|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
143-431 |
1.23e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 143 FVLEQLVSHKQTDVNLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEVILLKGeea 222
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 223 glsidAHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSYPKVcdliNI 302
Cdd:COG0666 78 -----ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV----NA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 303 TDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAIl 382
Cdd:COG0666 149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 55741815 383 qprgLKNLPTEVLQHESVRELLNDEDIEGCTPLHYACRLGIPDSVKNML 431
Cdd:COG0666 228 ----ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
358-599 |
1.00e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.06 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 358 LLLSHGADLTKKDKSGCNFLHLAILQPRGLKNLPTEVLQHESVRELLNDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSL 437
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 438 DQKSKEKKSALHFAAEFGRINTCHRLLEMVTDtrlLNEGDEKGLTPLHLASREGHVKVVELLLRKGA-LFHSDYRGWSGL 516
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 517 HHAASEGYTQTMDTLLTSNIKLlNKTDGDGNTALHLAARAGHVAAVRLLLYRGAKI-ILNKNDASFLHEAVHNARREVTN 595
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVK 236
|
....
gi 55741815 596 MVIE 599
Cdd:COG0666 237 LLLE 240
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
144-478 |
8.94e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 96.57 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 144 VLEQLVSHKQTDVNLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEVILlkgeeag 223
Cdd:PHA02874 16 AIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 224 lsidahINYVDKSCssplhLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSYPKVcdliNIT 303
Cdd:PHA02874 89 ------DNGVDTSI-----LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADV----NIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 304 DGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAILQ 383
Cdd:PHA02874 154 DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 384 PRGLKNLpteVLQHESVrellNDEDIEGCTPLHYAcrLGIP---DSVKNMLGLEVSLDQKSKEKKSALHFAAEFgrINTC 460
Cdd:PHA02874 234 NRSAIEL---LINNASI----NDQDIDGSTPLHHA--INPPcdiDIIDILLYHKADISIKDNKGENPIDTAFKY--INKD 302
|
330
....*....|....*...
gi 55741815 461 HRLLEMVTDTRLLNEGDE 478
Cdd:PHA02874 303 PVIKDIIANAVLIKEADK 320
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
784-963 |
3.35e-17 |
|
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: 82.31 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 784 ILQMFQQRL--NYLRDLSNYMDWAAaicallfVVPLLMNLKSSWHWQAGALAALTSW--LNLLLYLQRFERIGIYVVMFR 859
Cdd:pfam00520 51 LLKIIAAGFkkRYFRSPWNILDFVV-------VLPSLISLVLSSVGSLSGLRVLRLLrlLRLLRLIRRLEGLRTLVNSLI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 860 EISRTLLSIIVLFFYLILGFALSFYAL-------MIEQQ----HFGRMFLSLLQTFVMMVGEmNYQDNFMKPYlqgDLPF 928
Cdd:pfam00520 124 RSLKSLGNLLLLLLLFLFIFAIIGYQLfggklktWENPDngrtNFDNFPNAFLWLFQTMTTE-GWGDIMYDTI---DGKG 199
|
170 180 190
....*....|....*....|....*....|....*
gi 55741815 929 PDLTLAIFVWFVLLVPILLMNLLIGLAVGDIAEVQ 963
Cdd:pfam00520 200 EFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELT 234
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
241-337 |
9.36e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 241 LHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLssypKVCDLINITDGanQTPLHKAVIFDHF 320
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDNG--RTALHYAARSGHL 74
|
90
....*....|....*..
gi 55741815 321 ELSEYLMSQGANIDFVD 337
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
484-575 |
8.45e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 484 LHLASREGHVKVVELLLRKGA-LFHSDYRGWSGLHHAASEGYTQTMDTLLTSNIKllnKTDGDGNTALHLAARAGHVAAV 562
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 55741815 563 RLLLYRGAKIILN 575
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
298-671 |
2.23e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.01 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 298 DLINITDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGAD------------ 365
Cdd:PHA02874 26 NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 366 -----------LTKKDKSGCNFLHLAIlqprglKNLPTEVLQHE-SVRELLNDEDIEGCTPLHYACRLGIPDSVKNMLGL 433
Cdd:PHA02874 106 miktildcgidVNIKDAELKTFLHYAI------KKGDLESIKMLfEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 434 EVSLDQKSKEKKSALHFAAEFGRINTCHRLLemvTDTRLLNEGDEKGLTPLHLASREGHvKVVELLLRKGALFHSDYRGW 513
Cdd:PHA02874 180 GAYANVKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDIDGS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 514 SGLHHAASEGYTQ-TMDTLLTSNIKLLNKtDGDGNTALHLAARagHVAAVRLLLYRGAKIILNKN-----DASFLHEAVH 587
Cdd:PHA02874 256 TPLHHAINPPCDIdIIDILLYHKADISIK-DNKGENPIDTAFK--YINKDPVIKDIIANAVLIKEadklkDSDFLEHIEI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 588 NARREVTNMVIESDRCEEAMTTYKPNSTKRCIVMDMIEFL------PESFKHLLDTCIRESEE-----DVNCTNYYIEYN 656
Cdd:PHA02874 333 KDNKEFSDFIKECNEEIEDMKKTKCGCDKNIFDLCLIRIKhkfdgnEDSIKDYLNCLDDNSHRmlktiDINEFPIYSMYI 412
|
410
....*....|....*
gi 55741815 657 FRWLQHPLQNLKKTG 671
Cdd:PHA02874 413 SRCISDNGKILKDMG 427
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
413-986 |
7.58e-15 |
|
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: 79.29 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 413 TPLHYACRLGIPDSVKNMLGLE-VSLDQKSKEKKSALHFAAEFGRINTCHRLLEmvTDTRLLNE---GD-EKGLTPLHLA 487
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtSDlYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 488 SREGHVKVVELLLRKGA------------LFHSD---YRGWSGLHHAASEGYTQTMDTLLTSNIKLLNKtDGDGNTALHL 552
Cdd:cd22192 97 VVNQNLNLVRELIARGAdvvspratgtffRPGPKnliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLGNTVLHI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 553 aaraghvaavrLLLyrgakiILNKNDASFLHEAVHNARREVTNMVIESDRCEEAMTTYKPNSTKRCIVMdmieflpesFK 632
Cdd:cd22192 176 -----------LVL------QPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVM---------FQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 633 HLLDTcireseedvnctNYYIEYNFRWLQHPLQNLKktgmEKDMAYKPLSALNAMVN----FNRVNLLTHPVcKKYLEMK 708
Cdd:cd22192 230 HLVQK------------RRHIQWTYGPLTSTLYDLT----EIDSWGDEQSVLELIVSskkrEARKILDVTPV-KELVSLK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 709 WSAYGIKAHLLNMTVYALGVFPLTYLIVN--LKPTLVTSRNVTSVNMVCTSLYKQSYLTTSSMLLvLAMNMYAVGKEILQ 786
Cdd:cd22192 293 WKRYGRPYFRILALLYLLYIIIFTLCCVYrpLKPRPENNTDPRDITLYVQKTLQESYVTPKDYLR-LVGELISVLGAIVI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 787 MFQQRLNYLR-DLSNYMDWAA--------AIC-ALLFVVPLLMNLKSSwhwqAG-----ALAALTSWLNLLLYLQRFERI 851
Cdd:cd22192 372 LLLEIPDILRvGVKRYFGQTVlggpfhviIITyACLVLLTLVLRLTSL----SGevvpmSLALVLGWCNVMYFARGFQML 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 852 GIYVVMfreISRTLLSIIVLFFYL----ILGFALSFYALMIEQQ-----HFGRMFLSLLQTFVMMVGEMNYQDNfmkpyl 922
Cdd:cd22192 448 GPFTIM---IQKIIFGDLMKFCWLmfvvILGFSSAFYMIFQTEDpdslgHFYDFPMTLFSTFELFLGLIDGPAN------ 518
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741815 923 qGDLPFPDLTLAIFVWFVLLVPILLMNLLIGLaVGDIaevqtnacLKRIA--------MQIELHT-NLEERLP 986
Cdd:cd22192 519 -YTVDLPFMYKVLYTAFAVIAYLLMLNLLIAM-MGDT--------HWRVAherdelwrAQVVATTlMLERRLP 581
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
691-1019 |
3.58e-10 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 64.05 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 691 NRVNLLTHPVCKKYLEMKWSAYGIKAHLLNMTVYALGVFPLTyLIVNLKPTLVTSRNVTSVNmvctslYKQSYLTTSSML 770
Cdd:cd22193 282 NRHEMLTLEPLNTLLQDKWDKFAKYMFFFSFCFYLFYMIIFT-LVAYYRPREDEPPPPLAKT------TKMDYMRLLGEI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 771 LVLAMNMYAVGKEILQMFQQRLNYLRDLSN-YMDWAAAICALLFVVPLLMNL-KSSWHWQAGALAALTSWLNLLLYLQRF 848
Cdd:cd22193 355 LVLLGGVYFFVKEIAYFLLRRSDLQSSFSDsYFEILFFVQAVLVILSVVLYLfAYKEYLACLVLALALGWANMLYYTRGF 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 849 ERIGIYVVMFRE-ISRTLLSIIVLFFYLILGFALSFYALMIE-------QQHFGRMFLSLLQTFVMMV--GEMNYQDNfm 918
Cdd:cd22193 435 QSMGIYSVMIQKvILRDLLRFLFVYLLFLFGFAVALVSLIEKcssdkkdCSSYGSFSDAVLELFKLTIgmGDLEFQEN-- 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 919 kpylqgdLPFPDLTLAIFVWFVLLVPILLMNLLIGLAVGDIAEVQTNAclKRIAMQIELHTNLE-ERLPYWFMKRVDQVT 997
Cdd:cd22193 513 -------STYPAVFLILLLTYVILTFVLLLNMLIALMGETVNNVSKES--KRIWKLQRAITILEfEKSFPECMRKAFRSG 583
|
330 340
....*....|....*....|....
gi 55741815 998 IREYPNRCFSGK--KRWFFGGNEV 1019
Cdd:cd22193 584 RLLKVGLCKDGTpdFRWCFRVDEV 607
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
55-126 |
8.48e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 8.48e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55741815 55 DTRDNIGASPLHYASANGHFRIIRHIVQivgHQELNVRDEeGNTPLHWAVQKDQPGSCSVLLSLGADPNVLN 126
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
690-954 |
1.20e-09 |
|
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: 62.41 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 690 FNRVNLLTHPvCKKYLEMKWSAYGIKAHLLNMTVYALGVFPLTYLIVnLKPTLVTSRNVTSvnmvctslyKQSYLTTSSM 769
Cdd:TIGR00870 328 ELSDMYLIAP-LSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAY-YRPTRTDLRVTGL---------QQTPLEMLIV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 770 LLVLAMnmyAVGKEILQMFQQRLNYLRDLSNYMD-------WAAAIC---ALLFVVPLLMNLKSSWH------WQAGALA 833
Cdd:TIGR00870 397 TWVDGL---RLGEEKLIWLGGIFEYIHQLWNILDfgmnsfyLATFLDrpfAILFVTQAFLVLREHWLrfdptlIEEALFA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 834 A--LTSWLNLLLYLQRFERIGIYVVMF-REISRTLLSIIVLFFYLILGFALSFYAL----------------MIEQQHFG 894
Cdd:TIGR00870 474 FalVLSWLNLLYIFRGNQHLGPLQIMIgRMILGDILRFLFIYAVVLFGFACGLNQLyqyydelklnecsnphARSCEKQG 553
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55741815 895 RMFLSLLQTFvmmvgemnyQDNFMKPYLQGDLP------FPDLTLAIFVWFVLLVPILLMNLLIGL 954
Cdd:TIGR00870 554 NAYSTLFETS---------QELFWAIIGLGDLLanehkfTEFVGLLLFGAYNVIMYILLLNMLIAM 610
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
63-187 |
4.60e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.00 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 63 SPLHYASANGHFRIIRHIVQIvGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKN 142
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELLDL-GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 55741815 143 FVLEQLVSHKQTdVNLEGDLGNTPVILSAALDNHEALGILYKHGA 187
Cdd:PHA02875 149 KGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
218-436 |
8.71e-05 |
|
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: 46.61 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 218 KGEEAGLSidaHINYVDKSCSSPL-HLAVRGGNLDIIKLCIGYGAKIDQQQcdksTALHfACSQGATEVVKVMLS----- 291
Cdd:TIGR00870 36 DLEEPKKL---NINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLhllaa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 292 -----SYPKVCDLINITDGANQTPLHKAVIFDHFELSEYLMSQGANI------------DFVDCKGHS--PLLLATSCGA 352
Cdd:TIGR00870 108 frksgPLELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVparacgdffvksQGVDSFYHGesPLNAAACLGS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 353 WRTVNLLLSHGADLTKKDKSGCNFLHLAILQP----------RGLKNLPTEVLQHesVRELLNDEDI---EGCTPLHYAC 419
Cdd:TIGR00870 188 PSIVALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelsCQMYNFALSLLDK--LRDSKELEVIlnhQGLTPLKLAA 265
|
250
....*....|....*..
gi 55741815 420 RLGIPDSVKNMLGLEVS 436
Cdd:TIGR00870 266 KEGRIVLFRLKLAIKYK 282
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
545-572 |
3.98e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.98e-04
10 20
....*....|....*....|....*...
gi 55741815 545 DGNTALHLAARAGHVAAVRLLLYRGAKI 572
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
239-264 |
4.55e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 4.55e-03
10 20
....*....|....*....|....*.
gi 55741815 239 SPLHLAVRGGNLDIIKLCIGYGAKID 264
Cdd:smart00248 4 TPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| YybS |
COG4241 |
Uncharacterized conserved protein YybS, DUF2232 family [Function unknown]; |
708-952 |
8.50e-03 |
|
Uncharacterized conserved protein YybS, DUF2232 family [Function unknown];
Pssm-ID: 443383 Cd Length: 318 Bit Score: 39.82 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 708 KWSAYGIkahLLNMTVYALGVFPLTYLIVnlkpTLVTSRNVTSVNMvctSLYKQSYLTTSSMllvlaMNMYAVGKEILQM 787
Cdd:COG4241 97 KKSAFET---LLAGTLAFLISTVILFLLS----QLLFGINPFDELI---NAMKESFNEAIEL-----YESMGMSEEQLEQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 788 FQQRLNYLRDLSNYMdwaaaICALLFVVpllmnlksswhwqagalAALTSWLNLLLYLQRFERIGIYVVMFREISRTLLS 867
Cdd:COG4241 162 MREQLEEMIELLKLL-----LPAILIIA-----------------SFLLAFINYLVARKILKRLGYKVPKFPPFREWRLP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 868 IIVLFFYLIlGFALSFYALMIEQQHFGRMFLSLLQTFVMMVgemnyqdnfmkpYLQGdlpfpdltLAIFVWFV------L 941
Cdd:COG4241 220 RSVLWIYII-VLLLLLFGDPEEISLLYIIGLNLLVILSFLF------------LLQG--------LSFIFYYLkkkklpK 278
|
250
....*....|.
gi 55741815 942 LVPILLMNLLI 952
Cdd:COG4241 279 FVRILIVILLI 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
143-431 |
1.23e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 143 FVLEQLVSHKQTDVNLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEVILLKGeea 222
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 223 glsidAHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSYPKVcdliNI 302
Cdd:COG0666 78 -----ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV----NA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 303 TDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAIl 382
Cdd:COG0666 149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 55741815 383 qprgLKNLPTEVLQHESVRELLNDEDIEGCTPLHYACRLGIPDSVKNML 431
Cdd:COG0666 228 ----ENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
358-599 |
1.00e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.06 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 358 LLLSHGADLTKKDKSGCNFLHLAILQPRGLKNLPTEVLQHESVRELLNDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSL 437
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 438 DQKSKEKKSALHFAAEFGRINTCHRLLEMVTDtrlLNEGDEKGLTPLHLASREGHVKVVELLLRKGA-LFHSDYRGWSGL 516
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 517 HHAASEGYTQTMDTLLTSNIKLlNKTDGDGNTALHLAARAGHVAAVRLLLYRGAKI-ILNKNDASFLHEAVHNARREVTN 595
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVK 236
|
....
gi 55741815 596 MVIE 599
Cdd:COG0666 237 LLLE 240
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
298-579 |
1.43e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 119.67 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 298 DLINITDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFL 377
Cdd:COG0666 12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 378 HLAILQPrglknlptevlQHESVRELL------NDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFA 451
Cdd:COG0666 92 HAAARNG-----------DLEIVKLLLeagadvNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 452 AEFGRINTCHRLLEMVTDtrlLNEGDEKGLTPLHLASREGHVKVVELLLRKGA-LFHSDYRGWSGLHHAASEGYTQTMDT 530
Cdd:COG0666 161 AANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 55741815 531 LLtSNIKLLNKTDGDGNTALHLAARAGHVAAVRLLLYRGAKIILNKNDA 579
Cdd:COG0666 238 LL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
46-341 |
3.46e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.52 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 46 ALEKNSRYLDTRDNIGASPLHYASANGHFRIIRHIVQIVGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVL 125
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 126 NNSHQAPIHMAVSLGKNFVLEQLVSHKqTDVNLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAF 205
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 206 SGAKKSMEVILLKGeeaglsidAHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEV 285
Cdd:COG0666 163 NGNLEIVKLLLEAG--------ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 55741815 286 VKVMLSSYPKvcdlINITDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGH 341
Cdd:COG0666 235 VKLLLEAGAD----LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
320-578 |
7.88e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 114.67 E-value: 7.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 320 FELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAILqprglKNLPTEVLQHES 399
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAAL-----AGDLLVALLLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 400 VRELLNDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRINTCHRLLEMVTDtrlLNEGDEK 479
Cdd:COG0666 76 AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDND 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 480 GLTPLHLASREGHVKVVELLLRKGA-LFHSDYRGWSGLHHAASEGYTQTMDTLLTSNIKlLNKTDGDGNTALHLAARAGH 558
Cdd:COG0666 153 GNTPLHLAAANGNLEIVKLLLEAGAdVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDGKTALDLAAENGN 231
|
250 260
....*....|....*....|
gi 55741815 559 VAAVRLLLYRGAKIILNKND 578
Cdd:COG0666 232 LEIVKLLLEAGADLNAKDKD 251
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
44-274 |
9.04e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 111.58 E-value: 9.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 44 AAALEKNSRYLDTRDNIGASPLHYASANGHFRIIRHIVQivGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPN 123
Cdd:COG0666 70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 124 VLNNSHQAPIHMAVSLGKNFVLEQLVSHKqTDVNLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAA 203
Cdd:COG0666 148 AQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741815 204 AFSGAKKSMEVILLKGeeaglsidAHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTAL 274
Cdd:COG0666 227 AENGNLEIVKLLLEAG--------ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
144-478 |
8.94e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 96.57 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 144 VLEQLVSHKQTDVNLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEVILlkgeeag 223
Cdd:PHA02874 16 AIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 224 lsidahINYVDKSCssplhLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSYPKVcdliNIT 303
Cdd:PHA02874 89 ------DNGVDTSI-----LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADV----NIE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 304 DGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAILQ 383
Cdd:PHA02874 154 DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 384 PRGLKNLpteVLQHESVrellNDEDIEGCTPLHYAcrLGIP---DSVKNMLGLEVSLDQKSKEKKSALHFAAEFgrINTC 460
Cdd:PHA02874 234 NRSAIEL---LINNASI----NDQDIDGSTPLHHA--INPPcdiDIIDILLYHKADISIKDNKGENPIDTAFKY--INKD 302
|
330
....*....|....*...
gi 55741815 461 HRLLEMVTDTRLLNEGDE 478
Cdd:PHA02874 303 PVIKDIIANAVLIKEADK 320
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
157-365 |
1.95e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 86.20 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 157 NLEGDLGNTPVILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEVILLKGEEAGlsidahiNYVDKS 236
Cdd:PHA02875 29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD-------DVFYKD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 237 CSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSypKVCdlINITDGANQTPLHKAVI 316
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH--KAC--LDIEDCCGCTPLIIAMA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 55741815 317 FDHFELSEYLMSQGANIDFVDCKGHSPLLlatsCGAWRT-----VNLLLSHGAD 365
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDYFGKNGCVAAL----CYAIENnkidiVRLFIKRGAD 227
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
784-963 |
3.35e-17 |
|
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: 82.31 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 784 ILQMFQQRL--NYLRDLSNYMDWAAaicallfVVPLLMNLKSSWHWQAGALAALTSW--LNLLLYLQRFERIGIYVVMFR 859
Cdd:pfam00520 51 LLKIIAAGFkkRYFRSPWNILDFVV-------VLPSLISLVLSSVGSLSGLRVLRLLrlLRLLRLIRRLEGLRTLVNSLI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 860 EISRTLLSIIVLFFYLILGFALSFYAL-------MIEQQ----HFGRMFLSLLQTFVMMVGEmNYQDNFMKPYlqgDLPF 928
Cdd:pfam00520 124 RSLKSLGNLLLLLLLFLFIFAIIGYQLfggklktWENPDngrtNFDNFPNAFLWLFQTMTTE-GWGDIMYDTI---DGKG 199
|
170 180 190
....*....|....*....|....*....|....*
gi 55741815 929 PDLTLAIFVWFVLLVPILLMNLLIGLAVGDIAEVQ 963
Cdd:pfam00520 200 EFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELT 234
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
241-337 |
9.36e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 9.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 241 LHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLssypKVCDLINITDGanQTPLHKAVIFDHF 320
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDNG--RTALHYAARSGHL 74
|
90
....*....|....*..
gi 55741815 321 ELSEYLMSQGANIDFVD 337
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
484-575 |
8.45e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.61 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 484 LHLASREGHVKVVELLLRKGA-LFHSDYRGWSGLHHAASEGYTQTMDTLLTSNIKllnKTDGDGNTALHLAARAGHVAAV 562
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 55741815 563 RLLLYRGAKIILN 575
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
298-671 |
2.23e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.01 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 298 DLINITDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGAD------------ 365
Cdd:PHA02874 26 NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 366 -----------LTKKDKSGCNFLHLAIlqprglKNLPTEVLQHE-SVRELLNDEDIEGCTPLHYACRLGIPDSVKNMLGL 433
Cdd:PHA02874 106 miktildcgidVNIKDAELKTFLHYAI------KKGDLESIKMLfEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 434 EVSLDQKSKEKKSALHFAAEFGRINTCHRLLemvTDTRLLNEGDEKGLTPLHLASREGHvKVVELLLRKGALFHSDYRGW 513
Cdd:PHA02874 180 GAYANVKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDIDGS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 514 SGLHHAASEGYTQ-TMDTLLTSNIKLLNKtDGDGNTALHLAARagHVAAVRLLLYRGAKIILNKN-----DASFLHEAVH 587
Cdd:PHA02874 256 TPLHHAINPPCDIdIIDILLYHKADISIK-DNKGENPIDTAFK--YINKDPVIKDIIANAVLIKEadklkDSDFLEHIEI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 588 NARREVTNMVIESDRCEEAMTTYKPNSTKRCIVMDMIEFL------PESFKHLLDTCIRESEE-----DVNCTNYYIEYN 656
Cdd:PHA02874 333 KDNKEFSDFIKECNEEIEDMKKTKCGCDKNIFDLCLIRIKhkfdgnEDSIKDYLNCLDDNSHRmlktiDINEFPIYSMYI 412
|
410
....*....|....*
gi 55741815 657 FRWLQHPLQNLKKTG 671
Cdd:PHA02874 413 SRCISDNGKILKDMG 427
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
415-504 |
4.83e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 4.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 415 LHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRINTCHRLLEMVTdtrllNEGDEKGLTPLHLASREGHVK 494
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-----VNLKDNGRTALHYAARSGHLE 75
|
90
....*....|
gi 55741815 495 VVELLLRKGA 504
Cdd:pfam12796 76 IVKLLLEKGA 85
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
215-504 |
4.90e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.55 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 215 ILLKGEEAGLSIDAHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGAT-----EVVKVM 289
Cdd:PHA03100 13 IKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 290 LssypKVCDLINITDGANQTPLHKAVI--FDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRT--VNLLLSHGAD 365
Cdd:PHA03100 93 L----EYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 366 LTKKDKSGCnFLHLAIlqprglknlptevlqhesvreLLNDEDIEGCTPLHYACRLGIPDSVKnmLGLEVSLDqkskekk 445
Cdd:PHA03100 169 INAKNRVNY-LLSYGV---------------------PINIKDVYGFTPLHYAVYNNNPEFVK--YLLDLGAN------- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 55741815 446 salhfaaefgrINTChrllemvtdtrllnegDEKGLTPLHLASREGHVKVVELLLRKGA 504
Cdd:PHA03100 218 -----------PNLV----------------NKYGDTPLHIAILNNNKEIFKLLLNNGP 249
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
413-986 |
7.58e-15 |
|
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: 79.29 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 413 TPLHYACRLGIPDSVKNMLGLE-VSLDQKSKEKKSALHFAAEFGRINTCHRLLEmvTDTRLLNE---GD-EKGLTPLHLA 487
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtSDlYQGETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 488 SREGHVKVVELLLRKGA------------LFHSD---YRGWSGLHHAASEGYTQTMDTLLTSNIKLLNKtDGDGNTALHL 552
Cdd:cd22192 97 VVNQNLNLVRELIARGAdvvspratgtffRPGPKnliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ-DSLGNTVLHI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 553 aaraghvaavrLLLyrgakiILNKNDASFLHEAVHNARREVTNMVIESDRCEEAMTTYKPNSTKRCIVMdmieflpesFK 632
Cdd:cd22192 176 -----------LVL------QPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVM---------FQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 633 HLLDTcireseedvnctNYYIEYNFRWLQHPLQNLKktgmEKDMAYKPLSALNAMVN----FNRVNLLTHPVcKKYLEMK 708
Cdd:cd22192 230 HLVQK------------RRHIQWTYGPLTSTLYDLT----EIDSWGDEQSVLELIVSskkrEARKILDVTPV-KELVSLK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 709 WSAYGIKAHLLNMTVYALGVFPLTYLIVN--LKPTLVTSRNVTSVNMVCTSLYKQSYLTTSSMLLvLAMNMYAVGKEILQ 786
Cdd:cd22192 293 WKRYGRPYFRILALLYLLYIIIFTLCCVYrpLKPRPENNTDPRDITLYVQKTLQESYVTPKDYLR-LVGELISVLGAIVI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 787 MFQQRLNYLR-DLSNYMDWAA--------AIC-ALLFVVPLLMNLKSSwhwqAG-----ALAALTSWLNLLLYLQRFERI 851
Cdd:cd22192 372 LLLEIPDILRvGVKRYFGQTVlggpfhviIITyACLVLLTLVLRLTSL----SGevvpmSLALVLGWCNVMYFARGFQML 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 852 GIYVVMfreISRTLLSIIVLFFYL----ILGFALSFYALMIEQQ-----HFGRMFLSLLQTFVMMVGEMNYQDNfmkpyl 922
Cdd:cd22192 448 GPFTIM---IQKIIFGDLMKFCWLmfvvILGFSSAFYMIFQTEDpdslgHFYDFPMTLFSTFELFLGLIDGPAN------ 518
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741815 923 qGDLPFPDLTLAIFVWFVLLVPILLMNLLIGLaVGDIaevqtnacLKRIA--------MQIELHT-NLEERLP 986
Cdd:cd22192 519 -YTVDLPFMYKVLYTAFAVIAYLLMLNLLIAM-MGDT--------HWRVAherdelwrAQVVATTlMLERRLP 581
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
433-954 |
7.68e-15 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 79.15 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 433 LEVSLDQKSKEKKSALHFAA---EFGRINTCHRLLEMVTDTRLLNE------GDE--KGLTPLHLASREGHVKVVELLLR 501
Cdd:cd21882 15 LTDSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapcTDEfyQGQTALHIAIENRNLNLVRLLVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 502 KGALFHSD--------------YRGWSGLHHAASEGYTQTMDTLL--TSNIKLLNKTDGDGNTALHL----AARAGHVAA 561
Cdd:cd21882 95 NGADVSARatgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLenGAQPAALEAQDSLGNTVLHAlvlqADNTPENSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 562 VRLLLYRGAKIILNKNDASFLHEavhnarrEVTNmviesdrcEEAMTTYKPNSTKRCIVMdmieflpesFKHLLDTCIRE 641
Cdd:cd21882 175 FVCQMYNLLLSYGAHLDPTQQLE-------EIPN--------HQGLTPLKLAAVEGKIVM---------FQHILQREFSG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 642 SEEDVncTNYYIEYNFRWLQHPLQNLKKTGMEKDMAYKPLSALNAMVNFNRVNLLTHPVcKKYLEMKWSAYGIKAHLLNM 721
Cdd:cd21882 231 PYQPL--SRKFTEWTYGPVTSSLYDLSEIDSWEKNSVLELIAFSKKREARHQMLVQEPL-NELLQEKWDRYGRPYFCFNF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 722 TVYALGVFPLTYLIVNlKPTLVTSRNVTSVNMVctslykQSYLTTSSMLLVLAMNMYAVGKEILQMFQQRLN-YLRDLSN 800
Cdd:cd21882 308 ACYLLYMIIFTVCAYY-RPLKDRPANQEAKATF------GDSIRLVGEILTVLGGVYILLGEIPYFFRRRLSrWFGFLDS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 801 YMDWAAAICALLFVVPLLMNLKS-SWHWQAGALAALTSWLNLLLYLQRFERIGIYVVMFRE-ISRTLLSIIVLFFYLILG 878
Cdd:cd21882 381 YFEILFITQALLVLLSMVLRFMEtEGYVVPLVFSLVLGWCNVLYYTRGFQMLGIYTVMIQKmILRDLMRFCWVYLVFLFG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 879 FALSFYALMIEQQ-----HFGRMFLSLLQTF--VMMVGEMNYQDNFmkpylqgDLPFpdLTLAIFVWFVLLVPILLMNLL 951
Cdd:cd21882 461 FASAFVILFQTEDpnklgEFRDYPDALLELFkfTIGMGDLPFNENV-------DFPF--VYLILLLAYVILTYLLLLNML 531
|
...
gi 55741815 952 IGL 954
Cdd:cd21882 532 IAL 534
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
98-365 |
5.45e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.47 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 98 TPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHmavslgknfvleqlvSHKQTDVNLEgdlgntpvilsaalDNHE 177
Cdd:PHA03100 37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH---------------YLSNIKYNLT--------------DVKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 178 ALGILYKHGAKFCRQNNLGHFPIHAAAF--SGAKKSMEVILLKGeeaglsidAHINYVDKSCSSPLHLAVRGG--NLDII 253
Cdd:PHA03100 88 IVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNG--------ANVNIKNSDGENLLHLYLESNkiDLKIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 254 KLCIGYGAKIDqqqcdkstalhfacsqgATEVVKVMLSS-YPkvcdlINITDGANQTPLHKAVIFDHFELSEYLMSQGAN 332
Cdd:PHA03100 160 KLLIDKGVDIN-----------------AKNRVNYLLSYgVP-----INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
|
250 260 270
....*....|....*....|....*....|...
gi 55741815 333 IDFVDCKGHSPLLLATSCGAWRTVNLLLSHGAD 365
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
99-438 |
1.67e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 74.15 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 99 PLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKNFVLEQLVSHKQTDvnlegDLGNTPVILSAAldnhea 178
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKC-----SVFYTLVAIKDA------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 179 lgilykhgakfCRQNNLGHFPIHAAAFSGAKKSMEVILLKGEEAGLSIDAhinyvdkscssplhlavrggnlDIIKLCIG 258
Cdd:PHA02878 109 -----------FNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEA----------------------EITKLLLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 259 YGAKIDQQQCDK-STALHFACSQGATEVVKVMLSSYPKVcdliNITDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVD 337
Cdd:PHA02878 156 YGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANV----NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 338 CKGHSPLLLATS-CGAWRTVNLLLSHGADLTKKDK-SGCNFLHLAILQPRGLKNLptevLQHESVRELLNDE-------- 407
Cdd:PHA02878 232 KCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLL----LEYGADINSLNSYkltplssa 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 55741815 408 -----DIEGCTPL--HYACRLGIPDSVKNMLGLEVSLD 438
Cdd:PHA02878 308 vkqylCINIGRILisNICLLKRIKPDIKNSEGFIDNMD 345
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
44-366 |
3.25e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 73.94 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 44 AAALEKNSRYLDTRDNIGASPLHYASANGHFRIIRHI------VQIVGHQELNVRD---------------------EEG 96
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLlsygadVNIIALDDLSVLEcavdsknidtikaiidnrsniNKN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 97 NTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKNFVLEQLVSHKQTDVNLEGDLGNTPVILSAALD-N 175
Cdd:PHA02876 241 DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 176 HEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEVILLkgeEAGLSIDAHiNYVDKScssPLHLAVRGGNLDIIKL 255
Cdd:PHA02876 321 TENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLL---ELGANVNAR-DYCDKT---PIHYAAVRNNVVIINT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 256 CIGYGAKIDQQQCDKSTALHFA-CSQGATEVVKVMLSSYPKVcdliNITDGANQTPLHKAVIFD-HFELSEYLMSQGANI 333
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANV----NSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
|
330 340 350
....*....|....*....|....*....|...
gi 55741815 334 DFVDCKGHSPLLLATscGAWRTVNLLLSHGADL 366
Cdd:PHA02876 470 NAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
228-588 |
7.20e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.79 E-value: 7.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 228 AHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSYPKVcdlinitdGAN 307
Cdd:PHA02876 169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI--------NKN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 308 QTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAW-RTVNLLLSHGADLTKKDKSGCNFLHLAILQPRG 386
Cdd:PHA02876 241 DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 387 LKNLPTEVLQHESVrellNDEDIEGCTPLHYACRLG-IPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRINTCHRLLE 465
Cdd:PHA02876 321 TENIRTLIMLGADV----NAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 466 MVTDTRLLNegdEKGLTPLHLA-SREGHVKVVELLLRKGALFHSDYRGWSG-LHHAASEGYTQTMDTLLTSNIKLLNKTD 543
Cdd:PHA02876 397 YGADIEALS---QKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTpLHYACKKNCKLDVIEMLLDNGADVNAIN 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 55741815 544 GDGNTALHLAarAGHVAAVRLLLYRGAKIilnkNDASFLHEAVHN 588
Cdd:PHA02876 474 IQNQYPLLIA--LEYHGIVNILLHYGAEL----RDSRVLHKSLND 512
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
74-361 |
1.67e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 71.21 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 74 FRIIRHIVQIVGhqELNVRDEEGNTPLHWAVQKDQPGSCSV---LLSLGADPNVLNNSHQAPIHMAVSLGKNF-VLEQLV 149
Cdd:PHA03095 27 VEEVRRLLAAGA--DVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 150 SHKqTDVNLEGDLGNTP--VILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAA-AFSGAkkSMEVI-LLkgeeagLS 225
Cdd:PHA03095 105 KAG-ADVNAKDKVGRTPlhVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLlKSRNA--NVELLrLL------ID 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 226 IDAHINYVDKSCSSPLH--LAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFA---CSQGATEVVKVMLSSYPkvcdlI 300
Cdd:PHA03095 176 AGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLLIAGIS-----I 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741815 301 NITDGANQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLS 361
Cdd:PHA03095 251 NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
57-431 |
2.12e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 71.25 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 57 RDNIGASPLHYASANGHFRIIRHIVQIVGHQEL-------------NVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPN 123
Cdd:PHA02876 126 KEAISGNDIHYDKINESIEYMKLIKERIQQDELliaemlleggadvNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 124 VlnnshqapihmaVSLGKNFVLEQLVSHKQTDVnlegdlgntpviLSAALDNHEALGilykhgakfcrQNNLGHFpihaA 203
Cdd:PHA02876 206 I------------IALDDLSVLECAVDSKNIDT------------IKAIIDNRSNIN-----------KNDLSLL----K 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 204 AFSGAKKSMEVILLkgeEAGLSidahINYVDKSCSSPLHLAVRGGNLD-IIKLCIGYGAKIDQQQCDKSTALHFACSQG- 281
Cdd:PHA02876 247 AIRNEDLETSLLLY---DAGFS----VNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGy 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 282 ATEVVKVMLSSYPKVcdliNITDGANQTPLHKAVIFDHF-ELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLL 360
Cdd:PHA02876 320 DTENIRTLIMLGADV----NAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55741815 361 SHGADLTKKDKSGCNFLHLAILQPRGLKNLPTEVLQHESVrellNDEDIEGCTPLHYACRLGIPDSVKNML 431
Cdd:PHA02876 396 DYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANV----NSKNKDLSTPLHYACKKNCKLDVIEML 462
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
300-648 |
2.37e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 70.44 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 300 INITDGANQTPLHKAVIFDHFELSE---YLMSQGANIDFVDCKGHSPL-LLATSCGAWRTVNLLLSHGADLTKKDKSGCN 375
Cdd:PHA03095 40 VNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 376 FLHLAilqprgLKNLPTevlqHESVRELL-------NDEDIEGCTPLH-YACRLGIPDSVKNMLgLEVSLDQKSKE--KK 445
Cdd:PHA03095 120 PLHVY------LSGFNI----NPKVIRLLlrkgadvNALDLYGMTPLAvLLKSRNANVELLRLL-IDAGADVYAVDdrFR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 446 SALHFAAEFGRINTC--HRLLEMVTDTRLLNEGdekGLTPLHLASREGHVK--VVELLLRKGALFHS-DYRGWSGLHHAA 520
Cdd:PHA03095 189 SLLHHHLQSFKPRARivRELIRAGCDPAATDML---GNTPLHSMATGSSCKrsLVLPLLIAGISINArNRYGQTPLHYAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 521 seGYTQTM--DTLltsnIKL---LNKTDGDGNTALHLAARAGHVAAVRLLlyrgakiiLNKN-DASFLHEAVHNArrEVT 594
Cdd:PHA03095 266 --VFNNPRacRRL----IALgadINAVSSDGNTPLSLMVRNNNGRAVRAA--------LAKNpSAETVAATLNTA--SVA 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 55741815 595 NMVIESDrceeamttykpnSTKRCIVMDMI----EFLPESFKHLLDTCIRESEEDVNC 648
Cdd:PHA03095 330 GGDIPSD------------ATRLCVAKVVLrgafSLLPEPIRAYHADFIRECEAEIAV 375
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
230-487 |
7.09e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 68.84 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 230 INYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMlssypkvcdlinITDGANQT 309
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL------------IDNGVDTS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 310 PLHKAVIFDhfELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAIlqpRGLKN 389
Cdd:PHA02874 96 ILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI---KHNFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 390 LPTEVLQHESVRELLNDEDIEgcTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRintchRLLEMVTD 469
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGE--SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-----SAIELLIN 243
|
250
....*....|....*...
gi 55741815 470 TRLLNEGDEKGLTPLHLA 487
Cdd:PHA02874 244 NASINDQDIDGSTPLHHA 261
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
225-504 |
3.78e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.83 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 225 SIDAHINYVDK-SCSS--PLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVMLSSYPKvCDLIN 301
Cdd:PHA02878 22 YIDHTENYSTSaSLIPfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINK-CSVFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 302 ITDGANQTPLHKAV-IFDHFELSEYLMSQGANIDFVDCKGHSPLLLAtscgawRTVNLLLSHGADLTKKDK-SGCNFLHL 379
Cdd:PHA02878 101 TLVAIKDAFNNRNVeIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMKDRhKGNTALHY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 380 AILQPrglknlptevlqHESVRELL-------NDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAA 452
Cdd:PHA02878 175 ATENK------------DQRLTELLlsyganvNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 55741815 453 EFGR-INTCHRLLEMVTDTRLlnEGDEKGLTPLHLASREGhvKVVELLLRKGA 504
Cdd:PHA02878 243 GYCKdYDILKLLLEHGVDVNA--KSYILGLTALHSSIKSE--RKLKLLLEYGA 291
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
100-193 |
9.27e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.36 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 100 LHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKNFVLEQLVSHKQTDVNlegDLGNTPVILSAALDNHEAL 179
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 55741815 180 GILYKHGAKFCRQN 193
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
471-1020 |
1.52e-10 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 65.16 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 471 RLLN----EGDEKGLTPLHLASREGHVKVVELLLRKGALFHSdyrgwsglhHAASEGYTQTMdtlltsnikllnKTDGD- 545
Cdd:cd22194 128 RFINaeytEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNA---------HAKGVFFNPKY------------KHEGFy 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 546 -GNTALHLAARAGHVAAVRLLLYRGAKIILNKND--ASFLHEAVHNAR--REVTNMVIE---------SDRCEEAMTTyK 611
Cdd:cd22194 187 fGETPLALAACTNQPEIVQLLMEKESTDITSQDSrgNTVLHALVTVAEdsKTQNDFVKRmydmillksENKNLETIRN-N 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 612 PNSTKRCIVMDMIEFlpESFKHLLDTCIREsEEDVNCTNYYIEYNFRWLQHPLQNLKKTGMEKDMAYKPLSALNAMVNfN 691
Cdd:cd22194 266 EGLTPLQLAAKMGKA--EILKYILSREIKE-KPNRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEIIVYNTNID-N 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 692 RVNLLTHPVCKKYLEMKWSAYGikAHLLNMTVyalgvfpLTYLIVNLKPTLVT---SRNVTSVNMVCTSLYKQSYLTTSS 768
Cdd:cd22194 342 RHEMLTLEPLHTLLHMKWKKFA--RYMFFISF-------LFYFFYNITLTLVSyyrPREDEDPPHPLALSHKMGWLQLLG 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 769 MLLVLAMNMYAVGKEILQMFQQRLNYLRDL--SNYMDWAAAICALLFVVPLLMNLKSSWHWQAGALAALT-SWLNLLLYL 845
Cdd:cd22194 413 QMFVLIWATCLSVKEGIAIFLLRPSDLKSIlsDAWFHILFFIQAVLVIVSVFLYLFAYKEYLACLVLAMAlGWANMLYYT 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 846 QRFERIGIYVVMFRE-ISRTLLSIIVLFFYLILGFALSFYALM------IEQQHFGRMFLSLLQTFVMMVGEMNYQdnfm 918
Cdd:cd22194 493 RGFQSLGIYSVMIQKvILNDVLKFLLVYILFLLGFGVALASLIedcpddSECSSYGSFSDAVLELFKLTIGLGDLE---- 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 919 kpyLQGDLPFPDLTLAIFVWFVLLVPILLMNLLIGL---AVGDIAEVQTNACLKRIAMQIelhTNLEERLPYWFMKRVdq 995
Cdd:cd22194 569 ---IQQNSKYPILFLLLLITYVILTFVLLLNMLIALmgeTVENVSKESERIWRLQRARTI---LEFEKSLPEWLRKRF-- 640
|
570 580
....*....|....*....|....*..
gi 55741815 996 vtirEYPNRCFSGKK--RWFFGGNEVK 1020
Cdd:cd22194 641 ----RLGELCKVADEdfRLCLRINEVK 663
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
47-264 |
2.68e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.92 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 47 LEKNSRYLDTRDNIGASPLHYASANGHfrIIRHIVQIV------GHQeLNVRDEEGNTPLHWAVQK--DQPGSCSVLLSL 118
Cdd:PHA03100 54 LLDNGADINSSTKNNSTPLHYLSNIKY--NLTDVKEIVkllleyGAN-VNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 119 GADPNVLNNSHQAPIHMAVSLGKN--FVLEQLVSHKqTDVNlegdlgntpvilsaALDNHEalgILYKHGAKFCRQNNLG 196
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG-VDIN--------------AKNRVN---YLLSYGVPINIKDVYG 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55741815 197 HFPIHAAAFSGAKKSMEVILLKGeeaglsidAHINYVDKSCSSPLHLAVRGGNLDIIKLCIGYGAKID 264
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDLG--------ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
691-1019 |
3.58e-10 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 64.05 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 691 NRVNLLTHPVCKKYLEMKWSAYGIKAHLLNMTVYALGVFPLTyLIVNLKPTLVTSRNVTSVNmvctslYKQSYLTTSSML 770
Cdd:cd22193 282 NRHEMLTLEPLNTLLQDKWDKFAKYMFFFSFCFYLFYMIIFT-LVAYYRPREDEPPPPLAKT------TKMDYMRLLGEI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 771 LVLAMNMYAVGKEILQMFQQRLNYLRDLSN-YMDWAAAICALLFVVPLLMNL-KSSWHWQAGALAALTSWLNLLLYLQRF 848
Cdd:cd22193 355 LVLLGGVYFFVKEIAYFLLRRSDLQSSFSDsYFEILFFVQAVLVILSVVLYLfAYKEYLACLVLALALGWANMLYYTRGF 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 849 ERIGIYVVMFRE-ISRTLLSIIVLFFYLILGFALSFYALMIE-------QQHFGRMFLSLLQTFVMMV--GEMNYQDNfm 918
Cdd:cd22193 435 QSMGIYSVMIQKvILRDLLRFLFVYLLFLFGFAVALVSLIEKcssdkkdCSSYGSFSDAVLELFKLTIgmGDLEFQEN-- 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 919 kpylqgdLPFPDLTLAIFVWFVLLVPILLMNLLIGLAVGDIAEVQTNAclKRIAMQIELHTNLE-ERLPYWFMKRVDQVT 997
Cdd:cd22193 513 -------STYPAVFLILLLTYVILTFVLLLNMLIALMGETVNNVSKES--KRIWKLQRAITILEfEKSFPECMRKAFRSG 583
|
330 340
....*....|....*....|....
gi 55741815 998 IREYPNRCFSGK--KRWFFGGNEV 1019
Cdd:cd22193 584 RLLKVGLCKDGTpdFRWCFRVDEV 607
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
55-126 |
8.48e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 56.66 E-value: 8.48e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55741815 55 DTRDNIGASPLHYASANGHFRIIRHIVQivgHQELNVRDEeGNTPLHWAVQKDQPGSCSVLLSLGADPNVLN 126
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
690-954 |
1.20e-09 |
|
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: 62.41 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 690 FNRVNLLTHPvCKKYLEMKWSAYGIKAHLLNMTVYALGVFPLTYLIVnLKPTLVTSRNVTSvnmvctslyKQSYLTTSSM 769
Cdd:TIGR00870 328 ELSDMYLIAP-LSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAY-YRPTRTDLRVTGL---------QQTPLEMLIV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 770 LLVLAMnmyAVGKEILQMFQQRLNYLRDLSNYMD-------WAAAIC---ALLFVVPLLMNLKSSWH------WQAGALA 833
Cdd:TIGR00870 397 TWVDGL---RLGEEKLIWLGGIFEYIHQLWNILDfgmnsfyLATFLDrpfAILFVTQAFLVLREHWLrfdptlIEEALFA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 834 A--LTSWLNLLLYLQRFERIGIYVVMF-REISRTLLSIIVLFFYLILGFALSFYAL----------------MIEQQHFG 894
Cdd:TIGR00870 474 FalVLSWLNLLYIFRGNQHLGPLQIMIgRMILGDILRFLFIYAVVLFGFACGLNQLyqyydelklnecsnphARSCEKQG 553
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55741815 895 RMFLSLLQTFvmmvgemnyQDNFMKPYLQGDLP------FPDLTLAIFVWFVLLVPILLMNLLIGL 954
Cdd:TIGR00870 554 NAYSTLFETS---------QELFWAIIGLGDLLanehkfTEFVGLLLFGAYNVIMYILLLNMLIAM 610
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
405-624 |
1.67e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 405 NDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRINTCHRLLEMvtDTRLLNEGDEKGLTPL 484
Cdd:PHA02875 29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 485 HLASREGHVKVVELLLRKGALFH-SDYRGWSGLHHAASEGYTQtMDTLLTSNIKLLNKTDGDGNTALHLAARAGHVAAVR 563
Cdd:PHA02875 107 HLATILKKLDIMKLLIARGADPDiPNTDKFSPLHLAVMMGDIK-GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741815 564 LLLYRGAKI--ILNKNDASFLHEAVHNARREVTNMVIESDRCEEAMTTYKpnsTKRCIVMDMI 624
Cdd:PHA02875 186 MLLDSGANIdyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIE---GEECTILDMI 245
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
307-515 |
1.71e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 307 NQTPLHKAVIFDHFELSEYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAILQPRG 386
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 387 LKnlptevlqhesVRELLND----EDI---EGCTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRINt 459
Cdd:PHA02875 82 KA-----------VEELLDLgkfaDDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 55741815 460 chrLLEMVTDTR-LLNEGDEKGLTPLHLASREGHVKVVELLLRKGAlfHSDYRGWSG 515
Cdd:PHA02875 150 ---GIELLIDHKaCLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA--NIDYFGKNG 201
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
412-641 |
2.14e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 60.83 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 412 CTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFAAEFGRINTCHR-----LLEMVTDtrlLNEGDEKGLTPLHL 486
Cdd:PHA03100 36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLLEYGAN---VNAPDNNGITPLLY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 487 ASRE--GHVKVVELLLRKGALFHSD-YRGWSGLHHAASEGYTQT------------------MDTLLTSNIKLLNKtDGD 545
Cdd:PHA03100 113 AISKksNSYSIVEYLLDNGANVNIKnSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIK-DVY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 546 GNTALHLAARAGHVAAVRLLLYRGAKI-ILNKNDASFLHEAVHNARREVTNMVIESDRCEEAMTTY-------KPNS--- 614
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETllyfkdkDLNTitk 271
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 55741815 615 ---TKRCIVMdMIEFLP------------ESFKHLLDTCIRE 641
Cdd:PHA03100 272 ikmLKKSIMY-MFLLDPgfyknrkliensKSLKDVINECEKE 312
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
63-187 |
4.60e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.00 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 63 SPLHYASANGHFRIIRHIVQIvGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKN 142
Cdd:PHA02875 70 SELHDAVEEGDVKAVEELLDL-GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 55741815 143 FVLEQLVSHKQTdVNLEGDLGNTPVILSAALDNHEALGILYKHGA 187
Cdd:PHA02875 149 KGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
344-440 |
5.47e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 54.35 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 344 LLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLAILqpRGlknlptevlQHESVRELLN----DEDIEGCTPLHYAC 419
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAK--NG---------HLEIVKLLLEhadvNLKDNGRTALHYAA 69
|
90 100
....*....|....*....|.
gi 55741815 420 RLGIPDSVKNMLGLEVSLDQK 440
Cdd:pfam12796 70 RSGHLEIVKLLLEKGADINVK 90
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
88-257 |
1.14e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 58.74 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 88 ELNVRDEE-GNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKNFVLEQLVSHKqTDVNLEGDLGNTP 166
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 167 V-ILSAALDNHEALGILYKHGAKFCRQNN-LGHFPIHAAAFSGAKKSmeviLLkgeeagLSIDAHINYVDKSCSSPLHLA 244
Cdd:PHA02878 238 LhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLK----LL------LEYGADINSLNSYKLTPLSSA 307
|
170
....*....|....*....
gi 55741815 245 VRG------GNLDIIKLCI 257
Cdd:PHA02878 308 VKQylciniGRILISNICL 326
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
88-263 |
1.17e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.82 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 88 ELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSlGKNFVLEQLVSHKQTDVNLEGDLGNTPV 167
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK-HNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 168 ILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSgaKKSMEVILLKgeeaglsiDAHINYVDKSCSSPLHLAVR- 246
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH--NRSAIELLIN--------NASINDQDIDGSTPLHHAINp 264
|
170
....*....|....*..
gi 55741815 247 GGNLDIIKLCIGYGAKI 263
Cdd:PHA02874 265 PCDIDIIDILLYHKADI 281
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
59-187 |
2.61e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 57.58 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 59 NIGASPLHYASANGHFRIIRHIvqIVGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVS 138
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELL--LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 55741815 139 LGKNFVLEQLVSHKQTDVNLEGD-LGNTPviLSAALDNHEALGILYKHGA 187
Cdd:PHA02878 244 YCKDYDILKLLLEHGVDVNAKSYiLGLTA--LHSSIKSERKLKLLLEYGA 291
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
65-158 |
2.93e-08 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 52.04 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 65 LHYASANGHFRIIRHIVQivGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSlGADPNVlNNSHQAPIHMAVSLGKNFV 144
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEI 76
|
90
....*....|....
gi 55741815 145 LEQLVSHKQtDVNL 158
Cdd:pfam12796 77 VKLLLEKGA-DINV 89
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
456-603 |
3.06e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.31 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 456 RINTCHRLL--EMVTDTRLLNEGDE------KGLTPLHLASREGHVKVVELLLRKGALFHSDYRGW-SGLHHAASEGYTQ 526
Cdd:PHA02875 3 QVALCDAILfgELDIARRLLDIGINpnfeiyDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIeSELHDAVEEGDVK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55741815 527 TMDTLLTSNIKLLNKTDGDGNTALHLAARAGHVAAVRLLLYRGAKI-ILNKNDASFLHEAVHNARREVTNMVIESDRC 603
Cdd:PHA02875 83 AVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPdIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
512-566 |
8.40e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 8.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 55741815 512 GWSGLHHAASEGYTQTMDTLLtSNIKLLNKTDGDGNTALHLAARAGHVAAVRLLL 566
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
770-992 |
1.47e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 55.63 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 770 LLVLAMNMYAVGKEILQMFQQRLNYLrdlSNYMDWAAAICALLFVVPLLMN-----LKSSWHWQAGALAALTSWLNLLLY 844
Cdd:cd22197 369 ILILLGGIYLLLGQLWYFWRRRLFIW---ISFMDSYFEILFLLQALLTVLSqvlyfMGSEWYLPLLVFSLVLGWLNLLYY 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 845 LQRFERIGIYVVMFRE-ISRTLLSIIVLFFYLILGFALSFYAL---------------------MIEQQHFGRMFLSLLQ 902
Cdd:cd22197 446 TRGFQHTGIYSVMIQKvILRDLLRFLLVYLVFLFGFAVALVSLsreapspkapednnstvteqpTVGQEEEPAPYRSILD 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 903 T------FVMMVGEMNYQDNfmkpylqgdLPFPDLTLAIFVWFVLLVPILLMNLLIGLAVGDIAEVQTNAC----LKRIA 972
Cdd:cd22197 526 AslelfkFTIGMGELAFQEQ---------LRFRGVVLLLLLAYVLLTYVLLLNMLIALMSETVNHVADNSWsiwkLQKAI 596
|
250 260
....*....|....*....|
gi 55741815 973 MQIELhtnleERLPYWFMKR 992
Cdd:cd22197 597 SVLEM-----ENGYWWCRRK 611
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
690-954 |
1.50e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 55.58 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 690 FNRVNLLTHPVcKKYLEMKWSAYGIKAHLLNMTVYALGVFPLTylivnlkpTLVTSRNVTSVNMVCTSLYKQSYLTTSSM 769
Cdd:cd22196 300 NRHEMLLVEPL-NKLLQDKWDKFVKRIFYFNFFVYFIYMIIFT--------LAAYYRPVNKTPPFPIENTTGEYLRLTGE 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 770 LLVLAMNMYAVGKEIlQMFQQRLNYLRDLSnymdwAAAICALLFVVPLLMNLKSSWHWQAG--------ALAALTSWLNL 841
Cdd:cd22196 371 IISVSGGVYFFFRGI-QYFLQRRPSLKKLI-----VDSYCEILFFVQSLFLLASTVLYFCGrneyvafmVISLALGWANV 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 842 LLYLQRFERIGIYVVMFRE-ISRTLLSIIVLFFYLILGFALSFYALMIEQQHFGRM---------------FLSLLQT-- 903
Cdd:cd22196 445 LYYTRGFQQMGIYSVMIQKmILRDICRFLFVYLVFLFGFSAALVTLIEDGPPKGDVntsqkecvcksgynsYNSLYSTcl 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 55741815 904 ----FVMMVGEMNYQDNFmkpylqgdlPFPDLTLAIFVWFVLLVPILLMNLLIGL 954
Cdd:cd22196 525 elfkFTIGMGDLEFTENY---------KFKEVFIFLLISYVILTYILLLNMLIAL 570
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
237-290 |
7.93e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 7.93e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 55741815 237 CSSPLHLAVRGGNLDIIKLCIGYGAKIDQQQCDKSTALHFACSQGATEVVKVML 290
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
446-500 |
9.65e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 9.65e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 55741815 446 SALHFAAEFGRINTCHRLLEMVTDtrlLNEGDEKGLTPLHLASREGHVKVVELLL 500
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
54-203 |
9.91e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 52.66 E-value: 9.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 54 LDTRDNIGASPLHYASANGHFRIIRHIVQIvgHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPI 133
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEY--GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 134 HMAVSLGKNFVLEQLVSHKqTDVNLEGDLGNTPvILSAALDNHEALGILYKHgAKFCRQNNLGHFPIHAA 203
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTP-LHNAIIHNRSAIELLINN-ASINDQDIDGSTPLHHA 261
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
168-266 |
2.53e-06 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 46.65 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 168 ILSAALDNHEALGILYKHGAKFCRQNNLGHFPIHAAAFSGAKKSMEvILLKGeeaglsidAHINYVDKSCSsPLHLAVRG 247
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEH--------ADVNLKDNGRT-ALHYAARS 71
|
90
....*....|....*....
gi 55741815 248 GNLDIIKLCIGYGAKIDQQ 266
Cdd:pfam12796 72 GHLEIVKLLLEKGADINVK 90
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
85-159 |
9.89e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.90 E-value: 9.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55741815 85 GHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMAVSLGKNFVLEQLVSHKQTDVNLE 159
Cdd:PTZ00322 104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
56-137 |
1.03e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 49.25 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 56 TRDNIGASPLHYASANGHFRIIrHIVQ-IVGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIH 134
Cdd:PHA03095 217 ATDMLGNTPLHSMATGSSCKRS-LVLPlLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295
|
...
gi 55741815 135 MAV 137
Cdd:PHA03095 296 LMV 298
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
476-581 |
1.40e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.48 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 476 GDEKGLTPLHLASREGHVKVVELLLRKGALFH-SDYRG----WSGL---HH------------------------AASEG 523
Cdd:PLN03192 554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHiRDANGntalWNAIsakHHkifrilyhfasisdphaagdllctAAKRN 633
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 55741815 524 YTQTMDTLLTSNIKLLNKtDGDGNTALHLAARAGHVAAVRLLLYRGAKIILNKNDASF 581
Cdd:PLN03192 634 DLTAMKELLKQGLNVDSE-DHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
516-614 |
3.13e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.97 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 516 LHHAASEGYTQTMDTLLTSNIKLlNKTDGDGNTALHLAARAGHVAAVRLLLYRGAKI-ILNKNDASFLHEAVHNARREVT 594
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADP-NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPtLLDKDGKTPLELAEENGFREVV 164
|
90 100
....*....|....*....|.
gi 55741815 595 NMVIESDRCE-EAMTTYKPNS 614
Cdd:PTZ00322 165 QLLSRHSQCHfELGANAKPDS 185
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
47-103 |
3.80e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 55741815 47 LEKNSRYLDTRDNIGASPLHYASANGHFRIIRHIvqIVGHQELNVRDEEGNTPLHWA 103
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVL--LAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
271-326 |
8.01e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 8.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 55741815 271 STALHFACSQGATEVVKVMLSSYPKvcdlINITDGANQTPLHKAVIFDHFELSEYL 326
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD----INAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
545-572 |
8.46e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 8.46e-05
10 20
....*....|....*....|....*....
gi 55741815 545 DGNTALHLAA-RAGHVAAVRLLLYRGAKI 572
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADV 29
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
218-436 |
8.71e-05 |
|
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: 46.61 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 218 KGEEAGLSidaHINYVDKSCSSPL-HLAVRGGNLDIIKLCIGYGAKIDQQQcdksTALHfACSQGATEVVKVMLS----- 291
Cdd:TIGR00870 36 DLEEPKKL---NINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLhllaa 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 292 -----SYPKVCDLINITDGANQTPLHKAVIFDHFELSEYLMSQGANI------------DFVDCKGHS--PLLLATSCGA 352
Cdd:TIGR00870 108 frksgPLELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVparacgdffvksQGVDSFYHGesPLNAAACLGS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 353 WRTVNLLLSHGADLTKKDKSGCNFLHLAILQP----------RGLKNLPTEVLQHesVRELLNDEDI---EGCTPLHYAC 419
Cdd:TIGR00870 188 PSIVALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelsCQMYNFALSLLDK--LRDSKELEVIlnhQGLTPLKLAA 265
|
250
....*....|....*..
gi 55741815 420 RLGIPDSVKNMLGLEVS 436
Cdd:TIGR00870 266 KEGRIVLFRLKLAIKYK 282
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
85-136 |
1.21e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 55741815 85 GHQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNNSHQAPIHMA 136
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
31-151 |
1.42e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 45.72 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 31 ISANVFEWTKqgnaaALEKNSRYLDTRDNIGASPLHYASANGHFRIIRHIVQ---------------------------- 82
Cdd:PHA02874 165 IKHNFFDIIK-----LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDhgnhimnkckngftplhnaiihnrsaie 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55741815 83 -IVGHQELNVRDEEGNTPLHWAVQkdQPGSCSV---LLSLGADPNVLNNSHQAPIHMAVS-LGKNFVLEQLVSH 151
Cdd:PHA02874 240 lLINNASINDQDIDGSTPLHHAIN--PPCDIDIidiLLYHKADISIKDNKGENPIDTAFKyINKDPVIKDIIAN 311
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
199-255 |
1.43e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 55741815 199 PIHAAAFSGAKKSMEVILLKGeeaglsidAHINYVDKSCSSPLHLAVRGGNLDIIKL 255
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKG--------ADINAVDGNGETALHFAASNGNVEVLKL 52
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
448-629 |
2.19e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 45.26 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 448 LHFAAEFGRINTCHRLLEMVTDtrlLNEGDEKGLTPLHLASREGHVKVVELLLR---KGALFHSDYRGWSGLHHAASEGY 524
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHN---VNQPDHRDLTPLHIICKEPNKLGMKEMIRsinKCSVFYTLVAIKDAFNNRNVEIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 525 ----TQTMDTLLTSNIKLLNKTDGD-------------------------GNTALHLAARAGHVAAVRLLLYRGAKI-IL 574
Cdd:PHA02878 118 kiilTNRYKNIQTIDLVYIDKKSKDdiieaeitklllsygadinmkdrhkGNTALHYATENKDQRLTELLLSYGANVnIP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 55741815 575 NKNDASFLHEAVHNARREVTNMVIESDRCEEAMTTYKPN----STKRCIVMDMIEFLPE 629
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTplhiSVGYCKDYDILKLLLE 256
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
479-504 |
2.49e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.19 E-value: 2.49e-04
10 20
....*....|....*....|....*..
gi 55741815 479 KGLTPLHLAS-REGHVKVVELLLRKGA 504
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
545-572 |
3.98e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.98e-04
10 20
....*....|....*....|....*...
gi 55741815 545 DGNTALHLAARAGHVAAVRLLLYRGAKI 572
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
546-598 |
4.99e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.18 E-value: 4.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 55741815 546 GNTALHLAARAGHVAAVRLLLYRGAKI-ILNKNDASFLHEAVHNARREVTNMVI 598
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
46-137 |
5.13e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 44.10 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 46 ALEKNSRYLDTRDNIGASPLHYASAnghfRIIRH-IVQIVGHQELNVRDEE---GNTPLHWAVQKDQpgSCSVLLSLGAD 121
Cdd:PHA02878 219 ILLENGASTDARDKCGNTPLHISVG----YCKDYdILKLLLEHGVDVNAKSyilGLTALHSSIKSER--KLKLLLEYGAD 292
|
90
....*....|....*.
gi 55741815 122 PNVLNNSHQAPIHMAV 137
Cdd:PHA02878 293 INSLNSYKLTPLSSAV 308
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
479-504 |
5.24e-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: 5.24e-04
10 20
....*....|....*....|....*.
gi 55741815 479 KGLTPLHLASREGHVKVVELLLRKGA 504
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
63-116 |
1.07e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 55741815 63 SPLHYASANGHFRIIRHIVQivGHQELNVRDEEGNTPLHWAVQKDQPGSCSVLL 116
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
545-572 |
1.17e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.24 E-value: 1.17e-03
10 20
....*....|....*....|....*...
gi 55741815 545 DGNTALHLAARAGHVAAVRLLLYRGAKI 572
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
395-451 |
1.27e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 1.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 55741815 395 LQHESVRelLNDEDIEGCTPLHYACRLGIPDSVKNMLGLEVSLDQKSKEKKSALHFA 451
Cdd:pfam13857 2 LEHGPID--LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
95-127 |
1.39e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|....
gi 55741815 95 EGNTPLHWAV-QKDQPGSCSVLLSLGADPNVLNN 127
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
388-508 |
1.57e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 388 KNLPTEVLQHESVRELLNDEdiegctplhyACRLGIP-DSVKNMLGLEVSLDQKSKE--KKSALHFAAEFGRINTCHRLL 464
Cdd:PTZ00322 66 HNLTTEEVIDPVVAHMLTVE----------LCQLAASgDAVGARILLTGGADPNCRDydGRTPLHIACANGHVQVVRVLL 135
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 55741815 465 EMVTDTRLLnegDEKGLTPLHLASREGHVKVVELLLRKGALFHS 508
Cdd:PTZ00322 136 EFGADPTLL---DKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
56-179 |
3.16e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.55 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 56 TRDNIGASPLHY--ASANGHFRIIRHIvqIVGHQELNVRDEEGNTPLHWAVQKdqpGSC--SVLLSL---GADPNVLNNS 128
Cdd:PHA03095 182 AVDDRFRSLLHHhlQSFKPRARIVREL--IRAGCDPAATDMLGNTPLHSMATG---SSCkrSLVLPLliaGISINARNRY 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 55741815 129 HQAPIHMAVSLGKNFVLEQLVshKQ-TDVNLEGDLGNTPVILSAALDNHEAL 179
Cdd:PHA03095 257 GQTPLHYAAVFNNPRACRRLI--ALgADINAVSSDGNTPLSLMVRNNNGRAV 306
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
54-127 |
3.69e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 41.19 E-value: 3.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55741815 54 LDTRDNIGASPLHYASANGHFRIIRHIVQiVGhQELNVRDEEGNTPLHWAVQKDQPGSCSVLLSLGADPNVLNN 127
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLD-LG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
239-264 |
4.55e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 4.55e-03
10 20
....*....|....*....|....*.
gi 55741815 239 SPLHLAVRGGNLDIIKLCIGYGAKID 264
Cdd:smart00248 4 TPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
479-504 |
5.89e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 5.89e-03
10 20
....*....|....*....|....*.
gi 55741815 479 KGLTPLHLASREGHVKVVELLLRKGA 504
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGA 26
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
239-264 |
6.56e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.31 E-value: 6.56e-03
10 20
....*....|....*....|....*.
gi 55741815 239 SPLHLAVRGGNLDIIKLCIGYGAKID 264
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
324-500 |
6.87e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 40.42 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 324 EYLMSQGANIDFVDCKGHSPLLLATSCGAWRTVNLLLSHGADLTKKDKSGCNFLHLailqprgLKNLPTEVLQHESV--- 400
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-------LSGTDDEVIERINLlvq 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 401 --RELLNDEDIEGCTPLhYACRLGIPDSVKNML--GLEVSLDQKSKEKKSALHFAAEFGRINTCHRLLEMVTDTrllNEG 476
Cdd:PHA02946 129 ygAKINNSVDEEGCGPL-LACTDPSERVFKKIMsiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISP---SKP 204
|
170 180
....*....|....*....|....*.
gi 55741815 477 DEKGLTPLHLASRE--GHVKVVELLL 500
Cdd:PHA02946 205 DHDGNTPLHIVCSKtvKNVDIINLLL 230
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
54-206 |
7.10e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.43 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 54 LDTRDNIGASPLHYASANGHFRIIRHIVQIvgHQELNVRDEEGNTPLHWAVQKDQP-GSCSVLLSLGADPNVLNNSHQAP 132
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDY--GADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTP 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55741815 133 IHMAVSLG-KNFVLEQLVSHKqTDVNLEGDLGNTPVILsaALDNHEALGILYKHGAKFcRQNNLGHFPIHAAAFS 206
Cdd:PHA02876 446 LHYACKKNcKLDVIEMLLDNG-ADVNAINIQNQYPLLI--ALEYHGIVNILLHYGAEL-RDSRVLHKSLNDNMFS 516
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
538-570 |
7.58e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 7.58e-03
10 20 30
....*....|....*....|....*....|...
gi 55741815 538 LLNKTDGDGNTALHLAARAGHVAAVRLLLYRGA 570
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV 40
|
|
| YybS |
COG4241 |
Uncharacterized conserved protein YybS, DUF2232 family [Function unknown]; |
708-952 |
8.50e-03 |
|
Uncharacterized conserved protein YybS, DUF2232 family [Function unknown];
Pssm-ID: 443383 Cd Length: 318 Bit Score: 39.82 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 708 KWSAYGIkahLLNMTVYALGVFPLTYLIVnlkpTLVTSRNVTSVNMvctSLYKQSYLTTSSMllvlaMNMYAVGKEILQM 787
Cdd:COG4241 97 KKSAFET---LLAGTLAFLISTVILFLLS----QLLFGINPFDELI---NAMKESFNEAIEL-----YESMGMSEEQLEQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 788 FQQRLNYLRDLSNYMdwaaaICALLFVVpllmnlksswhwqagalAALTSWLNLLLYLQRFERIGIYVVMFREISRTLLS 867
Cdd:COG4241 162 MREQLEEMIELLKLL-----LPAILIIA-----------------SFLLAFINYLVARKILKRLGYKVPKFPPFREWRLP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 868 IIVLFFYLIlGFALSFYALMIEQQHFGRMFLSLLQTFVMMVgemnyqdnfmkpYLQGdlpfpdltLAIFVWFV------L 941
Cdd:COG4241 220 RSVLWIYII-VLLLLLFGDPEEISLLYIIGLNLLVILSFLF------------LLQG--------LSFIFYYLkkkklpK 278
|
250
....*....|.
gi 55741815 942 LVPILLMNLLI 952
Cdd:COG4241 279 FVRILIVILLI 289
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
20-104 |
8.59e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 40.24 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741815 20 DNVMDGDESNqISANVFEWTKQGNAAALE---KNSRYLDTRDNIGASPLHYASANGH----FRIIRHIVQIvghqelNVR 92
Cdd:PLN03192 515 DNGGEHDDPN-MASNLLTVASTGNAALLEellKAKLDPDIGDSKGRTPLHIAASKGYedcvLVLLKHACNV------HIR 587
|
90
....*....|..
gi 55741815 93 DEEGNTPLHWAV 104
Cdd:PLN03192 588 DANGNTALWNAI 599
|
|
| |
