|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
32-883 |
0e+00 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 644.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 32 EHDDGSMYSLTGGAP--LPPLGDFGAKRTKLRRR--TISPNDRRYRWWQMFLVVLVFYTAWVSPFEFGFLN-EPLRPLSI 106
Cdd:PLN03192 17 EEDDSGSLSLRNLSKviLPPLGVPSYNQNHIGSDgwIISPMDSRYRWWETLMVVLVAYSAWVYPFEVAFLNaSPKRGLEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 107 TDNVVNIIFFFDIWLTFFVAYYDKTTYLLVDSHGPIARRYLRTWFLFDLVSTIPYELAHRLFP---RLD-TYGYFGMLRL 182
Cdd:PLN03192 97 ADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITgtvKLNlSYSLLGLLRF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 183 WRLRRVSAMFARLEKDRHYNYFWLRCSKFICVTLFVVHNGACIFYFLADHYAKDlSTTWLGLVPDAVDKKNTMSLYVASV 262
Cdd:PLN03192 177 WRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQ-GKTWIGAVIPNFRETSLWIRYISAI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 263 YWSIITVSTVGYGDLHPVNTREMLFDIFFILFNQGLTAYIIGNMTNLAVHATSRTRQYRYTVQAAANFARRNKIPIHLEE 342
Cdd:PLN03192 256 YWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVGRNRLPPRLKD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 343 QMLSHLFMKYRTdlEGVQQQEIIDSLPKAIQSSISYYLFFSMMDNVYLFKGVSKDLIFQLVTEMKAEYFPPKEDVILDNE 422
Cdd:PLN03192 336 QILAYMCLRFKA--ESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAEYIPPREDVIMQNE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 423 APTDFYIFVTGAAELIKRVNGVEHVVGKVHAKDLVGEVGVLCYRPQPYTVRTKRLSQILRLSRATFLNILHSSVGDGTII 502
Cdd:PLN03192 414 APDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLIEAMQTRQEDNVVI 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 503 MNNFLNH------LQTSDIPGlDAILEETEAMLARGktdlpISTCFAAGRSDkrLLQRLLKKGSDPNETDRNGRTALHIS 576
Cdd:PLN03192 494 LKNFLQHhkelhdLNVGDLLG-DNGGEHDDPNMASN-----LLTVASTGNAA--LLEELLKAKLDPDIGDSKGRTPLHIA 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 577 ASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLIDKGADIFCVDAGHLACSAVDKNSIELLKELKELG 656
Cdd:PLN03192 566 ASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQG 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 657 VDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKVDMQDDHgwtpralaenqghdeiknifqnikenkqtapvspipED 736
Cdd:PLN03192 646 LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD------------------------------------DD 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 737 GTPNvssfqsapvmpdargSLDNMLQppnQEELpwldSHRRQRANTfhnsifgMISAANYDKKDLGVSESRITNTANMNG 816
Cdd:PLN03192 690 FSPT---------------ELRELLQ---KREL----GHSITIVDS-------VPADEPDLGRDGGSRPGRLQGTSSDNQ 740
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 817 IVARVTL-----------ICPEKGehavKLAFLPDSLEELLDIGAKKFDFSPTK--ILTKEGAEIDDIDLIRDGDHLIIA 883
Cdd:PLN03192 741 CRPRVSIykghpllrnerCCNEAG----KLINLPPSLEELKAIAGEKLGFDARKamVTNEEGAEIDSIEVIRDNDKLFVV 816
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
72-318 |
9.55e-39 |
|
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 144.33 E-value: 9.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 72 YRWWQMFLVVLVFYTAWVSPFEFGFLNEP--LRPLSITDNVVNIIFFFDIWLTFFVAYYDkttyllvdshgpiaRRYLRT 149
Cdd:pfam00520 1 SRYFELFILLLILLNTIFLALETYFQPEEplTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFRS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 150 -WFLFDLVSTIPYELAHRLFpRLDTYGYFGMLRLWRLRRVSAMFARLEKDRHYNYFWLRCSKFICVTLFVVHNGACIFYF 228
Cdd:pfam00520 67 pWNILDFVVVLPSLISLVLS-SVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 229 LADHYAKDLSTTWlglvPDAVDKKNTMSLYVASVYWSIITVSTVGYGDLHPVNTREM-------LFDIFFILFNQGLTAY 301
Cdd:pfam00520 146 IGYQLFGGKLKTW----ENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNL 221
|
250
....*....|....*..
gi 357466307 302 IIGNMTNLAVHATSRTR 318
Cdd:pfam00520 222 FIAVIIDNFQELTERTE 238
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
483-728 |
2.68e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 144.71 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 483 LSRATFLNILHSSVGDGTIIMNNFLNHLQTSDIPGLDAILEETEAMLARGKTDLPISTCFAAGRSDKRLLQRLLKKGSDP 562
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 563 NETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLIDKGADIFCVDAG-----HLA 637
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDgntplHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 638 CSavdKNSIELLKELKELGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKVDMQDDHGWTPRALAENQGHDEIKNI 717
Cdd:COG0666 161 AA---NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
|
250
....*....|.
gi 357466307 718 FQNIKENKQTA 728
Cdd:COG0666 238 LLEAGADLNAK 248
|
|
| KHA |
pfam11834 |
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ... |
820-882 |
1.88e-24 |
|
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus.
Pssm-ID: 463367 Cd Length: 65 Bit Score: 97.14 E-value: 1.88e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357466307 820 RVTLICPEKGEHAV-KLAFLPDSLEELLDIGAKKFDFSPTKILTKEGAEIDDIDLIRDGDHLII 882
Cdd:pfam11834 2 RVTIFPNHDGKRRNgKLIWLPDSLEELLKIASEKFGISATKILTEDGAEIDDIDVIRDGDHLYL 65
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
390-493 |
2.91e-21 |
|
effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels
Pssm-ID: 237999 [Multi-domain] Cd Length: 115 Bit Score: 89.69 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 390 LFKGVSKDLIFQLVTEMKAEYFPPKEDVILDNEAPTDFYIFVTGAAELIKR-VNGVEHVVGKVHAKDLVGEVGVLCYRPQ 468
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLdEDGREQIVGFLGPGDLFGELALLGNGPR 80
|
90 100
....*....|....*....|....*
gi 357466307 469 PYTVRTKRLSQILRLSRATFLNILH 493
Cdd:cd00038 81 SATVRALTDSELLVLPRSDFRRLLQ 105
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
550-702 |
4.01e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 94.71 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 550 RLLQRLLKKGSDPNETDRNGRTALHISASNGN--ESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVK--KMLIDKG 625
Cdd:PHA03095 98 DVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 626 ADIFCVDA------GHLACSAVDKNSIelLKELKELGVDVTKPEMSGITALHKAV---SDRNVEMVKFLLDlGAKVDMQD 696
Cdd:PHA03095 178 ADVYAVDDrfrsllHHHLQSFKPRARI--VRELIRAGCDPAATDMLGNTPLHSMAtgsSCKRSLVLPLLIA-GISINARN 254
|
....*.
gi 357466307 697 DHGWTP 702
Cdd:PHA03095 255 RYGQTP 260
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
390-494 |
8.86e-18 |
|
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.
Pssm-ID: 197516 [Multi-domain] Cd Length: 120 Bit Score: 80.14 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 390 LFKGVSKDLIFQLVTEMKAEYFPPKEDVILDNEAPTDFYIFVTGAAELIKR-VNGVEHVVGKVHAKDLVGEVGVLCYRPQ 468
Cdd:smart00100 1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVlEDGEEQIVGTLGPGDFFGELALLTNSRR 80
|
90 100
....*....|....*....|....*...
gi 357466307 469 PY--TVRTKRLSQILRLSRATFLNILHS 494
Cdd:smart00100 81 AAsaAAVALELATLLRIDFRDFLQLLPE 108
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
546-727 |
8.30e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 83.95 E-value: 8.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 546 RSDKRLLQRLLKKGSDPNETDRNGRTALHISASN--GNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVK--KML 621
Cdd:PHA03100 83 TDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKilKLL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 622 IDKGADIfcvDAghlacsavdKNSIELLKELkelGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKVDMQDDHGWT 701
Cdd:PHA03100 163 IDKGVDI---NA---------KNRVNYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
|
170 180
....*....|....*....|....*.
gi 357466307 702 PRALAENQGHDEIKNIFQNIKENKQT 727
Cdd:PHA03100 228 PLHIAILNNNKEIFKLLLNNGPSIKT 253
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
542-632 |
4.86e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.00 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 542 FAAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFgADPNAKDlDGNIPLWEAMIGGHESVKKML 621
Cdd:pfam12796 3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLL 80
|
90
....*....|.
gi 357466307 622 IDKGADIFCVD 632
Cdd:pfam12796 81 LEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
573-696 |
3.34e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 573 LHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLIDKgADIFCVDAGHlacsavdknsiellkel 652
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR----------------- 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 357466307 653 kelgvdvtkpemsgiTALHKAVSDRNVEMVKFLLDLGAKVDMQD 696
Cdd:pfam12796 63 ---------------TALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
538-714 |
4.29e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 75.41 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 538 ISTCFAAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESV 617
Cdd:PHA02875 4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 618 KKMLIDKGA---DIFCVDAGHLACSAVDKNSIELLKELKELGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKVDM 694
Cdd:PHA02875 84 VEELLDLGKfadDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
|
170 180
....*....|....*....|
gi 357466307 695 QDDHGWTPRALAENQGHDEI 714
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAI 183
|
|
| cNMP_binding |
pfam00027 |
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
409-495 |
1.93e-13 |
|
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 459637 [Multi-domain] Cd Length: 89 Bit Score: 66.48 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 409 EYFPPKEDVILDNEAPTDFYIFVTGAAELIKR-VNGVEHVVGKVHAKDLVGEVGVLCYRPQPYTVRTKRLSQILRLSRAT 487
Cdd:pfam00027 2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTlEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81
|
....*...
gi 357466307 488 FLNILHSS 495
Cdd:pfam00027 82 FLELLERD 89
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
554-702 |
1.21e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 71.21 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 554 RLLKKGSDPNETDRNGRTALHISASNGNE---SFVTLLLKFGADPNAKDLDGNIPL-WEAMIGGHESVKKMLIDKGADI- 628
Cdd:PHA03095 32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 629 FCVDAG------HLACSAVDKNSIELlkeLKELGVDVTKPEMSGITALHKAVSDRN--VEMVKFLLDLGAKVDMQDDHGW 700
Cdd:PHA03095 112 AKDKVGrtplhvYLSGFNINPKVIRL---LLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFR 188
|
..
gi 357466307 701 TP 702
Cdd:PHA03095 189 SL 190
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
501-706 |
5.19e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.14 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 501 IIMNNFLNHLQTSDIPGLDAILEE-------TEAMLARG-----KTDLPISTC--FAAGRSDKRLLQRLLKKGSDPNETD 566
Cdd:PHA02878 119 IILTNRYKNIQTIDLVYIDKKSKDdiieaeiTKLLLSYGadinmKDRHKGNTAlhYATENKDQRLTELLLSYGANVNIPD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 567 RNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLweamiggHESVKKMLidkgadifcvdaghlacsavdknSI 646
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL-------HISVGYCK-----------------------DY 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357466307 647 ELLKELKELGVDVT-KPEMSGITALHKAVSDRNVemVKFLLDLGAKVDMQDDHGWTPRALA 706
Cdd:PHA02878 249 DILKLLLEHGVDVNaKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
536-633 |
6.93e-12 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 69.16 E-value: 6.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 536 LPISTCFAAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHE 615
Cdd:PTZ00322 82 LTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161
|
90
....*....|....*...
gi 357466307 616 SVKKMLIDKGADIFCVDA 633
Cdd:PTZ00322 162 EVVQLLSRHSQCHFELGA 179
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
550-712 |
8.42e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 65.86 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 550 RLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLIDKGADIF 629
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 630 CVDAGHLacSAVDKNSIELLKELKELGVDVTKPEMSGITALHKAVSDRNV-EMVKFLLDLGAKVDMQDDHGWTPRALAEN 708
Cdd:PHA02876 239 KNDLSLL--KAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAK 316
|
....
gi 357466307 709 QGHD 712
Cdd:PHA02876 317 NGYD 320
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
542-633 |
9.89e-11 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 63.82 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 542 FAAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKML 621
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
|
90
....*....|..
gi 357466307 622 IDKGADIFCVDA 633
Cdd:COG0666 272 LLALLLLAAALL 283
|
|
| KHA |
cd17073 |
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ... |
820-883 |
1.01e-10 |
|
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found in potassium channel tetramerization domain containing 9 (KCTD9) and similar proteins; This family corresponds to KHA, the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins, mainly found in vertebrates KCTD9 and plants AKT proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus. KHA shows high sequence similarity with doublecortin-like domain, which has a stable ubiquitin-like tertiary fold. KCTD9, also termed BTB/POZ domain-containing protein 9, belongs to the KCTD protein family, which corresponds to potassium channel tetramerization domain proteins, a class of BTB-domain-containing proteins. It is involved in potassium channel formation. Moreover, KCTD9 contributes to liver injury through NK cell activation during hepatitis B virus (HBV)-induced acute-on-chronic liver failure. AKT proteins play crucial roles in K+ uptake and translocation in plant cells.
Pssm-ID: 340593 Cd Length: 65 Bit Score: 58.00 E-value: 1.01e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357466307 820 RVTLI---CPEKGehavKLAFLPDSLEELLDIGAKKFDFSPTKILTKEGAEIDDIDLIRDGDHLIIA 883
Cdd:cd17073 2 RVTVFvngSSSGG----KVIALPSTLSELLKIASEKLGIPAKRLYTGSGGEIDDIALIRDDDVLYVS 64
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
640-714 |
1.15e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.59 E-value: 1.15e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357466307 640 AVDKNSIELLKELKELGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDlGAKVDMQdDHGWTPRALAENQGHDEI 714
Cdd:pfam12796 4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEI 76
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
540-730 |
3.13e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 63.44 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 540 TCFAAGrsDKRLLQRLLK-KGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVK 618
Cdd:PHA02874 7 MCIYSG--DIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 619 KMLIDKGadifcVDAGHLACSAVDKnsiELLKELKELGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKVDMQDDH 698
Cdd:PHA02874 85 KLLIDNG-----VDTSILPIPCIEK---DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 357466307 699 GWTPRALAENQGHDEI------KNIFQNIKENKQTAPV 730
Cdd:PHA02874 157 GCYPIHIAIKHNFFDIikllleKGAYANVKDNNGESPL 194
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
548-702 |
6.35e-10 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 62.38 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 548 DKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKK--MLIDKG 625
Cdd:PHA02946 51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERinLLVQYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 626 ADI-FCVD----AGHLACSavdKNSIELLKELKELGVDVTKPEMSGITALHKAVSDRN--VEMVKFLLDLGAKVDMQDDH 698
Cdd:PHA02946 131 AKInNSVDeegcGPLLACT---DPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHD 207
|
....
gi 357466307 699 GWTP 702
Cdd:PHA02946 208 GNTP 211
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
541-589 |
7.01e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 7.01e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 357466307 541 CFAAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLL 589
Cdd:pfam13637 6 HAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
391-511 |
1.54e-09 |
|
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];
Pssm-ID: 440428 [Multi-domain] Cd Length: 207 Bit Score: 58.84 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 391 FKGVSKDLIFQLVTEMKAEYFPPKEDVILDNEAPTDFYIFVTGAAELIKRV-NGVEHVVGKVHAKDLVGEVGVLCYRPQP 469
Cdd:COG0664 1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISeDGREQILGFLGPGDFFGELSLLGGEPSP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 357466307 470 YTVRTKRLSQILRLSRATFLNILHSSVGdgtiIMNNFLNHLQ 511
Cdd:COG0664 81 ATAEALEDSELLRIPREDLEELLERNPE----LARALLRLLA 118
|
|
| Ion_trans_2 |
pfam07885 |
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
258-311 |
1.61e-09 |
|
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
Pssm-ID: 462301 [Multi-domain] Cd Length: 78 Bit Score: 54.97 E-value: 1.61e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 357466307 258 YVASVYWSIITVSTVGYGDLHPVNTREMLFDIFFILFNQGLTAYIIGNMTNLAV 311
Cdd:pfam07885 24 FLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLT 77
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
547-720 |
6.83e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 59.69 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 547 SDKRLLQRLLKKGSDPNETDRNGRTALHISASNG--NESFVTLLLKfGADPNAKDLDGNIPLWEA-MIGGHESVKKMLID 623
Cdd:PHA02876 285 SLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGydTENIRTLIML-GADVNAADRLYITPLHQAsTLDRNKDIVITLLE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 624 KGADI----FCvDAGHLACSAVdKNSIELLKELKELGVDVTKPEMSGITALHKAVSDRNVEM-VKFLLDLGAKVDMQDDH 698
Cdd:PHA02876 364 LGANVnardYC-DKTPIHYAAV-RNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKD 441
|
170 180
....*....|....*....|....
gi 357466307 699 GWTP--RALAENQGHDEIKNIFQN 720
Cdd:PHA02876 442 LSTPlhYACKKNCKLDVIEMLLDN 465
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
548-702 |
1.08e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.44 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 548 DKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLIDKGA- 626
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAy 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 627 ----DIFCVDAGHLACSAVDKNSIELlkeLKELGVDVTKPEMSGITALHKAVSdRNVEMVKFLLDlGAKVDMQDDHGWTP 702
Cdd:PHA02874 183 anvkDNNGESPLHNAAEYGDYACIKL---LIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLIN-NASINDQDIDGSTP 257
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
575-702 |
1.17e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 58.50 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 575 ISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKM---LIDKGADIFCVD---AGHLACSAVDKNSIEL 648
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPErcgFTPLHLYLYNATTLDV 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 357466307 649 LKELKELGVDVTKPEMSGITALHKAVSDRNV--EMVKFLLDLGAKVDMQDDHGWTP 702
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTP 155
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
486-693 |
3.06e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.38 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 486 ATFLNILHSSVGDGTIIMNNFLNHLQ----TSDIPGLDAILEETEAMlarGKTDLPISTCFAAGRSDKRLLqrLLKKGSD 561
Cdd:PHA02876 191 AKMVNLLLSYGADVNIIALDDLSVLEcavdSKNIDTIKAIIDNRSNI---NKNDLSLLKAIRNEDLETSLL--LYDAGFS 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 562 PNETDRNGRTALHISASNGNES-FVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVK-KMLIDKGADIFCVDAGHLA-- 637
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENiRTLIMLGADVNAADRLYITpl 345
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 357466307 638 --CSAVDKNSiELLKELKELGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKVD 693
Cdd:PHA02876 346 hqASTLDRNK-DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
543-624 |
6.30e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 56.19 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 543 AAGRSDKR-LLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKML 621
Cdd:PHA03095 230 ATGSSCKRsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309
|
...
gi 357466307 622 IDK 624
Cdd:PHA03095 310 LAK 312
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
551-658 |
1.74e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 54.61 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 551 LLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLIDKGADIFC 630
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
|
90 100 110
....*....|....*....|....*....|.
gi 357466307 631 VDAG---HLACSAVDKNSIELLKELKELGVD 658
Cdd:PHA02875 197 FGKNgcvAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
551-696 |
2.64e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 53.90 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 551 LLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPL-----WEAMIGGHESVKKMLIDKG 625
Cdd:PHA03100 17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYG 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357466307 626 ADIFCVDAGH----LACSAVDKNSIELLKELKELGVDVTKPEMSGITALHKAVS--DRNVEMVKFLLDLGAKVDMQD 696
Cdd:PHA03100 97 ANVNAPDNNGitplLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKN 173
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
652-706 |
4.59e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 4.59e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 357466307 652 LKELGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKVDMQDDHGWTPRALA 706
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
670-728 |
4.98e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.57 E-value: 4.98e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357466307 670 LHKAVSDRNVEMVKFLLDLGAKVDMQDDHGWTPRALAENQGHDE-----IKNIFQNIKENKQTA 728
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEivkllLEHADVNLKDNGRTA 64
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
542-702 |
5.21e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 53.04 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 542 FAAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKML 621
Cdd:PHA02874 130 YAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 622 IDKGADIF--CVDAGHLACSAV--DKNSIELLkeLKELGVDVTkpEMSGITALHKAVSDR-NVEMVKFLLDLGAKVDMQD 696
Cdd:PHA02874 210 IDHGNHIMnkCKNGFTPLHNAIihNRSAIELL--INNASINDQ--DIDGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285
|
....*.
gi 357466307 697 DHGWTP 702
Cdd:PHA02874 286 NKGENP 291
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
569-622 |
6.10e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 6.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 357466307 569 GRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLI 622
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
569-686 |
1.53e-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: 51.94 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 569 GRTALHISASNGNESFVTLLLKFGAD------------PNAKDL--DGNIPLWEAMIGGHESVKKMLIDKGADIFCVDA- 633
Cdd:cd22192 89 GETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSl 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357466307 634 -----GHLACSAVDKNSIELL-------KELKELGVDvTKPEMSGITALHKAVSDRNVEMVKFLL 686
Cdd:cd22192 169 gntvlHILVLQPNKTFACQMYdlilsydKEDDLQPLD-LVPNNQGLTPFKLAAKEGNIVMFQHLV 232
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
568-599 |
3.72e-06 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.20 E-value: 3.72e-06
10 20 30
....*....|....*....|....*....|...
gi 357466307 568 NGRTALHISA-SNGNESFVTLLLKFGADPNAKD 599
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
635-686 |
5.33e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 5.33e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 357466307 635 HLACSAVDKNSIELLKELKELGVDVTKPEMSGITALHKAVSDRNVEMVKFLL 686
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
555-606 |
7.45e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 7.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 357466307 555 LLKKGS-DPNETDRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPL 606
Cdd:pfam13857 1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
543-705 |
9.04e-06 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 49.28 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 543 AAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNGNESF--VTLLLKFGAD-PNAKDLDGNIPLWeAMIGGHESVKK 619
Cdd:PHA02946 79 ASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKiNNSVDEEGCGPLL-ACTDPSERVFK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 620 MLIDKGADIFCVD---AGHLACSAVDKN-SIELLKELKELGVDVTKPEMSGITALHKAVSD--RNVEMVKFLLDlGAKVD 693
Cdd:PHA02946 158 KIMSIGFEARIVDkfgKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVN 236
|
170
....*....|..
gi 357466307 694 MQDDHGWTPRAL 705
Cdd:PHA02946 237 KQNKFGDSPLTL 248
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
543-722 |
1.45e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.45 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 543 AAGRSDKRLLQRLLKKGSDPNET-DRNGRTALHISASNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKML 621
Cdd:PHA02875 75 AVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 622 IDKGADIFCVDAghLACS----AVDKNSIELLKELKELGVDVTKPEMSG-ITALHKAVSDRNVEMVKFLLDLGAKVDMQd 696
Cdd:PHA02875 155 IDHKACLDIEDC--CGCTpliiAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIM- 231
|
170 180
....*....|....*....|....*....
gi 357466307 697 dhgwtprALAENQGH---DEIKNIFQNIK 722
Cdd:PHA02875 232 -------FMIEGEECtilDMICNMCTNLE 253
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
668-702 |
2.62e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 2.62e-05
10 20 30
....*....|....*....|....*....|....*
gi 357466307 668 TALHKAVSDRNVEMVKFLLDLGAKVDMQDDHGWTP 702
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
542-702 |
4.86e-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: 46.93 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 542 FAAGRSDKRLLQRLLK-KGSDPNETDRNGRTALHISASNGNESFVTLLLKfgadpNAKDLdGNIPLWEAMIGGHESVkkm 620
Cdd:cd22192 23 LAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME-----AAPEL-VNEPMTSDLYQGETAL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 621 lidkgadifcvdagHLacsAVDKNSIELLKELKELGVDVTKPEMSGiTALHK---------------AVSDRNVEMVKFL 685
Cdd:cd22192 94 --------------HI---AVVNQNLNLVRELIARGADVVSPRATG-TFFRPgpknliyygehplsfAACVGNEEIVRLL 155
|
170
....*....|....*..
gi 357466307 686 LDLGAKVDMQDDHGWTP 702
Cdd:cd22192 156 IEHGADIRAQDSLGNTV 172
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
568-597 |
6.02e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.65 E-value: 6.02e-05
10 20 30
....*....|....*....|....*....|
gi 357466307 568 NGRTALHISASNGNESFVTLLLKFGADPNA 597
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
554-654 |
1.04e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 45.81 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 554 RLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLKFGadPNAKDLDGNIPLWEAMIGGHESVKKMLIDKGADIFCVDA 633
Cdd:PHA03100 210 YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG--PSIKTIIETLLYFKDKDLNTITKIKMLKKSIMYMFLLDP 287
|
90 100
....*....|....*....|.
gi 357466307 634 GhlacSAVDKNSIELLKELKE 654
Cdd:PHA03100 288 G----FYKNRKLIENSKSLKD 304
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
614-752 |
2.43e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 614 HESVKKMLIDKG-ADIFCVDAGHLACSAvDKNSIELLKELkelGVDVTKPEMSGITALHKAVSDRNVEMVKFLLDLGAKV 692
Cdd:PTZ00322 66 HNLTTEEVIDPVvAHMLTVELCQLAASG-DAVGARILLTG---GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357466307 693 DMQDDHGWTPRALAENQGHDEIKNIFQNIKENKQTAPVSPIPEDGTPNVSSFQSAPVM---PD 752
Cdd:PTZ00322 142 TLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFTGKPPSLEDSPISshhPD 204
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
666-697 |
2.63e-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: 38.81 E-value: 2.63e-04
10 20 30
....*....|....*....|....*....|...
gi 357466307 666 GITALHKAVSDR-NVEMVKFLLDLGAKVDMQDD 697
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
666-694 |
4.59e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.34 E-value: 4.59e-04
10 20
....*....|....*....|....*....
gi 357466307 666 GITALHKAVSDRNVEMVKFLLDLGAKVDM 694
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
666-694 |
4.98e-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: 38.01 E-value: 4.98e-04
10 20
....*....|....*....|....*....
gi 357466307 666 GITALHKAVSDRNVEMVKFLLDLGAKVDM 694
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
551-644 |
5.56e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 551 LLQRLLKKGSDPNETDRNGRTALHISASNGNESF--VTLLLKFGADPNAKDLDGNIPLWE-AMIGGHESVKKMLIDKGAD 627
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRInvIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSLGID 184
|
90
....*....|....*..
gi 357466307 628 IFCVDAGHLACSAVDKN 644
Cdd:PHA02859 185 INETNKSGYNCYDLIKF 201
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
542-702 |
7.59e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 43.13 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 542 FAAGRSDKRLLQRLLKKGSDPNETDRNGRTALHISASNG---------------------------NESFVTLLLKF--G 592
Cdd:PHA02876 184 YAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnidtikaiidnrsninkndlsllkairNEDLETSLLLYdaG 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 593 ADPNAKDLDGNIPLWEAMIGGHES--VKKMLiDKGADIFCVD-AGHLACSAVDKN--SIELLKELKELGVDVTKPEMSGI 667
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASQAPSLSrlVPKLL-ERGADVNAKNiKGETPLYLMAKNgyDTENIRTLIMLGADVNAADRLYI 342
|
170 180 190
....*....|....*....|....*....|....*.
gi 357466307 668 TALHKAVS-DRNVEMVKFLLDLGAKVDMQDDHGWTP 702
Cdd:PHA02876 343 TPLHQASTlDRNKDIVITLLELGANVNARDYCDKTP 378
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
537-668 |
7.66e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 41.73 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 537 PISTCFAAGRSDKRLLQRLLKKGSDPN-ETDRNGRTALHISAS---NGNESFVTLLLKFGADPNAKDLDGNIPLWEAM-- 610
Cdd:PHA02859 54 PIFSCLEKDKVNVEILKFLIENGADVNfKTRDNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHMYMcn 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357466307 611 IGGHESVKKMLIDKGADIFCVDAghlacsavDKNSI-----------ELLKELKELGVDVTKPEMSGIT 668
Cdd:PHA02859 134 FNVRINVIKLLIDSGVSFLNKDF--------DNNNIlysyilfhsdkKIFDFLTSLGIDINETNKSGYN 194
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
568-597 |
9.80e-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: 37.24 E-value: 9.80e-04
10 20 30
....*....|....*....|....*....|
gi 357466307 568 NGRTALHISASNGNESFVTLLLKFGADPNA 597
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
551-689 |
1.22e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.51 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 551 LLQRLLKKGSDPNETDRNGRTALHISASNGNE-----SFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKML---I 622
Cdd:PHA02798 53 IVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmI 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357466307 623 DKGADIFCVDAGHLACSAVDKNS-----IELLKELKELGVDV-TKPEMSGITALH----KAVSDRNVEMVKFLLDLG 689
Cdd:PHA02798 133 ENGADTTLLDKDGFTMLQVYLQSnhhidIEIIKLLLEKGVDInTHNNKEKYDTLHcyfkYNIDRIDADILKLFVDNG 209
|
|
| PRK10537 |
PRK10537 |
voltage-gated potassium channel protein; |
259-315 |
1.75e-03 |
|
voltage-gated potassium channel protein;
Pssm-ID: 236711 [Multi-domain] Cd Length: 393 Bit Score: 41.55 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 357466307 259 VASVYWSIITVSTVGYGDLHPVNTREMLFDIFFIlfnqgltayIIGnmtnLAVHATS 315
Cdd:PRK10537 170 STAFYFSIVTMSTVGYGDIVPVSESARLFTISVI---------ILG----ITVFATS 213
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
546-633 |
2.09e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.55 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 546 RSDKRLLQRLLKKGSDPNETDRNGRTALHISA--SNGNESFVTLLLKFGADPNAKDLDGNIPLWEAMIGGHESVKKMLID 623
Cdd:PHA03095 199 KPRARIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIA 278
|
90
....*....|
gi 357466307 624 KGADIFCVDA 633
Cdd:PHA03095 279 LGADINAVSS 288
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
551-696 |
3.49e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.02 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 551 LLQRLLKKGSDPNETDRNGRTALHISASNGNESFVTLLLkfgADPNAKDLDGNIPLWEAMIGGH--ESVKKMLIDKGADI 628
Cdd:PHA02878 52 VVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRnvEIFKIILTNRYKNI 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357466307 629 FCVDAGHLaCSAVDKNSIE--LLKELKELGVDVT-KPEMSGITALHKAVSDRNVEMVKFLLDLGAKVDMQD 696
Cdd:PHA02878 129 QTIDLVYI-DKKSKDDIIEaeITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
619-699 |
8.73e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 38.65 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357466307 619 KMLIDKGADIFCVDAGHLACS-----AVDKN-SIELLKELKELGVDVTKPEMSGITALHKAVSDRNV--EMVKFLLDLGA 690
Cdd:PHA02859 70 KFLIENGADVNFKTRDNNLSAlhhylSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSGV 149
|
....*....
gi 357466307 691 KVDMQDDHG 699
Cdd:PHA02859 150 SFLNKDFDN 158
|
|
| |
