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Conserved domains on  [gi|2462626518|ref|XP_054219818|]
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histone-lysine N-methyltransferase EHMT1 isoform X35 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 15337343)

ankyrin repeat (ANK) domain-containing protein may be involved in mediating protein-protein interactions, such as myotrophin that promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 507-637 3.57e-72

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


:

Pssm-ID: 411018  Cd Length: 133  Bit Score: 233.82  E-value: 3.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 507 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 585
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462626518 586 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 637
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
713-901 6.66e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 6.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 713 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 792
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 793 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 872
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192

                         170       180
                  ....*....|....*....|....*....
gi 2462626518 873 ATEYKHVDLVKLLLSKGSDINIRDNDDGT 901
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKT 221
 
Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 507-637 3.57e-72

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 233.82  E-value: 3.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 507 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 585
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462626518 586 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 637
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
713-901 6.66e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 6.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 713 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 792
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 793 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 872
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192

                         170       180
                  ....*....|....*....|....*....
gi 2462626518 873 ATEYKHVDLVKLLLSKGSDINIRDNDDGT 901
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKT 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
803-896 3.93e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 111.36  E-value: 3.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 803 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 882
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 2462626518 883 KLLLSKGSDINIRD 896
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 737-898 1.57e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 737 FSARQGELQKVLLMLVD-GIDPNFKMEhqNKRSPLHAAAEAGHV-----DICHMLVQAGANIDTCSEDQRTPLMEAAEN- 809
Cdd:PHA03100   40 YLAKEARNIDVVKILLDnGADINSSTK--NNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 810 -NHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV------------------VQYLLSNGqMDVNCQDDGGWTPM 870
Cdd:PHA03100  118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPL 196

                         170       180
                  ....*....|....*....|....*...
gi 2462626518 871 IWATEYKHVDLVKLLLSKGSDINIRDND 898
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKY 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 801-892 1.96e-06

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: 51.55  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 801 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 874
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97

                          90
                  ....*....|....*...
gi 2462626518 875 EYKHVDLVKLLLSKGSDI 892
Cdd:cd22192    98 VNQNLNLVRELIARGADV 115
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 800-895 8.98e-06

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: 49.69  E-value: 8.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 800 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 866
Cdd:TIGR00870  53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128

                          90       100
                  ....*....|....*....|....*....
gi 2462626518 867 WTPMIWATEYKHVDLVKLLLSKGSDINIR 895
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 831-861 1.00e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.00e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462626518  831 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 861
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
 
Name Accession Description Interval E-value
EHMT_ZBD cd20905
Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 ...
 507-637 3.57e-72

Zinc-binding domain of euchromatic histone lysine methyltransferases EHMT1 and EHTM2; EHMT1 (also known as GLP) and EHMT2 (also known as NG36 and G9a) are histone methyltransferases that methylate the K9 position of histone H3, marking genomic regions for transcriptional repression. They may play a role in the G0/G1 cell cycle transition and are associated with promoting various types of cancer. Mutations in EHMT1 are associated with the genetic disorder Kleefstra syndrome. A functional role for the zinc-binding domain has not been established.


Pssm-ID: 411018  Cd Length: 133  Bit Score: 233.82  E-value: 3.57e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 507 LQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTN-SVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCG 585
Cdd:cd20905     1 STELPLCSCRMESPLYASITELAPVYCQAIDSIDGKLIGCSNlPVSKQELLRPSPRVPFLVLCEDHRARLVKHQCCPGCG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462626518 586 YFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEESS-KAKEVTIAK 637
Cdd:cd20905    81 LFCTQGTFVQCSPDGSIKHLFHRECALLIGGKPYCPHCGEDSPpSAKEVFLPL 133
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
713-901 6.66e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 6.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 713 LESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVDICHMLVQAGANI 792
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN--TLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 793 DTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIW 872
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHL 192

                         170       180
                  ....*....|....*....|....*....
gi 2462626518 873 ATEYKHVDLVKLLLSKGSDINIRDNDDGT 901
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVNAKDNDGKT 221
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
735-918 4.49e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.13  E-value: 4.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 735 LYFSARQGELQKVLLMLVDGIDPNFKMEhqNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEA 814
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDK--DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 815 VKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINI 894
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                         170       180
                  ....*....|....*....|....
gi 2462626518 895 RDNDDGTMKRGALSRQKEEKREAE 918
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
716-901 6.99e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 6.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 716 ALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTC 795
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 796 SEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATE 875
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAA 162

                         170       180
                  ....*....|....*....|....*.
gi 2462626518 876 YKHVDLVKLLLSKGSDINIRDNDDGT 901
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGET 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
735-901 6.84e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 6.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 735 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEA 814
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 815 VKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINI 894
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                  ....*..
gi 2462626518 895 RDNDDGT 901
Cdd:COG0666   281 ALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
803-896 3.93e-29

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 111.36  E-value: 3.93e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 803 LMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNgqMDVNCQDDgGWTPMIWATEYKHVDLV 882
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 2462626518 883 KLLLSKGSDINIRD 896
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
770-863 3.00e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 100.19  E-value: 3.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 770 LHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKaGALVDPKDaEGSTCLHLAAKKGHYEVVQ 849
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....
gi 2462626518 850 YLLSNGQmDVNCQD 863
Cdd:pfam12796  79 LLLEKGA-DINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 737-898 1.57e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 737 FSARQGELQKVLLMLVD-GIDPNFKMEhqNKRSPLHAAAEAGHV-----DICHMLVQAGANIDTCSEDQRTPLMEAAEN- 809
Cdd:PHA03100   40 YLAKEARNIDVVKILLDnGADINSSTK--NNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 810 -NHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV------------------VQYLLSNGqMDVNCQDDGGWTPM 870
Cdd:PHA03100  118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYG-VPINIKDVYGFTPL 196

                         170       180
                  ....*....|....*....|....*...
gi 2462626518 871 IWATEYKHVDLVKLLLSKGSDINIRDND 898
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKY 224
Ank_2 pfam12796
Ankyrin repeats (3 copies);
735-829 1.91e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 735 LYFSARQGELQKVLLMLVDGIDPNFKmeHQNKRSPLHAAAEAGHVDICHMLVQaGANIDtCSEDQRTPLMEAAENNHLEA 814
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 2462626518 815 VKYLIKAGALVDPKD 829
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 743-897 7.42e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 7.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 743 ELQKVLLMLVDGIDPNFKMehqnKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH-----LEAVKY 817
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 818 LIKAGALVDPKDAEGSTCLHLAA--KKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDL--VKLLLSKGSDIN 893
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDIN 170


                  ....
gi 2462626518 894 IRDN 897
Cdd:PHA03100  171 AKNR 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 700-898 1.04e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 700 PTPGLSQGPGKETLESAlIALDSEKPKKLRFhpkqLYFSARQGELQKVLLMLVDGIDPNfkMEHQNKRSPLHAAAEAGHV 779
Cdd:PHA02874   98 PIPCIEKDMIKTILDCG-IDVNIKDAELKTF----LHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFF 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 780 DICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHyEVVQYLLSNGQmdV 859
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS--I 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462626518 860 NCQDDGGWTPMIWATEYK-HVDLVKLLLSKGSDINIRDND 898
Cdd:PHA02874  248 NDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNK 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 758-897 6.33e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 6.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 758 NFKMEHQNKRSPLHAAAEA--GHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLE------------------AVKY 817
Cdd:PHA03100   98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkllidkgvdinaknRVNY 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 818 LIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 897
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
767-819 6.46e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 66.91  E-value: 6.46e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462626518 767 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLI 819
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 734-894 1.09e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 734 QLYFSARQGELQKV--LLMLVDGIDPNFkmeHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH 811
Cdd:PHA02875   71 ELHDAVEEGDVKAVeeLLDLGKFADDVF---YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 812 LEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSD 891
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227


                  ...
gi 2462626518 892 INI 894
Cdd:PHA02875  228 CNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 747-902 1.11e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 747 VLLMLVDGIDPNFKMEHqnKRSPLHAAAEAGH---VDICHMLVQAGANIDTCSEDQRTPLMEAAEN-NHLEAVKYLIKAG 822
Cdd:PHA03095   30 VRRLLAAGADVNFRGEY--GKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 823 ALVDPKDAEGSTCLH--LAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVD--LVKLLLSKGSDINIRDND 898
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDR 186


                  ....
gi 2462626518 899 DGTM 902
Cdd:PHA03095  187 FRSL 190
Ank_4 pfam13637
Ankyrin repeats (many copies);
799-852 2.32e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 65.37  E-value: 2.32e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462626518 799 QRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLL 852
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 743-901 6.46e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.22  E-value: 6.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 743 ELQKVLLMLVDGIDPNFKMEHQNKrSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAG 822
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 823 ALVDPKDAEGSTCLHLAAKK-GHYEVVQYLLSNGqMDVNCQDD-GGWTPMiwATEYKHVDLVKLLLSKGSDINIRDNDDG 900
Cdd:PHA02878  225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG-VDVNAKSYiLGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKL 301


                  .
gi 2462626518 901 T 901
Cdd:PHA02878  302 T 302
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 768-897 2.05e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 768 SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAE-------------------------NNhlEAVKYLIKAG 822
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpipciEK--DMIKTILDCG 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626518 823 ALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDN 897
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
832-886 4.06e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 4.06e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462626518 832 GSTCLHLAAKKGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLL 886
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 740-901 4.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 4.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 740 RQGELQKVLLMLVDGIDPNfkmeHQNKR--SPLHAAAEAGHVDICHMLV-----------------------QAGANIDT 794
Cdd:PHA02874   44 RSGDAKIVELFIKHGADIN----HINTKipHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktilDCGIDVNI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 795 CSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMdVNCQDDGGWTPMIWAT 874
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAA 198

                         170       180
                  ....*....|....*....|....*..
gi 2462626518 875 EYKHVDLVKLLLSKGSDINIRDNDDGT 901
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCKNGFT 225
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 767-916 2.26e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 767 RSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLhlAAKKGHYE 846
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCT--AAKRNDLT 636

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 847 VVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDInIRDNDDGTMKRGALsRQKEEKRE 916
Cdd:PLN03192  637 AMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV-DKANTDDDFSPTEL-RELLQKRE 703
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 742-893 7.69e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 7.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 742 GELQKVLLMLVDGIDPNFKMehQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKA 821
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 822 GALVDP---KDaeGSTCLHLAAKKGHYEVVQYLLSNG-QMDV-------------------------------NCQDDGG 866
Cdd:PHA02875   91 GKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGaDPDIpntdkfsplhlavmmgdikgiellidhkaclDIEDCCG 168

                         170       180
                  ....*....|....*....|....*..
gi 2462626518 867 WTPMIWATEYKHVDLVKLLLSKGSDIN 893
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANID 195
PHA02798 PHA02798
ankyrin-like protein; Provisional
 779-900 1.49e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 58.31  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 779 VDICHMLVQAGANIDTCSEDQRTPLMEAAEN----NH-LEAVKYLIKAGALVDPKDAEGST---CLHLAAKKGHYEVVQY 850
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHmLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462626518 851 LLSNGqMDVNCQDDGGWTPM-IWATEYKHVDL--VKLLLSKGSDINIRDNDDG 900
Cdd:PHA02798  131 MIENG-ADTTLLDKDGFTMLqVYLQSNHHIDIeiIKLLLEKGVDINTHNNKEK 182
PHA03095 PHA03095
ankyrin-like protein; Provisional
 804-901 1.59e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 804 MEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHY---EVVQYLLSNGqMDVNCQDDGGWTPMIWATEYKHV- 879
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNATTl 97

                          90       100
                  ....*....|....*....|..
gi 2462626518 880 DLVKLLLSKGSDINIRDNDDGT 901
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRT 119
PHA03095 PHA03095
ankyrin-like protein; Provisional
 747-901 1.60e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 747 VLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDI--CHMLVQAGANIDTCSEDQRTPLmeaaeNNHLEAVK-------Y 817
Cdd:PHA03095  135 IRLLLRKGADVNALDLYG--MTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLL-----HHHLQSFKprarivrE 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 818 LIKAGALVDPKDAEGSTCLHLAAKKGHYE---VVQYLLSNgqMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINI 894
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAG--ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285


                  ....*..
gi 2462626518 895 RDNDDGT 901
Cdd:PHA03095  286 VSSDGNT 292
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 766-897 2.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 766 KRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEA-AENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKG- 843
Cdd:PHA02876  375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462626518 844 HYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVdlVKLLLSKGSDinIRDN 897
Cdd:PHA02876  455 KLDVIEMLLDNGA-DVNAINIQNQYPLLIALEYHGI--VNILLHYGAE--LRDS 503
Ank_5 pfam13857
Ankyrin repeats (many copies);
851-901 2.65e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 2.65e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462626518 851 LLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNDDGT 901
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLT 51
Ank_5 pfam13857
Ankyrin repeats (many copies);
818-873 2.93e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 2.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626518 818 LIKAG-ALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWA 873
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 765-898 5.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 765 NKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGH 844
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626518 845 YEVVQYLLSNGQM--DVNCQDdgGWTPMIWATEYKHVDLVKLLLSKGSDINIRDND 898
Cdd:PHA02875   81 VKAVEELLDLGKFadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
PHA03095 PHA03095
ankyrin-like protein; Provisional
 746-897 1.19e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 746 KVLLMLVD-GIDPNFKmeHQNKRSPLHA--AAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNH--LEAVKYLIK 820
Cdd:PHA03095   98 DVIKLLIKaGADVNAK--DKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLID 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 821 AGALVDPKDAEGSTCLHLAAK--KGHYEVVQYLLSNGqMDVNCQDDGGWTPMIWATEY---KHVDLVKLLLsKGSDINIR 895
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGsscKRSLVLPLLI-AGISINAR 253


                  ..
gi 2462626518 896 DN 897
Cdd:PHA03095  254 NR 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 740-896 2.93e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 740 RQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLI 819
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYC--ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462626518 820 KAGALVDPKDAEgstcLHLAAKKGHYEvVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVD-LVKLLLSKGSDINIRD 896
Cdd:PHA02876  232 DNRSNINKNDLS----LLKAIRNEDLE-TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKN 304
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 735-861 3.90e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 735 LYFSARQGELQKVLLMLVDGIdpNFKMEHQNKRSPLHAAAEAGHVDICHMLVQ-AGANIDTCSEDQrtpLMEAAENNHLE 813
Cdd:PLN03192  562 LHIAASKGYEDCVLVLLKHAC--NVHIRDANGNTALWNAISAKHHKIFRILYHfASISDPHAAGDL---LCTAAKRNDLT 636

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462626518 814 AVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 861
Cdd:PLN03192  637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA-DVDK 683
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 801-892 1.96e-06

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: 51.55  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 801 TPLMEAAENNHLEAVKYLIKAGAlVDP--KDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVN----CQDDGGWTPMIWAT 874
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPS-CDLfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALHIAV 97

                          90
                  ....*....|....*...
gi 2462626518 875 EYKHVDLVKLLLSKGSDI 892
Cdd:cd22192    98 VNQNLNLVRELIARGADV 115
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 675-892 2.07e-06

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: 51.68  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 675 DDKLQGAASHVPEgfDPTGPAGLGRPTPGLSQGPGKETlesaliALDSEKPKKLRFHPKQLYFSARQGELQKV---LLML 751
Cdd:cd22194     3 DSNIRQCPSGNCD--DMDSPQSPQDDTPSNPNSPSAEL------AKEEQRDKKKRLKKVSEAAVEELGELLKElkdLSRR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 752 VDGIDPNFKMEHQNKrsplhaAAEAGHVdiChmLVQAGANIDTCSEDQRTPLMEAAENNHLeaVKYLIKAGalVDPKDAE 831
Cdd:cd22194    75 RRKTDVPDFLMHKLT------ASDTGKT--C--LMKALLNINENTKEIVRILLAFAEENGI--LDRFINAE--YTEEAYE 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462626518 832 GSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQ-----------DDG---GWTPMIWATEYKHVDLVKLLLSKGSDI 892
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGA-DVNAHakgvffnpkykHEGfyfGETPLALAACTNQPEIVQLLMEKESTD 214
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 740-907 3.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 740 RQGELQKVLLMLVDGIDPNFKMEHQNkrSPLHAAAEAGHVD-ICHMLVQAGANIDTCSEDQRTPLMEAAENNH-LEAVKY 817
Cdd:PHA02876  249 RNEDLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 818 LIKAGALVDPKDAEGSTCLHLAAKKGHY-EVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRD 896
Cdd:PHA02876  327 LIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGA-NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405

                         170
                  ....*....|.
gi 2462626518 897 NDDGTMKRGAL 907
Cdd:PHA02876  406 QKIGTALHFAL 416
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 779-860 3.65e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 779 VDICHM-----------LVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEV 847
Cdd:PTZ00322   84 VELCQLaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                          90
                  ....*....|...
gi 2462626518 848 VQYLLSNGQMDVN 860
Cdd:PTZ00322  164 VQLLSRHSQCHFE 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 866-897 5.09e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 5.09e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462626518 866 GWTPMIWA-TEYKHVDLVKLLLSKGSDINIRDN 897
Cdd:pfam00023   2 GNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 746-830 7.46e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 746 KVLLMLVDGIDPNFKmehqNKR--SPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGA 823
Cdd:PHA03100  174 RVNYLLSYGVPINIK----DVYgfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                  ....*..
gi 2462626518 824 LVDPKDA 830
Cdd:PHA03100  250 SIKTIIE 256
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 800-895 8.98e-06

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: 49.69  E-value: 8.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 800 RTPLMEAA-ENNHLEAVKYLIKAGALVDpkdaEGSTCLHLAAKKGH---YEVVQYLLSNGQMDVN-------CQDD--GG 866
Cdd:TIGR00870  53 RSALFVAAiENENLELTELLLNLSCRGA----VGDTLLHAISLEYVdavEAILLHLLAAFRKSGPlelandqYTSEftPG 128

                          90       100
                  ....*....|....*....|....*....
gi 2462626518 867 WTPMIWATEYKHVDLVKLLLSKGSDINIR 895
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 831-861 1.00e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 1.00e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462626518  831 EGSTCLHLAAKKGHYEVVQYLLSNGQmDVNC 861
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 831-864 1.01e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 1.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462626518 831 EGSTCLHLAAKK-GHYEVVQYLLSNGQmDVNCQDD 864
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGA-DVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 798-887 1.04e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 798 DQRTPLMEAAENNHLEA------VKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMI 871
Cdd:PTZ00322   75 DPVVAHMLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLE 153

                          90
                  ....*....|....*.
gi 2462626518 872 WATEYKHVDLVKLLLS 887
Cdd:PTZ00322  154 LAEENGFREVVQLLSR 169
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 805-896 1.13e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 805 EAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKL 884
Cdd:PHA02876  151 ERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKA 229

                          90
                  ....*....|..
gi 2462626518 885 LLSKGSDINIRD 896
Cdd:PHA02876  230 IIDNRSNINKND 241
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 765-793 1.36e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.36e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462626518  765 NKRSPLHAAAEAGHVDICHMLVQAGANID 793
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
785-839 1.51e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462626518 785 LVQAG-ANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLA 839
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 866-894 3.76e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.76e-05
                           10        20
                   ....*....|....*....|....*....
gi 2462626518  866 GWTPMIWATEYKHVDLVKLLLSKGSDINI 894
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 765-793 6.99e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 6.99e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462626518 765 NKRSPLHAAAE-AGHVDICHMLVQAGANID 793
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 739-820 7.71e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 7.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 739 ARQGELQKVLLMLVDGIDPNFKMEHQnkRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYL 818
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDG--RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ..
gi 2462626518 819 IK 820
Cdd:PTZ00322  168 SR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 798-826 1.53e-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: 39.49  E-value: 1.53e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462626518  798 DQRTPLMEAAENNHLEAVKYLIKAGALVD 826
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 746-853 2.45e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 746 KVLLMLVD-GIDPNFKMEHQNkrSPLHAAAEAGHVDICHM--LVQAGANIDTCSEDQRTPLMEAAENNHLEAVKYLIKAG 822
Cdd:PHA03095  203 RIVRELIRaGCDPAATDMLGN--TPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462626518 823 ALVDPKDAEGSTCLHLAAKKGHYEVVQYLLS 853
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 798-829 3.64e-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: 3.64e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462626518 798 DQRTPLMEAAE-NNHLEAVKYLIKAGALVDPKD 829
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 767-888 3.96e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 3.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 767 RSPLHAAAEAGHVD--ICHMLVQAGANIDTCSEDQRTPLMEAAENNHLEA--VKYLIKAGALVDPKDAEGSTCLHLAAKK 842
Cdd:PHA03095  188 RSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVF 267

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462626518 843 GHYEVVQYLLSNGQmDVNCQDDGGWTPMIWATEYKHVDLVKLLLSK 888
Cdd:PHA03095  268 NNPRACRRLIALGA-DINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 800-868 7.62e-04

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: 43.21  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 800 RTPLMEAAENNHLEAVKYLIKAGALVD---------PKDAE-----GSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDDG 865
Cdd:cd22194   142 QTALNIAIERRQGDIVKLLIAKGADVNahakgvffnPKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDSR 221


                  ...
gi 2462626518 866 GWT 868
Cdd:cd22194   222 GNT 224
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 866-894 8.71e-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: 37.62  E-value: 8.71e-04
                          10        20
                  ....*....|....*....|....*....
gi 2462626518 866 GWTPMIWATEYKHVDLVKLLLSKGSDINI 894
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 831-861 1.02e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462626518 831 EGSTCLHLAAKKGHYEVVQYLLSNGqMDVNC 861
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 765-794 1.07e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.07e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462626518 765 NKRSPLHAAAEAGHVDICHMLVQAGANIDT 794
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 798-823 1.08e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462626518 798 DQRTPLMEAAENNHLEAVKYLIKAGA 823
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA 26
Ank_4 pfam13637
Ankyrin repeats (many copies);
866-901 2.24e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 2.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2462626518 866 GWTPMIWATEYKHVDLVKLLLSKGSDINIRDNDDGT 901
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET 36
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 851-902 3.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 3.90e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462626518 851 LLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNDDGTM 902
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSV 214
RING-HC_PCGF2 cd16734
RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, ...
 571-641 4.60e-03

RING finger found in polycomb group RING finger protein 2 (PCGF2) and similar proteins; PCGF2, also known as DNA-binding protein Mel-18, RING finger protein 110 (RNF110), or zinc finger protein 144 (ZNF144), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a canonical Polycomb repressive complex 1 (PRC1), which is composed of a chromodomain-containing protein (CBX2, CBX4, CBX6, CBX7 or CBX8) and a Polyhomeotic protein (PHC1, PHC2, or PHC3). Like other PCGF homologs, PCGF2 associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF2 uniquely regulates PRC1 to specify mesoderm cell fate in embryonic stem cells. It is required for PRC1 stability and maintenance of gene repression in embryonic stem cells (ESCs) and essential for ESC differentiation into early cardiac-mesoderm precursors. PCGF2 also plays a significant role in the angiogenic function of endothelial cells (ECs) by regulating endothelial gene expression. Furthermore, PCGF2 is a SUMO-dependent regulator of hormone receptors. It facilitates the deSUMOylation process by inhibiting PCGF4/BMI1-mediated ubiquitin-proteasomal degradation of SUMO1/sentrin-specific protease 1 (SENP1). It is also a novel negative regulator of breast cancer stem cells (CSCs) that inhibits the stem cell population and in vitro and in vivo self-renewal through the inactivation of Wnt-mediated Notch signaling. PCGF2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438392 [Multi-domain]  Cd Length: 80  Bit Score: 36.89  E-value: 4.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462626518 571 HRGRMVK------HQCCPGCG-YFCTAGNFMECQpessisHRFHKDCASRVNNAS-YCPHCGEESSKAKEVTIAKADTT 641
Cdd:cd16734     1 HRTTRIKitelnpHLMCALCGgYFIDAATIVECL------HSFCKTCIVRYLETNkYCPMCDVQVHKTRPLLSIRSDKT 73
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 768-893 6.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 768 SPLHAAAEAGHV--DICHMLVQAGANIDTCSEDQRTPLMEA----AENNHLEAVKYLIKAGALVDPKDAEGSTCLH--LA 839
Cdd:PHA02859   53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHylsfNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462626518 840 AKKGHYEVVQYLLSNGQMDVNCQDDGG---WTPMIWATEYKHVDlvkLLLSKGSDIN 893
Cdd:PHA02859  133 NFNVRINVIKLLIDSGVSFLNKDFDNNnilYSYILFHSDKKIFD---FLTSLGIDIN 186
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 749-909 7.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.11  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 749 LMLVDGIDPNfkmEHQNKR--SPLHAAAEAGHV--DICHMLVQAGANI-DTCSEDQRTP----LMEAAENNHLEAVKYLI 819
Cdd:PHA02989  129 FLLSKGINVN---DVKNSRgyNLLHMYLESFSVkkDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLI 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 820 KAGALVDPKDAEGSTCL------HLAAKKGHYEVVQYLLSngQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDIN 893
Cdd:PHA02989  206 KKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILK--YIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIY 283

                         170
                  ....*....|....*.
gi 2462626518 894 IRDNDDGTMKRGALSR 909
Cdd:PHA02989  284 NVSKDGDTVLTYAIKH 299
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 807-909 8.88e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 807 AENNHLEAVKYLIKAGALVDPKDAEGSTCLHlaakkghyevvQYLLSNgqmdvncqddggwtpmiwateYKHVDLVKLLL 886
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLH-----------QYILRH---------------------NISTDIIKLLH 339

                          90       100
                  ....*....|....*....|...
gi 2462626518 887 SKGSDINIRDNDDGTMKRGALSR 909
Cdd:PHA02716  340 EYGNDLNEPDNIGNTVLHTYLSM 362
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 768-840 9.10e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 9.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462626518 768 SPLHAAAEAGHVDICHMLVQAGANID---TCSEDQRT-----------PLMEAAENNHLEAVKYLIKAGALVDPKDAEGS 833
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVParaCGDFFVKSqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209


                  ....*..
gi 2462626518 834 TCLHLAA 840
Cdd:TIGR00870 210 TLLHLLV 216
 
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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