|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
20-811 |
0e+00 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 1562.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 20 KREDHSRKSLKKPEEKQHDDSKPFNSRNLSKVILPPLGVSSYNQNPLAPKGWIISPMDSRYRCWETFMVVLVAYSLWIYP 99
Cdd:PLN03192 1 FQSTGSAGGGRGKGTGEEDDSGSLSLRNLSKVILPPLGVPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 100 FQVAFLKASPNRQLYITDNVVDLFFAVDIVLTFFVAYIDRRTQLLVCDWRKIAVRYLSTWFLMDMASTMPFEALGSLITG 179
Cdd:PLN03192 81 FEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 180 KQKVGLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWVRCARLLSVTLFLVHCAGCLYYLLADRYPHQGKTWIGAVIP 259
Cdd:PLN03192 161 TVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 260 NFRETSLWIRYISALYWSITTMTTVGYGDMHAVNTMEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 339
Cdd:PLN03192 241 NFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 340 SNFVCRNRLPPRLKEQILAYMCLRFKAESLNQHQLIEQLPKSICKSICQHLFLPTVEKVYLFKGISREILLLLVAKMKAE 419
Cdd:PLN03192 321 SNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 420 YIPPREDVIMQNEAPDDVYIIVSGEVEIIDYEGEKEHVVGTLQSADMFGEVGALCCRPQTYTFRTKTLSQLLRLKTSALI 499
Cdd:PLN03192 401 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 500 EAMQTKKEDNVIILKNFLQHHKRLKDLNIGDLLVENGEEDVNPNMAFNLLTVASTGNAAFLDELLKAKLDPDIGDSKGRT 579
Cdd:PLN03192 481 EAMQTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 580 PLHIAASKGHEDCVMVLLKHACNVHVRD------------------------------PYTSGDLLCTAAKRNDLTAMKE 629
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDangntalwnaisakhhkifrilyhfasisdPHAAGDLLCTAAKRNDLTAMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 630 LLKQGLNIDSKNRQGLTAIQIAMAEDHTDMVKLLVMNGADVIHANTYE-FSSETLNEMLQKREMGHRIMVPDTLPTDHET 708
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPTELRELLQKRELGHSITIVDSVPADEPD 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 709 LLRDQGGEKEFNTNGGFKGTNVPRVSIYRGHPLQRKESCCTEAGRLIRLPNSLMELKAIAGEKLGFDARNAMVTNEEGAE 788
Cdd:PLN03192 721 LGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAE 800
|
810 820
....*....|....*....|...
gi 1104537548 789 IDSIEVIRDNDTLFLVEDPNSLM 811
Cdd:PLN03192 801 IDSIEVIRDNDKLFVVEDEDSRR 823
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
80-330 |
1.77e-41 |
|
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: 151.65 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 80 YRCWETFMVVLVAYSLWIYPFQVAFLKASPNRQ-LYITDNVVDLFFAVDIVLTFFVAYIDRRtqllvcdwrkiavrYL-S 157
Cdd:pfam00520 1 SRYFELFILLLILLNTIFLALETYFQPEEPLTTvLEILDYVFTGIFTLEMLLKIIAAGFKKR--------------YFrS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 158 TWFLMDMASTMPfealgSLITGKQKVGLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWVRCARLLSVTLFLVHCAGC 237
Cdd:pfam00520 67 PWNILDFVVVLP-----SLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 238 LYYLLADRYPHQ-GKTWIGAV--IPNFREtslwirYISALYWSITTMTTVGYGDMHAVNTMEM-------IFIIFYMLFN 307
Cdd:pfam00520 142 IFAIIGYQLFGGkLKTWENPDngRTNFDN------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215
|
250 260
....*....|....*....|...
gi 1104537548 308 LGLTAYLIGNMTNLVVEGTRRTM 330
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
489-676 |
3.25e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.44 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 489 QLLRLKTSALIEAMQTKKEDNVIILKNFLQHHKRLKDLNIGDLLVENGEEDVNPNMAFN--LLTVASTGNAAFLDELLKA 566
Cdd:COG0666 30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNtlLHAAARNGDLEIVKLLLEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 567 KLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPYtsGD-LLCTAAKRNDLTAMKELLKQGLNIDSKNRQGL 645
Cdd:COG0666 110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND--GNtPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187
|
170 180 190
....*....|....*....|....*....|.
gi 1104537548 646 TAIQIAMAEDHTDMVKLLVMNGADVIHANTY 676
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
400-513 |
5.32e-25 |
|
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: 100.48 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 400 LFKGISREILLLLVAKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEII-DYEGEKEHVVGTLQSADMFGEVGALCCRPQ 478
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1104537548 479 TYTFRTKTLSQLLRLKTSALIEAMQTKKEDNVIIL 513
Cdd:cd00038 81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
400-516 |
1.85e-22 |
|
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: 93.23 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 400 LFKGISREILLLLVAKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEII-DYEGEKEHVVGTLQSADMFGEVGAL--CCR 476
Cdd:smart00100 1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLtnSRR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1104537548 477 PQTYTFRTKTLSQLLRLKTSALIEAMQTKKEDNVIILKNF 516
Cdd:smart00100 81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
566-670 |
3.39e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.83 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 566 AKLDPDIGDSKGRTPLHIAASKG-HEDCVMVLLKHACNVHVrdpytsGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQ- 643
Cdd:TIGR00870 41 KKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPl 114
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1104537548 644 -------------GLTAIQIAMAEDHTDMVKLLVMNGADV 670
Cdd:TIGR00870 115 elandqytseftpGITALHLAAHRQNYEIVKLLLERGASV 154
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
20-811 |
0e+00 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 1562.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 20 KREDHSRKSLKKPEEKQHDDSKPFNSRNLSKVILPPLGVSSYNQNPLAPKGWIISPMDSRYRCWETFMVVLVAYSLWIYP 99
Cdd:PLN03192 1 FQSTGSAGGGRGKGTGEEDDSGSLSLRNLSKVILPPLGVPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 100 FQVAFLKASPNRQLYITDNVVDLFFAVDIVLTFFVAYIDRRTQLLVCDWRKIAVRYLSTWFLMDMASTMPFEALGSLITG 179
Cdd:PLN03192 81 FEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 180 KQKVGLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWVRCARLLSVTLFLVHCAGCLYYLLADRYPHQGKTWIGAVIP 259
Cdd:PLN03192 161 TVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 260 NFRETSLWIRYISALYWSITTMTTVGYGDMHAVNTMEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 339
Cdd:PLN03192 241 NFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 340 SNFVCRNRLPPRLKEQILAYMCLRFKAESLNQHQLIEQLPKSICKSICQHLFLPTVEKVYLFKGISREILLLLVAKMKAE 419
Cdd:PLN03192 321 SNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 420 YIPPREDVIMQNEAPDDVYIIVSGEVEIIDYEGEKEHVVGTLQSADMFGEVGALCCRPQTYTFRTKTLSQLLRLKTSALI 499
Cdd:PLN03192 401 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 500 EAMQTKKEDNVIILKNFLQHHKRLKDLNIGDLLVENGEEDVNPNMAFNLLTVASTGNAAFLDELLKAKLDPDIGDSKGRT 579
Cdd:PLN03192 481 EAMQTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 580 PLHIAASKGHEDCVMVLLKHACNVHVRD------------------------------PYTSGDLLCTAAKRNDLTAMKE 629
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDangntalwnaisakhhkifrilyhfasisdPHAAGDLLCTAAKRNDLTAMKE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 630 LLKQGLNIDSKNRQGLTAIQIAMAEDHTDMVKLLVMNGADVIHANTYE-FSSETLNEMLQKREMGHRIMVPDTLPTDHET 708
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPTELRELLQKRELGHSITIVDSVPADEPD 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 709 LLRDQGGEKEFNTNGGFKGTNVPRVSIYRGHPLQRKESCCTEAGRLIRLPNSLMELKAIAGEKLGFDARNAMVTNEEGAE 788
Cdd:PLN03192 721 LGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAE 800
|
810 820
....*....|....*....|...
gi 1104537548 789 IDSIEVIRDNDTLFLVEDPNSLM 811
Cdd:PLN03192 801 IDSIEVIRDNDKLFVVEDEDSRR 823
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
80-330 |
1.77e-41 |
|
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: 151.65 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 80 YRCWETFMVVLVAYSLWIYPFQVAFLKASPNRQ-LYITDNVVDLFFAVDIVLTFFVAYIDRRtqllvcdwrkiavrYL-S 157
Cdd:pfam00520 1 SRYFELFILLLILLNTIFLALETYFQPEEPLTTvLEILDYVFTGIFTLEMLLKIIAAGFKKR--------------YFrS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 158 TWFLMDMASTMPfealgSLITGKQKVGLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWVRCARLLSVTLFLVHCAGC 237
Cdd:pfam00520 67 PWNILDFVVVLP-----SLISLVLSSVGSLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 238 LYYLLADRYPHQ-GKTWIGAV--IPNFREtslwirYISALYWSITTMTTVGYGDMHAVNTMEM-------IFIIFYMLFN 307
Cdd:pfam00520 142 IFAIIGYQLFGGkLKTWENPDngRTNFDN------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215
|
250 260
....*....|....*....|...
gi 1104537548 308 LGLTAYLIGNMTNLVVEGTRRTM 330
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
489-676 |
3.25e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.44 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 489 QLLRLKTSALIEAMQTKKEDNVIILKNFLQHHKRLKDLNIGDLLVENGEEDVNPNMAFN--LLTVASTGNAAFLDELLKA 566
Cdd:COG0666 30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNtlLHAAARNGDLEIVKLLLEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 567 KLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPYtsGD-LLCTAAKRNDLTAMKELLKQGLNIDSKNRQGL 645
Cdd:COG0666 110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND--GNtPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187
|
170 180 190
....*....|....*....|....*....|.
gi 1104537548 646 TAIQIAMAEDHTDMVKLLVMNGADVIHANTY 676
Cdd:COG0666 188 TPLHLAAENGHLEIVKLLLEAGADVNAKDND 218
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
400-513 |
5.32e-25 |
|
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: 100.48 E-value: 5.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 400 LFKGISREILLLLVAKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEII-DYEGEKEHVVGTLQSADMFGEVGALCCRPQ 478
Cdd:cd00038 1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1104537548 479 TYTFRTKTLSQLLRLKTSALIEAMQTKKEDNVIIL 513
Cdd:cd00038 81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
491-679 |
1.47e-23 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 101.57 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 491 LRLKTSALIEAMQTKKEDNVIILKNFLQHHKRLKDLNIGDLLVENGEEDVNPNMAFNLLTVASTGNAAFLDELLKAKLDP 570
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 571 DIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPYTsGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQGLTAIQI 650
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180
....*....|....*....|....*....
gi 1104537548 651 AMAEDHTDMVKLLVMNGADVIHANTYEFS 679
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGET 188
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
400-516 |
1.85e-22 |
|
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: 93.23 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 400 LFKGISREILLLLVAKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEII-DYEGEKEHVVGTLQSADMFGEVGAL--CCR 476
Cdd:smart00100 1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLtnSRR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1104537548 477 PQTYTFRTKTLSQLLRLKTSALIEAMQTKKEDNVIILKNF 516
Cdd:smart00100 81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
|
|
| KHA |
pfam11834 |
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ... |
731-803 |
1.85e-21 |
|
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: 88.28 E-value: 1.85e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1104537548 731 PRVSIYRGHPLQRKEsccteaGRLIRLPNSLMELKAIAGEKLGFDARnaMVTNEEGAEIDSIEVIRDNDTLFL 803
Cdd:pfam11834 1 KRVTIFPNHDGKRRN------GKLIWLPDSLEELLKIASEKFGISAT--KILTEDGAEIDDIDVIRDGDHLYL 65
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
525-674 |
1.01e-17 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 84.62 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 525 DLNIGDLLVENGeedVNPNMAFN-----LLTVASTGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKH 599
Cdd:COG0666 132 NLEIVKLLLEAG---ADVNAQDNdgntpLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1104537548 600 ACNVHVRDPYtSGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQGLTAIQIAMAEDHTDMVKLLVMNGADVIHAN 674
Cdd:COG0666 209 GADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| cNMP_binding |
pfam00027 |
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
419-504 |
1.51e-15 |
|
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: 72.26 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 419 EYIPPREDVIMQNEAPDDVYIIVSGEVEIIDYEGE-KEHVVGTLQSADMFGEVGALCCRPQTYTFRTKTLSQLLRLKTSA 497
Cdd:pfam00027 2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDgREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81
|
....*..
gi 1104537548 498 LIEAMQT 504
Cdd:pfam00027 82 FLELLER 88
|
|
| Ion_trans_2 |
pfam07885 |
Ion channel; This family includes the two membrane helix type ion channels found in bacteria. |
253-324 |
5.82e-15 |
|
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: 70.37 E-value: 5.82e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1104537548 253 WIGAVIPNFRETSLWiRYISALYWSITTMTTVGYGDMHAVNTMEMIFIIFYMLFNLGLTAYLIGNMTNLVVE 324
Cdd:pfam07885 8 IFGTVYYLLEEGWEW-SFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
548-670 |
4.63e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.22 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 548 LLTVASTGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHAcnvhvrdpytsgdllctaakrndltam 627
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1104537548 628 kellkqglNIDSKNrQGLTAIQIAMAEDHTDMVKLLVMNGADV 670
Cdd:pfam12796 54 --------DVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
|
|
| KHA |
cd17073 |
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ... |
731-805 |
7.62e-12 |
|
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: 61.08 E-value: 7.62e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1104537548 731 PRVSIYR-GHPlqrkescctEAGRLIRLPNSLMELKAIAGEKLGFDARNamVTNEEGAEIDSIEVIRDNDTLFLVE 805
Cdd:cd17073 1 KRVTVFVnGSS---------SGGKVIALPSTLSELLKIASEKLGIPAKR--LYTGSGGEIDDIALIRDDDVLYVSE 65
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
401-526 |
7.07e-11 |
|
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: 62.31 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 401 FKGISREILLLLVAKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEI--IDYEGeKEHVVGTLQSADMFGEVGALCCRPQ 478
Cdd:COG0664 1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLyrISEDG-REQILGFLGPGDFFGELSLLGGEPS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1104537548 479 TYTFRTKTLSQLLRLKTSALIEAMQTKKEDNVIILK----NFLQHHKRLKDL 526
Cdd:COG0664 80 PATAEALEDSELLRIPREDLEELLERNPELARALLRllarRLRQLQERLVSL 131
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
563-687 |
5.19e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.23 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 563 LLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPYTSGDLLCTAAKRNdLTAMKELLKQGLNIDSKNR 642
Cdd:PHA02875 121 LIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD-IAICKMLLDSGANIDYFGK 199
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1104537548 643 QG-LTAIQIAMAEDHTDMVKLLVMNGADVIHANTYEFSSETLNEML 687
Cdd:PHA02875 200 NGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECTILDMI 245
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
525-648 |
3.02e-08 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 56.12 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 525 DLNIGDLLVENGeedVNPNMAFN-----LLTVASTGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKH 599
Cdd:COG0666 165 NLEIVKLLLEAG---ADVNARDNdgetpLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1104537548 600 ACNVHVRDPYtSGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQGLTAI 648
Cdd:COG0666 242 GADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
576-607 |
1.23e-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: 45.36 E-value: 1.23e-06
10 20 30
....*....|....*....|....*....|...
gi 1104537548 576 KGRTPLHIAASK-GHEDCVMVLLKHACNVHVRD 607
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
613-664 |
1.29e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1104537548 613 DLLCTAAKRNDLTAMKELLKQGLNIDSKNRQGLTAIQIAMAEDHTDMVKLLV 664
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
537-631 |
1.51e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.82 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 537 EEDVNPNMAfNLLTV-----ASTGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHV--RDPY 609
Cdd:PTZ00322 71 EEVIDPVVA-HMLTVelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLldKDGK 149
|
90 100
....*....|....*....|..
gi 1104537548 610 TSGDLlctaAKRNDLTAMKELL 631
Cdd:PTZ00322 150 TPLEL----AEENGFREVVQLL 167
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
534-677 |
6.92e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 49.25 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 534 ENGEEDVNPNMAFNLLTVASTGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDC---VMVLLKHACNVHVRDPYT 610
Cdd:PHA03095 4 DESVDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1104537548 611 SGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQGLTAIQIAMAED--HTDMVKLLVMNGADVIHANTYE 677
Cdd:PHA03095 84 FTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYG 152
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
525-696 |
9.41e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.11 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 525 DLNIGDLLVENGEE--DVNPNMAFNLLTVASTGNAAFLDELLKAK-LDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHAC 601
Cdd:PHA02878 146 EAEITKLLLSYGADinMKDRHKGNTALHYATENKDQRLTELLLSYgANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 602 NVHVRDPYTSGDLLCTAAKRNDLTAMKELLKQGLNIDSKNR-QGLTAIQIAMAEDhtDMVKLLVMNGADVihaNTYEFSS 680
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADI---NSLNSYK 300
|
170
....*....|....*.
gi 1104537548 681 ETLNEMLQKREMGHRI 696
Cdd:PHA02878 301 LTPLSSAVKQYLCINI 316
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
522-682 |
2.92e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 47.27 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 522 RLKDLNIGDLLVENGEE--DVNPNMAFNLLTVASTGNAAFLDELLKAKLDPDIgdskgrtplhIAASKGHEDCVMVLLKH 599
Cdd:PHA02874 44 RSGDAKIVELFIKHGADinHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI----------LPIPCIEKDMIKTILDC 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 600 ACNVHVRDPyTSGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQGLTAIQIAMAEDHTDMVKLLVMNGAdviHANTYEFS 679
Cdd:PHA02874 114 GIDVNIKDA-ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA---YANVKDNN 189
|
...
gi 1104537548 680 SET 682
Cdd:PHA02874 190 GES 192
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
576-605 |
3.66e-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: 41.03 E-value: 3.66e-05
10 20 30
....*....|....*....|....*....|
gi 1104537548 576 KGRTPLHIAASKGHEDCVMVLLKHACNVHV 605
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
563-670 |
1.17e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 45.43 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 563 LLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPYTSGDLLCTAAKRNDLTAMKE----LLKQGLNID 638
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKEivklLLEYGANVN 100
|
90 100 110
....*....|....*....|....*....|....
gi 1104537548 639 SKNRQGLTAIQIAMAE--DHTDMVKLLVMNGADV 670
Cdd:PHA03100 101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANV 134
|
|
| PRK11753 |
PRK11753 |
cAMP-activated global transcriptional regulator CRP; |
422-471 |
1.20e-04 |
|
cAMP-activated global transcriptional regulator CRP;
Pssm-ID: 236969 [Multi-domain] Cd Length: 211 Bit Score: 44.20 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1104537548 422 PPREDVIMQNEAPDDVYIIVSGEVEI-IDYEGEKEHVVGTLQSADMFGEVG 471
Cdd:PRK11753 26 PAKSTLIHAGEKAETLYYIVKGSVAVlIKDEEGKEMILSYLNQGDFIGELG 76
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
568-609 |
1.35e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.41 E-value: 1.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1104537548 568 LDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPY 609
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE 48
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
554-692 |
1.68e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.98 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 554 TGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPYTSGDLLcTAAKRNDLTAMKELLKQ 633
Cdd:PHA02875 12 FGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELH-DAVEEGDVKAVEELLDL 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 634 GLNIDSK-NRQGLTAIQIAMAEDHTDMVKLLVMNGADVIHANTYEFSSETLNEMLQKREM 692
Cdd:PHA02875 91 GKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150
|
|
| PRK10537 |
PRK10537 |
voltage-gated potassium channel protein; |
273-334 |
2.71e-04 |
|
voltage-gated potassium channel protein;
Pssm-ID: 236711 [Multi-domain] Cd Length: 393 Bit Score: 44.24 E-value: 2.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1104537548 273 ALYWSITTMTTVGYGDMHAVNTMEMIFIIFYMLfnLGLTAY----------LIGNMTNLVVEGTRRTMEFRN 334
Cdd:PRK10537 172 AFYFSIVTMSTVGYGDIVPVSESARLFTISVII--LGITVFatsisaifgpVIRGNLKRLVKGRISHMHRKD 241
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
552-597 |
3.06e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.18 E-value: 3.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1104537548 552 ASTGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLL 597
Cdd:pfam13637 9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
563-670 |
4.27e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.50 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 563 LLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMV--LLKHACNVHVRDP--------YTSGD---------LLCTAAKRND 623
Cdd:PHA03100 92 LLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSdgenllhlYLESNkidlkilklLIDKGVDINA 171
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1104537548 624 LTAMKELLKQGLNIDSKNRQGLTAIQIAMAEDHTDMVKLLVMNGADV 670
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP 218
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
596-651 |
8.69e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 8.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1104537548 596 LLKHACNVHVRDPYTSGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQGLTAIQIA 651
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
477-670 |
1.12e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 42.36 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 477 PQTYTFRTKTLSQLLR--LKTSALIEAMQTKKEDNViilknFLQHHKRLKDLNIGDLLVENGEEDVNPNMAFNLLTVAST 554
Cdd:PHA02876 276 PLHHASQAPSLSRLVPklLERGADVNAKNIKGETPL-----YLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAST 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 555 --GNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVHVRDPYTSGDLLCTAAKRNDLTAMKELLK 632
Cdd:PHA02876 351 ldRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLID 430
|
170 180 190
....*....|....*....|....*....|....*....
gi 1104537548 633 QGLNIDSKNRQGLTAIQIAMAED-HTDMVKLLVMNGADV 670
Cdd:PHA02876 431 RGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
495-689 |
2.19e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.19 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 495 TSALIEAMQTKKEDNVIIlKNFLQHHKRLK-------------------DLNIGDLLVENGEeDVNpnmafnlltvastg 555
Cdd:PHA03100 107 ITPLLYAISKKSNSYSIV-EYLLDNGANVNiknsdgenllhlylesnkiDLKILKLLIDKGV-DIN-------------- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 556 NAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVmvllkhacnvhvrdpytsgdllctaakrndltamKELLKQGL 635
Cdd:PHA03100 171 AKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV----------------------------------KYLLDLGA 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1104537548 636 NIDSKNRQGLTAIQIAMAEDHTDMVKLLVMNGADVIHANTY-------EFSSETLNEMLQK 689
Cdd:PHA03100 217 NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETllyfkdkDLNTITKIKMLKK 277
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
548-673 |
2.87e-03 |
|
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: 41.15 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 548 LLTVASTGNAAFLDELLKAK-LDPDIGDSKGRTPLHIAASKGHEDCVMVLLKHACNVhVRDPYTSgDLLctaakrndlta 626
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL-VNEPMTS-DLY----------- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1104537548 627 mkellkqglnidsknrQGLTAIQIAMAEDHTDMVKLLVMNGADVIHA 673
Cdd:cd22192 88 ----------------QGETALHIAVVNQNLNLVRELIARGADVVSP 118
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
566-670 |
3.39e-03 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 40.83 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 566 AKLDPDIGDSKGRTPLHIAASKG-HEDCVMVLLKHACNVHVrdpytsGDLLCTAAKRNDLTAMKELLKQGLNIDSKNRQ- 643
Cdd:TIGR00870 41 KKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPl 114
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1104537548 644 -------------GLTAIQIAMAEDHTDMVKLLVMNGADV 670
Cdd:TIGR00870 115 elandqytseftpGITALHLAAHRQNYEIVKLLLERGASV 154
|
|
| ftrB |
PRK09392 |
transcriptional activator FtrB; Provisional |
392-508 |
3.74e-03 |
|
transcriptional activator FtrB; Provisional
Pssm-ID: 181817 [Multi-domain] Cd Length: 236 Bit Score: 39.62 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 392 LPTVEKVYLFKGISREILLLLVAKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEIIDYEGEKEHVVGTLQSADMFgeVG 471
Cdd:PRK09392 6 LIRLRNLPLFADMADATFERLMRGAFLQRFPPGTMLITEGEPADFLFVVLDGLVELSASSQDRETTLAILRPVSTF--IL 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1104537548 472 ALCCRPQTY--TFRTKTLSQLLRLKTSALIEAMqtkKED 508
Cdd:PRK09392 84 AAVVLDAPYlmSARTLTRSRVLMIPAELVREAM---SED 119
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
525-661 |
9.36e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 39.24 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104537548 525 DLNIGDLLVENGEE----DVNPNMAFNLLTVASTGNAAFLDELLKAKLDPDIGDSKGRTPLHIAASKGHEDCVMV--LLK 598
Cdd:PHA03095 166 NVELLRLLIDAGADvyavDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLI 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1104537548 599 HACNVHVRDPYTSGDLLCTAAKRNDlTAMKELLKQGLNIDSKNRQGLTAIQIAMAEDHTDMVK 661
Cdd:PHA03095 246 AGISINARNRYGQTPLHYAAVFNNP-RACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
|
|
| |
