYdTENIRTLIMLgadVNAAdrlyitplhqASTLDRNKDIVITLLELGanvnardycdktpiHY 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 244 FLKQNIVQFIQ-----GAEYEGshLDDQDDLAFpgHVAAFKGDLEM-LKKLIDDGViNLNERDENGSTPMHKAAGQG-HI 316
Cdd:PHA02876 382 AAVRNNVVIINtlldyGADIEA--LSQKIGTAL--HFALCGTNPYMsVKTLIDRGA-NVNSKNKDLSTPLHYACKKNcKL 456
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 203096504 317 DCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLLEGLQ 359
Cdd:PHA02876 457 DVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYGAE 499
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
133-184 |
4.92e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 4.92e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 203096504 133 TPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLV 184
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
24-204 |
5.41e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.27 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 24 SSSRNKVPFGSIHDAVRAGDVKQLSDIVERGANVNEVDalHQF-TPLHW------------------------------- 71
Cdd:PHA02878 30 STSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPD--HRDlTPLHIickepnklgmkemirsinkcsvfytlvaikd 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 72 AAHSGSLECLHWLLWNGADATQTTTrgwtaahVAAIR--GQDACLQALIIN-----GANLATQD-DRGCTPVHLAATHGH 143
Cdd:PHA02878 108 AFNNRNVEIFKIILTNRYKNIQTID-------LVYIDkkSKDDIIEAEITKlllsyGADINMKDrHKGNTALHYATENKD 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 203096504 144 SFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLA 204
Cdd:PHA02878 181 QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
98-143 |
7.08e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 7.08e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 203096504 98 GWTAAHVAAIRGQDACLQALIINGANLATQDDRGCTPVHLAATHGH 143
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
303-355 |
1.26e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 1.26e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 203096504 303 GSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLL 355
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
116-352 |
1.45e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 53.88 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 116 ALIINGANLATQDDRGCTPVHlaaTHGHSFS------LQVMLRSGVDPSVTDKREWRPVH-YAAFHGRLGCLQLLVKWGC 188
Cdd:PHA03095 32 RLLAAGADVNFRGEYGKTPLH---LYLHYSSekvkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 189 GIEDVDYNGNLP--VHLAAMEGHLHCFKFLLsRVNSAVQALKAFNDNGenvldlAHRFLKQN-----IVQFIQGAEYEGS 261
Cdd:PHA03095 109 DVNAKDKVGRTPlhVYLSGFNINPKVIRLLL-RKGADVNALDLYGMTP------LAVLLKSRnanveLLRLLIDAGADVY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 262 HLDDQDDLAFPGHVAAFKGDLEMLKKLIDDGViNLNERDENGSTPMHKAAGQG---HIDCLQwLVEMGADSNITNKAGER 338
Cdd:PHA03095 182 AVDDRFRSLLHHHLQSFKPRARIVRELIRAGC-DPAATDMLGNTPLHSMATGSsckRSLVLP-LLIAGISINARNRYGQT 259
|
250
....*....|....
gi 203096504 339 PsdvakrfAHLAAV 352
Cdd:PHA03095 260 P-------LHYAAV 266
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
35-85 |
1.69e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.04 E-value: 1.69e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 203096504 35 IHDAVRAGDVKQLSDIVERGANVNEVDALhQFTPLHWAAHSGSLECLHWLL 85
Cdd:pfam13637 5 LHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
50-233 |
2.41e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 53.35 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 50 IVERGANVNEVDALHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALIINGANLATQDD 129
Cdd:PHA02878 153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 130 RGCTPVHLAATHGHSFS-LQVMLRSGVDPSVTDK-REWRPVHYAAFHGRLgcLQLLVKWGCGIEDVDYNGNLPVHLAAME 207
Cdd:PHA02878 233 CGNTPLHISVGYCKDYDiLKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
170 180 190
....*....|....*....|....*....|...
gi 203096504 208 GH-LHCFKFLLS------RVNSAVQALKAFNDN 233
Cdd:PHA02878 311 YLcINIGRILISnicllkRIKPDIKNSEGFIDN 343
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
54-217 |
3.45e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.95 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 54 GANVNEVDALHQFTplhwAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQALIINGANLATQDDRGCT 133
Cdd:PLN03192 518 GEHDDPNMASNLLT----VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 134 PV--HLAATHGHSFSLQVMLRSGVDPSVTDKRewrpVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAMEGHLH 211
Cdd:PLN03192 594 ALwnAISAKHHKIFRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
|
....*.
gi 203096504 212 CFKFLL 217
Cdd:PLN03192 670 MVRLLI 675
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
274-355 |
3.54e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.66 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 274 HVAAFKGDLEMLKKLIDDGViNLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVK 353
Cdd:PHA02874 129 HYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
|
..
gi 203096504 354 LL 355
Cdd:PHA02874 208 LL 209
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
274-371 |
5.92e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 274 HVAAfKGDLEMLKKLIDDGViNLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVK 353
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGA-DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|....*...
gi 203096504 354 LLEGlqkYEIDDIEGDKN 371
Cdd:PTZ00322 166 LLSR---HSQCHFELGAN 180
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
131-336 |
1.34e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.76 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 131 GCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVDY-NGNLPVHLAAMEGH 209
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 210 LHCFKFLLSRvnsavqalkafndngenvldlahrflkqnivqfiqGAEYEGSHLDDQDDLafpgHVAAFKGDLEMLKKLI 289
Cdd:PHA02875 115 LDIMKLLIAR-----------------------------------GADPDIPNTDKFSPL----HLAVMMGDIKGIELLI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 203096504 290 DDGVInLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAG 336
Cdd:PHA02875 156 DHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
50-105 |
2.85e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 2.85e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 203096504 50 IVERGANVNEVDALHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVA 105
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
103-200 |
3.70e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.51 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 103 HVAAiRGQDACLQALIINGANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQL 182
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*...
gi 203096504 183 LVkwGCGIEDVDYNGNLP 200
Cdd:PTZ00322 167 LS--RHSQCHFELGANAK 182
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
50-192 |
1.20e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.14 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 50 IVERGANVNEVDALHQfTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAaIRGQD--ACLQALIINGANLATQ 127
Cdd:PHA02876 361 LLELGANVNARDYCDK-TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSK 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 203096504 128 DDRGCTPVHLAATHGHSFS-LQVMLRSGVDPSVTDKREWRPVHYA-AFHgrlGCLQLLVKWGCGIED 192
Cdd:PHA02876 439 NKDLSTPLHYACKKNCKLDvIEMLLDNGADVNAINIQNQYPLLIAlEYH---GIVNILLHYGAELRD 502
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
167-339 |
2.21e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 46.80 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 167 PVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAMEGHLHCFKFLLSRVNS-----AVQALK-AFNDNGENVLD- 239
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKcsvfyTLVAIKdAFNNRNVEIFKi 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 240 -LAHRFLKQ---NIVQ------------------FIQGAEyegSHLDDQDDLAFPGHVAAFKGDLEMLKKLIDDGViNLN 297
Cdd:PHA02878 120 iLTNRYKNIqtiDLVYidkkskddiieaeitkllLSYGAD---INMKDRHKGNTALHYATENKDQRLTELLLSYGA-NVN 195
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 203096504 298 ERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERP 339
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
123-218 |
2.29e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 123 NLATQDDRGCTPVH--------LAAThGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIEDVD 194
Cdd:PTZ00322 67 NLTTEEVIDPVVAHmltvelcqLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
|
90 100
....*....|....*....|....
gi 203096504 195 YNGNLPVHLAAMEGHLHCFKFLLS 218
Cdd:PTZ00322 146 KDGKTPLELAEENGFREVVQLLSR 169
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
67-220 |
3.94e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 46.16 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 67 TPLHWAAHSGSLECLHWLL-WNGADATQTTTRGWTAAHVAAIRGQDACLQALIING---ANLATQDD--RGCTPVHLAAT 140
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 141 HGHSFSLQVMLRSGVD---PSVTDK--REWR---------PVHYAAFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAM 206
Cdd:cd22192 99 NQNLNLVRELIARGADvvsPRATGTffRPGPknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
|
170
....*....|....*...
gi 203096504 207 EGH--LHC--FKFLLSRV 220
Cdd:cd22192 179 QPNktFACqmYDLILSYD 196
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
302-334 |
4.48e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.35 E-value: 4.48e-05
10 20 30
....*....|....*....|....*....|....
gi 203096504 302 NGSTPMHKAAGQ-GHIDCLQWLVEMGADSNITNK 334
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
89-138 |
2.22e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 2.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 203096504 89 ADATQTTTRGWTAAHVAAIRGQDACLQALIINGANLATQDDRGCTPVHLA 138
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
337-510 |
3.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 337 ERPSDVAKRFAHLAAvkLLEGLQKyEIDDIEGDKNHISFFIRHGVEgstdAKDDLSLSESDkanarmraHKKIVELRQLL 416
Cdd:PRK03918 307 DELREIEKRLSRLEE--EINGIEE-RIKELEEKEERLEELKKKLKE----LEKRLEELEER--------HELYEEAKAKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 417 EIAESNFKHLGGITEEDLKQKKELLESKKtiTELQEQLAYERLRREKLECQLDEYRVEVNQLKEALEKIQVPSAEAMEDD 496
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEH 449
|
170
....*....|....*...
gi 203096504 497 S----CEYSKEKRRMKKK 510
Cdd:PRK03918 450 RkellEEYTAELKRIEKE 467
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
302-331 |
4.04e-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: 4.04e-04
10 20 30
....*....|....*....|....*....|
gi 203096504 302 NGSTPMHKAAGQGHIDCLQWLVEMGADSNI 331
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
302-331 |
4.59e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 4.59e-04
10 20 30
....*....|....*....|....*....|
gi 203096504 302 NGSTPMHKAAGQGHIDCLQWLVEMGADSNI 331
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
37-258 |
6.41e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 42.29 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 37 DAVRAGDVKQLSDIVERGANVNeVDALHQFTPLHWAAHSGSLECLHWLLWNGADATQTTTRGWTAAHVAAIRGQDACLQA 116
Cdd:PHA02875 8 DAILFGELDIARRLLDIGINPN-FEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 117 LIINGANLatqDD----RGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCGIED 192
Cdd:PHA02875 87 LLDLGKFA---DDvfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 203096504 193 VDYNGNLPVHLAAMEGHLHCFKFLLSR--------VNSAVQALKAFNDNgeNVLDLAHRFLKQ----NIVQFIQGAEY 258
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSganidyfgKNGCVAALCYAIEN--NKIDIVRLFIKRgadcNIMFMIEGEEC 239
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
64-90 |
6.86e-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: 37.18 E-value: 6.86e-04
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
402-508 |
7.16e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 402 RMRAHKKIVELRQLLEIAEsnfkhlggitEEDLKQKKELLESKKTITELQEQLAYERLRREKLECQLDEYRVEVNQLKEA 481
Cdd:pfam20492 1 REEAEREKQELEERLKQYE----------EETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES 70
|
90 100
....*....|....*....|....*..
gi 203096504 482 LEKIQVpSAEAMEDDSCEYSKEKRRMK 508
Cdd:pfam20492 71 AEMEAE-EKEQLEAELAEAQEEIARLE 96
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
117-337 |
1.20e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.36 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 117 LIINGANLATQDDRGCTPVHLAATHGHSFSLQV---MLRSGVDPSVTDKREWRpvhyaafhgrlgCLQLLVKWGCGIE-- 191
Cdd:PHA02798 95 LIENGADINKKNSDGETPLYCLLSNGYINNLEIllfMIENGADTTLLDKDGFT------------MLQVYLQSNHHIDie 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 192 ----------DVDYNGNlpvhlaaMEGH--LHC-FKFLLSRVNsaVQALKAFNDNGEnvldLAHRFLKQNIVQFIqgaEY 258
Cdd:PHA02798 163 iiklllekgvDINTHNN-------KEKYdtLHCyFKYNIDRID--ADILKLFVDNGF----IINKENKSHKKKFM---EY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 259 EGSHLDDQddlafpghvaafkgdlEMLKKLIDDGV---INLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKA 335
Cdd:PHA02798 227 LNSLLYDN----------------KRFKKNILDFIfsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITEL 290
|
..
gi 203096504 336 GE 337
Cdd:PHA02798 291 GN 292
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
122-171 |
1.33e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 1.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 203096504 122 ANLATQDDRGCTPVHLAATHGHSFSLQVMLRSGVDPSVTDKREWRPVHYA 171
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
283-355 |
1.42e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 41.10 E-value: 1.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 203096504 283 EMLKKLIDDGvINLNERDENGSTPMHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLL 355
Cdd:PHA02874 105 DMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
307-371 |
2.29e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.40 E-value: 2.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 203096504 307 MHKAAGQGHIDCLQWLVEMGADSNITNKAGERPSDVAKRFAHLAAVKLLegLQKYEIDDIEGDKN 371
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDNGRT 63
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
64-95 |
4.46e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.96 E-value: 4.46e-03
10 20 30
....*....|....*....|....*....|...
gi 203096504 64 HQFTPLHWAA-HSGSLECLHWLLWNGADATQTT 95
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
407-486 |
4.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 407 KKIVELRQLLEIAESNFKHLggitEEDLKQ-KKELLESKKTITELQEQLAYERLRREKLECQLDEYRVEVNQLKEALEKI 485
Cdd:COG4372 45 EELEQLREELEQAREELEQL----EEELEQaRSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
.
gi 203096504 486 Q 486
Cdd:COG4372 121 Q 121
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-509 |
7.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 407 KKIVELRQLLEIAESNFKHLGGITEEDLKQKKELLESKKTITELQEQLAYERLRREKLECQLDEYRVEVNQLKEALEKiq 486
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-- 291
|
90 100
....*....|....*....|...
gi 203096504 487 VPSAEAMEDDSCEYSKEKRRMKK 509
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEK 314
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
196-219 |
9.02e-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: 34.10 E-value: 9.02e-03
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
344-487 |
9.94e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.07 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 203096504 344 KRFAHLAA--------VKLLEGLQK--YEIDDI-EGDKNHISFFIrhgvEGSTDAKDDLSlsesDKANARMRahkKIVEL 412
Cdd:smart00787 123 KTFARLEAkkmwyewrMKLLEGLKEglDENLEGlKEDYKLLMKEL----ELLNSIKPKLR----DRKDALEE---ELRQL 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 203096504 413 RQLL-EIAESNFKHLGGITEEDLKQKKELLESKKTITELQEQLAYERLRREKLECQLDEYRVEVNQLKEALEKIQV 487
Cdd:smart00787 192 KQLEdELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
|