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Conserved domains on  [gi|1074286255|emb|SBR87500|]
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notch homolog 1b, partial [Nothobranchius pienaari]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
450-663 5.00e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 5.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  450 ASANVINDFIYQGANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNR 529
Cdd:COG0666     64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  530 AtDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETP 609
Cdd:COG0666    144 A-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1074286255  610 LFLAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRLMDEYNL 663
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
JMTM_Notch1 cd21702
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
264-343 2.96e-33

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 1 (Notch1) and similar proteins; Neurogenic locus notch homolog protein 1 (Notch1), also called translocation-associated notch protein TAN-1, functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. It affects the implementation of differentiation, proliferation and apoptotic programs. It is also involved in angiogenesis, and also negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch1, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


:

Pssm-ID: 411985  Cd Length: 80  Bit Score: 122.98  E-value: 2.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  264 AVYSGVDLQSTDNGLYPIYLVLGGVGILAFLGVGMVAARKRRHEHGRLWLPEGFKTTETSKKKRCEPVGGDSVGLKPLKN 343
Cdd:cd21702      1 AVKSETVEPPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPSKKKRREPVGEDSVGLKPLKN 80
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
109-164 1.79e-27

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. Role of NOD domain remains to be elucidated.


:

Pssm-ID: 462014  Cd Length: 56  Bit Score: 105.67  E-value: 1.79e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1074286255  109 PEKIAVGQLVLVVHITPEHLLNNSFGFLRELSRVLRTNVLFRKDANGELMVYPYYG 164
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGNPMIYPWYG 56
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
215-267 3.68e-23

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.


:

Pssm-ID: 462229  Cd Length: 59  Bit Score: 93.49  E-value: 3.68e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1074286255  215 IKGSVVYLEMDNRQCFQQTSECFQSTDDAAAFLGALESSGKLDVPFTIEAVYS 267
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRS 53
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
69-105 1.30e-13

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


:

Pssm-ID: 459658  Cd Length: 35  Bit Score: 65.63  E-value: 1.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1074286255   69 EGQCNPlydQYCKDHYADGHCDQGCNNAECEWDGLDC 105
Cdd:pfam00066    1 WPNCPY---PYCWDKFGNGVCDEECNNAECLWDGGDC 34
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
28-65 1.41e-13

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


:

Pssm-ID: 197463  Cd Length: 38  Bit Score: 65.43  E-value: 1.41e-13
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1074286255    28 DDPWKNCSAsLQCWRYFNDEKCDSQCDNAGCLYDGFDC 65
Cdd:smart00004    2 QDPWSRCED-AQCWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
1-24 1.16e-07

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


:

Pssm-ID: 459658  Cd Length: 35  Bit Score: 48.68  E-value: 1.16e-07
                           10        20
                   ....*....|....*....|....
gi 1074286255    1 HKHNKYCDVLCNNHACGWDNGDCS 24
Cdd:pfam00066   12 KFGNGVCDEECNNAECLWDGGDCS 35
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
450-663 5.00e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 5.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  450 ASANVINDFIYQGANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNR 529
Cdd:COG0666     64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  530 AtDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETP 609
Cdd:COG0666    144 A-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1074286255  610 LFLAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRLMDEYNL 663
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
JMTM_Notch1 cd21702
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
264-343 2.96e-33

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 1 (Notch1) and similar proteins; Neurogenic locus notch homolog protein 1 (Notch1), also called translocation-associated notch protein TAN-1, functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. It affects the implementation of differentiation, proliferation and apoptotic programs. It is also involved in angiogenesis, and also negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch1, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


Pssm-ID: 411985  Cd Length: 80  Bit Score: 122.98  E-value: 2.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  264 AVYSGVDLQSTDNGLYPIYLVLGGVGILAFLGVGMVAARKRRHEHGRLWLPEGFKTTETSKKKRCEPVGGDSVGLKPLKN 343
Cdd:cd21702      1 AVKSETVEPPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPSKKKRREPVGEDSVGLKPLKN 80
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
109-164 1.79e-27

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. Role of NOD domain remains to be elucidated.


Pssm-ID: 462014  Cd Length: 56  Bit Score: 105.67  E-value: 1.79e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1074286255  109 PEKIAVGQLVLVVHITPEHLLNNSFGFLRELSRVLRTNVLFRKDANGELMVYPYYG 164
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGNPMIYPWYG 56
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
215-267 3.68e-23

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.


Pssm-ID: 462229  Cd Length: 59  Bit Score: 93.49  E-value: 3.68e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1074286255  215 IKGSVVYLEMDNRQCFQQTSECFQSTDDAAAFLGALESSGKLDVPFTIEAVYS 267
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRS 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
477-570 2.76e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  477 LHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDarmHDGTTPLILAARLAVEGMV 556
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1074286255  557 EELINCHADVNAID 570
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
69-105 1.30e-13

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 65.63  E-value: 1.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1074286255   69 EGQCNPlydQYCKDHYADGHCDQGCNNAECEWDGLDC 105
Cdd:pfam00066    1 WPNCPY---PYCWDKFGNGVCDEECNNAECLWDGGDC 34
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
28-65 1.41e-13

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 65.43  E-value: 1.41e-13
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1074286255    28 DDPWKNCSAsLQCWRYFNDEKCDSQCDNAGCLYDGFDC 65
Cdd:smart00004    2 QDPWSRCED-AQCWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
31-66 1.93e-13

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 65.24  E-value: 1.93e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1074286255   31 WKNCSASlQCWRYFNDEKCDSQCDNAGCLYDGFDCQ 66
Cdd:pfam00066    1 WPNCPYP-YCWDKFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
65-105 2.65e-13

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 64.65  E-value: 2.65e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1074286255    65 CQNLEGQCNplyDQYCKDHYADGHCDQGCNNAECEWDGLDC 105
Cdd:smart00004    1 PQDPWSRCE---DAQCWDKFGDGVCDEECNNAECLWDGGDC 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
417-625 1.91e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 1.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  417 DVNVRGPDGYTPLmiASCsgggLETGNSEEEEdasanVINDFIYQGANLhNQTDRTGETALHLAARYA-RSDAAKRLLEA 495
Cdd:PHA03095    39 DVNFRGEYGKTPL--HLY----LHYSSEKVKD-----IVRLLLEAGADV-NAPERCGFTPLHLYLYNAtTLDVIKLLIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  496 SADANIQDNMGRTPLHAAVAADA--QGVFQILIRNRAtDLDARMHDGTTPL---ILAARLAVEgMVEELINCHADVNAID 570
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGA-DVNALDLYGMTPLavlLKSRNANVE-LLRLLIDAGADVYAVD 184
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1074286255  571 DFGKSALHWAAAVNNVEAAIV--LLKNGANKDMQNNKEETPLFLAAREGSYETAKVL 625
Cdd:PHA03095   185 DRFRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVL 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
473-633 5.01e-11

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: 66.57  E-value: 5.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  473 GETALHLAARYARSDAAKRLLEASADAnIQDNM------GRTPLHAAVAADAQGVFQILIRNRATDLDAR---------- 536
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgp 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  537 ---MHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAI----VLLKNGANKD------MQN 603
Cdd:cd22192    130 knlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDDlqpldlVPN 209
                          170       180       190
                   ....*....|....*....|....*....|
gi 1074286255  604 NKEETPLFLAAREGSYetakVLLEHFANRE 633
Cdd:cd22192    210 NQGLTPFKLAAKEGNI----VMFQHLVQKR 235
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
1-24 1.16e-07

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 48.68  E-value: 1.16e-07
                           10        20
                   ....*....|....*....|....
gi 1074286255    1 HKHNKYCDVLCNNHACGWDNGDCS 24
Cdd:pfam00066   12 KFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
1-23 5.38e-07

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 46.94  E-value: 5.38e-07
                            10        20
                    ....*....|....*....|...
gi 1074286255     1 HKHNKYCDVLCNNHACGWDNGDC 23
Cdd:smart00004   16 KFGDGVCDEECNNAECLWDGGDC 38
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
450-663 5.00e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 5.00e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  450 ASANVINDFIYQGANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNR 529
Cdd:COG0666     64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  530 AtDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETP 609
Cdd:COG0666    144 A-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1074286255  610 LFLAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRLMDEYNL 663
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
417-637 6.73e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 6.73e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  417 DVNVRGPDGYTPLMIASCSGggletgnseeeedaSANVINDFIYQGANLhNQTDRTGETALHLAARYARSDAAKRLLEAS 496
Cdd:COG0666     79 DINAKDDGGNTLLHAAARNG--------------DLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAG 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  497 ADANIQDNMGRTPLHAAVAADAQGVFQILIRNRAtDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSA 576
Cdd:COG0666    144 ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1074286255  577 LHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLEHFANREITDH 637
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
452-663 7.51e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 7.51e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  452 ANVINDFIYQGANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRAt 531
Cdd:COG0666     33 LLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA- 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  532 DLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWaaAVNNVEAAIV--LLKNGANKDMQNNKEETP 609
Cdd:COG0666    112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL--AAANGNLEIVklLLEAGADVNARDNDGETP 189
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1074286255  610 LFLAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRLMDEYNL 663
Cdd:COG0666    190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
JMTM_Notch1 cd21702
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
264-343 2.96e-33

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 1 (Notch1) and similar proteins; Neurogenic locus notch homolog protein 1 (Notch1), also called translocation-associated notch protein TAN-1, functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. It affects the implementation of differentiation, proliferation and apoptotic programs. It is also involved in angiogenesis, and also negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch1, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


Pssm-ID: 411985  Cd Length: 80  Bit Score: 122.98  E-value: 2.96e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  264 AVYSGVDLQSTDNGLYPIYLVLGGVGILAFLGVGMVAARKRRHEHGRLWLPEGFKTTETSKKKRCEPVGGDSVGLKPLKN 343
Cdd:cd21702      1 AVKSETVEPPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPSKKKRREPVGEDSVGLKPLKN 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
417-610 1.09e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  417 DVNVRGPDGYTPLMIASCSGggletgnseeeedaSANVINDFIYQGANLhNQTDRTGETALHLAARYARSDAAKRLLEAS 496
Cdd:COG0666    112 DVNARDKDGETPLHLAAYNG--------------NLEIVKLLLEAGADV-NAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  497 ADANIQDNMGRTPLHAAVAADAQGVFQILIRNRAtDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSA 576
Cdd:COG0666    177 ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1074286255  577 LHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPL 610
Cdd:COG0666    256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
109-164 1.79e-27

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. Role of NOD domain remains to be elucidated.


Pssm-ID: 462014  Cd Length: 56  Bit Score: 105.67  E-value: 1.79e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1074286255  109 PEKIAVGQLVLVVHITPEHLLNNSFGFLRELSRVLRTNVLFRKDANGELMVYPYYG 164
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGNPMIYPWYG 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
455-657 9.68e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 9.68e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  455 INDFIYQGANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRAtDLD 534
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  535 ARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLAA 614
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1074286255  615 REGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRL 657
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
215-267 3.68e-23

NOTCH protein; NOTCH signalling plays a fundamental role during a great number of developmental processes in multicellular animals. NOD and NODP represent a region present in many NOTCH proteins and NOTCH homologs in multiple species such as NOTCH2 and NOTCH3, LIN12, SC1 and TAN1. The role of the NOD and NODP domains remains to be elucidated.


Pssm-ID: 462229  Cd Length: 59  Bit Score: 93.49  E-value: 3.68e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1074286255  215 IKGSVVYLEMDNRQCFQQTSECFQSTDDAAAFLGALESSGKLDVPFTIEAVYS 267
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRS 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
477-570 2.76e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.76e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  477 LHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDarmHDGTTPLILAARLAVEGMV 556
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1074286255  557 EELINCHADVNAID 570
Cdd:pfam12796   78 KLLLEKGADINVKD 91
JMTM_Notch cd21701
juxtamembrane and transmembrane (JMTM) domain found in Notch protein family; Neurogenic locus ...
259-341 2.63e-16

juxtamembrane and transmembrane (JMTM) domain found in Notch protein family; Neurogenic locus notch homolog (Notch) proteins are a family of type-1 transmembrane proteins that form a core component of the Notch signaling pathway. They operate in a variety of different tissues and play a role in a variety of developmental processes by controlling cell fate decisions. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch proteins, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


Pssm-ID: 411984  Cd Length: 85  Bit Score: 74.72  E-value: 2.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  259 PFTIEAVYS--GVDLQSTD-NGLYPIYLVLGGVGI-LAFLGVgMVAARKRRHehGRLWLPEGFKTTE-TSKKKRCEPVGG 333
Cdd:cd21701      1 PYPIYSVRSepGPATKTTPpAQLSPLVVAAVCVLLvLVVLGV-LVARKRRRH--GTLWFPEGFPRTRaSRRSRRRDPVGQ 77

                   ....*...
gi 1074286255  334 DSVGLKPL 341
Cdd:cd21701     78 DSVGLKNL 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-658 7.26e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 7.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  492 LLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDD 571
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  572 FGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMH 651
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                   ....*..
gi 1074286255  652 HDIVRLM 658
Cdd:COG0666    166 LEIVKLL 172
JMTM_Notch3 cd21704
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
254-339 2.88e-14

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 3 (Notch3) and similar proteins; Neurogenic locus notch homolog protein 3 (Notch3) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch3, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


Pssm-ID: 411987  Cd Length: 90  Bit Score: 69.39  E-value: 2.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  254 GKLDVPFTIEAVYSGVDLQSTDNGLYPIYLVLGGVGILAFLGVGMVAARKRRhEHGRLWLPEGFK-TTETSKKKRCEPVG 332
Cdd:cd21704      1 ERLEFPYPIKEVRGEKLEPPPPPVRLLPLLGVAAVILLVILVLGVLVARRKR-EHSTLWFPEGFFlKKESSNKNRREPVG 79

                   ....*..
gi 1074286255  333 GDSVGLK 339
Cdd:cd21704     80 QDALGMK 86
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
69-105 1.30e-13

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 65.63  E-value: 1.30e-13
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1074286255   69 EGQCNPlydQYCKDHYADGHCDQGCNNAECEWDGLDC 105
Cdd:pfam00066    1 WPNCPY---PYCWDKFGNGVCDEECNNAECLWDGGDC 34
JMTM_Notch2 cd21703
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
258-341 1.34e-13

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 2 (Notch2) and similar proteins; Neurogenic locus notch homolog protein 2 (Notch2) functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Notch2 is involved in bone remodeling and homeostasis. In collaboration with RELA/p65, it enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation. Notch2 positively regulates self-renewal of liver cancer cells. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch2, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


Pssm-ID: 411986  Cd Length: 82  Bit Score: 67.09  E-value: 1.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  258 VPFTIEAVYSGVDLQSTDNGLYPIYLVLGGVGILAFLGVgMVAARKRRHehGRLWLPEGF-KTTETSKKKRCEPVGGDSV 336
Cdd:cd21703      1 LPYPLVSVTSEPLKETKFNLLYLLAVAVAIILLILLLGV-LVAKRKRKH--GPLWFPEGFiLNKENSNRKRREPVGQDAV 77

                   ....*
gi 1074286255  337 GLKPL 341
Cdd:cd21703     78 GMKNL 82
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
28-65 1.41e-13

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 65.43  E-value: 1.41e-13
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1074286255    28 DDPWKNCSAsLQCWRYFNDEKCDSQCDNAGCLYDGFDC 65
Cdd:smart00004    2 QDPWSRCED-AQCWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
31-66 1.93e-13

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 65.24  E-value: 1.93e-13
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1074286255   31 WKNCSASlQCWRYFNDEKCDSQCDNAGCLYDGFDCQ 66
Cdd:pfam00066    1 WPNCPYP-YCWDKFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
65-105 2.65e-13

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 64.65  E-value: 2.65e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1074286255    65 CQNLEGQCNplyDQYCKDHYADGHCDQGCNNAECEWDGLDC 105
Cdd:smart00004    1 PQDPWSRCE---DAQCWDKFGDGVCDEECNNAECLWDGGDC 38
JMTM_Notch4 cd21705
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
258-342 6.10e-13

juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein 4 (Notch4) and similar proteins; Neurogenic locus notch homolog protein 4 (Notch4) functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. It affects the implementation of differentiation, proliferation and apoptotic programs. This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of Notch4, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


Pssm-ID: 411988  Cd Length: 92  Bit Score: 65.49  E-value: 6.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  258 VPFTIEAVYSGVDLQSTDNGL-----YPIY-LVLGGVGIL--AFLGVGMvaARKRRHEHGRLWLPEGF-KTTETSKKKRC 328
Cdd:cd21705      1 LPFPLLAVTVEEAEKDPQLVAaqlpwPLVCsSVAGVLALVlgALLGVQL--IRRRQREHGALWLPPGFaRHRDPNPHRRR 78
                           90
                   ....*....|....
gi 1074286255  329 EPVGGDSVGLKPLK 342
Cdd:cd21705     79 EPVGEDAIGLKPLK 92
Ank_2 pfam12796
Ankyrin repeats (3 copies);
544-636 1.41e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 1.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  544 LILAARLAVEGMVEELINCHADVNAIDDFGKSALHWaaAVNNVEAAIV-LLKNGANKDMQNNKeETPLFLAAREGSYETA 622
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL--AAKNGHLEIVkLLLEHADVNLKDNG-RTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1074286255  623 KVLLEHFANREITD 636
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
417-625 1.91e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 1.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  417 DVNVRGPDGYTPLmiASCsgggLETGNSEEEEdasanVINDFIYQGANLhNQTDRTGETALHLAARYA-RSDAAKRLLEA 495
Cdd:PHA03095    39 DVNFRGEYGKTPL--HLY----LHYSSEKVKD-----IVRLLLEAGADV-NAPERCGFTPLHLYLYNAtTLDVIKLLIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  496 SADANIQDNMGRTPLHAAVAADA--QGVFQILIRNRAtDLDARMHDGTTPL---ILAARLAVEgMVEELINCHADVNAID 570
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGA-DVNALDLYGMTPLavlLKSRNANVE-LLRLLIDAGADVYAVD 184
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1074286255  571 DFGKSALHWAAAVNNVEAAIV--LLKNGANKDMQNNKEETPLFLAAREGSYETAKVL 625
Cdd:PHA03095   185 DRFRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVL 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
463-631 1.62e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  463 ANLHNQTDRTGETALH---LAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQ---GVFQILIRNRAtDLDAR 536
Cdd:PHA03095     1 DEEDESVDIIMEAALYdylLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGA-DVNAP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  537 MHDGTTPLILAARLA-VEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIV--LLKNGANKDMQNNKEETPL--F 611
Cdd:PHA03095    80 ERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPKVIrlLLRKGADVNALDLYGMTPLavL 159
                          170       180
                   ....*....|....*....|
gi 1074286255  612 LAAREGSYETAKVLLEHFAN 631
Cdd:PHA03095   160 LKSRNANVELLRLLIDAGAD 179
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
473-633 5.01e-11

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: 66.57  E-value: 5.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  473 GETALHLAARYARSDAAKRLLEASADAnIQDNM------GRTPLHAAVAADAQGVFQILIRNRATDLDAR---------- 536
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgp 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  537 ---MHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAI----VLLKNGANKD------MQN 603
Cdd:cd22192    130 knlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDDlqpldlVPN 209
                          170       180       190
                   ....*....|....*....|....*....|
gi 1074286255  604 NKEETPLFLAAREGSYetakVLLEHFANRE 633
Cdd:cd22192    210 NQGLTPFKLAAKEGNI----VMFQHLVQKR 235
PHA02878 PHA02878
ankyrin repeat protein; Provisional
462-633 1.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  462 GANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRATdLDARMHDGT 541
Cdd:PHA02878   157 GADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCGN 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  542 TPL-ILAARLAVEGMVEELINCHADVNAIDDF-GKSALHWAAAVNNVEAaiVLLKNGANKDMQNNKEETPLFLAAREGS- 618
Cdd:PHA02878   236 TPLhISVGYCKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSAVKQYLc 313
                          170
                   ....*....|....*
gi 1074286255  619 YETAKVLLEHFANRE 633
Cdd:PHA02878   314 INIGRILISNICLLK 328
PHA03095 PHA03095
ankyrin-like protein; Provisional
417-627 3.55e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  417 DVNVRGPDGYTPLMIASCSgggletgnseeeEDASANVINDFIYQGANLhNQTDRTGETALHLAARYARSDAA--KRLLE 494
Cdd:PHA03095   109 DVNAKDKVGRTPLHVYLSG------------FNINPKVIRLLLRKGADV-NALDLYGMTPLAVLLKSRNANVEllRLLID 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  495 ASADANIQDNMGRTPLH--AAVAADAQGVFQILIRnRATDLDARMHDGTTPLILAARLAV--EGMVEELINCHADVNAID 570
Cdd:PHA03095   176 AGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIR-AGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARN 254
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1074286255  571 DFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLE 627
Cdd:PHA03095   255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA03100 PHA03100
ankyrin repeat protein; Provisional
477-657 1.95e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  477 LHLAARYARSDAAKRLLEASADANIQDNMGRTPLH-----AAVAADAQGVFQILIRNRAtDLDARMHDGTTPLILAARLA 551
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAISKK 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  552 VEG--MVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIV------------------LLKNGANKDMQNNKEETPLF 611
Cdd:PHA03100   118 SNSysIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPINIKDVYGFTPLH 197
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1074286255  612 LAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRL 657
Cdd:PHA03100   198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
Ank_5 pfam13857
Ankyrin repeats (many copies);
462-513 2.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.81e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1074286255  462 GANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAA 513
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
416-688 3.79e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 3.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  416 MDVNVRGPDGYTPLMIAScsGGGLETGNseeeedasanvINDFIYQGANLhNQTDRTGETALHLAARYAR-SDAAKRLLE 494
Cdd:PHA02876   298 ADVNAKNIKGETPLYLMA--KNGYDTEN-----------IRTLIMLGADV-NAADRLYITPLHQASTLDRnKDIVITLLE 363
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  495 ASADANIQDNMGRTPLHAAVAADAqgvfqILIRNRATDLDARMHDGTTPLILAARLAVEGM-----VEELINCHADVNAI 569
Cdd:PHA02876   364 LGANVNARDYCDKTPIHYAAVRNN-----VVIINTLLDYGADIEALSQKIGTALHFALCGTnpymsVKTLIDRGANVNSK 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  570 DDFGKSALHWAAAVNNVEAAI-VLLKNGANKDMQNNKEETPLFLAAreGSYETAKVLLEHFA--------NREITDHMDR 640
Cdd:PHA02876   439 NKDLSTPLHYACKKNCKLDVIeMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAelrdsrvlHKSLNDNMFS 516
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1074286255  641 LPRDIA----QERMHHDIvrlMDEYNLVRSPPMHGGSLSTTLSPPLCSPSGF 688
Cdd:PHA02876   517 FRYIIAhiciQDFIRHDI---RNEVNPLKRVPTRFTSLRESFKEIIQSDDTF 565
PHA02875 PHA02875
ankyrin repeat protein; Provisional
467-658 4.27e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 4.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  467 NQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVA-ADAQGVFQILIRNRATDlDARMHDGTTPLI 545
Cdd:PHA02875    29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEeGDVKAVEELLDLGKFAD-DVFYKDGMTPLH 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  546 LAARLAVEGMVEELINCHA--DVNAIDDFgkSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLAAREGSYETAK 623
Cdd:PHA02875   108 LATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1074286255  624 VLLEHFANreiTDHMDRLPrDI-----AQERMHHDIVRLM 658
Cdd:PHA02875   186 MLLDSGAN---IDYFGKNG-CVaalcyAIENNKIDIVRLF 221
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
469-607 1.17e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  469 TDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIR-NRATDldarMHDGTTPLILA 547
Cdd:PLN03192   554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfASISD----PHAAGDLLCTA 629
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  548 ARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEE 607
Cdd:PLN03192   630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
Ank_2 pfam12796
Ankyrin repeats (3 copies);
411-503 2.13e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 2.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  411 IENDCmDVNVRGPDGYTPLMIASCSGggletgnseeeedaSANVInDFIYQGANLHNQTDrtGETALHLAARYARSDAAK 490
Cdd:pfam12796   17 LENGA-DANLQDKNGRTALHLAAKNG--------------HLEIV-KLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1074286255  491 RLLEASADANIQD 503
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
592-657 1.01e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 1.01e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1074286255  592 LLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLEHFANREITDhmDRLPRDIAQERMHHDIVRL 657
Cdd:pfam12796   16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKL 79
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
1-24 1.16e-07

LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch related proteins. The structure of the domain has been determined by NMR and was shown to contain three disulphide bonds and coordinate a calcium ion. Three repeats are also found in the PAPP-A peptidase.


Pssm-ID: 459658  Cd Length: 35  Bit Score: 48.68  E-value: 1.16e-07
                           10        20
                   ....*....|....*....|....
gi 1074286255    1 HKHNKYCDVLCNNHACGWDNGDCS 24
Cdd:pfam00066   12 KFGNGVCDEECNNAECLWDGGDCS 35
PHA03100 PHA03100
ankyrin repeat protein; Provisional
453-531 1.72e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.06  E-value: 1.72e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1074286255  453 NVINDFIYQGANLhNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRAT 531
Cdd:PHA03100   173 NRVNYLLSYGVPI-NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
417-642 3.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 3.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  417 DVNVRGPDGYTPLMIASCSGggletgnseeeedaSANVINDFIYQGANLhNQTDRTGETALHLAARYARSDAAKRLLEAS 496
Cdd:PHA02874   149 DVNIEDDNGCYPIHIAIKHN--------------FFDIIKLLLEKGAYA-NVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  497 ADANIQDNMGRTPLHAAVAADaQGVFQILIRNRA-TDLDArmhDGTTPLILAarlavegmveelINCHADVNAIDdfgks 575
Cdd:PHA02874   214 NHIMNKCKNGFTPLHNAIIHN-RSAIELLINNASiNDQDI---DGSTPLHHA------------INPPCDIDIID----- 272
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1074286255  576 alhwaaavnnveaaiVLLKNGANKDMQNNKEETPLFLAARegSYETAKVLLEHFANREITDHMDRLP 642
Cdd:PHA02874   273 ---------------ILLYHKADISIKDNKGENPIDTAFK--YINKDPVIKDIIANAVLIKEADKLK 322
Ank_4 pfam13637
Ankyrin repeats (many copies);
475-526 4.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.39e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1074286255  475 TALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILI 526
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
473-640 4.47e-07

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: 53.99  E-value: 4.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  473 GETALHLAARYARSDAAKRLLEASADANIQdnmgrtplhaavaadAQGVFqilirNRATDLDARMHDGTTPLILAARLAV 552
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAH---------------AKGVF-----FNPKYKHEGFYFGETPLALAACTNQ 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  553 EGMVEELI-NCHADVNAIDDFGKSALHW----AAAVNNVEAAIV-----LLKNGANKD---MQNNKEETPLFLAAREGSY 619
Cdd:cd22194    201 PEIVQLLMeKESTDITSQDSRGNTVLHAlvtvAEDSKTQNDFVKrmydmILLKSENKNletIRNNEGLTPLQLAAKMGKA 280
                          170       180
                   ....*....|....*....|.
gi 1074286255  620 EtakvLLEHFANREITDHMDR 640
Cdd:cd22194    281 E----ILKYILSREIKEKPNR 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
455-642 4.60e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 4.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  455 INDFIYQGANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRATdld 534
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--- 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  535 arMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAI-VLLKNGANKDMQNNKEETPLFLA 613
Cdd:PHA02876   237 --INKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKGETPLYLM 314
                          170       180       190
                   ....*....|....*....|....*....|
gi 1074286255  614 AREG-SYETAKVLLEHFANREITDHMDRLP 642
Cdd:PHA02876   315 AKNGyDTENIRTLIMLGADVNAADRLYITP 344
PHA02876 PHA02876
ankyrin repeat protein; Provisional
492-633 4.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 4.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  492 LLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGM-VEELINCHADVNAID 570
Cdd:PHA02876   259 LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAAD 338
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1074286255  571 DFGKSALHWAAAVNNVEAAIV-LLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLEHFANRE 633
Cdd:PHA02876   339 RLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
1-23 5.38e-07

Domain found in Notch and Lin-12; The Notch protein is essential for the proper differentiation of the Drosophila ectoderm. This protein contains 3 NL domains.


Pssm-ID: 197463  Cd Length: 38  Bit Score: 46.94  E-value: 5.38e-07
                            10        20
                    ....*....|....*....|...
gi 1074286255     1 HKHNKYCDVLCNNHACGWDNGDC 23
Cdd:smart00004   16 KFGDGVCDEECNNAECLWDGGDC 38
PHA03100 PHA03100
ankyrin repeat protein; Provisional
417-628 9.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 9.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  417 DVNVRGPDGYTPLMIASCsgggletgnseeEEDASANVINDFIYQGANLhNQTDRTGETALHLAARYARSDA--AKRLLE 494
Cdd:PHA03100    98 NVNAPDNNGITPLLYAIS------------KKSNSYSIVEYLLDNGANV-NIKNSDGENLLHLYLESNKIDLkiLKLLID 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  495 ASADANIQDNMgrtplhaavaadaqgvfQILIRNrATDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGK 574
Cdd:PHA03100   165 KGVDINAKNRV-----------------NYLLSY-GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1074286255  575 SALHWAAAVNNVEAAIVLLKNGANKDMqnnKEETPLFLAAREGSYETAKVLLEH 628
Cdd:PHA03100   227 TPLHIAILNNNKEIFKLLLNNGPSIKT---IIETLLYFKDKDLNTITKIKMLKK 277
PHA03100 PHA03100
ankyrin repeat protein; Provisional
447-640 1.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  447 EEDASANVINDFIYQGANLhNQTDRTGETALHLAARYARS-----DAAKRLLEASADANIQDNMGRTPLHAAVAADAQGV 521
Cdd:PHA03100    43 KEARNIDVVKILLDNGADI-NSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSY 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  522 FQI-LIRNRATDLDARMHDGTTPLilaaRLAVEG------MVEELINCHADVNAI----------------DDFGKSALH 578
Cdd:PHA03100   122 SIVeYLLDNGANVNIKNSDGENLL----HLYLESnkidlkILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLH 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1074286255  579 WAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLEHFANreiTDHMDR 640
Cdd:PHA03100   198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS---IKTIIE 256
JMTM_dNotch cd21706
juxtamembrane and transmembrane (JMTM) domain found in Drosophila melanogaster neurogenic ...
259-327 3.62e-06

juxtamembrane and transmembrane (JMTM) domain found in Drosophila melanogaster neurogenic locus Notch protein (dNotch) and similar proteins; Drosophila melanogaster neurogenic locus Notch protein (dNotch) is an essential signaling protein which has a major role in many developmental processes. It functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination. It regulates oogenesis, the differentiation of the ectoderm and the development of the central and peripheral nervous system, eye, wing disk, muscles and segmental appendages such as antennae and legs, through lateral inhibition or induction. It also regulates neuroblast self-renewal, identity and proliferation through the regulation of bHLH-O proteins; in larval brains, it is involved in the maintenance of type II neuroblast self-renewal and identity by suppressing erm expression together with pnt. It might also regulate dpn expression through the activation of the transcriptional regulator Su(H). This model corresponds to the juxtamembrane and transmembrane (JMTM) domain of dNotch, which comprises an extended coil, a transmembrane helix (TM), and a beta-strand.


Pssm-ID: 411989  Cd Length: 90  Bit Score: 46.10  E-value: 3.62e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1074286255  259 PFTIEAVYSGVDLQSTDNGLYP--IYLVLGGVGIL---AFLGVGMVAARKRrhEHGRLWLPEGFKTTETSKKKR 327
Cdd:cd21706      1 DFPIYQVRGEDPPDPPPEPPPSnlTYVVIGVVVVLligLLLGVLVTTQRKR--ARGITWFPEGFFTTSSSQRRR 72
PHA02874 PHA02874
ankyrin repeat protein; Provisional
487-631 4.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 4.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  487 DAAKRLLEASADANIQDNMGRTPLHAAVaadaqgvfqilirnRATDLDArmhdgttplilaarlavegmVEELINCHADV 566
Cdd:PHA02874   105 DMIKTILDCGIDVNIKDAELKTFLHYAI--------------KKGDLES--------------------IKMLFEYGADV 150
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1074286255  567 NAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLEHFAN 631
Cdd:PHA02874   151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH 215
PHA02874 PHA02874
ankyrin repeat protein; Provisional
523-660 1.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  523 QILIRNRATDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGA----- 597
Cdd:PHA02874    18 EKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsil 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  598 -----NKDM-------------QNNKEETPLFLAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRLMD 659
Cdd:PHA02874    98 pipciEKDMiktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                   .
gi 1074286255  660 E 660
Cdd:PHA02874   178 E 178
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
472-647 2.93e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 47.95  E-value: 2.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  472 TGETALHLAARY---ARSDAAKRLLEASADANIQDNM-----------GRTPLHAAVAADAQGVFQILIRNRAtDLDAR- 536
Cdd:cd21882     25 TGKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGA-DVSARa 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  537 ------------MHDGTTPLILAARLAVEGMVEELINCHADVNAI---DDFGKSALH---WAAAVNNVEAAIV------L 592
Cdd:cd21882    104 tgrffrkspgnlFYFGELPLSLAACTNQEEIVRLLLENGAQPAALeaqDSLGNTVLHalvLQADNTPENSAFVcqmynlL 183
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1074286255  593 LKNGANKD-------MQNNKEETPLFLAAREGSYetakVLLEHFANREITDHMDRLPRDIAQ 647
Cdd:cd21882    184 LSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKI----VMFQHILQREFSGPYQPLSRKFTE 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
492-547 4.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1074286255  492 LLEA-SADANIQDNMGRTPLHAAVAADAQGVFQILIRNRAtDLDARMHDGTTPLILA 547
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
467-631 1.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  467 NQTDRTGETALHLAARY-ARSDAAKRLLEASADANIQDNMGRTPLH--AAVAADAQGVFQILIRNRATDLDARMHDgtTP 543
Cdd:PHA02876   267 NSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYlmAKNGYDTENIRTLIMLGADVNAADRLYI--TP 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  544 LILAARL-AVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPL-FLAAREGSYET 621
Cdd:PHA02876   345 LHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMS 424
                          170
                   ....*....|
gi 1074286255  622 AKVLLEHFAN 631
Cdd:PHA02876   425 VKTLIDRGAN 434
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
591-692 1.44e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  591 VLLKNGANKDMQNNKEETPLFLAAREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRLMDEYNL------V 664
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQchfelgA 179
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1074286255  665 RSPPMH-GGSLSTTLSPPLCS--------PSGFLGSM 692
Cdd:PTZ00322   180 NAKPDSfTGKPPSLEDSPISShhpdfsavPQPMMGSL 216
PHA02874 PHA02874
ankyrin repeat protein; Provisional
454-658 1.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  454 VINDFIYQGANLHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNratdl 533
Cdd:PHA02874    16 AIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN----- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  534 darmhdGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETPLFLA 613
Cdd:PHA02874    91 ------GVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1074286255  614 AREGSYETAKVLLEHFANREITDHMDRLPRDIAQERMHHDIVRLM 658
Cdd:PHA02874   165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
467-535 2.07e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 2.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1074286255  467 NQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAVAADAQGVFQILIRNRATDLDA 535
Cdd:PTZ00322   109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
PHA03100 PHA03100
ankyrin repeat protein; Provisional
526-631 2.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  526 IRNRATDLDARMHDGTTPLILAARLAVEGMVEELINCHADVNAIDDFGKSALHWAAAVNNVEAAI-----VLLKNGANKD 600
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVkeivkLLLEYGANVN 100
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1074286255  601 MQNNKEETPLFLAARE--GSYETAKVLLEHFAN 631
Cdd:PHA03100   101 APDNNGITPLLYAISKksNSYSIVEYLLDNGAN 133
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
473-501 3.08e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 3.08e-04
                           10        20
                   ....*....|....*....|....*....
gi 1074286255  473 GETALHLAARYARSDAAKRLLEASADANI 501
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
473-504 3.09e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 3.09e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1074286255  473 GETALHLAA-RYARSDAAKRLLEASADANIQDN 504
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
454-661 3.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.49  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  454 VINDFIYQGANLhNQTDRTGETALHLAARYARSDAAKRLLEASadanIQDNMGRTPLHAAVAADAQGV--FQILIRNRAT 531
Cdd:PHA02878    52 VVKSLLTRGHNV-NQPDHRDLTPLHIICKEPNKLGMKEMIRSI----NKCSVFYTLVAIKDAFNNRNVeiFKIILTNRYK 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  532 DLdaRMHDGTTPLILAARLAVEGMVEELINCH-ADVNAID-DFGKSALHWAAAVNNVEAAIVLLKNGANKDMQNNKEETP 609
Cdd:PHA02878   127 NI--QTIDLVYIDKKSKDDIIEAEITKLLLSYgADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1074286255  610 LFLAAREGSYETAKVLLEHFANreiTDHMDR---LPRDIAQER-MHHDIVRLMDEY 661
Cdd:PHA02878   205 LHHAVKHYNKPIVHILLENGAS---TDARDKcgnTPLHISVGYcKDYDILKLLLEH 257
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
473-646 3.98e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.40  E-value: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  473 GETALHLAARYARSDAAKRLLEASADANIQDN--------------MGRTPLHAAVAADAQGVFQILIRNRATDLDARMH 538
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  539 DGTTPLILAARLAVegmveelinchADvNAID--DFGKSALHwaaavnnveaaiVLLKNGAN-------KDMQNNKEETP 609
Cdd:cd22193    156 DSRGNTVLHALVTV-----------AD-NTKEntKFVTRMYD------------MILIRGAKlcptvelEEIRNNDGLTP 211
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1074286255  610 LFLAAREGSYEtakvLLEHFANREITD----HMDRLPRDIA 646
Cdd:cd22193    212 LQLAAKMGKIE----ILKYILQREIKEpelrHLSRKFTDWA 248
PHA02946 PHA02946
ankyin-like protein; Provisional
423-578 1.55e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  423 PDGYTPLMIASCSGGGLETGNSEEeedasanvindFIYQGANlHNQTDRTGETALHLAARYARSDAAKRLLEASADANIQ 502
Cdd:PHA02946    34 PSGNYHILHAYCGIKGLDERFVEE-----------LLHRGYS-PNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNAC 101
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1074286255  503 DNMGRTPLHAAVAADAQGVFQI--LIRNRATDLDARMHDGTTPLiLAARLAVEGMVEELINCHADVNAIDDFGKSALH 578
Cdd:PHA02946   102 DKQHKTPLYYLSGTDDEVIERInlLVQYGAKINNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
539-571 4.23e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 4.23e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1074286255  539 DGTTPLILAA-RLAVEGMVEELINCHADVNAIDD 571
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02917 PHA02917
ankyrin-like protein; Provisional
467-514 6.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 40.75  E-value: 6.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1074286255  467 NQTDRTGETALHLAARYARSDAAKRLLEASADANIQDNMGRTPLHAAV 514
Cdd:PHA02917   446 NMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAI 493
PHA02736 PHA02736
Viral ankyrin protein; Provisional
453-547 6.52e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 6.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1074286255  453 NVINDfiyQGANLHNQTDRTGETALHLAARYARSD---AAKRLLEASADANIQDNM-GRTPLHAAVAADAQGVFQILIRN 528
Cdd:PHA02736    38 NAISD---ENRYLVLEYNRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQ 114
                           90
                   ....*....|....*....
gi 1074286255  529 RATDLDARMHDGTTPLILA 547
Cdd:PHA02736   115 PGVNMEILNYAFKTPYYVA 133
 
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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