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Conserved domains on  [gi|223530981|gb|EEF32836|]
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Potassium channel AKT2/3, putative [Ricinus communis]

Protein Classification

ion transporter; cyclic nucleotide-gated ion channel family protein( domain architecture ID 11477558)

ion transporter such as a voltage-gated cation channel, which enables the selective translocation of cations such as sodium, calcium, or potassium, across cell membranes; cyclic nucleotide-gated ion channel is a nonselective channel that is opened by the direct binding of cyclic nucleotides, cAMP and cGMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-845 0e+00

Voltage-dependent potassium channel; Provisional


:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1628.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  24 KDYHGETESNTTATHQEEDDDTSLSLSSLSKIILPPLGVSSYNNNPIETRGWIISPMDSRYRWWGSFMVLLVAYSAWVYP 103
Cdd:PLN03192   1 FQSTGSAGGGRGKGTGEEDDSGSLSLRNLSKVILPPLGVPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 104 FEVAFLNSSPNKRLYIADNIVDLFFAIDIVLTFFVAYIDSRTQLMVRDRKKIATRYLSTWFLMDVASTIPFEALAYLFTG 183
Cdd:PLN03192  81 FEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 184 TQKLALSYSLLGILRFWRLRRVKQLFTRLEKDIRFSYFRIRCARLLCVTLFLVHCAGCLYYLLADRYPHQGRTWIGAVIP 263
Cdd:PLN03192 161 TVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 264 NFRETSLWIRYISAMYWSITTMTTVGYGDLHAVNTMEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 343
Cdd:PLN03192 241 NFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 344 SNFVCRNRLPRRLKDQILAYMCLRFKAESLNQNHLIEQLPKSICKSICQHLFLPTVEKVYLFKGVSREILMLLVAEMKAE 423
Cdd:PLN03192 321 SNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 424 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSDLEKERVVGTLQCGDMFGDVGALCCRPQSFTFRTKTLSQLLRLKTSSLI 503
Cdd:PLN03192 401 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLI 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 504 EAMQTRQHDYIAIMKNFLQHHKTLKDLKVGEFPFESGEEDGDPNMASNLLTVASTGNAAFLEELLKAKLDPDIGDSKGRT 583
Cdd:PLN03192 481 EAMQTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 584 PLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIFRILHHFASISDPQTAGDLLCTAAKRNDLTMMKE 663
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKE 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 664 LLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADVTASNTYE-FSSTTLNEMLKKREIGHRITVPDTVTSDEVI 742
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPTELRELLQKRELGHSITIVDSVPADEPD 720

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 743 LKRDEGEQECNSCGKSDELKCIIRVSIYKGHPLVRKQACCKEPGRLIRLPDSLEELKRIAGDKFGFDARNAMVTDVEGSV 822
Cdd:PLN03192 721 LGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAE 800

                        810       820
                 ....*....|....*....|...
gi 223530981 823 IDSIEVIRDNDKLFIAEDPYSSV 845
Cdd:PLN03192 801 IDSIEVIRDNDKLFVVEDEDSRR 823
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-845 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1628.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  24 KDYHGETESNTTATHQEEDDDTSLSLSSLSKIILPPLGVSSYNNNPIETRGWIISPMDSRYRWWGSFMVLLVAYSAWVYP 103
Cdd:PLN03192   1 FQSTGSAGGGRGKGTGEEDDSGSLSLRNLSKVILPPLGVPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 104 FEVAFLNSSPNKRLYIADNIVDLFFAIDIVLTFFVAYIDSRTQLMVRDRKKIATRYLSTWFLMDVASTIPFEALAYLFTG 183
Cdd:PLN03192  81 FEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 184 TQKLALSYSLLGILRFWRLRRVKQLFTRLEKDIRFSYFRIRCARLLCVTLFLVHCAGCLYYLLADRYPHQGRTWIGAVIP 263
Cdd:PLN03192 161 TVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 264 NFRETSLWIRYISAMYWSITTMTTVGYGDLHAVNTMEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 343
Cdd:PLN03192 241 NFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 344 SNFVCRNRLPRRLKDQILAYMCLRFKAESLNQNHLIEQLPKSICKSICQHLFLPTVEKVYLFKGVSREILMLLVAEMKAE 423
Cdd:PLN03192 321 SNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 424 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSDLEKERVVGTLQCGDMFGDVGALCCRPQSFTFRTKTLSQLLRLKTSSLI 503
Cdd:PLN03192 401 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLI 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 504 EAMQTRQHDYIAIMKNFLQHHKTLKDLKVGEFPFESGEEDGDPNMASNLLTVASTGNAAFLEELLKAKLDPDIGDSKGRT 583
Cdd:PLN03192 481 EAMQTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 584 PLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIFRILHHFASISDPQTAGDLLCTAAKRNDLTMMKE 663
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKE 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 664 LLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADVTASNTYE-FSSTTLNEMLKKREIGHRITVPDTVTSDEVI 742
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPTELRELLQKRELGHSITIVDSVPADEPD 720

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 743 LKRDEGEQECNSCGKSDELKCIIRVSIYKGHPLVRKQACCKEPGRLIRLPDSLEELKRIAGDKFGFDARNAMVTDVEGSV 822
Cdd:PLN03192 721 LGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAE 800

                        810       820
                 ....*....|....*....|...
gi 223530981 823 IDSIEVIRDNDKLFIAEDPYSSV 845
Cdd:PLN03192 801 IDSIEVIRDNDKLFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 84-334 1.16e-44

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: 160.90  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981   84 YRWWGSFMVLLVAYSAWVYPFEVAFLNSSP-NKRLYIADNIVDLFFAIDIVLTFFVAYIDsrtqlmvrdrkkiaTRYL-S 161
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  162 TWFLMDVASTIPFEALAYLFTGTqklalSYSLLGILRFWRLRRVKQLFTRLEKDIRFSYFRIRCARLLCVTLFLVHCAGC 241
Cdd:pfam00520  67 PWNILDFVVVLPSLISLVLSSVG-----SLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  242 LYYLLADRYPHQ-GRTWIGAV--IPNFREtslwirYISAMYWSITTMTTVGYGDLHAVNTMEM-------IFIIFYMLFN 311
Cdd:pfam00520 142 IFAIIGYQLFGGkLKTWENPDngRTNFDN------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 223530981  312 LGLTAYLIGNMTNLVVEGTRRTM 334
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
545-708 1.82e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 1.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 545 DPNMASNLLTVASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSS 624
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 625 KHQTIFRIL-HHFASISDPQTAGD-LLCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGA 702
Cdd:COG0666  164 GNLEIVKLLlEAGADVNARDNDGEtPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243


                 ....*.
gi 223530981 703 DVTASN 708
Cdd:COG0666  244 DLNAKD 249
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 404-517 1.32e-24

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 99.32  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 404 LFKGVSREILMLLVAEMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEII-DSDLEKERVVGTLQCGDMFGDVGALCCRPQ 482
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 223530981 483 SFTFRTKTLSQLLRLKTSSLIEAMQTRQHDYIAIM 517
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 404-520 1.03e-20

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 88.23  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981   404 LFKGVSREILMLLVAEMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEII-DSDLEKERVVGTLQCGDMFGDVGAL--CCR 480
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLtnSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 223530981   481 PQSFTFRTKTLSQLLRLKTSSLIEAMQTRQHDYIAIMKNF 520
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
 
Name Accession Description Interval E-value
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-845 0e+00

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 1628.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  24 KDYHGETESNTTATHQEEDDDTSLSLSSLSKIILPPLGVSSYNNNPIETRGWIISPMDSRYRWWGSFMVLLVAYSAWVYP 103
Cdd:PLN03192   1 FQSTGSAGGGRGKGTGEEDDSGSLSLRNLSKVILPPLGVPSYNQNHIGSDGWIISPMDSRYRWWETLMVVLVAYSAWVYP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 104 FEVAFLNSSPNKRLYIADNIVDLFFAIDIVLTFFVAYIDSRTQLMVRDRKKIATRYLSTWFLMDVASTIPFEALAYLFTG 183
Cdd:PLN03192  81 FEVAFLNASPKRGLEIADNVVDLFFAVDIVLTFFVAYIDPRTQLLVRDRKKIAVRYLSTWFLMDVASTIPFQALAYLITG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 184 TQKLALSYSLLGILRFWRLRRVKQLFTRLEKDIRFSYFRIRCARLLCVTLFLVHCAGCLYYLLADRYPHQGRTWIGAVIP 263
Cdd:PLN03192 161 TVKLNLSYSLLGLLRFWRLRRVKQLFTRLEKDIRFSYFWIRCARLLSVTLFLVHCAGCLYYLIADRYPHQGKTWIGAVIP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 264 NFRETSLWIRYISAMYWSITTMTTVGYGDLHAVNTMEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 343
Cdd:PLN03192 241 NFRETSLWIRYISAIYWSITTMTTVGYGDLHAVNTIEMIFIIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 344 SNFVCRNRLPRRLKDQILAYMCLRFKAESLNQNHLIEQLPKSICKSICQHLFLPTVEKVYLFKGVSREILMLLVAEMKAE 423
Cdd:PLN03192 321 SNFVGRNRLPPRLKDQILAYMCLRFKAESLNQQQLIDQLPKSICKSICQHLFLPVVEKVYLFKGVSREILLLLVTKMKAE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 424 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSDLEKERVVGTLQCGDMFGDVGALCCRPQSFTFRTKTLSQLLRLKTSSLI 503
Cdd:PLN03192 401 YIPPREDVIMQNEAPDDVYIVVSGEVEIIDSEGEKERVVGTLGCGDIFGEVGALCCRPQSFTFRTKTLSQLLRLKTSTLI 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 504 EAMQTRQHDYIAIMKNFLQHHKTLKDLKVGEFPFESGEEDGDPNMASNLLTVASTGNAAFLEELLKAKLDPDIGDSKGRT 583
Cdd:PLN03192 481 EAMQTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRT 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 584 PLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIFRILHHFASISDPQTAGDLLCTAAKRNDLTMMKE 663
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKE 640

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 664 LLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADVTASNTYE-FSSTTLNEMLKKREIGHRITVPDTVTSDEVI 742
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPTELRELLQKRELGHSITIVDSVPADEPD 720

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 743 LKRDEGEQECNSCGKSDELKCIIRVSIYKGHPLVRKQACCKEPGRLIRLPDSLEELKRIAGDKFGFDARNAMVTDVEGSV 822
Cdd:PLN03192 721 LGRDGGSRPGRLQGTSSDNQCRPRVSIYKGHPLLRNERCCNEAGKLINLPPSLEELKAIAGEKLGFDARKAMVTNEEGAE 800

                        810       820
                 ....*....|....*....|...
gi 223530981 823 IDSIEVIRDNDKLFIAEDPYSSV 845
Cdd:PLN03192 801 IDSIEVIRDNDKLFVVEDEDSRR 823
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 84-334 1.16e-44

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: 160.90  E-value: 1.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981   84 YRWWGSFMVLLVAYSAWVYPFEVAFLNSSP-NKRLYIADNIVDLFFAIDIVLTFFVAYIDsrtqlmvrdrkkiaTRYL-S 161
Cdd:pfam00520   1 SRYFELFILLLILLNTIFLALETYFQPEEPlTTVLEILDYVFTGIFTLEMLLKIIAAGFK--------------KRYFrS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  162 TWFLMDVASTIPFEALAYLFTGTqklalSYSLLGILRFWRLRRVKQLFTRLEKDIRFSYFRIRCARLLCVTLFLVHCAGC 241
Cdd:pfam00520  67 PWNILDFVVVLPSLISLVLSSVG-----SLSGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  242 LYYLLADRYPHQ-GRTWIGAV--IPNFREtslwirYISAMYWSITTMTTVGYGDLHAVNTMEM-------IFIIFYMLFN 311
Cdd:pfam00520 142 IFAIIGYQLFGGkLKTWENPDngRTNFDN------FPNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGG 215

                         250       260
                  ....*....|....*....|...
gi 223530981  312 LGLTAYLIGNMTNLVVEGTRRTM 334
Cdd:pfam00520 216 FLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
545-708 1.82e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 1.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 545 DPNMASNLLTVASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSS 624
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 625 KHQTIFRIL-HHFASISDPQTAGD-LLCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGA 702
Cdd:COG0666  164 GNLEIVKLLlEAGADVNARDNDGEtPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243


                 ....*.
gi 223530981 703 DVTASN 708
Cdd:COG0666  244 DLNAKD 249
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 404-517 1.32e-24

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 99.32  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 404 LFKGVSREILMLLVAEMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEII-DSDLEKERVVGTLQCGDMFGDVGALCCRPQ 482
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYkLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 223530981 483 SFTFRTKTLSQLLRLKTSSLIEAMQTRQHDYIAIM 517
Cdd:cd00038   81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
545-713 9.22e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 9.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 545 DPNMASNLLTVASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWdalss 624
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH----- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 625 khqtifrilhhfasisdpqtagdllcTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADV 704
Cdd:COG0666  126 --------------------------LAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179


                 ....*....
gi 223530981 705 TASNTYEFS 713
Cdd:COG0666  180 NARDNDGET 188
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 404-520 1.03e-20

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 88.23  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981   404 LFKGVSREILMLLVAEMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEII-DSDLEKERVVGTLQCGDMFGDVGAL--CCR 480
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYkVLEDGEEQIVGTLGPGDFFGELALLtnSRR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 223530981   481 PQSFTFRTKTLSQLLRLKTSSLIEAMQTRQHDYIAIMKNF 520
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
KHA pfam11834
KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of ...
 766-837 1.47e-19

KHA, dimerization domain of potassium ion channel; KHA is the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus.


Pssm-ID: 463367  Cd Length: 65  Bit Score: 82.89  E-value: 1.47e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223530981  766 RVSIYKGHPLVRKqacckePGRLIRLPDSLEELKRIAGDKFGFdARNAMVTDvEGSVIDSIEVIRDNDKLFI 837
Cdd:pfam11834   2 RVTIFPNHDGKRR------NGKLIWLPDSLEELLKIASEKFGI-SATKILTE-DGAEIDDIDVIRDGDHLYL 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
585-708 2.76e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  585 LHIAASKGHEECVMVLLRHGCNIHLRDINGNTALwdalsskhqtifrilHHfasisdpqtagdllctAAKRNDLTMMKEL 664
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL---------------HL----------------AAKNGHLEIVKLL 49

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 223530981  665 LKHGlNVDAKDrQGKTAIQIAMAEKYVDMVDLLVMNGADVTASN 708
Cdd:pfam12796  50 LEHA-DVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 423-508 3.50e-15

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 71.49  E-value: 3.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  423 EYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSDLE-KERVVGTLQCGDMFGDVGALCCRPQSFTFRTKTLSQLLRLKTSS 501
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDgREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                  ....*..
gi 223530981  502 LIEAMQT 508
Cdd:pfam00027  82 FLELLER 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
552-633 4.03e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 4.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  552 LLTVASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHgCNIHLRDiNGNTALWDALSSKHQTIFR 631
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ..
gi 223530981  632 IL 633
Cdd:pfam12796  79 LL 80
Ion_trans_2 pfam07885
Ion channel; This family includes the two membrane helix type ion channels found in bacteria.
 257-328 5.50e-14

Ion channel; This family includes the two membrane helix type ion channels found in bacteria.


Pssm-ID: 462301 [Multi-domain]  Cd Length: 78  Bit Score: 67.68  E-value: 5.50e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223530981  257 WIGAVIPNFRETSLWiRYISAMYWSITTMTTVGYGDLHAVNTMEMIFIIFYMLFNLGLTAYLIGNMTNLVVE 328
Cdd:pfam07885   8 IFGTVYYLLEEGWEW-SFLDALYFSFVTLTTVGYGDIVPLTDAGRLFTIFYILIGIPLFAIFLAVLGRFLTE 78
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 405-523 2.20e-10

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 61.16  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 405 FKGVSREILMLLVAEMKAEYIPPREDVIMQNEAPDDVYIVVSGEVEIIDSDLE-KERVVGTLQCGDMFGDVGALCCRPQS 483
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDgREQILGFLGPGDFFGELSLLGGEPSP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 223530981 484 FTFRTKTLSQLLRLKTSSLIEAMqtrqHDYIAIMKNFLQH 523
Cdd:COG0664   81 ATAEALEDSELLRIPREDLEELL----ERNPELARALLRL 116
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
545-633 1.89e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 545 DPNMASN-----LLTVASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALW 619
Cdd:COG0666  178 DVNARDNdgetpLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                         90
                 ....*....|....
gi 223530981 620 DALSSKHQTIFRIL 633
Cdd:COG0666  258 LAAAAGAALIVKLL 271
KHA cd17073
KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found ...
 766-839 1.93e-09

KHA, dimerization domain of potassium ion channel, similar to doublecortin-like domain, found in potassium channel tetramerization domain containing 9 (KCTD9) and similar proteins; This family corresponds to KHA, the tetramerization domain of eukaryotic voltage-dependent potassium ion-channel proteins, mainly found in vertebrates KCTD9 and plants AKT proteins. In plants the domain lies at the C-terminus whereas in many chordates it lies at the N-terminus. KHA shows high sequence similarity with doublecortin-like domain, which has a stable ubiquitin-like tertiary fold. KCTD9, also termed BTB/POZ domain-containing protein 9, belongs to the KCTD protein family, which corresponds to potassium channel tetramerization domain proteins, a class of BTB-domain-containing proteins. It is involved in potassium channel formation. Moreover, KCTD9 contributes to liver injury through NK cell activation during hepatitis B virus (HBV)-induced acute-on-chronic liver failure. AKT proteins play crucial roles in K+ uptake and translocation in plant cells.


Pssm-ID: 340593  Cd Length: 65  Bit Score: 54.53  E-value: 1.93e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223530981 766 RVSIYK-GHPlvrkqacckEPGRLIRLPDSLEELKRIAGDKFGFDARNAMVTDveGSVIDSIEVIRDNDKLFIAE 839
Cdd:cd17073    2 RVTVFVnGSS---------SGGKVIALPSTLSELLKIASEKLGIPAKRLYTGS--GGEIDDIALIRDDDVLYVSE 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 567-711 4.17e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 567 LLKAKLDPDIGDSKGRTPLHIAASKGHEEC---VMVLLRHGCNIHLRDINGNTALwdalsskhqtifrilhHFasisdpq 643
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPL----------------HL------- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 644 tagdLLCTAakrNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVD--MVDLLVMNGADVTASNTYE 711
Cdd:PHA03095  90 ----YLYNA---TTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYG 152
Ank_2 pfam12796
Ankyrin repeats (3 copies);
514-611 7.80e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981  514 IAIMKNflqHHKTLKDLKvgEFPFESGEEDGDPNMAsnLLTVASTGNAAFLEELLKaKLDPDIGDsKGRTPLHIAASKGH 593
Cdd:pfam12796   3 LAAKNG---NLELVKLLL--ENGADANLQDKNGRTA--LHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 223530981  594 EECVMVLLRHGCNIHLRD 611
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 541-618 8.35e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 8.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 541 EEDGDPNMAsNLLTV-----ASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGN 615
Cdd:PTZ00322  71 EEVIDPVVA-HMLTVelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK 149


                 ...
gi 223530981 616 TAL 618
Cdd:PTZ00322 150 TPL 152
Ank_5 pfam13857
Ankyrin repeats (many copies);
572-618 4.60e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 4.60e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 223530981  572 LDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTAL 618
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
581-634 5.27e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 5.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 223530981  581 GRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIFRILH 634
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 580-611 1.81e-07

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: 48.05  E-value: 1.81e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 223530981  580 KGRTPLHIAASK-GHEECVMVLLRHGCNIHLRD 611
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 560-748 1.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 560 NAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIFRILhhfasi 639
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML------ 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 640 sdpqtagdllctaakrndltmmkelLKHGLNVDAKDRQGK-TAIQIAMAEKYVDMVDLLVMNGADVTASNTYEFSSTTLN 718
Cdd:PHA02875 188 -------------------------LDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 223530981 719 EMLKKREIGHRITVPDTVTSDEVI------LKRDEG 748
Cdd:PHA02875 243 DMICNMCTNLESEAIDALIADIAIrihkktIRRDEG 278
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 545-730 1.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 545 DPNMASNLLTVASTGNAAFLEELLKAK-LDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALwdals 623
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYgANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL----- 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 624 skhqtifrilhHFASisdpqtaGDLLctaakrnDLTMMKELLKHGLNVDAKDR-QGKTAIQIAMAEKyvDMVDLLVMNGA 702
Cdd:PHA02878 239 -----------HISV-------GYCK-------DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGA 291

                        170       180       190
                 ....*....|....*....|....*....|.
gi 223530981 703 DVTASNTYefSSTTLNEMLKKR---EIGHRI 730
Cdd:PHA02878 292 DINSLNSY--KLTPLSSAVKQYlciNIGRIL 320
Ank_4 pfam13637
Ankyrin repeats (many copies);
647-698 3.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 223530981  647 DLLCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLV 698
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 564-708 3.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 564 LEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKH------QTIFRILHHFA 637
Cdd:PHA03100  18 IKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvkEIVKLLLEYGA 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223530981 638 SIS---DPQTAGDLLCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVD--MVDLLVMNGADVTASN 708
Cdd:PHA03100  98 NVNapdNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKN 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 580-609 3.69e-06

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: 44.12  E-value: 3.69e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 223530981   580 KGRTPLHIAASKGHEECVMVLLRHGCNIHL 609
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 565-708 4.52e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 565 EELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKH-QTIFRILHHFASISDpq 643
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNiDTIKAIIDNRSNINK-- 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223530981 644 taGDL-LCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAM-AEKYVDMVDLLVMNGADVTASN 708
Cdd:PHA02876 240 --NDLsLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKN 304
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 567-711 9.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 9.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 567 LLKAKLDPDIGDSKGRTPLHIAASK--GHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIfrilhhfasisdpQT 644
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL-------------KI 158

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223530981 645 AGDLLCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADVTASNTYE 711
Cdd:PHA03100 159 LKLLIDKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225
Ank_5 pfam13857
Ankyrin repeats (many copies);
649-685 1.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.43e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 223530981  649 LCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIA 685
Cdd:pfam13857  20 LHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 567-705 1.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 567 LLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALS-SKHQTIFRILHHFASISDPQTA 645
Cdd:PHA02874 143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEyGDYACIKLLIDHGNHIMNKCKN 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223530981 646 G-DLLCTAAKRNDLTMmkELLKHGLNVDAKDRQGKTAIQIAMAEK-YVDMVDLLVMNGADVT 705
Cdd:PHA02874 223 GfTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 567-641 2.93e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 2.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223530981 567 LLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIFR-ILHHFASISD 641
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKlLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 551-713 3.70e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 3.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 551 NLLTVASTG---NAAFLEELLKAKLDPDIGDSKGRTPLHIA-ASKGHE-ECVMVLLRHGCNIHLRDINGNTAlwdalssk 625
Cdd:PHA03095 119 TPLHVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLlKSRNANvELLRLLIDAGADVYAVDDRFRSL-------- 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 626 hqtifriLHHFASISDPQTAgdllctaakrndltMMKELLKHGLNVDAKDRQGKTAIQIAMAE---KYVDMVDLLVmNGA 702
Cdd:PHA03095 191 -------LHHHLQSFKPRAR--------------IVRELIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLLI-AGI 248

                        170
                 ....*....|.
gi 223530981 703 DVTASNTYEFS 713
Cdd:PHA03095 249 SINARNRYGQT 259
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 552-710 3.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 552 LLTVASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLrhgcnihlrdING-NTALWDALSSKHQTIF 630
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI----------DNGvDTSILPIPCIEKDMIK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 631 RILHHFASIS-DPQTAGDLLCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADVTASNT 709
Cdd:PHA02874 109 TILDCGIDVNiKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188


                 .
gi 223530981 710 Y 710
Cdd:PHA02874 189 N 189
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 560-704 3.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 560 NAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRhgCNIHLRDI---NGNTALWDALSSKHQTIFRILHHF 636
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--LGKFADDVfykDGMTPLHLATILKKLDIMKLLIAR 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 637 ASISD-PQT-AGDLLCTAAKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADV 704
Cdd:PHA02875 125 GADPDiPNTdKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 575-697 7.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 7.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 575 DIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSsKHQTIFRILHHFASISDPQTAGDLLCTAAK 654
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLINNASINDQDIDGSTPLHHAI 262

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 223530981 655 RN--DLTMMKELLKHGLNVDAKDRQGKTAIQIAMaeKYVDMVDLL 697
Cdd:PHA02874 263 NPpcDIDIIDILLYHKADISIKDNKGENPIDTAF--KYINKDPVI 305
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 564-708 8.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 8.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 564 LEELLKAKLDPDIGDSKGRTPLHIAAS-KGHEECVMVLLRHGCNIHLRDINGNTAL-WDALSSKHQTIFRILHHFASISD 641
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIhYAAVRNNVVIINTLLDYGADIEA 403

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 642 -PQTAGDLLCTA-AKRNDLTMMKELLKHGLNVDAKDRQGKTAIQIAMAEK-YVDMVDLLVMNGADVTASN 708
Cdd:PHA02876 404 lSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAIN 473
PHA02946 PHA02946
ankyin-like protein; Provisional
 563-730 2.32e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 563 FLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKHQTIFRI---LHHFASI 639
Cdd:PHA02946  54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERInllVQYGAKI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 640 S---DPQTAGDLL-CTAAK---------------------RNDL-----------TMMKELLKHGLNVDAKDRQGKTAIQ 683
Cdd:PHA02946 134 NnsvDEEGCGPLLaCTDPServfkkimsigfearivdkfgKNHIhrhlmsdnpkaSTISWMMKLGISPSKPDHDGNTPLH 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 223530981 684 IAMAE--KYVDMVDLLvMNGADVTASNtyEFSSTTLNEMLKKREIGHRI 730
Cdd:PHA02946 214 IVCSKtvKNVDIINLL-LPSTDVNKQN--KFGDSPLTLLIKTLSPAHLI 259
Ank_4 pfam13637
Ankyrin repeats (many copies);
556-601 2.52e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 223530981  556 ASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLL 601
Cdd:pfam13637   9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
426-475 3.39e-04

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 42.66  E-value: 3.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 223530981 426 PPREDVIMQNEAPDDVYIVVSGEVEI-IDSDLEKERVVGTLQCGDMFGDVG 475
Cdd:PRK11753  26 PAKSTLIHAGEKAETLYYIVKGSVAVlIKDEEGKEMILSYLNQGDFIGELG 76
PRK10537 PRK10537
voltage-gated potassium channel protein;
277-338 4.93e-04

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 43.47  E-value: 4.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223530981 277 AMYWSITTMTTVGYGDLHAVNTMEMIFIIFYMLfnLGLTAY----------LIGNMTNLVVEGTRRTMEFRN 338
Cdd:PRK10537 172 AFYFSIVTMSTVGYGDIVPVSESARLFTISVII--LGITVFatsisaifgpVIRGNLKRLVKGRISHMHRKD 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 560-695 1.74e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 560 NAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMV--LLRHGCNIHLRDINGNTALwdalsskhqtifrilhHFA 637
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPL----------------HYA 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 223530981 638 SISDPQTAGDllctaakrndltmmkELLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVD 695
Cdd:PHA03095 265 AVFNNPRACR---------------RLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 583-704 2.26e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 583 TPLHIAASKGHEECVMVLLR-HGCNIHLRDINGNTALwdalsskhqtifrilhHFASISDPQTAGDLLCTAAKR-NDLTM 660
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETAL----------------HVAALYDNLEAAVVLMEAAPElVNEPM 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 223530981 661 MKELLkhglnvdakdrQGKTAIQIAMAEKYVDMVDLLVMNGADV 704
Cdd:cd22192   83 TSDLY-----------QGETALHIAVVNQNLNLVRELIARGADV 115
PHA03095 PHA03095
ankyrin-like protein; Provisional
 547-674 2.46e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 547 NMASNLLTVASTGNAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRHGCNIHLRDINGNTALWDALSSKH 626
Cdd:PHA03095 223 NTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223530981 627 --------------QTIFRILHHFAsisdpQTAGDLLCTAAKrndLTMMKELLKHGLNVDAK 674
Cdd:PHA03095 303 gravraalaknpsaETVAATLNTAS-----VAGGDIPSDATR---LCVAKVVLRGAFSLLPE 356
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 580-608 3.14e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 3.14e-03
                          10        20
                  ....*....|....*....|....*....
gi 223530981  580 KGRTPLHIAASKGHEECVMVLLRHGCNIH 608
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 560-708 5.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 560 NAAFLEELLKAKLDPDIGDSKGRTPLHIAASKGHEECVMVLLRhgcNIHLRDI-NGNTALWDALSSKHQTIFRIL--HHF 636
Cdd:PHA02878  49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSVfYTLVAIKDAFNNRNVEIFKIIltNRY 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223530981 637 ASIsdpQTAGDL-LCTAAKRN--DLTMMKELLKHGLNVDAKDR-QGKTAIQIAMAEKYVDMVDLLVMNGADVTASN 708
Cdd:PHA02878 126 KNI---QTIDLVyIDKKSKDDiiEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPD 198
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 566-706 6.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223530981 566 ELLKAKLDPDIGDSKGRTPLHIAASKGHE-ECVMVLLRHGCNIHLRDINGNTALwdalsskhqtifrilhHFASISDpqt 644
Cdd:PHA02876 292 KLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPL----------------HQASTLD--- 352

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223530981 645 agdllctaakRNDLTMMKeLLKHGLNVDAKDRQGKTAIQIAMAEKYVDMVDLLVMNGADVTA 706
Cdd:PHA02876 353 ----------RNKDIVIT-LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
 
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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