NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|284449631|emb|CBJ20653|]
View 

unnamed protein product, partial [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
JMTM_Notch1 cd21702
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
267-346 4.91e-49

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: 168.05  E-value: 4.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  267 AVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKN 346
Cdd:cd21702     1 AVKSETVEPPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPSKKKRREPVGEDSVGLKPLKN 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
451-665 5.76e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 5.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  451 EDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRN 530
Cdd:COG0666    63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  531 RAtDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREET 610
Cdd:COG0666   143 GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 284449631  611 PLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNL 665
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
113-168 2.78e-29

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: 110.68  E-value: 2.78e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 284449631   113 PERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYG 168
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGNPMIYPWYG 56
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
218-276 3.01e-25

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: 99.27  E-value: 3.01e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 284449631   218 VRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPP 276
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPPPP 59
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
34-69 6.03e-16

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: 72.18  E-value: 6.03e-16
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 284449631    34 WKNCTQSlQCWKYFSDGHCDSQCNSAGCLFDGFDCQ 69
Cdd:pfam00066    1 WPNCPYP-YCWDKFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
68-108 2.52e-14

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: 67.74  E-value: 2.52e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 284449631     68 CQRAEGQCNplyDQYCKDHFSDGHCDQGCNSAECEWDGLDC 108
Cdd:smart00004    1 PQDPWSRCE---DAQCWDKFGDGVCDEECNNAECLWDGGDC 38
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
1-26 2.54e-10

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: 56.18  E-value: 2.54e-10
                            10        20
                    ....*....|....*....|....*.
gi 284449631      1 CQEDAGNKVCSLQCNNHACGWDGGDC 26
Cdd:smart00004   13 CWDKFGDGVCDEECNNAECLWDGGDC 38
 
Name Accession Description Interval E-value
JMTM_Notch1 cd21702
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
267-346 4.91e-49

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: 168.05  E-value: 4.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  267 AVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKN 346
Cdd:cd21702     1 AVKSETVEPPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPSKKKRREPVGEDSVGLKPLKN 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
451-665 5.76e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 5.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  451 EDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRN 530
Cdd:COG0666    63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  531 RAtDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREET 610
Cdd:COG0666   143 GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 284449631  611 PLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNL 665
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
113-168 2.78e-29

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: 110.68  E-value: 2.78e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 284449631   113 PERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYG 168
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGNPMIYPWYG 56
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
218-276 3.01e-25

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: 99.27  E-value: 3.01e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 284449631   218 VRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPP 276
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPPPP 59
Ank_2 pfam12796
Ankyrin repeats (3 copies);
479-572 3.71e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 3.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631   479 LHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDarmHDGTTPLILAARLAVEGML 558
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 284449631   559 EDLINSHADVNAVD 572
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
34-69 6.03e-16

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: 72.18  E-value: 6.03e-16
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 284449631    34 WKNCTQSlQCWKYFSDGHCDSQCNSAGCLFDGFDCQ 69
Cdd:pfam00066    1 WPNCPYP-YCWDKFGNGVCDEECNNAECLWDGGDCS 35
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
32-68 1.45e-14

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: 68.51  E-value: 1.45e-14
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 284449631     32 DPWKNCtQSLQCWKYFSDGHCDSQCNSAGCLFDGFDC 68
Cdd:smart00004    3 DPWSRC-EDAQCWDKFGDGVCDEECNNAECLWDGGDC 38
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
68-108 2.52e-14

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: 67.74  E-value: 2.52e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 284449631     68 CQRAEGQCNplyDQYCKDHFSDGHCDQGCNSAECEWDGLDC 108
Cdd:smart00004    1 PQDPWSRCE---DAQCWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
72-108 9.06e-14

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: 66.01  E-value: 9.06e-14
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 284449631    72 EGQCNPlydQYCKDHFSDGHCDQGCNSAECEWDGLDC 108
Cdd:pfam00066    1 WPNCPY---PYCWDKFGNGVCDEECNNAECLWDGGDC 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
464-636 6.46e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 6.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  464 GASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATdLDARMHDGT 543
Cdd:PHA02878  157 GADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCGN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  544 TPL-ILAARLAVEGMLEDLINSHADVNAVDD-LGKSALHwaAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGS- 620
Cdd:PHA02878  236 TPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLc 313
                         170       180
                  ....*....|....*....|.
gi 284449631  621 YETAKVLLDH-----FANRDI 636
Cdd:PHA02878  314 INIGRILISNicllkRIKPDI 334
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
1-26 2.54e-10

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: 56.18  E-value: 2.54e-10
                            10        20
                    ....*....|....*....|....*.
gi 284449631      1 CQEDAGNKVCSLQCNNHACGWDGGDC 26
Cdd:smart00004   13 CWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
1-27 2.92e-10

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: 56.00  E-value: 2.92e-10
                           10        20
                   ....*....|....*....|....*..
gi 284449631     1 CQEDAGNKVCSLQCNNHACGWDGGDCS 27
Cdd:pfam00066    9 CWDKFGNGVCDEECNNAECLWDGGDCS 35
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
475-619 5.08e-10

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: 63.49  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  475 GETALHLAARYSRSDAAKRLLEASADAnIQDNM------GRTPLHAAVSADAQGVFQILIRNRATDLDAR---------- 538
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgp 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  539 ---MHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVV----LLKNGANKD------MQN 605
Cdd:cd22192   130 knlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQmydlILSYDKEDDlqpldlVPN 209
                         170
                  ....*....|....
gi 284449631  606 NREETPLFLAAREG 619
Cdd:cd22192   210 NQGLTPFKLAAKEG 223
 
Name Accession Description Interval E-value
JMTM_Notch1 cd21702
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
267-346 4.91e-49

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: 168.05  E-value: 4.91e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  267 AVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKN 346
Cdd:cd21702     1 AVKSETVEPPPPSQLYPMYVVLAALVLLAFVGVGVLVSRKRRREHGQLWFPEGFKVSEPSKKKRREPVGEDSVGLKPLKN 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
451-665 5.76e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 5.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  451 EDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRN 530
Cdd:COG0666    63 LAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  531 RAtDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREET 610
Cdd:COG0666   143 GA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 284449631  611 PLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNL 665
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
464-665 1.44e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 1.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  464 GASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRAtDLDARMHDGT 543
Cdd:COG0666    43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  544 TPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYET 623
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 284449631  624 AKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNL 665
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-639 2.80e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  420 DVNVRGPDGFTPLMIASCSGggletgnseeeedAPAVISDFIYQGASLhNQTDRTGETALHLAARYSRSDAAKRLLEASA 499
Cdd:COG0666    79 DINAKDDGGNTLLHAAARNG-------------DLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  500 DANIQDNMGRTPLHAAVSADAQGVFQILIRNRAtDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSAL 579
Cdd:COG0666   145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  580 HWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDH 639
Cdd:COG0666   224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-612 2.90e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  420 DVNVRGPDGFTPLMIASCSGggletgnseeeedAPAVISDFIYQGASLhNQTDRTGETALHLAARYSRSDAAKRLLEASA 499
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADV-NAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  500 DANIQDNMGRTPLHAAVSADAQGVFQILIRNRAtDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSAL 579
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGA-DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
                         170       180       190
                  ....*....|....*....|....*....|...
gi 284449631  580 HWAAAVNNVDAAVVLLKNGANKDMQNNREETPL 612
Cdd:COG0666   257 LLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
NOD pfam06816
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
113-168 2.78e-29

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: 110.68  E-value: 2.78e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 284449631   113 PERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYG 168
Cdd:pfam06816    1 PEKLAEGVLVIVVLMDPEELLNNSVQFLRELSTVLRTNVRFKKDENGNPMIYPWYG 56
JMTM_Notch cd21701
juxtamembrane and transmembrane (JMTM) domain found in Notch protein family; Neurogenic locus ...
262-344 1.48e-28

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: 109.78  E-value: 1.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  262 PYKIEAVQSET--VEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRqHGQLWFPEGFKVSEASK-KKRREPLGEDS 338
Cdd:cd21701     1 PYPIYSVRSEPgpATKTTPPAQLSPLVVAAVCVLLVLVVLGVLVARKRRR-HGTLWFPEGFPRTRASRrSRRRDPVGQDS 79

                  ....*.
gi 284449631  339 VGLKPL 344
Cdd:cd21701    80 VGLKNL 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
455-660 1.36e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  455 AVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRAtD 534
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  535 LDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFL 614
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 284449631  615 AAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLL 660
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
NODP pfam07684
NOTCH protein; NOTCH signalling plays a fundamental role during a great number of ...
218-276 3.01e-25

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: 99.27  E-value: 3.01e-25
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 284449631   218 VRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPP 276
Cdd:pfam07684    1 VIGSVVYLEIDNRKCSQSSDECFSTAQSAADFLAALAAKGGLDLPYPIKEVRSEPPPPP 59
JMTM_Notch2 cd21703
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
261-344 1.93e-22

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: 92.13  E-value: 1.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  261 IPYKIEAVQSEtvePPPPAQLHFMY-VAAAAFVLLFFVGCGVLLSrKRRRQHGQLWFPEGFKVS-EASKKKRREPLGEDS 338
Cdd:cd21703     1 LPYPLVSVTSE---PLKETKFNLLYlLAVAVAIILLILLLGVLVA-KRKRKHGPLWFPEGFILNkENSNRKRREPVGQDA 76

                  ....*.
gi 284449631  339 VGLKPL 344
Cdd:cd21703    77 VGMKNL 82
JMTM_Notch3 cd21704
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
259-342 6.32e-21

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: 88.27  E-value: 6.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  259 LNIPYKIEAVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRkRRRQHGQLWFPEGFKV-SEASKKKRREPLGED 337
Cdd:cd21704     3 LEFPYPIKEVRGEKLEPPPPPVRLLPLLGVAAVILLVILVLGVLVAR-RKREHSTLWFPEGFFLkKESSNKNRREPVGQD 81

                  ....*
gi 284449631  338 SVGLK 342
Cdd:cd21704    82 ALGMK 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
479-572 3.71e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 3.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631   479 LHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDarmHDGTTPLILAARLAVEGML 558
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 284449631   559 EDLINSHADVNAVD 572
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
34-69 6.03e-16

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: 72.18  E-value: 6.03e-16
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 284449631    34 WKNCTQSlQCWKYFSDGHCDSQCNSAGCLFDGFDCQ 69
Cdd:pfam00066    1 WPNCPYP-YCWDKFGNGVCDEECNNAECLWDGGDCS 35
JMTM_Notch4 cd21705
juxtamembrane and transmembrane (JMTM) domain found in neurogenic locus notch homolog protein ...
261-345 7.49e-16

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: 73.97  E-value: 7.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  261 IPYKIEAVQSETVEPPPPAQL-----HFMYVAAAAFVLLFF-VGCGVLLSRKRRRQHGQLWFPEGFKVSEASK-KKRREP 333
Cdd:cd21705     1 LPFPLLAVTVEEAEKDPQLVAaqlpwPLVCSSVAGVLALVLgALLGVQLIRRRQREHGALWLPPGFARHRDPNpHRRREP 80
                          90
                  ....*....|..
gi 284449631  334 LGEDSVGLKPLK 345
Cdd:cd21705    81 VGEDAIGLKPLK 92
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
32-68 1.45e-14

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: 68.51  E-value: 1.45e-14
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 284449631     32 DPWKNCtQSLQCWKYFSDGHCDSQCNSAGCLFDGFDC 68
Cdd:smart00004    3 DPWSRC-EDAQCWDKFGDGVCDEECNNAECLWDGGDC 38
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
68-108 2.52e-14

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: 67.74  E-value: 2.52e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 284449631     68 CQRAEGQCNplyDQYCKDHFSDGHCDQGCNSAECEWDGLDC 108
Cdd:smart00004    1 PQDPWSRCE---DAQCWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
72-108 9.06e-14

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: 66.01  E-value: 9.06e-14
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 284449631    72 EGQCNPlydQYCKDHFSDGHCDQGCNSAECEWDGLDC 108
Cdd:pfam00066    1 WPNCPY---PYCWDKFGNGVCDEECNNAECLWDGGDC 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
464-636 6.46e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 6.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  464 GASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATdLDARMHDGT 543
Cdd:PHA02878  157 GADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS-TDARDKCGN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  544 TPL-ILAARLAVEGMLEDLINSHADVNAVDD-LGKSALHwaAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGS- 620
Cdd:PHA02878  236 TPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLc 313
                         170       180
                  ....*....|....*....|.
gi 284449631  621 YETAKVLLDH-----FANRDI 636
Cdd:PHA02878  314 INIGRILISNicllkRIKPDI 334
JMTM_dNotch cd21706
juxtamembrane and transmembrane (JMTM) domain found in Drosophila melanogaster neurogenic ...
263-331 7.89e-12

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: 62.28  E-value: 7.89e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  263 YKIEAVQSETVEPPPPAQlHFMYVAAAAFVLLFFVGC-GVLLSRKRRRQHGQLWFPEGFKVSEASKKKRR 331
Cdd:cd21706     5 YQVRGEDPPDPPPEPPPS-NLTYVVIGVVVVLLIGLLlGVLVTTQRKRARGITWFPEGFFTTSSSQRRRR 73
PHA03095 PHA03095
ankyrin-like protein; Provisional
420-628 1.70e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  420 DVNVRGPDGFTPLMIASCsggGLETgnseeeedAPAVISDFIYQGASLhNQTDRTGETALHLAARYSRSDAA--KRLLEA 497
Cdd:PHA03095  109 DVNAKDKVGRTPLHVYLS---GFNI--------NPKVIRLLLRKGADV-NALDLYGMTPLAVLLKSRNANVEllRLLIDA 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  498 SADANIQDNMGRTPLHA-AVSADA-QGVFQILIRnRATDLDARMHDGTTPLILAARLAV--EGMLEDLINSHADVNAVDD 573
Cdd:PHA03095  177 GADVYAVDDRFRSLLHHhLQSFKPrARIVRELIR-AGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNR 255
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 284449631  574 LGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLL 628
Cdd:PHA03095  256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
420-580 5.32e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  420 DVNVRGPDGFTPL-MIASCSGggletgnseeeEDAPAVISDFIYQGASLhNQTDRTGETALHLAARYS-RSDAAKRLLEA 497
Cdd:PHA03095   39 DVNFRGEYGKTPLhLYLHYSS-----------EKVKDIVRLLLEAGADV-NAPERCGFTPLHLYLYNAtTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  498 SADANIQDNMGRTPLHAAVSADA--QGVFQILIRNRAtDLDARMHDGTTPL---ILAARLAVEgMLEDLINSHADVNAVD 572
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGA-DVNALDLYGMTPLavlLKSRNANVE-LLRLLIDAGADVYAVD 184

                  ....*...
gi 284449631  573 DLGKSALH 580
Cdd:PHA03095  185 DRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
546-638 8.12e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 8.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631   546 LILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNgANKDMQNNReETPLFLAAREGSYETAK 625
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 284449631   626 VLLDHFANRDITD 638
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
469-660 1.78e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  469 NQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAV-SADAQGVFQILIRNRATDlDARMHDGTTPLI 547
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeEGDVKAVEELLDLGKFAD-DVFYKDGMTPLH 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  548 LAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVL 627
Cdd:PHA02875  108 LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 284449631  628 LDHFANrdiTDHMDRLPrDI-----AQERMHHDIVRLL 660
Cdd:PHA02875  188 LDSGAN---IDYFGKNG-CVaalcyAIENNKIDIVRLF 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
461-633 2.07e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  461 IYQGASLhNQTDRTGETALHLAARYS---RSDAAKRLLEASADANIQDNMGRTPLHAAV-SADAQGVFQILIRNRAtDLD 536
Cdd:PHA03095   34 LAAGADV-NFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIKAGA-DVN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  537 ARMHDGTTPL--ILAARLAVEGMLEDLINSHADVNAVDDLGKSALHwaaavnnvdaavVLLKN-GANKDMQNnreetpLF 613
Cdd:PHA03095  112 AKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSrNANVELLR------LL 173
                         170       180
                  ....*....|....*....|....*
gi 284449631  614 LAAreGSYETAK-----VLLDHFAN 633
Cdd:PHA03095  174 IDA--GADVYAVddrfrSLLHHHLQ 196
NL smart00004
Domain found in Notch and Lin-12; The Notch protein is essential for the proper ...
1-26 2.54e-10

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: 56.18  E-value: 2.54e-10
                            10        20
                    ....*....|....*....|....*.
gi 284449631      1 CQEDAGNKVCSLQCNNHACGWDGGDC 26
Cdd:smart00004   13 CWDKFGDGVCDEECNNAECLWDGGDC 38
Notch pfam00066
LNR domain; The LNR (Lin-12/Notch repeat) domain is found in three tandem copies in Notch ...
1-27 2.92e-10

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: 56.00  E-value: 2.92e-10
                           10        20
                   ....*....|....*....|....*..
gi 284449631     1 CQEDAGNKVCSLQCNNHACGWDGGDCS 27
Cdd:pfam00066    9 CWDKFGNGVCDEECNNAECLWDGGDCS 35
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
475-619 5.08e-10

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: 63.49  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  475 GETALHLAARYSRSDAAKRLLEASADAnIQDNM------GRTPLHAAVSADAQGVFQILIRNRATDLDAR---------- 538
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPEL-VNEPMtsdlyqGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgp 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  539 ---MHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVV----LLKNGANKD------MQN 605
Cdd:cd22192   130 knlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQmydlILSYDKEDDlqpldlVPN 209
                         170
                  ....*....|....
gi 284449631  606 NREETPLFLAAREG 619
Cdd:cd22192   210 NQGLTPFKLAAKEG 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
492-633 8.52e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 8.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  492 KRLLEASADANIQDNMGRTPLHAAV---SADAQGVFQILIRNRAtDLDARMHDGTTPLILAARLA-VEGMLEDLINSHAD 567
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGAD 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  568 VNAVDDLGKSALH--WAAAVNNVDAAVVLLKNGANKDMQNNREETPL--FLAAREGSYETAKVLLDHFAN 633
Cdd:PHA03095  110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGAD 179
PHA02876 PHA02876
ankyrin repeat protein; Provisional
469-663 1.51e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  469 NQTDRTGETALHLAARYS-RSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLI 547
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIH 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  548 LAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNV-DAAVVLLKNGANKDMQNNREETPLFLAAREG-SYETAK 625
Cdd:PHA02876  381 YAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIE 460
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 284449631  626 VLLDHFANRDITDHMDRLPRDIAQErmHHDIVRLLDEY 663
Cdd:PHA02876  461 MLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHY 496
Ank_5 pfam13857
Ankyrin repeats (many copies);
464-515 5.84e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 5.84e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 284449631   464 GASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAA 515
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
594-660 7.28e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 7.28e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 284449631   594 LLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHfANRDITDHmDRLPRDIAQERMHHDIVRLL 660
Cdd:pfam12796   16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
471-609 1.21e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  471 TDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIR-NRATDldarMHDGTTPLILA 549
Cdd:PLN03192  554 GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfASISD----PHAAGDLLCTA 629
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  550 ARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREE 609
Cdd:PLN03192  630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA03100 PHA03100
ankyrin repeat protein; Provisional
479-660 1.55e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  479 LHLAARYSRSDAAKRLLEASADANIQDNMGRTPLH-----AAVSADAQGVFQILIRNRAtDLDARMHDGTTPLILAARLA 553
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGA-NVNAPDNNGITPLLYAISKK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  554 VEG--MLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAA------------------VVLLKNGANKDMQNNREETPLF 613
Cdd:PHA03100  118 SNSysIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKilkllidkgvdinaknrvNYLLSYGVPINIKDVYGFTPLH 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 284449631  614 LAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLL 660
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
420-505 2.91e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631   420 DVNVRGPDGFTPLMIAsCSGGGLEtgnseeeedapavISDFIYQGASLHNQTDrtGETALHLAARYSRSDAAKRLLEASA 499
Cdd:pfam12796   22 DANLQDKNGRTALHLA-AKNGHLE-------------IVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLEKGA 85

                   ....*.
gi 284449631   500 DANIQD 505
Cdd:pfam12796   86 DINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
469-657 1.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  469 NQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATdLDARMHDGTTPLIL 548
Cdd:PHA02874  118 NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHN 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  549 AARLAVEGMLEDLINSHADVNAVDDLGKSALHwaAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAR-EGSYETAKVL 627
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDIL 274
                         170       180       190
                  ....*....|....*....|....*....|
gi 284449631  628 LDHFANRDITDHMDRLPRDIAQERMHHDIV 657
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFKYINKDPV 304
PHA02876 PHA02876
ankyrin repeat protein; Provisional
457-661 2.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  457 ISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATdld 536
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--- 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  537 arMHDGTTPLILAAR---LAVEGMLEDlinSHADVNAVDDLGKSALHWAAAVNN-VDAAVVLLKNGANKDMQNNREETPL 612
Cdd:PHA02876  237 --INKNDLSLLKAIRnedLETSLLLYD---AGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 284449631  613 FLAAREG-SYETAKVLLDHFANRDITDHMDRLPRDIAQ--ERMHHDIVRLLD 661
Cdd:PHA02876  312 YLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStlDRNKDIVITLLE 363
JMTM_Notch_APP cd21700
juxtamembrane and transmembrane (JMTM) domain found in Notch and APP family proteins; The ...
268-307 2.89e-07

juxtamembrane and transmembrane (JMTM) domain found in Notch and APP family proteins; The substrates of gamma-secretase include amyloid precursor protein (APP) and the Notch receptor. APP, also called APPI, or Alzheimer disease amyloid protein (ABPP), or amyloid precursor protein, or amyloid-beta A4 protein, or cerebral vascular amyloid peptide (CVAP), or PreA4, or protease nexin-II (PN-II), functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. 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. Successive cleavage of the APP carboxyl-terminal fragment generates amyloid-beta (Abeta) peptides of varying lengths. Accumulation of Abeta peptides such as Abeta42 and Abeta43 leads to formation of amyloid plaques in the brain, a hallmark of Alzheimer's disease. Notch cleavage is involved in cell-fate determination during development and neurogenesis. The model corresponds to the juxtamembrane and transmembrane (JMTM) domain found in Notch and APP family proteins. It comprises a transmembrane helix (TM) with adjacent juxtamembrane (JM) regions. The JMTM domain is likely to be recognized by gamma-secretase in a similar fashion to both Notch and APP family proteins.


Pssm-ID: 411983  Cd Length: 41  Bit Score: 47.78  E-value: 2.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 284449631  268 VQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCG-VLLSRKR 307
Cdd:cd21700     1 LPFFALDDGSGKGAIIGLLVGAVVILLVFVITGgLVAARKK 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
477-528 3.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 284449631   477 TALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILI 528
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
469-533 2.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 2.79e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284449631  469 NQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRAT 533
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
461-642 6.40e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  461 IYQGASLhNQTDRTGETALHLAARYSRS-----DAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQI-LIRNRATD 534
Cdd:PHA03100   55 LDNGADI-NSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeYLLDNGAN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  535 LDARMHDGTTPLilaaRLAVEG------MLEDLINSHADVNA----------------VDDLGKSALHWAAAVNNVDAAV 592
Cdd:PHA03100  134 VNIKNSDGENLL----HLYLESnkidlkILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVK 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 284449631  593 VLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANrdiTDHMDR 642
Cdd:PHA03100  210 YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS---IKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
489-633 6.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  489 DAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRAtdldarmhdgttplilaarlavegmledlinshaDV 568
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA----------------------------------DV 150
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284449631  569 NAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFAN 633
Cdd:PHA02874  151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH 215
PHA02874 PHA02874
ankyrin repeat protein; Provisional
517-662 1.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  517 SADAQGVfQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLK 596
Cdd:PHA02874   11 SGDIEAI-EKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  597 NGA----------NKDMQN------------NRE-ETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMH 653
Cdd:PHA02874   90 NGVdtsilpipciEKDMIKtildcgidvnikDAElKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169

                  ....*....
gi 284449631  654 HDIVRLLDE 662
Cdd:PHA02874  170 FDIIKLLLE 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
494-549 2.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 2.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 284449631   494 LLEA-SADANIQDNMGRTPLHAAVSADAQGVFQILIRNRAtDLDARMHDGTTPLILA 549
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV-DLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
475-642 2.30e-05

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: 48.60  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  475 GETALHLAARYSRSDAAKRLLEASADANIQdnmgrtplhaavsadAQGVFqilirNRATDLDARMHDGTTPLILAA---R 551
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAH---------------AKGVF-----FNPKYKHEGFYFGETPLALAActnQ 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  552 LAVEGMLEDliNSHADVNAVDDLGKSALHWAAAVNNVDAAV---------VLLKNGANKD---MQNNREETPLFLAAREG 619
Cdd:cd22194   201 PEIVQLLME--KESTDITSQDSRGNTVLHALVTVAEDSKTQndfvkrmydMILLKSENKNletIRNNEGLTPLQLAAKMG 278
                         170       180
                  ....*....|....*....|...
gi 284449631  620 SYEtakvLLDHFANRDITDHMDR 642
Cdd:cd22194   279 KAE----ILKYILSREIKEKPNR 297
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
474-649 4.87e-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: 47.18  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  474 TGETALHLAARY---SRSDAAKRLLEASADANIQDNM-----------GRTPLHAAVSADAQGVFQILIRNRAtDLDAR- 538
Cdd:cd21882    25 TGKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGA-DVSARa 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  539 ------------MHDGTTPLILAARLAVEGMLEDLI-NSH--ADVNAVDDLGKSALH---------WAAAVNNVDAAVVL 594
Cdd:cd21882   104 tgrffrkspgnlFYFGELPLSLAACTNQEEIVRLLLeNGAqpAALEAQDSLGNTVLHalvlqadntPENSAFVCQMYNLL 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284449631  595 LKNGANKD-------MQNNREETPLFLAAREGSYetakVLLDHFANRDITDHMDRLPRDIAQ 649
Cdd:cd21882   184 LSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKI----VMFQHILQREFSGPYQPLSRKFTE 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
456-663 1.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  456 VISDFIYQGASLhNQTDRTGETALHLAARYSRSDAAKRLLEASadanIQDNMGRT--PLHAAVSADAQGVFQILIRNRAT 533
Cdd:PHA02878   52 VVKSLLTRGHNV-NQPDHRDLTPLHIICKEPNKLGMKEMIRSI----NKCSVFYTlvAIKDAFNNRNVEIFKIILTNRYK 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  534 DLdaRMHDGTTPLILAARLAVEGMLEDLINSH-ADVNAVD-DLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETP 611
Cdd:PHA02878  127 NI--QTIDLVYIDKKSKDDIIEAEITKLLLSYgADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 284449631  612 LFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQER-MHHDIVRLLDEY 663
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
469-537 1.96e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 284449631  469 NQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDA 537
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
475-506 2.53e-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: 2.53e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 284449631   475 GETALHLAA-RYSRSDAAKRLLEASADANIQDN 506
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
475-648 4.00e-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: 4.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  475 GETALHLAARYSRSDAAKRLLEASADANIQDN--------------MGRTPLHAAVSADAQGVFQILIRNRATDLDARMH 540
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  541 DGTTPLILAARLAVEgmlEDLINSHADVNAVDDLgksalhwaaavnnvdaavvLLKNGAN-------KDMQNNREETPLF 613
Cdd:cd22193   156 DSRGNTVLHALVTVA---DNTKENTKFVTRMYDM-------------------ILIRGAKlcptvelEEIRNNDGLTPLQ 213
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 284449631  614 LAAREGSYEtakvLLDHFANRDITD----HMDRLPRDIA 648
Cdd:cd22193   214 LAAKMGKIE----ILKYILQREIKEpelrHLSRKFTDWA 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
475-503 6.49e-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: 38.01  E-value: 6.49e-04
                           10        20
                   ....*....|....*....|....*....
gi 284449631   475 GETALHLAARYSRSDAAKRLLEASADANI 503
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
426-580 7.89e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.12  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  426 PDGFTPLMIASCSGGGLETGNSEEeedapavisdFIYQGASlHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQD 505
Cdd:PHA02946   34 PSGNYHILHAYCGIKGLDERFVEE----------LLHRGYS-PNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACD 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 284449631  506 NMGRTPLHAAVSADAQGVFQI--LIRNRATDLDARMHDGTTPLiLAARLAVEGMLEDLINSHADVNAVDDLGKSALH 580
Cdd:PHA02946  103 KQHKTPLYYLSGTDDEVIERInlLVQYGAKINNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
594-663 8.65e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 8.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  594 LLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEY 663
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
477-660 1.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  477 TALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNratdldarmhdGTTPLILAARLAVEG 556
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN-----------GVDTSILPIPCIEKD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  557 MLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDI 636
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
                         170       180
                  ....*....|....*....|....
gi 284449631  637 TDHMDRLPRDIAQERMHHDIVRLL 660
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLL 209
PHA02917 PHA02917
ankyrin-like protein; Provisional
469-517 1.48e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 42.68  E-value: 1.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 284449631  469 NQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVS 517
Cdd:PHA02917  446 NMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAIN 494
Ank_2 pfam12796
Ankyrin repeats (3 copies);
612-676 1.72e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.72e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284449631   612 LFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGAPL 676
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTAL 65
PHA02743 PHA02743
Viral ankyrin protein; Provisional
460-577 2.13e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.18  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  460 FIYQGASLHNQTDRTGETALHLAARYSRSDAAKR---LLEASADANIQD-NMGRTPLHAAVSADAQGVFQILIRNRATDL 535
Cdd:PHA02743   42 FISGDGHLLHRYDHHGRQCTHMVAWYDRANAVMKielLVNMGADINARElGTGNTLLHIAASTKNYELAEWLCRQLGVNL 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 284449631  536 DARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKS 577
Cdd:PHA02743  122 GAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPLSIGLS 163
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
526-660 2.33e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  526 ILIRNRATDLDARMhdgTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGAN---KD 602
Cdd:PLN03192  512 LLGDNGGEHDDPNM---ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNvhiRD 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284449631  603 MQNN----------------------REETP------LFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHH 654
Cdd:PLN03192  589 ANGNtalwnaisakhhkifrilyhfaSISDPhaagdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHV 668

                  ....*.
gi 284449631  655 DIVRLL 660
Cdd:PLN03192  669 DMVRLL 674
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
480-551 6.04e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 6.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284449631  480 HLAARySRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRAtDLDARMHDGTTPLILAAR 551
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEE 157
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure