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Conserved domains on  [gi|4581491|emb|CAB40138|]
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epithelial calcium channel [Oryctolagus cuniculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 29-637 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: 1157.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   29 WEQYRDRVNMLQQERIRDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPELAKE 108
Cdd:cd22192   1 WAQMLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  109 PALCEPFVGQTALHIAVMNQNLNLVRALLARGASV-SARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGA 187
Cdd:cd22192  81 PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvSPRATGTFFRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  188 DIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDEHsDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHVQ 267
Cdd:cd22192 161 DIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDKE-DDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQ 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  268 WTCGPLTSTLYDLTEIDSWGEELSFLELVVSSKKREARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCC 347
Cdd:cd22192 240 WTYGPLTSTLYDLTEIDSWGDEQSVLELIVSSKKREARKILDVTPVKELVSLKWKRYGRPYFRILALLYLLYIIIFTLCC 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  348 IYRPLKLRDDNRTDPRDITILQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTILGGPFHV 427
Cdd:cd22192 320 VYRPLKPRPENNTDPRDITLYVQKTLQESYVTPKDYLRLVGELISVLGAIVILLLEIPDILRVGVKRYFGQTVLGGPFHV 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  428 IIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASA 507
Cdd:cd22192 400 IIITYACLVLLTLVLRLTSLSGEVVPMSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIFGDLMKFCWLMFVVILGFSSA 479

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  508 FHITFQTEDPNNLGEFSDYPTALFSTFELFLTIIDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQ 587
Cdd:cd22192 480 FYMIFQTEDPDSLGHFYDFPMTLFSTFELFLGLIDGPANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAH 559

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|
gi 4581491  588 ERDELWRAQVVATTVMLERKMPRFLWPRSGICGYEYGLGDRWFLRVENHH 637
Cdd:cd22192 560 ERDELWRAQVVATTLMLERRLPRCLWPRSGICGKEYGLGDRWYLRVEDRN 609
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 649-726 5.10e-26

C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V member 5 (TRPV5) and similar proteins; TRPV5, also called calcium transport protein 2 (CaT2), epithelial calcium channel 1 (ECaC1), or Osm-9-like TRP channel 3 (OTRPC3), is a constitutively active calcium selective cation channel that might be involved in Ca(2+) reabsorption in kidney and intestine. The channel is activated by low internal calcium levels, and the current exhibits an inward rectification. The model corresponds to the C-terminal calmodulin (CaM) binding domain of TRPV5, which contains several CaM binding sites in the N- and C-terminal tails. The binding of CaM to the C-terminal binding site is essential for the fast Ca2+-dependent inactivation of the channel.


:

Pssm-ID: 412091  Cd Length: 73  Bit Score: 101.68  E-value: 5.10e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4581491  649 EAFKCSDKEDGQEQLSEkrpSTVESGMLSRAS-VAFQTPSLSRTTSQSSnSHRGWEILRRNTLGHLNlgLDLGEGDGEE 726
Cdd:cd22296   1 EARKDFDKELKQKYSSE---SKAEIGELARSTqLPFPTPSLSRSTSRSS-SHRGWEILRRNTLGQLN--GDLNYGLEEE 73
 
Name Accession Description Interval E-value
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 29-637 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: 1157.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   29 WEQYRDRVNMLQQERIRDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPELAKE 108
Cdd:cd22192   1 WAQMLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  109 PALCEPFVGQTALHIAVMNQNLNLVRALLARGASV-SARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGA 187
Cdd:cd22192  81 PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvSPRATGTFFRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  188 DIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDEHsDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHVQ 267
Cdd:cd22192 161 DIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDKE-DDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQ 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  268 WTCGPLTSTLYDLTEIDSWGEELSFLELVVSSKKREARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCC 347
Cdd:cd22192 240 WTYGPLTSTLYDLTEIDSWGDEQSVLELIVSSKKREARKILDVTPVKELVSLKWKRYGRPYFRILALLYLLYIIIFTLCC 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  348 IYRPLKLRDDNRTDPRDITILQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTILGGPFHV 427
Cdd:cd22192 320 VYRPLKPRPENNTDPRDITLYVQKTLQESYVTPKDYLRLVGELISVLGAIVILLLEIPDILRVGVKRYFGQTVLGGPFHV 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  428 IIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASA 507
Cdd:cd22192 400 IIITYACLVLLTLVLRLTSLSGEVVPMSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIFGDLMKFCWLMFVVILGFSSA 479

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  508 FHITFQTEDPNNLGEFSDYPTALFSTFELFLTIIDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQ 587
Cdd:cd22192 480 FYMIFQTEDPDSLGHFYDFPMTLFSTFELFLGLIDGPANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAH 559

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|
gi 4581491  588 ERDELWRAQVVATTVMLERKMPRFLWPRSGICGYEYGLGDRWFLRVENHH 637
Cdd:cd22192 560 ERDELWRAQVVATTLMLERRLPRCLWPRSGICGKEYGLGDRWYLRVEDRN 609
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-708 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: 812.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491     11 PWAQLQKLLISWPVGEQDWEQYRDRVN--MLQQE---RIRDSPLLQAAKENDLRLLKILLLNQSCdfqqRGAVGETALHV 85
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEpkKLNINcpdRLGRSALFVAAIENENLELTELLLNLSC----RGAVGDTLLHA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491     86 AAL--YDNLEAATLLMEAA------PELAKEPALCEPFVGQTALHIAVMNQNLNLVRALLARGASVSARATGAAFRRSPH 157
Cdd:TIGR00870  89 ISLeyVDAVEAILLHLLAAfrksgpLELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    158 -NLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQP-----NKTFACQMYNLLLSYDEHSDHLQS 231
Cdd:TIGR00870 169 vDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENefkaeYEELSCQMYNFALSLLDKLRDSKE 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    232 LELVPNHQGLTPFKLAGVEGNTVMFQHLMQ----KRKHVQWTCGPLTSTLYDLTEIDSWGEELSFLELVVSS----KKRE 303
Cdd:TIGR00870 249 LEVILNHQGLTPLKLAAKEGRIVLFRLKLAikykQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVFviglKFPE 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    304 ARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCCIYRPLklrddnRTDPRdITILQQKLLQEAYVTHQDN 383
Cdd:TIGR00870 329 LSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPT------RTDLR-VTGLQQTPLEMLIVTWVDG 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    384 IRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTILGGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWC 463
Cdd:TIGR00870 402 LRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWL 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    464 SVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFHITFQTEDPNNLGEFS------------DYPTALF 531
Cdd:TIGR00870 482 NLLYIFRGNQHLGPLQIMIGRMILGDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSnpharscekqgnAYSTLFE 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    532 STFELFLTIIDG---PANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKM 608
Cdd:TIGR00870 562 TSQELFWAIIGLgdlLANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREG 641

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    609 PRFLWPRSGICGYEYGLGdrWFLRVENHHDQNPLRVLRYVEAFKCSDKEDGQEQLSEK-RPSTVESGMLSRASVAFQTPS 687
Cdd:TIGR00870 642 GTCPPPFNIIPGPKSFVG--LFKRIEKHDGKKRQRWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLIKRYVLAEQRP 719

                         730       740
                  ....*....|....*....|....
gi 4581491    688 LS-RTTSQSSN--SHRGWEILRRN 708
Cdd:TIGR00870 720 RDdEGTTEEETkeLKQDISSLRFE 743
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 649-726 5.10e-26

C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V member 5 (TRPV5) and similar proteins; TRPV5, also called calcium transport protein 2 (CaT2), epithelial calcium channel 1 (ECaC1), or Osm-9-like TRP channel 3 (OTRPC3), is a constitutively active calcium selective cation channel that might be involved in Ca(2+) reabsorption in kidney and intestine. The channel is activated by low internal calcium levels, and the current exhibits an inward rectification. The model corresponds to the C-terminal calmodulin (CaM) binding domain of TRPV5, which contains several CaM binding sites in the N- and C-terminal tails. The binding of CaM to the C-terminal binding site is essential for the fast Ca2+-dependent inactivation of the channel.


Pssm-ID: 412091  Cd Length: 73  Bit Score: 101.68  E-value: 5.10e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4581491  649 EAFKCSDKEDGQEQLSEkrpSTVESGMLSRAS-VAFQTPSLSRTTSQSSnSHRGWEILRRNTLGHLNlgLDLGEGDGEE 726
Cdd:cd22296   1 EARKDFDKELKQKYSSE---SKAEIGELARSTqLPFPTPSLSRSTSRSS-SHRGWEILRRNTLGQLN--GDLNYGLEEE 73
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-282 4.21e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 4.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   37 NMLQQERIRDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPEL-AKEPAlcepf 115
Cdd:COG0666  45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVnARDKD----- 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  116 vGQTALHIAVMNQNLNLVRALLARGASVSARATgaafrrsphnliyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSL 195
Cdd:COG0666 120 -GETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-------------DGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  196 GNTVLHILILQPNKtfacQMYNLLLSYDEHSDHlqslelvPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHVQWTCGPLTS 275
Cdd:COG0666 186 GETPLHLAAENGHL----EIVKLLLEAGADVNA-------KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254


                ....*..
gi 4581491  276 TLYDLTE 282
Cdd:COG0666 255 ALLLAAA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-193 1.22e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491     83 LHVAALYDNLEAATLLMEAAPElakePALCEPFvGQTALHIAVMNQNLNLVRALLARGASvsaratgaafrrsphNLIYY 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD----ANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADV---------------NLKDN 60

                          90       100       110
                  ....*....|....*....|....*....|.
gi 4581491    163 GEHPLSFAACVGSEEIVRLLIEHGADIRAQD 193
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 79-261 3.06e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    79 GETALHVAALYDN-LEAATLLMEAAPELAKEPalcepFVGQTALHI--AVMNQNLNLVRALLARGASVSARATgaafrrs 155
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNAKD-----KVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDL------- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   156 phnliyYGEHPL-----SFAACVgseEIVRLLIEHGADIRAQDSLGNTVLHIlILQPNKTFACQMYNL------------ 218
Cdd:PHA03095 151 ------YGMTPLavllkSRNANV---ELLRLLIDAGADVYAVDDRFRSLLHH-HLQSFKPRARIVRELiragcdpaatdm 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4581491   219 -----LLSYDEHSDHLQSLEL----------VPNHQGLTPFKLAGVEGNTVMFQHLMQ 261
Cdd:PHA03095 221 lgntpLHSMATGSSCKRSLVLplliagisinARNRYGQTPLHYAAVFNNPRACRRLIA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-145 1.60e-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: 39.11  E-value: 1.60e-04
                           10        20
                   ....*....|....*....|....*....
gi 4581491     117 GQTALHIAVMNQNLNLVRALLARGASVSA 145
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 29-637 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: 1157.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   29 WEQYRDRVNMLQQERIRDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPELAKE 108
Cdd:cd22192   1 WAQMLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  109 PALCEPFVGQTALHIAVMNQNLNLVRALLARGASV-SARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGA 187
Cdd:cd22192  81 PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvSPRATGTFFRPGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  188 DIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDEHsDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHVQ 267
Cdd:cd22192 161 DIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDKE-DDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQ 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  268 WTCGPLTSTLYDLTEIDSWGEELSFLELVVSSKKREARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCC 347
Cdd:cd22192 240 WTYGPLTSTLYDLTEIDSWGDEQSVLELIVSSKKREARKILDVTPVKELVSLKWKRYGRPYFRILALLYLLYIIIFTLCC 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  348 IYRPLKLRDDNRTDPRDITILQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTILGGPFHV 427
Cdd:cd22192 320 VYRPLKPRPENNTDPRDITLYVQKTLQESYVTPKDYLRLVGELISVLGAIVILLLEIPDILRVGVKRYFGQTVLGGPFHV 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  428 IIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASA 507
Cdd:cd22192 400 IIITYACLVLLTLVLRLTSLSGEVVPMSLALVLGWCNVMYFARGFQMLGPFTIMIQKIIFGDLMKFCWLMFVVILGFSSA 479

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  508 FHITFQTEDPNNLGEFSDYPTALFSTFELFLTIIDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQ 587
Cdd:cd22192 480 FYMIFQTEDPDSLGHFYDFPMTLFSTFELFLGLIDGPANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAH 559

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|
gi 4581491  588 ERDELWRAQVVATTVMLERKMPRFLWPRSGICGYEYGLGDRWFLRVENHH 637
Cdd:cd22192 560 ERDELWRAQVVATTLMLERRLPRCLWPRSGICGKEYGLGDRWYLRVEDRN 609
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 71-636 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: 921.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   71 DFQQRGAVGETALHVAALYDN---LEAATLLMEAAP------ELAKEPALCEPFVGQTALHIAVMNQNLNLVRALLARGA 141
Cdd:cd21882  18 SAYQRGATGKTCLHKAALNLNdgvNEAIMLLLEAAPdsgnpkELVNAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  142 SVSARATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIR---AQDSLGNTVLHILILQPNKT-----FAC 213
Cdd:cd21882  98 DVSARATGRFFRKSPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAaleAQDSLGNTVLHALVLQADNTpensaFVC 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  214 QMYNLLLSYDEHSDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQK----------RKHVQWTCGPLTSTLYDLTEI 283
Cdd:cd21882 178 QMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQRefsgpyqplsRKFTEWTYGPVTSSLYDLSEI 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  284 DSWGEElSFLELVVSSKKREAR-QILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCCIYRPLKLRDDNrtdp 362
Cdd:cd21882 258 DSWEKN-SVLELIAFSKKREARhQMLVQEPLNELLQEKWDRYGRPYFCFNFACYLLYMIIFTVCAYYRPLKDRPAN---- 332

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  363 rditilqqkllQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGqtILGGPFHVIIITYASLVLLTMVM 442
Cdd:cd21882 333 -----------QEAKATFGDSIRLVGEILTVLGGVYILLGEIPYFFRRRLSRWFG--FLDSYFEILFITQALLVLLSMVL 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  443 RLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFHITFQTEDPNNLGE 522
Cdd:cd21882 400 RFMETEGYVVPLVFSLVLGWCNVLYYTRGFQMLGIYTVMIQKMILRDLMRFCWVYLVFLFGFASAFVILFQTEDPNKLGE 479

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  523 FSDYPTALFSTFELFLTIIDGPANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTV 602
Cdd:cd21882 480 FRDYPDALLELFKFTIGMGDLPFNENVDFPFVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQKAITTL 559

                       570       580       590       600
                ....*....|....*....|....*....|....*....|.
gi 4581491  603 MLERKMPRFLWPRSG-------ICGYEYGLGDRWFLRVENH 636
Cdd:cd21882 560 MLERKYPRCLRKRSRegrllkvGCGGDGGLDDRWCFRVEEV 600
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-708 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: 812.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491     11 PWAQLQKLLISWPVGEQDWEQYRDRVN--MLQQE---RIRDSPLLQAAKENDLRLLKILLLNQSCdfqqRGAVGETALHV 85
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEpkKLNINcpdRLGRSALFVAAIENENLELTELLLNLSC----RGAVGDTLLHA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491     86 AAL--YDNLEAATLLMEAA------PELAKEPALCEPFVGQTALHIAVMNQNLNLVRALLARGASVSARATGAAFRRSPH 157
Cdd:TIGR00870  89 ISLeyVDAVEAILLHLLAAfrksgpLELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFFVKSQG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    158 -NLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQP-----NKTFACQMYNLLLSYDEHSDHLQS 231
Cdd:TIGR00870 169 vDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENefkaeYEELSCQMYNFALSLLDKLRDSKE 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    232 LELVPNHQGLTPFKLAGVEGNTVMFQHLMQ----KRKHVQWTCGPLTSTLYDLTEIDSWGEELSFLELVVSS----KKRE 303
Cdd:TIGR00870 249 LEVILNHQGLTPLKLAAKEGRIVLFRLKLAikykQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVFviglKFPE 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    304 ARQILEQTPVKELVSFKWKKYGRPYFCVLASLYILYMICFTTCCIYRPLklrddnRTDPRdITILQQKLLQEAYVTHQDN 383
Cdd:TIGR00870 329 LSDMYLIAPLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVAYYRPT------RTDLR-VTGLQQTPLEMLIVTWVDG 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    384 IRLVGELVTVTGAVIILLLEIPDIFRVGASRYFGQTILGGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWC 463
Cdd:TIGR00870 402 LRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTQAFLVLREHWLRFDPTLIEEALFAFALVLSWL 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    464 SVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFHITFQTEDPNNLGEFS------------DYPTALF 531
Cdd:TIGR00870 482 NLLYIFRGNQHLGPLQIMIGRMILGDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSnpharscekqgnAYSTLFE 561

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    532 STFELFLTIIDG---PANYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKM 608
Cdd:TIGR00870 562 TSQELFWAIIGLgdlLANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREG 641

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    609 PRFLWPRSGICGYEYGLGdrWFLRVENHHDQNPLRVLRYVEAFKCSDKEDGQEQLSEK-RPSTVESGMLSRASVAFQTPS 687
Cdd:TIGR00870 642 GTCPPPFNIIPGPKSFVG--LFKRIEKHDGKKRQRWCRRVEEVNWTTWERKAETLIEDgLHYQRVMKRLIKRYVLAEQRP 719

                         730       740
                  ....*....|....*....|....
gi 4581491    688 LS-RTTSQSSN--SHRGWEILRRN 708
Cdd:TIGR00870 720 RDdEGTTEEETkeLKQDISSLRFE 743
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 113-634 6.08e-96

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: 309.80  E-value: 6.08e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  113 EPFVGQTALHIAVMNQNLNLVRALLARGASVSARATGAAFRRSP-HNLIYYGEHPLSFAACVGSEEIVRLLIEHG---AD 188
Cdd:cd22193  72 EYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQPKYqGEGFYFGELPLSLAACTNQPDIVQYLLENEhqpAD 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  189 IRAQDSLGNTVLHILIL-----QPNKTFACQMYNLLLSYDEHSDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQK- 262
Cdd:cd22193 152 IEAQDSRGNTVLHALVTvadntKENTKFVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQRe 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  263 ----------RKHVQWTCGPLTSTLYDLTEIDSWGEElSFLELVVSSKKREAR-QILEQTPVKELVSFKWKKYGRPYFCV 331
Cdd:cd22193 232 ikepelrhlsRKFTDWAYGPVSSSLYDLSNVDTCEKN-SVLEIIVYNSKIDNRhEMLTLEPLNTLLQDKWDKFAKYMFFF 310

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  332 LASLYILYMICFTTCCIYRPlklRDDnrtdprditilqQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRvg 411
Cdd:cd22193 311 SFCFYLFYMIIFTLVAYYRP---RED------------EPPPPLAKTTKMDYMRLLGEILVLLGGVYFFVKEIAYFLL-- 373

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  412 aSRYFGQTIL-GGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDL 490
Cdd:cd22193 374 -RRSDLQSSFsDSYFEILFFVQAVLVILSVVLYLFAYKEYLACLVLALALGWANMLYYTRGFQSMGIYSVMIQKVILRDL 452

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  491 MRFCWLMAVVILGFASAFhITFQTEDPNNLGEFSDYPTALFSTFELF-LTIIDGPANY--SVDLPFMYCITYAAFAIIAT 567
Cdd:cd22193 453 LRFLFVYLLFLFGFAVAL-VSLIEKCSSDKKDCSSYGSFSDAVLELFkLTIGMGDLEFqeNSTYPAVFLILLLTYVILTF 531

                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4581491  568 LLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKMPRFLWP--RSG--ICGYEYGLGD---RWFLRVE 634
Cdd:cd22193 532 VLLLNMLIALMGETVNNVSKESKRIWKLQRAITILEFEKSFPECMRKafRSGrlLKVGLCKDGTpdfRWCFRVD 605
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 113-633 4.44e-89

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: 293.59  E-value: 4.44e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  113 EPFVGQTALHIAVMNQNLNLVRALLARGASVSARATGAAFR-RSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGAD-IR 190
Cdd:cd22194 137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFNpKYKHEGFYFGETPLALAACTNQPEIVQLLMEKESTdIT 216

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  191 AQDSLGNTVLHILI-----LQPNKTFACQMYNLLLSYDEHsdhlQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQK--- 262
Cdd:cd22194 217 SQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMILLKSEN----KNLETIRNNEGLTPLQLAAKMGKAEILKYILSReik 292

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  263 --------RKHVQWTCGPLTSTLYDLTEIDSwGEELSFLELVVSSKKREARQ-ILEQTPVKELVSFKWKKYGRPYFCVLA 333
Cdd:cd22194 293 ekpnrslsRKFTDWAYGPVSSSLYDLTNVDT-TTDNSVLEIIVYNTNIDNRHeMLTLEPLHTLLHMKWKKFARYMFFISF 371

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  334 SLYILYMICFTTCCIYRPlklRDDnrtdprditilQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRVGAS 413
Cdd:cd22194 372 LFYFFYNITLTLVSYYRP---RED-----------EDPPHPLALSHKMGWLQLLGQMFVLIWATCLSVKEGIAIFLLRPS 437

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  414 RYfgQTILGGP-FHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMR 492
Cdd:cd22194 438 DL--KSILSDAwFHILFFIQAVLVIVSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSLGIYSVMIQKVILNDVLK 515

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  493 FCWLMAVVILGFASAFHITFQT-EDPNNLGEFSDYPTALFSTFELFLTIIDGPANYSVDLPFMYCITYAAFAIIATLLML 571
Cdd:cd22194 516 FLLVYILFLLGFGVALASLIEDcPDDSECSSYGSFSDAVLELFKLTIGLGDLEIQQNSKYPILFLLLLITYVILTFVLLL 595

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4581491  572 NLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKMPRFL--WPRSGICGYEYGLGDRWFLRV 633
Cdd:cd22194 596 NMLIALMGETVENVSKESERIWRLQRARTILEFEKSLPEWLrkRFRLGELCKVADEDFRLCLRI 659
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 117-634 1.84e-88

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: 290.94  E-value: 1.84e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  117 GQTALHIAVMNQNLNLVRALLARGASVSARATGAAFRRSP-HNLIYYGEHPLSFAACVGSEEIVRLLIEH---GADIRAQ 192
Cdd:cd22196  94 GQTALHIAIERRNMHLVELLVQNGADVHARASGEFFKKKKgGPGFYFGELPLSLAACTNQLDIVKFLLENphsPADISAR 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  193 DSLGNTVLHILI-----LQPNKTFACQMYNLLLSYDEHSDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQK----- 262
Cdd:cd22196 174 DSMGNTVLHALVevadnTPENTKFVTKMYNEILILGAKIRPLLKLEEITNKKGLTPLKLAAKTGKIGIFAYILGReikep 253

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  263 ------RKHVQWTCGPLTSTLYDLTEIDSWgEELSFLELVVSSKKREAR-QILEQTPVKELVSFKWKKYGRPYFCVLASL 335
Cdd:cd22196 254 ecrhlsRKFTEWAYGPVHSSLYDLSSIDTY-EKNSVLEIIAYSSETPNRhEMLLVEPLNKLLQDKWDKFVKRIFYFNFFV 332

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  336 YILYMICFTTCCIYRPlklrdDNRTDPRDITilqqkllqeayVTHQDNIRLVGELVTVTGAVIILLLEIPD-IFRvgasR 414
Cdd:cd22196 333 YFIYMIIFTLAAYYRP-----VNKTPPFPIE-----------NTTGEYLRLTGEIISVSGGVYFFFRGIQYfLQR----R 392

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  415 YFGQTILGGPFHVIIITYASLVLLT-MVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRF 493
Cdd:cd22196 393 PSLKKLIVDSYCEILFFVQSLFLLAsTVLYFCGRNEYVAFMVISLALGWANVLYYTRGFQQMGIYSVMIQKMILRDICRF 472

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  494 CWLMAVVILGFASAFhITFQTEDPN----NLGEF--------SDYPTALFSTFELF-LTIIDGPANYSVDLPF--MYCIT 558
Cdd:cd22196 473 LFVYLVFLFGFSAAL-VTLIEDGPPkgdvNTSQKecvcksgyNSYNSLYSTCLELFkFTIGMGDLEFTENYKFkeVFIFL 551

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  559 YAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKMPRFLWP--RSG---ICGYEYGLGD--RWFL 631
Cdd:cd22196 552 LISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQRAITILDLEKSLLRCLRDrfRSGksvLVGITPDGKEdyRWCF 631


                ...
gi 4581491  632 RVE 634
Cdd:cd22196 632 RVD 634
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 117-640 7.89e-86

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: 286.36  E-value: 7.89e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  117 GQTALHIAVMNQNLNLVRALLARGASVSARATGAAFR-RSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHG---ADIRAQ 192
Cdd:cd22195 137 GQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQpKDEGGYFYFGELPLSLAACTNQPDIVHYLTENAhkkADLRRQ 216

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  193 DSLGNTVLHILI-----LQPNKTFACQMYNLLLSYDEHSDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQK----- 262
Cdd:cd22195 217 DSRGNTVLHALVaiadnTRENTKFVTKMYDLLLIKCAKLYPDCNLEAILNNDGMSPLMMAAKLGKIGIFQHIIRReikde 296

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  263 ------RKHVQWTCGPLTSTLYDLTEIDSWGEELSFLELVVSSKKREAR-QILEQTPVKELVSFKWKKYGRPYFCVLASL 335
Cdd:cd22195 297 earhlsRKFKDWAYGPVYSSLYDLSSLDTCGEEVSVLEILVYNSKIENRhEMLAVEPINELLRDKWRKFGAVSFYISVVS 376

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  336 YILYMICFTTCCIYRPLKlrddnRTDPRditilqqkllqeAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRV---GA 412
Cdd:cd22195 377 YLVAMIIFTLIAYYRPME-----GTPPY------------PYRTTVDYLRLAGEIITLLTGIFFFFTNIKDLFMKkcpGV 439

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  413 SRYFgqtiLGGPFHVIIITYASLVLLTMVMRLTNMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMR 492
Cdd:cd22195 440 NSLF----IDGSFQLLYFIYSVLVIVTAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFR 515

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  493 FCWLMAVVILGFASAF--------HITFQTEDPNNLgEFSDYP----TALFSTF--ELF-LTIIDGPANY--SVDLPFMY 555
Cdd:cd22195 516 FLLVYLLFMIGYASALvsllnpcpTKETCKEDSTNC-TVPTYPscrdSNTFSKFllDLFkLTIGMGDLEMlnSAKYPAVF 594

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  556 CITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKMPRFLWP--RSG----ICGYEYGLGD-R 628
Cdd:cd22195 595 IILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQWATTILDIERSFPVFLRKafRSGemvtVGKNLDGTPDrR 674

                       570
                ....*....|....*.
gi 4581491  629 WFLRVE----NHHDQN 640
Cdd:cd22195 675 WCFRVDevnwSHWNQN 690
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 76-634 1.80e-79

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: 266.72  E-value: 1.80e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   76 GAVGETALHVAA--LYDNLEAAT--LLMEAAPELAKEP---ALC--EPFVGQTALHIAVMNQNLNLVRALLARGASVSAR 146
Cdd:cd22197  44 GSTGKTCLMKAVlnLQDGVNACImpLLEIDKDSGNPKPlvnAQCtdEYYRGHSALHIAIEKRSLQCVKLLVENGADVHAR 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  147 ATGAAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGAD---IRAQDSLGNTVLHILIL-----QPNKTFACQMYNL 218
Cdd:cd22197 124 ACGRFFQKKQGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMiadnsPENSALVIKMYDG 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  219 LLSYDEHSDHLQSLELVPNHQGLTPFKLAGVEGNTVMFQHLMQK----------RKHVQWTCGPLTSTLYDLTEIDSWgE 288
Cdd:cd22197 204 LLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEIFRHILQRefsgpyqhlsRKFTEWCYGPVRVSLYDLSSVDSW-E 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  289 ELSFLELVVSSKKREARQ---ILEqtPVKELVSFKWKKYGrPYFCVLASLYILYMICFTTCCIYRPLklrddnrtdprdi 365
Cdd:cd22197 283 KNSVLEIIAFHSKSPNRHrmvVLE--PLNKLLQEKWDRLV-SRFYFNFLCYLVYMFIFTVVAYHQPL------------- 346

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  366 tiLQQKLLQEAYVTHQDNIRLVGELVTVTGAVIILLLEIPDIFRvgASRYFGQTILGGPFHVIIITYASLVLLTMVMRLT 445
Cdd:cd22197 347 --LDQPPIPPLKATAGGSMLLLGHILILLGGIYLLLGQLWYFWR--RRLFIWISFMDSYFEILFLLQALLTVLSQVLYFM 422

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  446 NMNGEVVPLSFALVLGWCSVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFhITFQTEDPNNLG---- 521
Cdd:cd22197 423 GSEWYLPLLVFSLVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLLVYLVFLFGFAVAL-VSLSREAPSPKApedn 501

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  522 --------------EFSDYPTALFSTFELF-LTIIDGPANYSVDLPFMYCITY--AAFAIIATLLMLNLFIAMMGDTHWR 584
Cdd:cd22197 502 nstvteqptvgqeeEPAPYRSILDASLELFkFTIGMGELAFQEQLRFRGVVLLllLAYVLLTYVLLLNMLIALMSETVNH 581

                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4581491  585 VAQERDELWRAQVVATTVMLERKMPRFLWPRSGIcGYEYGLG--------DRWFLRVE 634
Cdd:cd22197 582 VADNSWSIWKLQKAISVLEMENGYWWCRRKKQRE-GRLLTVGtrpdgtpdERWCFRVE 638
CBD_TRPV5_C cd22296
C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V ...
 649-726 5.10e-26

C-terminal CaM binding domain found in transient receptor potential cation channel subfamily V member 5 (TRPV5) and similar proteins; TRPV5, also called calcium transport protein 2 (CaT2), epithelial calcium channel 1 (ECaC1), or Osm-9-like TRP channel 3 (OTRPC3), is a constitutively active calcium selective cation channel that might be involved in Ca(2+) reabsorption in kidney and intestine. The channel is activated by low internal calcium levels, and the current exhibits an inward rectification. The model corresponds to the C-terminal calmodulin (CaM) binding domain of TRPV5, which contains several CaM binding sites in the N- and C-terminal tails. The binding of CaM to the C-terminal binding site is essential for the fast Ca2+-dependent inactivation of the channel.


Pssm-ID: 412091  Cd Length: 73  Bit Score: 101.68  E-value: 5.10e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4581491  649 EAFKCSDKEDGQEQLSEkrpSTVESGMLSRAS-VAFQTPSLSRTTSQSSnSHRGWEILRRNTLGHLNlgLDLGEGDGEE 726
Cdd:cd22296   1 EARKDFDKELKQKYSSE---SKAEIGELARSTqLPFPTPSLSRSTSRSS-SHRGWEILRRNTLGQLN--GDLNYGLEEE 73
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-282 4.21e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 4.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   37 NMLQQERIRDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEAAPEL-AKEPAlcepf 115
Cdd:COG0666  45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVnARDKD----- 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  116 vGQTALHIAVMNQNLNLVRALLARGASVSARATgaafrrsphnliyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSL 195
Cdd:COG0666 120 -GETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-------------DGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  196 GNTVLHILILQPNKtfacQMYNLLLSYDEHSDHlqslelvPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHVQWTCGPLTS 275
Cdd:COG0666 186 GETPLHLAAENGHL----EIVKLLLEAGADVNA-------KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254


                ....*..
gi 4581491  276 TLYDLTE 282
Cdd:COG0666 255 ALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-209 1.79e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 1.79e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   36 VNMLQQERIRDSPLLQAAKENDlRLLKILLLNQSCDFQQRGAVGETALHVAALYDNLEAATLLMEA-APELAKEPAlcep 114
Cdd:COG0666  78 ADINAKDDGGNTLLHAAARNGD-LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVNAQDND---- 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  115 fvGQTALHIAVMNQNLNLVRALLARGASVSARAtgaafrrsphnliYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDS 194
Cdd:COG0666 153 --GNTPLHLAAANGNLEIVKLLLEAGADVNARD-------------NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                       170
                ....*....|....*
gi 4581491  195 LGNTVLHILILQPNK 209
Cdd:COG0666 218 DGKTALDLAAENGNL 232
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-220 1.91e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   71 DFQQRGAVGETALHVAALYDNLEAATLLMEA-APELAKEPAlcepfvGQTALHIAVMNQNLNLVRALLARGASVSARATg 149
Cdd:COG0666 145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAgADVNARDND------GETPLHLAAENGHLEIVKLLLEAGADVNAKDN- 217

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4581491  150 aafrrsphnliyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLL 220
Cdd:COG0666 218 ------------DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-193 1.22e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491     83 LHVAALYDNLEAATLLMEAAPElakePALCEPFvGQTALHIAVMNQNLNLVRALLARGASvsaratgaafrrsphNLIYY 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD----ANLQDKN-GRTALHLAAKNGHLEIVKLLLEHADV---------------NLKDN 60

                          90       100       110
                  ....*....|....*....|....*....|.
gi 4581491    163 GEHPLSFAACVGSEEIVRLLIEHGADIRAQD 193
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 397-590 3.47e-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: 72.68  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    397 VIILLLEIpdIFRVgASRYFGQTILGGPFHVIIITYASLVLLTMVMrltnmNGEVVPLSFALVLGWcSVMYFARGFQMLG 476
Cdd:pfam00520  43 TGIFTLEM--LLKI-IAAGFKKRYFRSPWNILDFVVVLPSLISLVL-----SSVGSLSGLRVLRLL-RLLRLLRLIRRLE 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    477 PFTIMIQ--KMIFGDLMRFCWLMAVVILGFASAFHITFQT------EDPNNLGEFSDYPTALFSTFELFLTIIDG---PA 545
Cdd:pfam00520 114 GLRTLVNslIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGklktweNPDNGRTNFDNFPNAFLWLFQTMTTEGWGdimYD 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 4581491    546 NYSVDLPFMYCITYAAFAIIATLLMLNLFIAMMGDTHWRVAQERD 590
Cdd:pfam00520 194 TIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-146 7.52e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 7.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491     49 LLQAAKENDLRLLKILLLNqSCDFQQRGAVGETALHVAALYDNLEAATLLMEaapelakEPALCEPFVGQTALHIAVMNQ 128
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKDNGRTALHYAARSG 72

                          90
                  ....*....|....*...
gi 4581491    129 NLNLVRALLARGASVSAR 146
Cdd:pfam12796  73 HLEIVKLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-262 2.49e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 2.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   82 ALHVAALYDNLEAATLLMEAAPELAKEPALCEPFVGQTALHIAVMNQNLNLVRALLARGASVSARAtgaafrrsphnliY 161
Cdd:COG0666  19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD-------------D 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491  162 YGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFAcqmyNLLLSYDEHSDhlqslelVPNHQGL 241
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV----KLLLEAGADVN-------AQDNDGN 154

                       170       180
                ....*....|....*....|.
gi 4581491  242 TPFKLAGVEGNTVMFQHLMQK 262
Cdd:COG0666 155 TPLHLAAANGNLEIVKLLLEA 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 79-261 3.06e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    79 GETALHVAALYDN-LEAATLLMEAAPELAKEPalcepFVGQTALHI--AVMNQNLNLVRALLARGASVSARATgaafrrs 155
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNAKD-----KVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDL------- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   156 phnliyYGEHPL-----SFAACVgseEIVRLLIEHGADIRAQDSLGNTVLHIlILQPNKTFACQMYNL------------ 218
Cdd:PHA03095 151 ------YGMTPLavllkSRNANV---ELLRLLIDAGADVYAVDDRFRSLLHH-HLQSFKPRARIVRELiragcdpaatdm 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4581491   219 -----LLSYDEHSDHLQSLEL----------VPNHQGLTPFKLAGVEGNTVMFQHLMQ 261
Cdd:PHA03095 221 lgntpLHSMATGSSCKRSLVLplliagisinARNRYGQTPLHYAAVFNNPRACRRLIA 278
PHA03095 PHA03095
ankyrin-like protein; Provisional
 117-202 1.73e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   117 GQTALHIAVMNQN---LNLVRALLARGASVSARATgaafrrsphnliyYGEHPLSFAACVGSEE-IVRLLIEHGADIRAQ 192
Cdd:PHA03095  47 GKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPER-------------CGFTPLHLYLYNATTLdVIKLLIKAGADVNAK 113

                         90
                 ....*....|
gi 4581491   193 DSLGNTVLHI 202
Cdd:PHA03095 114 DKVGRTPLHV 123
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 45-208 1.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    45 RDSPLLQAAKENDLRLLKILLLNQSCDFQQRGAVGETALHVAAL--YDNLEAATLLMEAAPELAKEPALCEPfvgqtaLH 122
Cdd:PHA02876 273 KNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKngYDTENIRTLIMLGADVNAADRLYITP------LH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   123 IA-VMNQNLNLVRALLARGASVSARAtgaafrrsphnliYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLH 201
Cdd:PHA02876 347 QAsTLDRNKDIVITLLELGANVNARD-------------YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALH 413


                 ....*..
gi 4581491   202 ILILQPN 208
Cdd:PHA02876 414 FALCGTN 420
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-202 1.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   117 GQTALHIAVMNQNLNLVRALLARGASVSARATGaafrrsphnliyyGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLG 196
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKT-------------NNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234


                 ....*.
gi 4581491   197 NTVLHI 202
Cdd:PHA02878 235 NTPLHI 240
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 123-263 1.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   123 IAVMNQNLNLVRALLARGASVSAratgaafrrsphnLIYYGEHPLSFAA--CVGSEEIVRLLIEHGADIRAQDSLGNTVL 200
Cdd:PHA03100  79 KYNLTDVKEIVKLLLEYGANVNA-------------PDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLL 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4581491   201 H--------------ILILQPNKTFACQMYNLLLSYDEHSDhlqslelVPNHQGLTPFKLAGVEGNTVMFQHLMQKR 263
Cdd:PHA03100 146 HlylesnkidlkilkLLIDKGVDINAKNRVNYLLSYGVPIN-------IKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215
Ank_2 pfam12796
Ankyrin repeats (3 copies);
167-266 2.56e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    167 LSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHIlilqpnktfACQMYN-----LLLSYdehsdhlqsLELVPNHQGL 241
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL---------AAKNGHleivkLLLEH---------ADVNLKDNGR 62

                          90       100
                  ....*....|....*....|....*
gi 4581491    242 TPFKLAGVEGNTVMFQHLMQKRKHV 266
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEKGADI 87
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 71-205 4.93e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    71 DFQQRGAVGETALHVAALYDNLEAATLLMEAAPEL-AKEPALCEPfvgqtaLHIAVMNQNLNLVRALLARGASVSARAtg 149
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYP------IHIAIKHNFFDIIKLLLEKGAYANVKD-- 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4581491   150 aafrrsphnliYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILIL 205
Cdd:PHA02874 188 -----------NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 162-222 6.89e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 6.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4581491   162 YGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFacqmYNLLLSY 222
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI----FKLLLNN 247
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 117-222 1.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   117 GQTALHIAVMNQNLNLVRALLARGASVsaratgaafrrsphNLI-YYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSl 195
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANP--------------NLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE- 256

                         90       100
                 ....*....|....*....|....*..
gi 4581491   196 gntvlHILILQPNKTFACQMYNLLLSY 222
Cdd:PHA03100 257 -----TLLYFKDKDLNTITKIKMLKKS 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
165-202 1.57e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 4581491    165 HPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHI 202
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-145 1.60e-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: 39.11  E-value: 1.60e-04
                           10        20
                   ....*....|....*....|....*....
gi 4581491     117 GQTALHIAVMNQNLNLVRALLARGASVSA 145
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 117-145 1.60e-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: 39.16  E-value: 1.60e-04
                          10        20
                  ....*....|....*....|....*....
gi 4581491    117 GQTALHIAVMNQNLNLVRALLARGASVSA 145
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 162-193 1.86e-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: 1.86e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 4581491    162 YGEHPLSFAAC-VGSEEIVRLLIEHGADIRAQD 193
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
150-202 2.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4581491    150 AAFRRSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHI 202
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 117-146 2.29e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 2.29e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 4581491    117 GQTALHIAV-MNQNLNLVRALLARGASVSAR 146
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-137 4.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4581491     81 TALHVAALYDNLEAATLLMEAAPELAKEPALcepfvGQTALHIAVMNQNLNLVRALL 137
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGN-----GETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 127-202 7.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 7.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4581491   127 NQNLNLVRALLARGASVSARatgaafrrSPHNLIYYGEHPLSFAACVgSEEIVRLLIEHGADIRAQDSLGNTVLHI 202
Cdd:PHA02859  63 KVNVEILKFLIENGADVNFK--------TRDNNLSALHHYLSFNKNV-EPEILKILIDSGSSITEEDEDGKNLLHM 129
PHA03095 PHA03095
ankyrin-like protein; Provisional
 130-205 8.45e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 8.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4581491   130 LNLVRALLARGASVSARatgAAFRRSP-HNLIYYGEHPlsfaacvgSEEIVRLLIEHGADIRAQDSLGNTVLHILIL 205
Cdd:PHA03095  27 VEEVRRLLAAGADVNFR---GEYGKTPlHLYLHYSSEK--------VKDIVRLLLEAGADVNAPERCGFTPLHLYLY 92
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 162-189 8.76e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 8.76e-04
                           10        20
                   ....*....|....*....|....*...
gi 4581491     162 YGEHPLSFAACVGSEEIVRLLIEHGADI 189
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 162-191 1.12e-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: 36.85  E-value: 1.12e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 4581491    162 YGEHPLSFAACVGSEEIVRLLIEHGADIRA 191
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 117-215 1.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   117 GQTALHIAVMNQNLNLVRALLARGASVSARATGAAfrrsphnliyygeHPLSFAACVGSEEIVRLLIEHGADIRAQDSLG 196
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-------------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         90
                 ....*....|....*....
gi 4581491   197 NTVLHILILQPNkTFACQM 215
Cdd:PHA02875 169 CTPLIIAMAKGD-IAICKM 186
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-221 1.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   117 GQTALHIAVMN-QNLNLVRALLARGASVSARATgaafrrsphnliYYGEHPLSFAacVGSEEIVRLLIEHGADIRAQDSL 195
Cdd:PHA02878 234 GNTPLHISVGYcKDYDILKLLLEHGVDVNAKSY------------ILGLTALHSS--IKSERKLKLLLEYGADINSLNSY 299

                         90       100
                 ....*....|....*....|....*..
gi 4581491   196 GNTVLHILIlqpnKTFAC-QMYNLLLS 221
Cdd:PHA02878 300 KLTPLSSAV----KQYLCiNIGRILIS 322
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 72-202 1.59e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    72 FQQRGAVGEtalHVAALYDNLEA--ATLLMEAAPELAKEPalcEPFVGQTALHIAVMNqnlnlVRALLARGASVSARA-- 147
Cdd:PTZ00322  34 FERMAAIQE---EIARIDTHLEAleATENKDATPDHNLTT---EEVIDPVVAHMLTVE-----LCQLAASGDAVGARIll 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4581491   148 TGAAfrrSPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHI 202
Cdd:PTZ00322 103 TGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 79-221 1.72e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    79 GETALHVAALYDNLEAATLLME--AAPELAKEPALcepfvgqTALHIAVMNQNLNLVRALLARGASVSARATgaafrrsp 156
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIArgADPDIPNTDKF-------SPLHLAVMMGDIKGIELLIDHKACLDIEDC-------- 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4581491   157 hnliyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTfacQMYNLLLS 221
Cdd:PHA02875 167 -----CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI---DIVRLFIK 223
PHA02741 PHA02741
hypothetical protein; Provisional
 177-271 1.84e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   177 EIVRLLIEHGADIRAQDSL-GNTVLHILILQPNKTFA---CQMYNLllsydehsdhlqSLELVpNHQGLTPFKLAGVEGN 252
Cdd:PHA02741  78 EIIDHLIELGADINAQEMLeGDTALHLAAHRRDHDLAewlCCQPGI------------DLHFC-NADNKSPFELAIDNED 144

                         90
                 ....*....|....*....
gi 4581491   253 TVMFQHLmqkRKHVQWTCG 271
Cdd:PHA02741 145 VAMMQIL---REIVATSRG 160
PHA03095 PHA03095
ankyrin-like protein; Provisional
 81-198 2.48e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491    81 TALHVAAlyDNLEAATLLMEAAPELAKEPALCEPFvGQTALHIAVMNQNLN--LVRALLARGASVSARatgaafrrsphN 158
Cdd:PHA03095 189 SLLHHHL--QSFKPRARIVRELIRAGCDPAATDML-GNTPLHSMATGSSCKrsLVLPLLIAGISINAR-----------N 254

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 4581491   159 LiyYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNT 198
Cdd:PHA03095 255 R--YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 121-222 2.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4581491   121 LHIAVMNQNLNLVRALLARGASVSAratgaafrrspHNLIYYGehPLSFAACVGSE-----EIVRLLIEHGADIRAQDSL 195
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINS-----------STKNNST--PLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNN 105

                         90       100
                 ....*....|....*....|....*..
gi 4581491   196 GNTVLHILILqpNKTFACQMYNLLLSY 222
Cdd:PHA03100 106 GITPLLYAIS--KKSNSYSIVEYLLDN 130
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 112-185 5.90e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 5.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4581491   112 CEPFVGQTALHIAVMNQNLNLVRALLARGASVSAratgaafrrsphnLIYYGEHPLSFAACVGSEEIVRLLIEH 185
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-------------LDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 180-212 7.07e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 7.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 4581491   180 RLLIEHGADIRAQDSL-GNTVLHILILQPNKTFA 212
Cdd:PHA02736  75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELA 108
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 79-145 8.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 8.44e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4581491    79 GETALHVAALYDNLEAATLLMeaapELAKEPALCEPFvGQTALHIAVMNQNLNLVRALLARGASVSA 145
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLL----DLGANPNLVNKY-GDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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