|
Name |
Accession |
Description |
Interval |
E-value |
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
29-636 |
0e+00 |
|
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: 1205.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 29 WAQSRDEQNLLQQKRIWESPLLLAAKENNVQALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEAAPELVFE 108
Cdd:cd22192 1 WAQMLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 109 PMTSELYEGQTALHIAVINQNVNLVRALLARGASV-SARATGSVFHYRPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGA 187
Cdd:cd22192 81 PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvSPRATGTFFRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 188 DIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDGGDHLKSLELVPNNQGLTPFKLAGVEGNIVMFQHLMQKRKHIQW 267
Cdd:cd22192 161 DIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 268 TYGPLTSTLYDLTEIDSSGDDQSLLELIVTTKKREARQILDQTPVKELVSLKWKRYGRPYFCVLGAIYVLYIICFTMCCV 347
Cdd:cd22192 241 TYGPLTSTLYDLTEIDSWGDEQSVLELIVSSKKREARKILDVTPVKELVSLKWKRYGRPYFRILALLYLLYIIIFTLCCV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 348 YRPLKPRITNRTNPRDNTLLQQKLLQEAYVTPKDDLRLVGELVSIVGAVIILLVEIPDIFRLGVTRFFGQTILGGPFHVI 427
Cdd:cd22192 321 YRPLKPRPENNTDPRDITLYVQKTLQESYVTPKDYLRLVGELISVLGAIVILLLEIPDILRVGVKRYFGQTVLGGPFHVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 428 IVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAF 507
Cdd:cd22192 401 IITYACLVLLTLVLRLTSLSGEVVPMSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIFGDLMKFCWLMFVVILGFSSAF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 508 YIIFQTEDPDELGHFYDYPMALFSTFELFLTIIDGPANYDVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHE 587
Cdd:cd22192 481 YMIFQTEDPDSLGHFYDFPMTLFSTFELFLGLIDGPANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHE 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1937369764 588 RDELWRAQVVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQ 636
Cdd:cd22192 561 RDELWRAQVVATTLMLERRLPRCLWPRSGICGKEYGLGDRWYLRVEDRN 609
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
61-635 |
0e+00 |
|
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: 878.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 61 LIKLLKFEGC-------EVHQKGAMGETALHIAALYDN---LEAAMVLMEAAP------ELVFEPMTSELYEGQTALHIA 124
Cdd:cd21882 1 LEELLGLLEClrwyltdSAYQRGATGKTCLHKAALNLNdgvNEAIMLLLEAAPdsgnpkELVNAPCTDEFYQGQTALHIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 125 VINQNVNLVRALLARGASVSARATGSVFHYRPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIR---AQDSLGNTVLH 201
Cdd:cd21882 81 IENRNLNLVRLLVENGADVSARATGRFFRKSPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAaleAQDSLGNTVLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 202 ILILQPNKT-----FACQMYNLLLSYDG-GDHLKSLELVPNNQGLTPFKLAGVEGNIVMFQHLMQK----------RKHI 265
Cdd:cd21882 161 ALVLQADNTpensaFVCQMYNLLLSYGAhLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQRefsgpyqplsRKFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 266 QWTYGPLTSTLYDLTEIDSSGDDqSLLELIVTTKKREAR-QILDQTPVKELVSLKWKRYGRPYFCVLGAIYVLYIICFTM 344
Cdd:cd21882 241 EWTYGPVTSSLYDLSEIDSWEKN-SVLELIAFSKKREARhQMLVQEPLNELLQEKWDRYGRPYFCFNFACYLLYMIIFTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 345 CCVYRPLKPRITNrtnprdntllqqkllQEAYVTPKDDLRLVGELVSIVGAVIILLVEIPDIFRLGVTRFFGqtILGGPF 424
Cdd:cd21882 320 CAYYRPLKDRPAN---------------QEAKATFGDSIRLVGEILTVLGGVYILLGEIPYFFRRRLSRWFG--FLDSYF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 425 HVIIVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFA 504
Cdd:cd21882 383 EILFITQALLVLLSMVLRFMETEGYVVPLVFSLVLGWCNVLYYTRGFQMLGIYTVMIQKMILRDLMRFCWVYLVFLFGFA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 505 SAFYIIFQTEDPDELGHFYDYPMALFSTFELFLTIIDGPANYDVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRV 584
Cdd:cd21882 463 SAFVILFQTEDPNKLGEFRDYPDALLELFKFTIGMGDLPFNENVDFPFVYLILLLAYVILTYLLLLNMLIALMGETVNRV 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369764 585 AHERDELWRAQVVATTVMLERKLPRCLWPRSG-------ICGREYGLGDRWFLRVEDR 635
Cdd:cd21882 543 AQESDEIWKLQKAITTLMLERKYPRCLRKRSRegrllkvGCGGDGGLDDRWCFRVEEV 600
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
12-708 |
0e+00 |
|
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: 796.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 12 ILCLWNKFCRWFHRRESWAQSRDEQN--LLQQK---RIWESPLLLAAKENNVQALIKLLKFEGCEvhqkGAMGETALHIA 86
Cdd:TIGR00870 14 LSDEEKAFLPAAERGDLASVYRDLEEpkKLNINcpdRLGRSALFVAAIENENLELTELLLNLSCR----GAVGDTLLHAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 87 AL--YDNLEAAMVLMEAA------PELVFEPMTSELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVFHYRPH- 157
Cdd:TIGR00870 90 SLeyVDAVEAILLHLLAAfrksgpLELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQGv 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 158 NLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQP-----NKTFACQMYNLLLSYDGG-DHLKSL 231
Cdd:TIGR00870 170 DSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENefkaeYEELSCQMYNFALSLLDKlRDSKEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 232 ELVPNNQGLTPFKLAGVEGNIVMFQHLMQ----KRKHIQWTYGPLTSTLYDLTEIDSSGDDQSLLELIVTT----KKREA 303
Cdd:TIGR00870 250 EVILNHQGLTPLKLAAKEGRIVLFRLKLAikykQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVFviglKFPEL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 304 RQILDQTPVKELVSLKWKRYGRPYFCVLGAIYVLYIICFTMCCVYRPLkpritnRTNPRdNTLLQQKLLQEAYVTPKDDL 383
Cdd:TIGR00870 330 SDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPT------RTDLR-VTGLQQTPLEMLIVTWVDGL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 384 RLVGELVSIVGAVIILLVEIPDIFRLGVTRFFGQTILGGPFHVIIVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCN 463
Cdd:TIGR00870 403 RLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWLN 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 464 VMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPDELGH------------FYDYPMALFS 531
Cdd:TIGR00870 483 LLYIFRGNQHLGPLQIMIGRMILGDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNEcsnpharscekqGNAYSTLFET 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 532 TFELFLTIIDG---PANYDVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQVVATTVMLERKLP 608
Cdd:TIGR00870 563 SQELFWAIIGLgdlLANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 609 RCLWPRSGICGREYGLGdrWFLRVEDRQDLNRQRIRRYAQAFQQQD-DLYSEDLEKD-SGEKLEMARPFGAYLSFPTPSV 686
Cdd:TIGR00870 643 TCPPPFNIIPGPKSFVG--LFKRIEKHDGKKRQRWCRRVEEVNWTTwERKAETLIEDgLHYQRVMKRLIKRYVLAEQRPR 720
|
730 740
....*....|....*....|...
gi 1937369764 687 SRSTSRSS-TNWERLRQGALRKD 708
Cdd:TIGR00870 721 DDEGTTEEeTKELKQDISSLRFE 743
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
104-634 |
1.87e-100 |
|
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: 321.36 E-value: 1.87e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 104 ELVFEPMTSELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVFH-YRPHNLIYYGEHPLSFAACVGSEEIVRLL 182
Cdd:cd22193 63 RFINAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQpKYQGEGFYFGELPLSLAACTNQPDIVQYL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 183 IEHG---ADIRAQDSLGNTVLHILIL-----QPNKTFACQMYNLLLSYDGGDH-LKSLELVPNNQGLTPFKLAGVEGNIV 253
Cdd:cd22193 143 LENEhqpADIEAQDSRGNTVLHALVTvadntKENTKFVTRMYDMILIRGAKLCpTVELEEIRNNDGLTPLQLAAKMGKIE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 254 MFQHLMQK-----------RKHIQWTYGPLTSTLYDLTEIDSSGDDqSLLELIVTTKKREAR-QILDQTPVKELVSLKWK 321
Cdd:cd22193 223 ILKYILQReikepelrhlsRKFTDWAYGPVSSSLYDLSNVDTCEKN-SVLEIIVYNSKIDNRhEMLTLEPLNTLLQDKWD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 322 RYGRPYFCVLGAIYVLYIICFTMCCVYRPLkpritnrtnprdntlLQQKLLQEAYVTPKDDLRLVGELVSIVGAVIILLV 401
Cdd:cd22193 302 KFAKYMFFFSFCFYLFYMIIFTLVAYYRPR---------------EDEPPPPLAKTTKMDYMRLLGEILVLLGGVYFFVK 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 402 EIPDIFRlgvTRFFGQTIL-GGPFHVIIVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIM 480
Cdd:cd22193 367 EIAYFLL---RRSDLQSSFsDSYFEILFFVQAVLVILSVVLYLFAYKEYLACLVLALALGWANMLYYTRGFQSMGIYSVM 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 481 IQKMIFGDLMRFCWLMAVVILGFASAFYII-----FQTEDPDELGHFYDYPMALFStfelfLTIIDGPANY--DVDLPFM 553
Cdd:cd22193 444 IQKVILRDLLRFLFVYLLFLFGFAVALVSLiekcsSDKKDCSSYGSFSDAVLELFK-----LTIGMGDLEFqeNSTYPAV 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 554 YSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQVVATTVMLERKLPRCLWP--RSG--ICGREYGLGD--- 626
Cdd:cd22193 519 FLILLLTYVILTFVLLLNMLIALMGETVNNVSKESKRIWKLQRAITILEFEKSFPECMRKafRSGrlLKVGLCKDGTpdf 598
|
....*...
gi 1937369764 627 RWFLRVED 634
Cdd:cd22193 599 RWCFRVDE 606
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
111-634 |
3.73e-95 |
|
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: 309.77 E-value: 3.73e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 111 TSELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVFHYR-PHNLIYYGEHPLSFAACVGSEEIVRLLIEHGAD- 188
Cdd:cd22194 135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFNPKyKHEGFYFGETPLALAACTNQPEIVQLLMEKESTd 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 189 IRAQDSLGNTVLHILI-----LQPNKTFACQMYNLLLSYDGGdhlKSLELVPNNQGLTPFKLAGVEGNIVMFQHLMQK-- 261
Cdd:cd22194 215 ITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMILLKSEN---KNLETIRNNEGLTPLQLAAKMGKAEILKYILSRei 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 262 ---------RKHIQWTYGPLTSTLYDLTEIDsSGDDQSLLELIVTTKKREARQ-ILDQTPVKELVSLKWKRYGRPYFCVL 331
Cdd:cd22194 292 kekpnrslsRKFTDWAYGPVSSSLYDLTNVD-TTTDNSVLEIIVYNTNIDNRHeMLTLEPLHTLLHMKWKKFARYMFFIS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 332 GAIYVLYIICFTMCCVYRplkpritnrtnPRDNTLLQQKLLQEAYVTPkddLRLVGELVSIVGAVIILLVEIPDIFRLGV 411
Cdd:cd22194 371 FLFYFFYNITLTLVSYYR-----------PREDEDPPHPLALSHKMGW---LQLLGQMFVLIWATCLSVKEGIAIFLLRP 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 412 TRFfgQTILGGP-FHVIIVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLM 490
Cdd:cd22194 437 SDL--KSILSDAwFHILFFIQAVLVIVSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSLGIYSVMIQKVILNDVL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 491 RFCWLMAVVILGFASAFYIIFQT-EDPDELGHFYDYPMALFSTFELFLTIIDGPANYDVDLPFMYSITYAAFAIIATLLM 569
Cdd:cd22194 515 KFLLVYILFLLGFGVALASLIEDcPDDSECSSYGSFSDAVLELFKLTIGLGDLEIQQNSKYPILFLLLLITYVILTFVLL 594
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369764 570 LNLLIAMMGDTHWRVAHERDELWRAQVVATTVMLERKLPRCL--WPRSGICGREYGLGDRWFLRVED 634
Cdd:cd22194 595 LNMLIALMGETVENVSKESERIWRLQRARTILEFEKSLPEWLrkRFRLGELCKVADEDFRLCLRINE 661
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
79-634 |
7.14e-91 |
|
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: 297.49 E-value: 7.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 79 GETALHIAALydNLEAAM-----VLMEAA------PELVFEPMTSELYEGQTALHIAVINQNVNLVRALLARGASVSARA 147
Cdd:cd22196 47 GKTCLLKAML--NLHNGQndtisLLLDIAektgnlKEFVNAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 148 TGSVFHY-RPHNLIYYGEHPLSFAACVGSEEIVRLLIEH---GADIRAQDSLGNTVLHILI-----LQPNKTFACQMYNL 218
Cdd:cd22196 125 SGEFFKKkKGGPGFYFGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLHALVevadnTPENTKFVTKMYNE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 219 LLSYDGGDH-LKSLELVPNNQGLTPFKLAGVEGNIVMFQHLMQK-----------RKHIQWTYGPLTSTLYDLTEIDSSg 286
Cdd:cd22196 205 ILILGAKIRpLLKLEEITNKKGLTPLKLAAKTGKIGIFAYILGReikepecrhlsRKFTEWAYGPVHSSLYDLSSIDTY- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 287 DDQSLLELIVTTKKREAR-QILDQTPVKELVSLKWKRYGRPYFCVLGAIYVLYIICFTMCCVYRPlkpritnrtnprdnt 365
Cdd:cd22196 284 EKNSVLEIIAYSSETPNRhEMLLVEPLNKLLQDKWDKFVKRIFYFNFFVYFIYMIIFTLAAYYRP--------------- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 366 llQQKLLQEAY-VTPKDDLRLVGELVSIVGAVIILLVEIPDIFRLGVTRffGQTILGGPFHVIIVTYAFMVLVTMVMRLT 444
Cdd:cd22196 349 --VNKTPPFPIeNTTGEYLRLTGEIISVSGGVYFFFRGIQYFLQRRPSL--KKLIVDSYCEILFFVQSLFLLASTVLYFC 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 445 NSDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPDELGHFYD 524
Cdd:cd22196 425 GRNEYVAFMVISLALGWANVLYYTRGFQQMGIYSVMIQKMILRDICRFLFVYLVFLFGFSAALVTLIEDGPPKGDVNTSQ 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 525 YPM----------ALFSTF-ELF-LTIIDGPANYDVDLPF--MYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDE 590
Cdd:cd22196 505 KECvcksgynsynSLYSTClELFkFTIGMGDLEFTENYKFkeVFIFLLISYVILTYILLLNMLIALMGETVSKIAQESKN 584
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1937369764 591 LWRAQVVATTVMLERKLPRCLWP--RSG---ICGREYGLGD--RWFLRVED 634
Cdd:cd22196 585 IWKLQRAITILDLEKSLLRCLRDrfRSGksvLVGITPDGKEdyRWCFRVDE 635
|
|
| TRPV4 |
cd22195 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ... |
104-634 |
5.13e-88 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain] Cd Length: 733 Bit Score: 292.14 E-value: 5.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 104 ELVFEPMTSELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVFHYRPHN-LIYYGEHPLSFAACVGSEEIVRLL 182
Cdd:cd22195 124 EFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGgYFYFGELPLSLAACTNQPDIVHYL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 183 IEHG---ADIRAQDSLGNTVLHILI-----LQPNKTFACQMYNLLLsydggdhLK--------SLELVPNNQGLTPFKLA 246
Cdd:cd22195 204 TENAhkkADLRRQDSRGNTVLHALVaiadnTRENTKFVTKMYDLLL-------IKcaklypdcNLEAILNNDGMSPLMMA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 247 GVEGNIVMFQHLMQK-----------RKHIQWTYGPLTSTLYDLTEIDSSGDDQSLLELIVTTKKREAR-QILDQTPVKE 314
Cdd:cd22195 277 AKLGKIGIFQHIIRReikdeearhlsRKFKDWAYGPVYSSLYDLSSLDTCGEEVSVLEILVYNSKIENRhEMLAVEPINE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 315 LVSLKWKRYGRPYFCVLGAIYVLYIICFTMCCVYRPLKPritnrTNPRdntllqqkllqeAYVTPKDDLRLVGELVSIVG 394
Cdd:cd22195 357 LLRDKWRKFGAVSFYISVVSYLVAMIIFTLIAYYRPMEG-----TPPY------------PYRTTVDYLRLAGEIITLLT 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 395 AVIILLVEIPDIFRL---GVTRFFgqtiLGGPFHVIIVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCNVMYFARGF 471
Cdd:cd22195 420 GIFFFFTNIKDLFMKkcpGVNSLF----IDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFALVLGWMNALYFTRGL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 472 QMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPDEL-------GHFYDYPM----ALFSTF--ELF-L 537
Cdd:cd22195 496 KLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPTKETckedstnCTVPTYPScrdsNTFSKFllDLFkL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 538 TIIDGpanyDVDL------PFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQVVATTVMLERKLPRCL 611
Cdd:cd22195 576 TIGMG----DLEMlnsakyPAVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTILDIERSFPVFL 651
|
570 580 590
....*....|....*....|....*....|
gi 1937369764 612 WP--RSG---ICGREY-GLGD-RWFLRVED 634
Cdd:cd22195 652 RKafRSGemvTVGKNLdGTPDrRWCFRVDE 681
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
104-634 |
2.83e-80 |
|
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: 269.03 E-value: 2.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 104 ELVFEPMTSELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVFHYRPHNLIYYGEHPLSFAACVGSEEIVRLLI 183
Cdd:cd22197 81 PLVNAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKQGTCFYFGELPLSLAACTKQWDVVNYLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 184 EHGAD---IRAQDSLGNTVLHILIL-----QPNKTFACQMYNLLLSYDGG-DHLKSLELVPNNQGLTPFKLAGVEGNIVM 254
Cdd:cd22197 161 ENPHQpasLQAQDSLGNTVLHALVMiadnsPENSALVIKMYDGLLQAGARlCPTVQLEEISNHEGLTPLKLAAKEGKIEI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 255 FQHLMQK----------RKHIQWTYGPLTSTLYDLTEIDSSGDDqSLLELIVTTKKREAR-QILDQTPVKELVSLKWKRY 323
Cdd:cd22197 241 FRHILQRefsgpyqhlsRKFTEWCYGPVRVSLYDLSSVDSWEKN-SVLEIIAFHSKSPNRhRMVVLEPLNKLLQEKWDRL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 324 GrPYFCVLGAIYVLYIICFTMCCVYRPLkpritnrtnprdntlLQQKLLQEAYVTPKDDLRLVGELVSIVGAVIILLVEI 403
Cdd:cd22197 320 V-SRFYFNFLCYLVYMFIFTVVAYHQPL---------------LDQPPIPPLKATAGGSMLLLGHILILLGGIYLLLGQL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 404 pdIFRLGVTRFFGQTILGGPFHVIIVTYAFMVLVTMVMRLTNSDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQK 483
Cdd:cd22197 384 --WYFWRRRLFIWISFMDSYFEILFLLQALLTVLSQVLYFMGSEWYLPLLVFSLVLGWLNLLYYTRGFQHTGIYSVMIQK 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 484 MIFGDLMRFCWLMAVVILGFASAF-------------------YIIFQTEDPDELGhfYDYPMALFSTFELF-LTIIDGP 543
Cdd:cd22197 462 VILRDLLRFLLVYLVFLFGFAVALvslsreapspkapednnstVTEQPTVGQEEEP--APYRSILDASLELFkFTIGMGE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 544 ANYDVDLPFMYSITY--AAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQVVATTVMLERKLPRCLWPRSGIcGRE 621
Cdd:cd22197 540 LAFQEQLRFRGVVLLllLAYVLLTYVLLLNMLIALMSETVNHVADNSWSIWKLQKAISVLEMENGYWWCRRKKQRE-GRL 618
|
570 580
....*....|....*....|.
gi 1937369764 622 YGLG--------DRWFLRVED 634
Cdd:cd22197 619 LTVGtrpdgtpdERWCFRVEE 639
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-294 |
2.71e-27 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 112.35 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 36 QNLLQQKRIWESPLLLAAKENNVQALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEAAPELvfepmTSELY 115
Cdd:COG0666 44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-----NARDK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 116 EGQTALHIAVINQNVNLVRALLARGASVSARATgsvfhyrphnliyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSL 195
Cdd:COG0666 119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-------------DGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 196 GNTVLHILILQPNKtfacQMYNLLLSYdGGDHlksleLVPNNQGLTPFKLAGVEGNIVMFQHLMQKRKHIQWTYGPLTST 275
Cdd:COG0666 186 GETPLHLAAENGHL----EIVKLLLEA-GADV-----NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250
....*....|....*....
gi 1937369764 276 LYDLTEIDSSGDDQSLLEL 294
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLA 274
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
37-229 |
2.12e-21 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 95.02 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 37 NLLQQKRIWESPLLLAAKENNVqALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPmtselYE 116
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNL-EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-----ND 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 117 GQTALHIAVINQNVNLVRALLARGASVSARATgsvfhyrphnliyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLG 196
Cdd:COG0666 186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDN-------------DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
|
170 180 190
....*....|....*....|....*....|...
gi 1937369764 197 NTVLHILILQPNKTFACQMYNLLLSYDGGDHLK 229
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
49-261 |
7.71e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 90.40 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 49 LLLAAKENNVQALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEAApelvfEPMTSELYEGQTALHIAVINQ 128
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG-----ADINAKDDGGNTLLHAAARNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 129 NVNLVRALLARGASVSARATgsvfhyrphnliyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPN 208
Cdd:COG0666 99 DLEIVKLLLEAGADVNARDK-------------DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937369764 209 KTFAcqmyNLLLSYdgGDHLKslelVPNNQGLTPFKLAGVEGNIVMFQHLMQK 261
Cdd:COG0666 166 LEIV----KLLLEA--GADVN----ARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
49-146 |
1.41e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.15 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 49 LLLAAKENNVQaLIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEaapelvfEPMTSELYEGQTALHIAVINQ 128
Cdd:pfam12796 1 LHLAAKNGNLE-LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKDNGRTALHYAARSG 72
|
90
....*....|....*...
gi 1937369764 129 NVNLVRALLARGASVSAR 146
Cdd:pfam12796 73 HLEIVKLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
83-193 |
2.16e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.07 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 83 LHIAALYDNLEAAMVLMEAAPElvfepMTSELYEGQTALHIAVINQNVNLVRALLARGASvsaratgsvfhyrphNLIYY 162
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAD-----ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---------------NLKDN 60
|
90 100 110
....*....|....*....|....*....|.
gi 1937369764 163 GEHPLSFAACVGSEEIVRLLIEHGADIRAQD 193
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ion_trans |
pfam00520 |
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
371-589 |
9.02e-14 |
|
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: 71.53 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 371 LLQEAYVTPKDDLRLVGELVSIVGAVIILLVEIPDIFRLGVTRFFgqtiLGGPFHVIIVTYAFMVLVTMVMRLTNSDGEV 450
Cdd:pfam00520 19 LALETYFQPEEPLTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRY----FRSPWNILDFVVVLPSLISLVLSSVGSLSGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 451 VPMSFALVLgwcnvmYFARGFQMLGPFTIMIQ--KMIFGDLMRFCWLMAVVILGFASAFYIIFQT------EDPDELGHF 522
Cdd:pfam00520 95 RVLRLLRLL------RLLRLIRRLEGLRTLVNslIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGklktweNPDNGRTNF 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 523 YDYPMALFSTFELFLTIIDG---PANYDVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERD 589
Cdd:pfam00520 169 DNFPNAFLWLFQTMTTEGWGdimYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
47-260 |
4.72e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.35 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 47 SPLLLAAKENNVQALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVlmEAAPELVFEPMTSELYeGQTALHIAVI 126
Cdd:PHA03095 85 TPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPKVI--RLLLRKGADVNALDLY-GMTPLAVLLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 127 NQNVN--LVRALLARGASVSARAT--GSVFHYrphnliyygeHPLSFAAcvgSEEIVRLLIEHGADIRAQDSLGNTVLHI 202
Cdd:PHA03095 162 SRNANveLLRLLIDAGADVYAVDDrfRSLLHH----------HLQSFKP---RARIVRELIRAGCDPAATDMLGNTPLHS 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369764 203 LILQpNKTFACQMYNLLLSYDGGDhlkslelVPNNQGLTPFKLAGVEGNIVMFQHLMQ 260
Cdd:PHA03095 229 MATG-SSCKRSLVLPLLIAGISIN-------ARNRYGQTPLHYAAVFNNPRACRRLIA 278
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
53-219 |
1.39e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 57.73 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 53 AKENNVQALIKllkfEGCEVHQKGAMGETALHIAALYDN---LEAAMVLMEA-----APELV-FEPMTSELYE------- 116
Cdd:PHA03095 25 VTVEEVRRLLA----AGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAgadvnAPERCgFTPLHLYLYNattldvi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 117 ----------------GQTALHIAVINQNVN--LVRALLARGASVSARATgsvfhyrphnliyYGEHPL-----SFAACV 173
Cdd:PHA03095 101 kllikagadvnakdkvGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDL-------------YGMTPLavllkSRNANV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937369764 174 gseEIVRLLIEHGADIRAQDSLGNTVLHIlILQPNKTFACQMYNLL 219
Cdd:PHA03095 168 ---ELLRLLIDAGADVYAVDDRFRSLLHH-HLQSFKPRARIVRELI 209
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
167-265 |
2.34e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.96 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 167 LSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHIlilqpnktfACQMYN-----LLLSYDGGDHlkslelvpNNQGLT 241
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL---------AAKNGHleivkLLLEHADVNL--------KDNGRT 63
|
90 100
....*....|....*....|....
gi 1937369764 242 PFKLAGVEGNIVMFQHLMQKRKHI 265
Cdd:pfam12796 64 ALHYAARSGHLEIVKLLLEKGADI 87
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
47-208 |
1.10e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 51.99 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 47 SPLLLAAKENNVQALIKLLKFEGCEVHQKGAMGETALHIAAL--YDNLEAAMVLMEAAPElvfePMTSELYegQTALHIA 124
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKngYDTENIRTLIMLGADV----NAADRLY--ITPLHQA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 125 -VINQNVNLVRALLARGASVSARAtgsvfhyrphnliYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHIL 203
Cdd:PHA02876 349 sTLDRNKDIVITLLELGANVNARD-------------YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
|
....*
gi 1937369764 204 ILQPN 208
Cdd:PHA02876 416 LCGTN 420
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
47-215 |
1.28e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.53 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 47 SPLLLAAKENNVQAlIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEA---APELVFEpmtselyEGQTALHI 123
Cdd:PHA02875 37 SPIKLAMKFRDSEA-IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkfADDVFYK-------DGMTPLHL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 124 AVINQNVNLVRALLARGASVSARATGSVfhyrphnliyygeHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHIL 203
Cdd:PHA02875 109 ATILKKLDIMKLLIARGADPDIPNTDKF-------------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
|
170
....*....|..
gi 1937369764 204 ILQPNkTFACQM 215
Cdd:PHA02875 176 MAKGD-IAICKM 186
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
48-222 |
1.30e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.59 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 48 PLLLAAKENNVQALIKLLKfEGCEVHQKGAMGETALHIAALY-----DNLEAAMVLME--AAPElvfepmtSELYEGQTA 120
Cdd:PHA03100 38 PLYLAKEARNIDVVKILLD-NGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEygANVN-------APDNNGITP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 121 LHIAVIN--QNVNLVRALLARGASVSA-RATG-SVFHY---RPHN-------LIY------------------------- 161
Cdd:PHA03100 110 LLYAISKksNSYSIVEYLLDNGANVNIkNSDGeNLLHLyleSNKIdlkilklLIDkgvdinaknrvnyllsygvpinikd 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369764 162 -YGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFacqmYNLLLSY 222
Cdd:PHA03100 190 vYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI----FKLLLNN 247
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
46-201 |
4.75e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 50.06 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 46 ESPLLLAAKENNVQALIKLLKFEGCEVHQKGAMGETALHIAALYD-NLEAAMVLMEAAPELvfepmTSELYEGQTALHIA 124
Cdd:PHA02876 308 ETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANV-----NARDYCDKTPIHYA 382
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369764 125 VINQNVNLVRALLARGASVSA--RATGSVFHYrphnlIYYGEHPLSfaacvgseeIVRLLIEHGADIRAQDSLGNTVLH 201
Cdd:PHA02876 383 AVRNNVVIINTLLDYGADIEAlsQKIGTALHF-----ALCGTNPYM---------SVKTLIDRGANVNSKNKDLSTPLH 447
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
69-205 |
6.55e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 69 GCEVHQKGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTselyeGQTALHIAVINQNVNLVRALLARGASVSARAt 148
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN-----GCYPIHIAIKHNFFDIIKLLLEKGAYANVKD- 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369764 149 gsvfhyrphnliYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILIL 205
Cdd:PHA02874 188 ------------NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
117-202 |
1.03e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 48.72 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 117 GQTALHIAVINQNVNLVRALLARGASVSARATGSvfhyrphnliyygEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLG 196
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTN-------------NSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234
|
....*.
gi 1937369764 197 NTVLHI 202
Cdd:PHA02878 235 NTPLHI 240
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
47-222 |
4.29e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.58 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 47 SPLLLAA-KENNVQALIKLLKFEGCEVHQKGAMGETALHIAALY--DNLEAAMVLMEAAP------------ELVFEPMT 111
Cdd:PHA03100 108 TPLLYAIsKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGVdinaknrvnyllSYGVPINI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 112 SELYeGQTALHIAVINQNVNLVRALLARGASVsaratgsvfhyrphNLI-YYGEHPLSFAACVGSEEIVRLLIEHGADIR 190
Cdd:PHA03100 188 KDVY-GFTPLHYAVYNNNPEFVKYLLDLGANP--------------NLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
170 180 190
....*....|....*....|....*....|..
gi 1937369764 191 AQDSlgntvlHILILQPNKTFACQMYNLLLSY 222
Cdd:PHA03100 253 TIIE------TLLYFKDKDLNTITKIKMLKKS 278
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
47-198 |
6.46e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 46.17 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 47 SPLLLAAKENNVQ-ALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAmvLMEAAPELVFEPMTSELYeGQTALHIAV 125
Cdd:PHA03095 154 TPLAVLLKSRNANvELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAR--IVRELIRAGCDPAATDML-GNTPLHSMA 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369764 126 INQNVN--LVRALLARGASVSARatgsvfhyrphNLiyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNT 198
Cdd:PHA03095 231 TGSSCKrsLVLPLLIAGISINAR-----------NR--YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
112-202 |
7.77e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 112 SELYEgqTALHIAVINQNVNL--VRALLARGASVSaratgsvfHYRPHNLIYYGEHPLSFAACVgSEEIVRLLIEHGADI 189
Cdd:PHA02859 48 NDLYE--TPIFSCLEKDKVNVeiLKFLIENGADVN--------FKTRDNNLSALHHYLSFNKNV-EPEILKILIDSGSSI 116
|
90
....*....|...
gi 1937369764 190 RAQDSLGNTVLHI 202
Cdd:PHA02859 117 TEEDEDGKNLLHM 129
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
162-193 |
1.66e-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: 1.66e-04
10 20 30
....*....|....*....|....*....|...
gi 1937369764 162 YGEHPLSFAAC-VGSEEIVRLLIEHGADIRAQD 193
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
165-202 |
1.68e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 1.68e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1937369764 165 HPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHI 202
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
116-145 |
3.34e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.39 E-value: 3.34e-04
10 20 30
....*....|....*....|....*....|
gi 1937369764 116 EGQTALHIAVINQNVNLVRALLARGASVSA 145
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
116-146 |
3.44e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.42 E-value: 3.44e-04
10 20 30
....*....|....*....|....*....|..
gi 1937369764 116 EGQTALHIAVI-NQNVNLVRALLARGASVSAR 146
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
47-152 |
4.41e-04 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 43.70 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 47 SPLLLAAKENNVQALIKLLKfEGCEVHQKGAMGETAL----------------HIAALYDNLEAAMVLMEAAPELVFEPM 110
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALwnaisakhhkifrilyHFASISDPHAAGDLLCTAAKRNDLTAM 638
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1937369764 111 T----------SELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVF 152
Cdd:PLN03192 639 KellkqglnvdSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
116-145 |
4.65e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.95 E-value: 4.65e-04
10 20 30
....*....|....*....|....*....|
gi 1937369764 116 EGQTALHIAVINQNVNLVRALLARGASVSA 145
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
46-105 |
4.96e-04 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 39.71 E-value: 4.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 46 ESPLLLAAKENNVQALIKLLKFEGCEVhqkGAMGETALHIAALYDNLEAAMVLMEAAPEL 105
Cdd:pfam12796 31 RTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADI 87
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
162-202 |
5.15e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 5.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1937369764 162 YGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHI 202
Cdd:pfam13857 15 EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
47-221 |
6.08e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.95 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 47 SPLLLAAkENNVQALIKLLKFEGCEVHQKGAMGETALHIAALYDNLEAAMVLMEAAPELvfEPMTSElyeGQTALHIAVI 126
Cdd:PHA02878 170 TALHYAT-ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST--DARDKC---GNTPLHISVG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 127 N-QNVNLVRALLARGASVSARATgsvfhyrphnliYYGEHPLSFAacVGSEEIVRLLIEHGADIRAQDSLGNTVLHILIl 205
Cdd:PHA02878 244 YcKDYDILKLLLEHGVDVNAKSY------------ILGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPLSSAV- 308
|
170
....*....|....*..
gi 1937369764 206 qpnKTFAC-QMYNLLLS 221
Cdd:PHA02878 309 ---KQYLCiNIGRILIS 322
|
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
177-270 |
1.05e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 40.41 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 177 EIVRLLIEHGADIRAQDSL-GNTVLHILILQPNKTFA---CQMYNLllsydggdhlkSLELVpNNQGLTPFKLAGVEGNI 252
Cdd:PHA02741 78 EIIDHLIELGADINAQEMLeGDTALHLAAHRRDHDLAewlCCQPGI-----------DLHFC-NADNKSPFELAIDNEDV 145
|
90
....*....|....*...
gi 1937369764 253 VMFQHLmqkRKHIQWTYG 270
Cdd:PHA02741 146 AMMQIL---REIVATSRG 160
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
162-189 |
1.10e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.10e-03
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
81-137 |
1.55e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 1.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369764 81 TALHIAALYDNLEAAMVLMEAAPELvfePMTSElyEGQTALHIAVINQNVNLVRALL 137
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADI---NAVDG--NGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
162-191 |
1.61e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|
gi 1937369764 162 YGEHPLSFAACVGSEEIVRLLIEHGADIRA 191
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
115-185 |
3.48e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.65 E-value: 3.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369764 115 YEGQTALHIAVINQNVNLVRALLARGASVSAratgsvfhyrphnLIYYGEHPLSFAACVGSEEIVRLLIEH 185
Cdd:PTZ00322 113 YDGRTPLHIACANGHVQVVRVLLEFGADPTL-------------LDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
46-188 |
3.61e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 40.36 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 46 ESPLLLAAKENNVQALIKLL---KFEGCEVHQKGamgETALHIAALYDNLEAAMVLME--AAPELvfePMTSELyegqTA 120
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLdlgKFADDVFYKDG---MTPLHLATILKKLDIMKLLIArgADPDI---PNTDKF----SP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 121 LHIAVINQNVNLVRALLARGASVS------------ARATGSVFHYR-----PHNLIYYGEHPLSFAACVGSE----EIV 179
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDiedccgctpliiAMAKGDIAICKmlldsGANIDYFGKNGCVAALCYAIEnnkiDIV 218
|
....*....
gi 1937369764 180 RLLIEHGAD 188
Cdd:PHA02875 219 RLFIKRGAD 227
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
43-191 |
4.88e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 40.43 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369764 43 RIWESPLLLAAK-ENNVQALIKLLKFeGCEVHQKGAMGETALHIAALYDNLEAAMVLMEAAPELvfEPMTSELyegQTAL 121
Cdd:PHA02876 339 RLYITPLHQASTlDRNKDIVITLLEL-GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI--EALSQKI---GTAL 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369764 122 HIAVINQNVNL-VRALLARGASVSARATgsvfhyrphnliyYGEHPLSFAACVGSE-EIVRLLIEHGADIRA 191
Cdd:PHA02876 413 HFALCGTNPYMsVKTLIDRGANVNSKNK-------------DLSTPLHYACKKNCKlDVIEMLLDNGADVNA 471
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
180-212 |
8.34e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 37.55 E-value: 8.34e-03
10 20 30
....*....|....*....|....*....|....
gi 1937369764 180 RLLIEHGADIRAQDSL-GNTVLHILILQPNKTFA 212
Cdd:PHA02736 75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELA 108
|
|
| |
