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Conserved domains on  [gi|50400170|gb|AAT76432|]
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samcystin [Rattus norvegicus]

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];
43-268 2.47e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.08  E-value: 2.47e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  43 AEPAGPEAARAVEAGTPVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLL 122
Cdd:COG0666  61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 123 DHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLM 202
Cdd:COG0666 141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE--------------TPLHLAAENGHLEIVKLLL 206

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50400170 203 EWGADPNHTARTvGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYL 268
Cdd:COG0666 207 EAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 771-835 1.08e-38

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


:

Pssm-ID: 188917  Cd Length: 65  Bit Score: 137.70  E-value: 1.08e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50400170 771 TITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNA 835
Cdd:cd09518   1 TITEEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-380 3.51e-20

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   287 IFHALKMGNFQLVKEIADEDPNhVNLVNGDGATPLMLAAVTGQLPLVQLLVEkHADMNKQDsvHGWTALMQATYHGNKEI 366
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD--NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 50400170   367 VKYLLNQGADVTLR 380
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
355-420 2.91e-07

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50400170   355 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAfdLVMLLNDPDTELVRLLASVCMQVNKDRGGRP 420
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA--LHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-268 2.47e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.08  E-value: 2.47e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  43 AEPAGPEAARAVEAGTPVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLL 122
Cdd:COG0666  61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 123 DHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLM 202
Cdd:COG0666 141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE--------------TPLHLAAENGHLEIVKLLL 206

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50400170 203 EWGADPNHTARTvGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYL 268
Cdd:COG0666 207 EAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 771-835 1.08e-38

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


Pssm-ID: 188917  Cd Length: 65  Bit Score: 137.70  E-value: 1.08e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50400170 771 TITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNA 835
Cdd:cd09518   1 TITEEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 85-396 2.21e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.56  E-value: 2.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   85 VRFLLRRGASVNSRNHYGWSALMQAARCGH---ASVAHLLLDHGADVNAQNRLGASVL-TVASRGGHLGVVKLLLEAGAT 160
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGAD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  161 VdhrnpsgesTASGGSRDELLGITALMAAVqhgHEAVVRLLMEWGADPNhtARTV-GWSPLmlAALLGK----LSVVQQL 235
Cdd:PHA03095 110 V---------NAKDKVGRTPLHVYLSGFNI---NPKVIRLLLRKGADVN--ALDLyGMTPL--AVLLKSrnanVELLRLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  236 VEKGANPdhlgvlektaFEValDRKHRDLADYLdpLTTVRPktdeekrRPDIFHALKMgnfqlvkeiADEDPNHVNLVng 315
Cdd:PHA03095 174 IDAGADV----------YAV--DDRFRSLLHHH--LQSFKP-------RARIVRELIR---------AGCDPAATDML-- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  316 dGATPLMLAAVTG--QLPLVQLLVEKHADMNKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLvML 393
Cdd:PHA03095 222 -GNTPLHSMATGSscKRSLVLPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL-MV 298


                 ...
gi 50400170  394 LND 396
Cdd:PHA03095 299 RNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-380 3.51e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   287 IFHALKMGNFQLVKEIADEDPNhVNLVNGDGATPLMLAAVTGQLPLVQLLVEkHADMNKQDsvHGWTALMQATYHGNKEI 366
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD--NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 50400170   367 VKYLLNQGADVTLR 380
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-165 3.83e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170    73 LQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHgADVNAQNRlGASVLTVASRGGHLGVVK 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 50400170   153 LLLEAGATVDHRN 165
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 228-386 2.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  228 KLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKH-----RDLADYLDPLTTVRPKTDEEKRRPDIFHAL-KMGNFQLVKE 301
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkKSNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  302 IADEDPNhVNLVNGDGATPLMLAA--VTGQLPLVQLLVEKHADMNKQDSV---------------HGWTALMQATYHGNK 364
Cdd:PHA03100 127 LLDNGAN-VNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVnyllsygvpinikdvYGFTPLHYAVYNNNP 205

                        170       180
                 ....*....|....*....|..
gi 50400170  365 EIVKYLLNQGADVTLRAKNGYT 386
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDT 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
264-405 7.13e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 7.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 264 LADYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADM 343
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50400170 344 NKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPdtELVRLL 405
Cdd:COG0666  81 NAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL--EIVKLL 139
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 774-833 8.44e-10

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 55.38  E-value: 8.44e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50400170    774 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDG-DLQELGIKTDGSRQQILAAISEL 833
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGITKLGHRKKILKAIQKL 65
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-238 8.51e-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: 62.34  E-value: 8.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  12 LLLRACEQGDTDTARRLLE-PGGEPVAGSEAGaEPA--------GPEAARAVEAGTP----VPVDCSDEAGNSALQLAAA 78
Cdd:cd22192  20 PLLLAAKENDVQAIKKLLKcPSCDLFQRGALG-ETAlhvaalydNLEAAVVLMEAAPelvnEPMTSDLYQGETALHIAVV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  79 GGHEPLVRFLLRRGASVNS------------RN--HYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLtvasr 144
Cdd:cd22192  99 NQNLNLVRELIARGADVVSpratgtffrpgpKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 145 ggHLgvvkLLLEAGATVdhrnpsgestasggsrdELLGITALMAAVQHGHEAVVRLLmewgadPNHTartvGWSPLMLAA 224
Cdd:cd22192 174 --HI----LVLQPNKTF-----------------ACQMYDLILSYDKEDDLQPLDLV------PNNQ----GLTPFKLAA 220

                       250
                ....*....|....
gi 50400170 225 LLGKLSVVQQLVEK 238
Cdd:cd22192 221 KEGNIVMFQHLVQK 234
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 782-833 4.04e-09

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 53.43  E-value: 4.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 50400170   782 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:pfam00536  12 LESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
355-420 2.91e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50400170   355 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAfdLVMLLNDPDTELVRLLASVCMQVNKDRGGRP 420
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA--LHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 289-424 6.68e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 6.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 289 HALKMGNFQLVKEIADEDPNHVNL-VNGD---GATPLMLAAVTGQLPLVQLLVEKHADMNK-----------QDSV--HG 351
Cdd:cd22192  57 VAALYDNLEAAVVLMEAAPELVNEpMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyYG 136

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50400170 352 WTALMQATYHGNKEIVKYLLNQGADvtLRAKNGYTAFDLVMLLNDPDTELVRLLASVCM-QVNKDRGGRPSHRP 424
Cdd:cd22192 137 EHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLGNTVLHILVLQPNKTFACQMYDLILsYDKEDDLQPLDLVP 208
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 350-379 2.13e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 50400170    350 HGWTALMQATYHGNKEIVKYLLNQGADVTL 379
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 101-130 3.18e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.18e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 50400170    101 YGWSALMQAARCGHASVAHLLLDHGADVNA 130
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 48-139 8.78e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170    48 PEAARAVEAGTP--VPVDCSDE--AGNSALQLAAAGGHEPLVRFLLRRGASVNSRNH--------------YGWSALMQA 109
Cdd:TIGR00870 103 HLLAAFRKSGPLelANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAA 182

                          90       100       110
                  ....*....|....*....|....*....|
gi 50400170   110 ARCGHASVAHLLLDHGADVNAQNRLGASVL 139
Cdd:TIGR00870 183 ACLGSPSIVALLSEDPADILTADSLGNTLL 212
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-268 2.47e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 182.08  E-value: 2.47e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  43 AEPAGPEAARAVEAGTPVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLL 122
Cdd:COG0666  61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 123 DHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLM 202
Cdd:COG0666 141 EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE--------------TPLHLAAENGHLEIVKLLL 206

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50400170 203 EWGADPNHTARTvGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYL 268
Cdd:COG0666 207 EAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-316 6.62e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 6.62e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  65 SDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASR 144
Cdd:COG0666  50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 145 GGHLGVVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLMEWGADPNHTARTvGWSPLMLAA 224
Cdd:COG0666 130 NGNLEIVKLLLEAGADVNAQDNDGN--------------TPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAA 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 225 LLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIAD 304
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                       250
                ....*....|..
gi 50400170 305 EDPNHVNLVNGD 316
Cdd:COG0666 275 LLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-406 1.32e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 1.32e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  62 VDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTV 141
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 142 ASRGGHLGVVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLMEWGADPNHTARTvGWSPLM 221
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGE--------------TPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 222 LAALLGKLSVVQQLVEKGANpdhlgvlektafevaldrkhrdladyldplttvrpktdeekrrpdifhalkmgnfqlvke 301
Cdd:COG0666 159 LAAANGNLEIVKLLLEAGAD------------------------------------------------------------ 178

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 302 iadedpnhVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMNKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRA 381
Cdd:COG0666 179 --------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                       330       340
                ....*....|....*....|....*
gi 50400170 382 KNGYTAFDLVMLLNDPDTELVRLLA 406
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-241 2.31e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 2.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   9 GLQLLLRACEQGDTDTARRLLEpggepvagseAGAEpagpeaaraveagtpvpVDCSDEAGNSALQLAAAGGHEPLVRFL 88
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLE----------AGAD-----------------VNARDKDGETPLHLAAYNGNLEIVKLL 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  89 LRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSG 168
Cdd:COG0666 140 LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG 219

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50400170 169 EstasggsrdellgiTALMAAVQHGHEAVVRLLMEWGADPNHTARTvGWSPLMLAALLGKLSVVQQLVEKGAN 241
Cdd:COG0666 220 K--------------TALDLAAENGNLEIVKLLLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-406 8.46e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 8.46e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  84 LVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDH 163
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 164 RNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLMEWGADPNHTARTvGWSPLMLAALLGKLSVVQQLVEKGANpd 243
Cdd:COG0666  83 KDDGGN--------------TLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGAD-- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 244 hlgvlektafevaldrkhrdladyldplttvrpktdeekrrpdifhalkmgnfqlvkeiadedpnhVNLVNGDGATPLML 323
Cdd:COG0666 146 ------------------------------------------------------------------VNAQDNDGNTPLHL 159

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 324 AAVTGQLPLVQLLVEKHADMNKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVR 403
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238


                ...
gi 50400170 404 LLA 406
Cdd:COG0666 239 LEA 241
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 771-835 1.08e-38

SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or SamCystin) subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. They are able to form self-associated complexes and both (SAM and ANK) domains play a role in such interactions. Mutations in Anks6 gene are associated with polycystic kidney disease. They cause formation of renal cysts in rodent models. It was suggested that the ANKS6 protein can interact indirectly (through RNA and protein intermediates) with BICC1, another polycystic kidney disease-associated protein.


Pssm-ID: 188917  Cd Length: 65  Bit Score: 137.70  E-value: 1.08e-38
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50400170 771 TITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNA 835
Cdd:cd09518   1 TITEEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 85-396 2.21e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.56  E-value: 2.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   85 VRFLLRRGASVNSRNHYGWSALMQAARCGH---ASVAHLLLDHGADVNAQNRLGASVL-TVASRGGHLGVVKLLLEAGAT 160
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGAD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  161 VdhrnpsgesTASGGSRDELLGITALMAAVqhgHEAVVRLLMEWGADPNhtARTV-GWSPLmlAALLGK----LSVVQQL 235
Cdd:PHA03095 110 V---------NAKDKVGRTPLHVYLSGFNI---NPKVIRLLLRKGADVN--ALDLyGMTPL--AVLLKSrnanVELLRLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  236 VEKGANPdhlgvlektaFEValDRKHRDLADYLdpLTTVRPktdeekrRPDIFHALKMgnfqlvkeiADEDPNHVNLVng 315
Cdd:PHA03095 174 IDAGADV----------YAV--DDRFRSLLHHH--LQSFKP-------RARIVRELIR---------AGCDPAATDML-- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  316 dGATPLMLAAVTG--QLPLVQLLVEKHADMNKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLvML 393
Cdd:PHA03095 222 -GNTPLHSMATGSscKRSLVLPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL-MV 298


                 ...
gi 50400170  394 LND 396
Cdd:PHA03095 299 RNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-380 3.51e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   287 IFHALKMGNFQLVKEIADEDPNhVNLVNGDGATPLMLAAVTGQLPLVQLLVEkHADMNKQDsvHGWTALMQATYHGNKEI 366
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD--NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 50400170   367 VKYLLNQGADVTLR 380
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-165 3.83e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 3.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170    73 LQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHgADVNAQNRlGASVLTVASRGGHLGVVK 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 50400170   153 LLLEAGATVDHRN 165
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-211 8.42e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 8.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   106 LMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAtvdhrnpsgestasggSRDELLGITA 185
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----------------VNLKDNGRTA 64

                          90       100
                  ....*....|....*....|....*.
gi 50400170   186 LMAAVQHGHEAVVRLLMEWGADPNHT 211
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINVK 90
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 776-835 1.28e-19

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.


Pssm-ID: 188919  Cd Length: 65  Bit Score: 83.50  E-value: 1.28e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 776 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNA 835
Cdd:cd09520   5 SDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELNK 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
139-243 2.95e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   139 LTVASRGGHLGVVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLMEwGADPNhtARTVGWS 218
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR--------------TALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRT 63

                          90       100
                  ....*....|....*....|....*
gi 50400170   219 PLMLAALLGKLSVVQQLVEKGANPD 243
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-245 8.39e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 8.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   66 DEAGNSALQLAAAG--GHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHA--SVAHLLLDHGADVNAQNRlgasvltv 141
Cdd:PHA03100 103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-------- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  142 asrgghlgvVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLMEWGADPNhtARTV-GWSPL 220
Cdd:PHA03100 175 ---------VNYLLSYGVPINIKDVYGF--------------TPLHYAVYNNNPEFVKYLLDLGANPN--LVNKyGDTPL 229

                        170       180
                 ....*....|....*....|....*
gi 50400170  221 MLAALLGKLSVVQQLVEKGANPDHL 245
Cdd:PHA03100 230 HIAILNNNKEIFKLLLNNGPSIKTI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
220-347 1.18e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   220 LMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAfevaldrkhrdladyldplttvrpktdeekrrpdIFHALKMGNFQLV 299
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA----------------------------------LHLAAKNGHLEIV 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 50400170   300 KEIADEdpNHVNLVNgDGATPLMLAAVTGQLPLVQLLVEKHADMNKQD 347
Cdd:pfam12796  47 KLLLEH--ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 183-425 2.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 2.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  183 ITALMAAVQHGHEAVVRLLMEWGADPNHTARTVGwSPLMLAALLGKLSVVQQLVEKGANPDHLGV--LEKTAFEVALDrk 260
Cdd:PHA02874  36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIP-HPLLTAIKIGAHDIIKLLIDNGVDTSILPIpcIEKDMIKTILD-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  261 hrdladyldplTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPNhVNLVNGDGATPLMLAAVTGQLPLVQLLVEKH 340
Cdd:PHA02874 113 -----------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  341 ADMNKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELvrLLASVCMQVNKDRGGRP 420
Cdd:PHA02874 181 AYANVKDN-NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIEL--LINNASINDQDIDGSTP 257


                 ....*...
gi 50400170  421 SH---RPP 425
Cdd:PHA02874 258 LHhaiNPP 265
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 782-832 4.04e-13

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 64.57  E-value: 4.04e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 50400170 782 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISE 832
Cdd:cd09487   6 LESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 777-835 7.95e-13

SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization.


Pssm-ID: 188918  Cd Length: 64  Bit Score: 64.05  E-value: 7.95e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50400170 777 ELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNA 835
Cdd:cd09519   6 DLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-209 1.08e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   69 GNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVA-SRGGH 147
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKD 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50400170  148 LGVVKLLLEAGATVDhrnpsgestasggSRDELLGITALMAAVQhgHEAVVRLLMEWGADPN 209
Cdd:PHA02878 248 YDILKLLLEHGVDVN-------------AKSYILGLTALHSSIK--SERKLKLLLEYGADIN 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 104-416 1.29e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  104 SALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATV----------DHRNPSGESTAS 173
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekDMIKTILDCGID 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  174 GGSRDELLGiTALMAAVQHGHEAVVRLLMEWGADPNhTARTVGWSPLMLAALLGKLSVVQQLVEKGAnpdhlgvlektaf 253
Cdd:PHA02874 117 VNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGA------------- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  254 evaldrkhrdladYLDplttvrpKTDEEKRRPdIFHALKMGNFQLVKEIADeDPNHVNLVNGDGATPLMLAAVTGQlPLV 333
Cdd:PHA02874 182 -------------YAN-------VKDNNGESP-LHNAAEYGDYACIKLLID-HGNHIMNKCKNGFTPLHNAIIHNR-SAI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  334 QLLVeKHADMNKQDsVHGWTALMQA-TYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMQV 412
Cdd:PHA02874 239 ELLI-NNASINDQD-IDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIK 316


                 ....
gi 50400170  413 NKDR 416
Cdd:PHA02874 317 EADK 320
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 228-386 2.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  228 KLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKH-----RDLADYLDPLTTVRPKTDEEKRRPDIFHAL-KMGNFQLVKE 301
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISkKSNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  302 IADEDPNhVNLVNGDGATPLMLAA--VTGQLPLVQLLVEKHADMNKQDSV---------------HGWTALMQATYHGNK 364
Cdd:PHA03100 127 LLDNGAN-VNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVnyllsygvpinikdvYGFTPLHYAVYNNNP 205

                        170       180
                 ....*....|....*....|..
gi 50400170  365 EIVKYLLNQGADVTLRAKNGYT 386
Cdd:PHA03100 206 EFVKYLLDLGANPNLVNKYGDT 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 84-461 5.46e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 5.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   84 LVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVK----------- 152
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsnink 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  153 ------------------LLLEAGATV----DHRNPSGESTASGGSRDELL----------------GITALMAAVQHGH 194
Cdd:PHA02876 240 ndlsllkairnedletslLLYDAGFSVnsidDCKNTPLHHASQAPSLSRLVpkllergadvnaknikGETPLYLMAKNGY 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  195 EAV-VRLLMEWGADPNHTARTVGwSPLMLAALLGKLS-VVQQLVEKGANPDHLGVLEKTAFEVALDRKH----RDLADYL 268
Cdd:PHA02876 320 DTEnIRTLIMLGADVNAADRLYI-TPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNvviiNTLLDYG 398

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  269 DPLTTVRPKTDEekrrpdIFHALKMGN--FQLVKEIADEDPNhVNLVNGDGATPLMLAAVTG-QLPLVQLLVEKHADMNK 345
Cdd:PHA02876 399 ADIEALSQKIGT------ALHFALCGTnpYMSVKTLIDRGAN-VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  346 QDSVHGWTALMQATYHGnkeIVKYLLNQGADvtLRAKNgytafDLVMLLNDPDTELVRLLASVCMQ--VNKD--RGGRPS 421
Cdd:PHA02876 472 INIQNQYPLLIALEYHG---IVNILLHYGAE--LRDSR-----VLHKSLNDNMFSFRYIIAHICIQdfIRHDirNEVNPL 541

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 50400170  422 HRPPLPHSKARQPWSIPMLPDDKggLKSWWSRMSNRFRKL 461
Cdd:PHA02876 542 KRVPTRFTSLRESFKEIIQSDDT--FKRIWLRCKEELKDI 579
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
264-405 7.13e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 7.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 264 LADYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADM 343
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50400170 344 NKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPdtELVRLL 405
Cdd:COG0666  81 NAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL--EIVKLL 139
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 63-165 4.48e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 4.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   63 DCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASV-------AHL--------------- 120
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrilyhfASIsdphaagdllctaak 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 50400170  121 ---------LLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRN 165
Cdd:PLN03192 632 rndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 105-419 1.36e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  105 ALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGEStasggsrdellgit 184
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIES-------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  185 ALMAAVQHGHEAVVRLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEKGANPDhlgvlektafevaldrkhrdl 264
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD--------------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  265 adyldplttvRPKTDeekRRPDIFHALKMGNFQLVKEIADEDPNhVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMN 344
Cdd:PHA02875 130 ----------IPNTD---KFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  345 KQDSVHGWTALMQATYHGNKEIVKYLLNQGAD---VTLRAKNGYTAFDLV--MLLNdPDTELV-RLLASVCMQVNKDRGG 418
Cdd:PHA02875 196 YFGKNGCVAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECTILDMIcnMCTN-LESEAIdALIADIAIRIHKKTIR 274


                 .
gi 50400170  419 R 419
Cdd:PHA02875 275 R 275
Ank_4 pfam13637
Ankyrin repeats (many copies);
319-371 1.84e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 1.84e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50400170   319 TPLMLAAVTGQLPLVQLLVEKHADMNKQDSvHGWTALMQATYHGNKEIVKYLL 371
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-122 3.94e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 3.94e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 50400170    69 GNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLL 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 774-833 8.44e-10

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 55.38  E-value: 8.44e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50400170    774 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDG-DLQELGIKTDGSRQQILAAISEL 833
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGITKLGHRKKILKAIQKL 65
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-238 8.51e-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: 62.34  E-value: 8.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  12 LLLRACEQGDTDTARRLLE-PGGEPVAGSEAGaEPA--------GPEAARAVEAGTP----VPVDCSDEAGNSALQLAAA 78
Cdd:cd22192  20 PLLLAAKENDVQAIKKLLKcPSCDLFQRGALG-ETAlhvaalydNLEAAVVLMEAAPelvnEPMTSDLYQGETALHIAVV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  79 GGHEPLVRFLLRRGASVNS------------RN--HYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLtvasr 144
Cdd:cd22192  99 NQNLNLVRELIARGADVVSpratgtffrpgpKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL----- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 145 ggHLgvvkLLLEAGATVdhrnpsgestasggsrdELLGITALMAAVQHGHEAVVRLLmewgadPNHTartvGWSPLMLAA 224
Cdd:cd22192 174 --HI----LVLQPNKTF-----------------ACQMYDLILSYDKEDDLQPLDLV------PNNQ----GLTPFKLAA 220

                       250
                ....*....|....
gi 50400170 225 LLGKLSVVQQLVEK 238
Cdd:cd22192 221 KEGNIVMFQHLVQK 234
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 83-264 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   83 PLVRFLLRRGASVNSRNHYGWSALMQAA--RCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGH--LGVVKLLLEAG 158
Cdd:PHA03100  87 EIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  159 ATVDHRNpsgestasggsrdellgitalmaavqhgheaVVRLLMEWGADPNhTARTVGWSPLMLAALLGKLSVVQQLVEK 238
Cdd:PHA03100 167 VDINAKN-------------------------------RVNYLLSYGVPIN-IKDVYGFTPLHYAVYNNNPEFVKYLLDL 214

                        170       180
                 ....*....|....*....|....*.
gi 50400170  239 GANPDHLGVLEKTAFEVALDRKHRDL 264
Cdd:PHA03100 215 GANPNLVNKYGDTPLHIAILNNNKEI 240
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-155 1.63e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 50400170   102 GWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLL 155
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 54-223 1.65e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   54 VEAGtpVPVDCSDEAGNSALQLAAAGG--HEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVA--HLLLDHGADV- 128
Cdd:PHA03095 104 IKAG--ADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVy 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  129 ----------------------------------NAQNRLGASVLTVASRGGHL--GVVKLLLEAGATVDHRNpsgesta 172
Cdd:PHA03095 182 avddrfrsllhhhlqsfkprarivreliragcdpAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARN------- 254

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 50400170  173 sggsrdeLLGITALMAAVQHGHEAVVRLLMEWGADPNHTARTvGWSPLMLA 223
Cdd:PHA03095 255 -------RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD-GNTPLSLM 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 69-209 1.97e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   69 GNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHL 148
Cdd:PHA02875 102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50400170  149 GVVKLLLEAGATVDH--RNPSgestasggsrdellgITALMAAVQHGHEAVVRLLMEWGADPN 209
Cdd:PHA02875 182 AICKMLLDSGANIDYfgKNGC---------------VAALCYAIENNKIDIVRLFIKRGADCN 229
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
 774-832 2.99e-09

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.


Pssm-ID: 188915  Cd Length: 69  Bit Score: 53.96  E-value: 2.99e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50400170 774 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTdGSRQQILAAISE 832
Cdd:cd09516   8 EPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPM-GPRKKLLGFLKD 65
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 774-831 3.19e-09

SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential protein-protein interaction domain. DDHD2 proteins contain at least two domains:a SAM domain and a predicted metal-binding domain. Phospholipase A1 activity was demonstrated for the mammalian DDHD2 protein. Mutation of the putative catalytic serine resulted in elimination of activity. Unlike SEC23IP, DDHD2 proteins do not have an N-terminal proline-rich region and correspondingly they are not able to interact with Sec23p/Sec24p complex. Overexpression of DDHD2 is the cause of dispersion of ER/Golgi intermediate compartment and dispersion of tethering proteins located in the Golgi region, leading to aggregation in the endoplasmic reticulum.


Pssm-ID: 188984  Cd Length: 69  Bit Score: 53.99  E-value: 3.19e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50400170 774 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTdGSRQQILAAIS 831
Cdd:cd09585   8 DTPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPL-GPRKKILNYIR 64
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 782-833 4.04e-09

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 53.43  E-value: 4.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 50400170   782 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:pfam00536  12 LESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-165 6.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 6.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   62 VDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSAL-MQAARCGHASVAHLLLDHGADVNAQNR-LGASVL 139
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTAL 273

                         90       100
                 ....*....|....*....|....*.
gi 50400170  140 TVASRGGHlgVVKLLLEAGATVDHRN 165
Cdd:PHA02878 274 HSSIKSER--KLKLLLEYGADINSLN 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 228-408 6.45e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 6.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  228 KLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYLDPLttvrpktdeekrrpdifhaLKMGnfqlvkeiADedp 307
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLL-------------------LEAG--------AD--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  308 nhVNLVNGDGATPL---MLAAVTgqLPLVQLLVEKHADMNKQDSVhGWTALmqATYHGNKEI----VKYLLNQGADVTLR 380
Cdd:PHA03095  76 --VNAPERCGFTPLhlyLYNATT--LDVIKLLIKAGADVNAKDKV-GRTPL--HVYLSGFNInpkvIRLLLRKGADVNAL 148

                        170       180
                 ....*....|....*....|....*...
gi 50400170  381 AKNGYTAFDLVMLLNDPDTELVRLLASV 408
Cdd:PHA03095 149 DLYGMTPLAVLLKSRNANVELLRLLIDA 176
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 775-833 6.88e-09

SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) proteins, also known as LRSAM1 (Leucine-rich repeat and sterile alpha motif-containing) proteins, is a putative protein-protein interaction domain. Proteins of this subfamily participate in the regulation of retrovirus budding and receptor endocytosis. They show E3 ubiquitin ligase activity. Human TAL protein interacts with Tsg101 and TAL's C-terminal ring finger domain is essential for the multiple monoubiquitylation of Tsg101.


Pssm-ID: 188922  Cd Length: 65  Bit Score: 52.68  E-value: 6.88e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50400170 775 EDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:cd09523   5 DPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQEL 63
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 74-155 1.72e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   74 QLAAAGGHEPlVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKL 153
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ..
gi 50400170  154 LL 155
Cdd:PTZ00322 167 LS 168
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 774-834 1.82e-07

SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a protein-protein interaction domain. Proteins of this subfamily have SAM domain at the N-terminus and protein kinase domain at the C-terminus. They participate in regulation of mating pheromone response, invasive growth and high osmolarity growth response. MAP triple kinase Ste11 from S.cerevisia is known to interact with Ste20 kinase and Ste50 regulator. These kinases are able to form homodimers interacting through their SAM domains as well as heterodimers or heterogenous complexes when either SAM domain of monomeric or homodimeric form of Ste11 interacts with Ste50 regulator.


Pssm-ID: 188933  Cd Length: 62  Bit Score: 48.75  E-value: 1.82e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50400170 774 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELN 834
Cdd:cd09534   2 DEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 104-339 1.92e-07

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: 54.63  E-value: 1.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 104 SALMQAARCGH-ASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVdhrnpSGESTASggsrDELLG 182
Cdd:cd22192  19 SPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL-----VNEPMTS----DLYQG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 183 ITALMAAVQHGHEAVVRLLMEWGADPNhTARTVGW--------------SPLMLAALLGKLSVVQQLVEKGANP---DHL 245
Cdd:cd22192  90 ETALHIAVVNQNLNLVRELIARGADVV-SPRATGTffrpgpknliyygeHPLSFAACVGNEEIVRLLIEHGADIraqDSL 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 246 G--VLEKTAfevaldrkhrdladyLDPLTTVrpktdeekrrpdifhALKMGNFQLVKEIADEDPNHVNLVNGDGATPLML 323
Cdd:cd22192 169 GntVLHILV---------------LQPNKTF---------------ACQMYDLILSYDKEDDLQPLDLVPNNQGLTPFKL 218

                       250
                ....*....|....*.
gi 50400170 324 AAVTGQLPLVQLLVEK 339
Cdd:cd22192 219 AAKEGNIVMFQHLVQK 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
355-420 2.91e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 2.91e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50400170   355 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAfdLVMLLNDPDTELVRLLASVCMQVNKDRGGRP 420
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA--LHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-99 3.94e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170    13 LLRACEQGDTDTARRLLEPGGEPVAGSEAGAEPAgpeaARAVEAGTP---------VPVDCSDEaGNSALQLAAAGGHEP 83
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL----HLAAKNGHLeivklllehADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 50400170    84 LVRFLLRRGASVNSRN 99
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 150-377 4.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  150 VVKLLLEAGATVdHRNPSGESTASGGSRDELLGITALMAavqhgheaVVRLLMEWGADPNHTARtVGWSPLMLAA--LLG 227
Cdd:PHA03100  50 VVKILLDNGADI-NSSTKNNSTPLHYLSNIKYNLTDVKE--------IVKLLLEYGANVNAPDN-NGITPLLYAIskKSN 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  228 KLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLaDYLDPLttVRPKTD-EEKRRPDIFhaLKMGNfqlvkeiaded 306
Cdd:PHA03100 120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL-KILKLL--IDKGVDiNAKNRVNYL--LSYGV----------- 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50400170  307 pnHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMNKQdSVHGWTALMQATYHGNKEIVKYLLNQGADV 377
Cdd:PHA03100 184 --PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV-NKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 782-832 1.14e-06

SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher syndrome type-1G/ Harmonin-interacting Ankyrin Repeat-containing protein) family is a protein-protein interaction domain. Members of this family have an N-terminal ankyrin repeat region and a C-terminal SAM domain. In mammals these proteins can interact via the SAM domain with the PDZ domain of harmonin to form a scaffolding complex that facilitates signal transduction in epithelial and inner ear sensory cells. It was suggested that USH1G and HARP can be tissue specific partners of harmonin. Mutations in ush1g genes lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188916  Cd Length: 66  Bit Score: 46.56  E-value: 1.14e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 50400170 782 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTdGSRQQILAAISE 832
Cdd:cd09517   9 LTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPL-GPRRKLLNAIAK 58
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 84-236 1.67e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   84 LVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDH 163
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50400170  164 RNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLLMEWGADPNHTARTvGWSPLMLAALLGKlSVVQQLV 236
Cdd:PHA02874 186 KDNNGE--------------SPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAIIHNR-SAIELLI 242
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 66-228 1.69e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   66 DEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQN------------- 132
Cdd:PLN03192 522 DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDangntalwnaisa 601

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  133 ------------------RLGASVLTVASRGGHLGVVKLLLEAGATVDHRNpsgestasggsRDellGITALMAAVQHGH 194
Cdd:PLN03192 602 khhkifrilyhfasisdpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSED-----------HQ---GATALQVAMAEDH 667

                        170       180       190
                 ....*....|....*....|....*....|....
gi 50400170  195 EAVVRLLMEWGADPNHTARTVGWSPLMLAALLGK 228
Cdd:PLN03192 668 VDMVRLLIMNGADVDKANTDDDFSPTELRELLQK 701
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 132-268 2.08e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  132 NRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGESTASggsrdellgITALMAAVQHGHEAV------VRLLMEWG 205
Cdd:PTZ00322  35 ERMAAIQEEIARIDTHLEALEATENKDATPDHNLTTEEVIDP---------VVAHMLTVELCQLAAsgdavgARILLTGG 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50400170  206 ADPNhTARTVGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYL 268
Cdd:PTZ00322 106 ADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 101-133 2.37e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 2.37e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 50400170   101 YGWSALMQAA-RCGHASVAHLLLDHGADVNAQNR 133
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 776-834 2.94e-06

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 45.36  E-value: 2.94e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50400170 776 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELN 834
Cdd:cd09521   6 DDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEVH 64
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
 778-826 3.02e-06

SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) group is a potential protein-protein interaction domain. Sec23ip proteins (also known as p125) contain an N-terminal proline-rich region, a central region containing a SAM domain and a C-terminal region with a predicted metal-binding domain. Sec23ip interacts with Sec23p/Sec24p part of COPII-coated vesicles complex involved in protein transport from the ER to the Golgi apparatus. The proline-rich region plays an essential role in this interaction. Overexpression of Sec23ip leads to disorganization of ER/Golgi intermediate compartment.


Pssm-ID: 188983  Cd Length: 69  Bit Score: 45.57  E-value: 3.02e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 50400170 778 LTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTdGSRQQI 826
Cdd:cd09584  12 LQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPL-GPRKKI 59
Ank_5 pfam13857
Ankyrin repeats (many copies);
88-142 3.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 50400170    88 LLRRG-ASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVA 142
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 148-422 3.84e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  148 LGVVKLLLEAGATVDHRNPSGESTasggsrdellgITALMAAVQHGHEAVVRLLMEWGADPNhTARTVGWSPLMLAALLG 227
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTP-----------LHLYLHYSSEKVKDIVRLLLEAGADVN-APERCGFTPLHLYLYNA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  228 -KLSVVQQLVEKGANPDHLGVLEKTAFEValdrkhrdladYLDPLTTvrpktdeekrRPDIFHAL-KMGnfqlvkeiADe 305
Cdd:PHA03095  95 tTLDVIKLLIKAGADVNAKDKVGRTPLHV-----------YLSGFNI----------NPKVIRLLlRKG--------AD- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  306 dpnhVNLVNGDGATPLmlaAVtgqlplvqLLVEKHADMnkqdsvhgwtalmqatyhgnkEIVKYLLNQGADVTLRAKNGY 385
Cdd:PHA03095 145 ----VNALDLYGMTPL---AV--------LLKSRNANV---------------------ELLRLLIDAGADVYAVDDRFR 188

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 50400170  386 TAFDLVMLLNDPDTELVR-LLASVCMQVNKDRGGR-PSH 422
Cdd:PHA03095 189 SLLHHHLQSFKPRARIVReLIRAGCDPAATDMLGNtPLH 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-200 3.88e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   66 DEAGNSALQLAAAGG--HEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVAS 143
Cdd:PHA03095 219 DMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  144 RGGHLGVVKLLLEA-------GATVDHRNPSGESTASGGSRD---ELL---GITALMAAVQHGHEAVVRL 200
Cdd:PHA03095 299 RNNNGRAVRAALAKnpsaetvAATLNTASVAGGDIPSDATRLcvaKVVlrgAFSLLPEPIRAYHADFIRE 368
Ank_5 pfam13857
Ankyrin repeats (many copies);
335-391 4.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 50400170   335 LLVEKHADMNKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLV 391
Cdd:pfam13857   1 LLEHGPIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 309-416 6.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 6.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  309 HVNLVNGDGATPLMLAAV-----TGQLPLVQLLVEKHADMNKQDSVHGWTALMQATYH-GNKEIVKYLLNQGADVTLRAK 382
Cdd:PHA03100  60 DINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNS 139

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 50400170  383 NGYTAFDLVMLLNDPDTELVRLLASVCMQVN-KDR 416
Cdd:PHA03100 140 DGENLLHLYLESNKIDLKILKLLIDKGVDINaKNR 174
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 289-424 6.68e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 6.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 289 HALKMGNFQLVKEIADEDPNHVNL-VNGD---GATPLMLAAVTGQLPLVQLLVEKHADMNK-----------QDSV--HG 351
Cdd:cd22192  57 VAALYDNLEAAVVLMEAAPELVNEpMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyYG 136

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50400170 352 WTALMQATYHGNKEIVKYLLNQGADvtLRAKNGYTAFDLVMLLNDPDTELVRLLASVCM-QVNKDRGGRPSHRP 424
Cdd:cd22192 137 EHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLGNTVLHILVLQPNKTFACQMYDLILsYDKEDDLQPLDLVP 208
Ank_4 pfam13637
Ankyrin repeats (many copies);
137-201 7.38e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 7.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50400170   137 SVLTVASRGGHLGVVKLLLEAGATVDHRNPSGEstasggsrdellgiTALMAAVQHGHEAVVRLL 201
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGE--------------TALHFAASNGNVEVLKLL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 283-413 1.08e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.06  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  283 RRPDIfhalkmgNFQLVKEIADEDPNhVNLVNGDGATPL--MLAAV---TGQLPLVQLLVEKHADMNKQDSvHGWT---A 354
Cdd:PHA02798  45 QRDSP-------STDIVKLFINLGAN-VNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNS-DGETplyC 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  355 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDP-DTELVRLLASVCMQVN 413
Cdd:PHA02798 116 LLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHiDIEIIKLLLEKGVDIN 175
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 101-130 1.37e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.63  E-value: 1.37e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 50400170   101 YGWSALMQAARCGHASVAHLLLDHGADVNA 130
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 774-846 1.60e-05

SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting Ankyrin Repeat-containing) proteins, also known as ANKS4B, is a protein-protein interaction domain. Proteins of this subfamily have an N-terminal ankyrin repeat region and C-terminal SAM. In mouse epithelial tissues, HARP protein interacts with the PDZ domain of harmonin. This scaffolding complex facilitates signal transduction in epithelia. HARP was found co-expressed with harmonin in a number of epithelial cells including pancreatic ductal epithelium, embryonic epithelia of the lung, kidney, salivary glands, and cochlea.


Pssm-ID: 188986  Cd Length: 67  Bit Score: 43.28  E-value: 1.60e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50400170 774 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTdGSRQQILAAISelnagkgRERQILQE 846
Cdd:cd09587   1 DATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQL-GPRKKILSAVA-------RRKQVLQQ 65
Ank_4 pfam13637
Ankyrin repeats (many copies);
9-89 1.99e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170     9 GLQLLLRACEQGDTDTARRLLEPGgepvagseagaepagpeaaraveagtpVPVDCSDEAGNSALQLAAAGGHEPLVRFL 88
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKG---------------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53


                  .
gi 50400170    89 L 89
Cdd:pfam13637  54 L 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 106-202 2.00e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  106 LMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVdhrnpsgestaSGGSRDellGITA 185
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP-----------TLLDKD---GKTP 151

                         90
                 ....*....|....*..
gi 50400170  186 LMAAVQHGHEAVVRLLM 202
Cdd:PTZ00322 152 LELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 350-379 2.13e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 2.13e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 50400170    350 HGWTALMQATYHGNKEIVKYLLNQGADVTL 379
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 49-238 2.60e-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: 2.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  49 EAARAVEAGTP-VPVDCSDE--AGNSALQLAAAGGHEPLVRFLLRRGASVNSRN-------------HYGWSALMQAARC 112
Cdd:cd21882  50 EAAPDSGNPKElVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLAACT 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 113 GHASVAHLLLDHGAD---VNAQNRLGASVLTVasrgghlgvvkLLLEAGATVDHrnpsgeSTASGGSRDELLGITAlmaa 189
Cdd:cd21882 130 NQEEIVRLLLENGAQpaaLEAQDSLGNTVLHA-----------LVLQADNTPEN------SAFVCQMYNLLLSYGA---- 188

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 50400170 190 vqHGHEAVVRLLMewgadPNHTartvGWSPLMLAALLGKLSVVQQLVEK 238
Cdd:cd21882 189 --HLDPTQQLEEI-----PNHQ----GLTPLKLAAVEGKIVMFQHILQR 226
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
782-833 2.80e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 42.64  E-value: 2.80e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50400170   782 LKKLSLEKYQPIFEEQEVD-MEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:pfam07647  13 LRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
Ank_5 pfam13857
Ankyrin repeats (many copies);
302-355 2.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 50400170   302 IADEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMNKQDSvHGWTAL 355
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 101-130 3.18e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.18e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 50400170    101 YGWSALMQAARCGHASVAHLLLDHGADVNA 130
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 60-133 3.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 3.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50400170   60 VPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNR 133
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
184-236 3.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50400170   184 TALMAAVQHGHEAVVRLLMEWGADPNHTARTvGWSPLMLAALLGKLSVVQQLV 236
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-241 3.48e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   20 GDTDTARRLLEPGGEPVAGSEAGAEPA-------GPEAARAVEAGTPVPvDCSDEAGNSALQLAAAGGHEPLVRFLLRRG 92
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIklamkfrDSEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGDVKAVEELLDLG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   93 ASVNSRNHY-GWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDhrnpsgest 171
Cdd:PHA02875  92 KFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD--------- 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  172 asggsRDELLGITALMAAVQHGHEAVVRLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEKGAN 241
Cdd:PHA02875 163 -----IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 350-377 4.16e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 4.16e-05
                          10        20
                  ....*....|....*....|....*...
gi 50400170   350 HGWTALMQATYHGNKEIVKYLLNQGADV 377
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 350-382 5.11e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 5.11e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 50400170   350 HGWTALMQATYH-GNKEIVKYLLNQGADVTLRAK 382
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
SAM_Smaug-like cd09489
SAM (Sterile alpha motif ); SAM (sterile alpha motif) domain of Smaug-like subfamily proteins ...
 782-830 6.06e-05

SAM (Sterile alpha motif ); SAM (sterile alpha motif) domain of Smaug-like subfamily proteins is an RNA binding domain. SAM interacts with stem-loop structures in target mRNAs. Proteins of this subfamily are post-transcriptional regulators involved in mRNA silencing and deadenylation; they can be implicated in transcript stability regulation and vacuolar protein transport as well. SAM_Smaug-like domain-containing proteins are found in metazoa from yeast to human. In animals they are active during early embryogenesis.


Pssm-ID: 188888  Cd Length: 57  Bit Score: 41.38  E-value: 6.06e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 50400170 782 LKKLSLEKYQPIFeeQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAI 830
Cdd:cd09489   6 LKSLRLHKYSDAF--KGTTWEELLYLTEETLEKKGVLTLGARRKLLKAF 52
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 197-377 6.72e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 6.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  197 VVRLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALdrkhrdladyldplttvrp 276
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV------------------- 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  277 ktdeEKRRPDIFHALKmgnfqlvkeiadEDPNHVNLVNGDGATPLMLAavTGQL---PLVQLLVEKHADMNKQDSVHGWT 353
Cdd:PHA02878 210 ----KHYNKPIVHILL------------ENGASTDARDKCGNTPLHIS--VGYCkdyDILKLLLEHGVDVNAKSYILGLT 271

                        170       180
                 ....*....|....*....|....
gi 50400170  354 ALMQATYhgNKEIVKYLLNQGADV 377
Cdd:PHA02878 272 ALHSSIK--SERKLKLLLEYGADI 293
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 316-347 9.03e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 9.03e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 50400170   316 DGATPLMLAAV-TGQLPLVQLLVEKHADMNKQD 347
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 782-833 9.17e-05

SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or Ubc2 for Ustilago bypass of cyclase) subfamily is a putative protein-protein interaction domain. This group includes only fungal proteins. Basidiomycetes have an N-terminal SAM domain, central UBQ domain, and C-terminal SH3 domain, while Ascomycetes lack the SH3 domain. Ubc2 of Ustilago maydis is a major virulence and maize pathogenicity factor. It is required for filamentous growth (the budding haploid form of Ustilago maydis is a saprophyte, while filamentous dikaryotic form is a pathogen). Also the Ubc2 protein is involved in the pheromone-responsive morphogenesis via the MAP kinase cascade. The SAM domain is necessary for ubc2 function; deletion of SAM eliminates this function. A Lys-to-Glu mutation in the SAM domain of ubc2 gene induces temperature sensitivity.


Pssm-ID: 188932  Cd Length: 58  Bit Score: 41.15  E-value: 9.17e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 50400170 782 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:cd09533   6 LSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYEL 57
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-209 9.84e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 9.84e-05
                           10        20
                   ....*....|....*....|....*...
gi 50400170    182 GITALMAAVQHGHEAVVRLLMEWGADPN 209
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-211 1.05e-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: 39.97  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 50400170   182 GITALMAAV-QHGHEAVVRLLMEWGADPNHT 211
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 69-100 1.12e-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: 39.97  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 50400170    69 GNSALQLAAA-GGHEPLVRFLLRRGASVNSRNH 100
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
SAM_ZCCH14 cd09558
SAM domain of ZCCH14 subfamily; SAM (sterile alpha motif) domain of ZCCH14 (Zinc finger CCHC ...
 777-826 1.42e-04

SAM domain of ZCCH14 subfamily; SAM (sterile alpha motif) domain of ZCCH14 (Zinc finger CCHC domain 14) protein subfamily (also known as BDG-29 or KIAA0579) is a putative RNA binding domain. Members of this group are believed to be involved in post-translational regulation during early embryogenesis.


Pssm-ID: 188957  Cd Length: 65  Bit Score: 40.84  E-value: 1.42e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 50400170 777 ELTGIL---KKLSLEKYQPIFeeQEVDMEAFLTLTDGDLQELGIKTDGSRQQI 826
Cdd:cd09558   4 EQNGILdwlRKLRLHKYYPVF--KQLTMEKFLSLTEEDLNKFESLTMGAKKKL 54
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 775-833 1.83e-04

SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins is a putative protein-protein interaction domain. Proteins of this group contain multiple domains: SAM, one or more WD40 repeats and U-box (derived version of the RING-finger domain). Apparently the WDSUB1 subfamily proteins participate in protein degradation through ubiquitination, since U-box domain are known as a member of E3 ubiquitin ligase family, while SAM and WD40 domains most probably are responsible for an E2 ubiquitin-conjugating enzyme binding and a target protein binding.


Pssm-ID: 188904  Cd Length: 72  Bit Score: 40.38  E-value: 1.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170 775 EDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQ-ELGIKTDGSRQQILAAISEL 833
Cdd:cd09505   7 EEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLSkDLKIESLGHRNKILRKIEEL 66
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-106 2.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 50400170    59 PVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSAL 106
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 782-834 2.60e-04

SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188897  Cd Length: 71  Bit Score: 39.97  E-value: 2.60e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 50400170 782 LKKLSLEKYQPIFEEQEVD-MEAFLTLTDGDLQELGIKTDGSRQQILAAISELN 834
Cdd:cd09498  14 LSLLGLPQYHKVLVENGYDsIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLK 67
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 199-268 2.88e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 2.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50400170  199 RLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEK-GANPDHLGVLEKTAFEVALDRKHRDLADYL 268
Cdd:PHA02736  75 KLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
SAM_Smaug cd09557
SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA ...
 782-833 3.39e-04

SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA recognition domain. It binds a specific RNA motif known as Smaug recognition element (SRE). Among members of this group are invertebrate Smaug (Smg) proteins and vertebrate Smaug1 and Smaug2 proteins. They are involved in post-transcriptional control during early embryogenesis in animals. In Drosophila, Smaug protein is a translational repressor of mRNA of Nanos (Nos) protein. Gradient of Nanos is required for proper abdominal segmentation. SAM domain interacts specifically with the Nanos mRNA regulatory regions. Moreover, Smaug protein is involved in regulation of specific maternal transcripts degradation in Drosophila early embryo via recruitment of the CCR4/POP2/NOT deadenylase.


Pssm-ID: 188956  Cd Length: 63  Bit Score: 39.62  E-value: 3.39e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 50400170 782 LKKLSLEKYQPIFeeQEVDMEAFLTLTDGDLQELGIkTDGSRQQILAAISEL 833
Cdd:cd09557  13 LKSLRLHKYASLF--SQMTYEEMLNLTEEQLEAQGV-TKGARHKIALSIQKL 61
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-170 3.52e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 50400170   121 LLDHG-ADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGES 170
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLT 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
351-405 4.07e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 4.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 50400170   351 GWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVmLLNDpDTELVRLL 405
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA-ASNG-NVEVLKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-210 4.51e-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: 38.39  E-value: 4.51e-04
                          10        20
                  ....*....|....*....|....*....
gi 50400170   182 GITALMAAVQHGHEAVVRLLMEWGADPNH 210
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
287-337 4.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 50400170   287 IFHALKMGNFQLVKEIAdEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLV 337
Cdd:pfam13637   5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 115-240 5.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  115 ASVAHLLLDHGADVNAQNR-LGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGEStasggsrdellgitALMAAVQHG 193
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS--------------PLHHAVKHY 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 50400170  194 HEAVVRLLMEWGADPNHTARtVGWSPLMLA-ALLGKLSVVQQLVEKGA 240
Cdd:PHA02878 213 NKPIVHILLENGASTDARDK-CGNTPLHISvGYCKDYDILKLLLEHGV 259
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-244 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: 37.62  E-value: 6.49e-04
                          10        20
                  ....*....|....*....|....*....
gi 50400170   216 GWSPLMLAALLGKLSVVQQLVEKGANPDH 244
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 286-390 8.68e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.18  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  286 DIFH-ALKMGNFQLVKEIADEDPNH-----VNLVNGDGATPLMLAAVTGQ----LPLVQLLVEKHADMNKQDSVHGWTAL 355
Cdd:PHA02741  23 NFFHeAARCGCFDIIARFTPFIRGDchaaaLNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMLEGDTAL 102

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 50400170  356 MQATYHGNKEIVKYLLNQ-GADVTLRAKNGYTAFDL 390
Cdd:PHA02741 103 HLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFEL 138
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 48-139 8.78e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 8.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170    48 PEAARAVEAGTP--VPVDCSDE--AGNSALQLAAAGGHEPLVRFLLRRGASVNSRNH--------------YGWSALMQA 109
Cdd:TIGR00870 103 HLLAAFRKSGPLelANDQYTSEftPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAA 182

                          90       100       110
                  ....*....|....*....|....*....|
gi 50400170   110 ARCGHASVAHLLLDHGADVNAQNRLGASVL 139
Cdd:TIGR00870 183 ACLGSPSIVALLSEDPADILTADSLGNTLL 212
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 316-345 1.72e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.72e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 50400170    316 DGATPLMLAAVTGQLPLVQLLVEKHADMNK 345
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-243 1.74e-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: 36.50  E-value: 1.74e-03
                          10        20
                  ....*....|....*....|....*....
gi 50400170   216 GWSPLMLAAL-LGKLSVVQQLVEKGANPD 243
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 778-836 1.89e-03

SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 subfamily is a protein-protein interaction domain. In addition to the SAM domain, proteins of this group have ankyrin repeats and a ADP- ribosyltransferase (poly-(ADP-ribose) synthase) domain. Tankyrases can polymerize through their SAM domains forming homoligomers and these complexes are disrupted by autoribosylation. Tankyrases apparently act as master scaffolding proteins and thus may interact simultaneously with multiple proteins, in particular with TRF1, NuMA, IRAP and Grb14 (ankyrin repeats are involved in these interactions). Tankyrases participate in a variety of cell signaling pathways as effector molecules. Their functions are different depending on the intracellular location: at telomeres they play a role in the regulation of telomere length via control of telomerase access to telomeres, at centrosomes they promote spindle assembly/disassembly, in Golgi vesicles they participate in the regulation of vesicle trafficking and Golgi dynamics. Tankyrase 1 may be of interest as new potential target for telomerase-directed cancer therapy.


Pssm-ID: 188923  Cd Length: 66  Bit Score: 37.69  E-value: 1.89e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50400170 778 LTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNAG 836
Cdd:cd09524   8 ISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 301-409 2.00e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  301 EIADEDPNHvNLVNGDGATPL---MLA------AVTGQLPLVQLLVEKHADMNKQDsVHGWTALMQATYHGNKEIVKYLL 371
Cdd:PTZ00322  58 ENKDATPDH-NLTTEEVIDPVvahMLTvelcqlAASGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLL 135

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 50400170  372 NQGADVTLRAKNGYTAFDLVMllNDPDTELVRLLASVC 409
Cdd:PTZ00322 136 EFGADPTLLDKDGKTPLELAE--ENGFREVVQLLSRHS 171
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 69-96 2.09e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 2.09e-03
                          10        20
                  ....*....|....*....|....*...
gi 50400170    69 GNSALQLAAAGGHEPLVRFLLRRGASVN 96
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 216-422 2.32e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   216 GWSPLMLAAllgKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYLDPLTTVRPKTdeekrrpdifhalkmGN 295
Cdd:TIGR00870  52 GRSALFVAA---IENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKS---------------GP 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   296 FQLVKEIADEDPNHvnlvngdGATPLMLAAVTGQLPLVQLLVEKHADMN------------KQDSV-HGWTALMQATYHG 362
Cdd:TIGR00870 114 LELANDQYTSEFTP-------GITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFyHGESPLNAAACLG 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   363 NKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTElVRLLASVCMQVNKDRGGRPSH 422
Cdd:TIGR00870 187 SPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAE-YEELSCQMYNFALSLLDKLRD 245
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 329-399 2.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 2.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50400170  329 QLPLVQLLVEKHADMNKQDsVHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDT 399
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
SAM_VTS1_fungal cd09556
SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily ...
 782-829 2.77e-03

SAM domain of VTS1 RNA-binding proteins; SAM (sterile alpha motif) domain of VTS1 subfamily proteins is RNA binding domain located in the C-terminal region. SAM interacts with stem-loop structures of mRNA. Proteins of this subfamily participate in regulation of transcript stability and degradation, and also may be involved in vacuolar protein transport regulation. VTS1 protein of S.cerevisiae induces mRNA degradation via the major deadenylation-dependent mRNA decay pathway; VTS1 recruits CCR4/POP2/NOT deadenylase complex to target mRNA. The recruitment is the initial step resulting in poly(A) tail removal transcripts. Potentially SAM domain may be responsible not only for RNA binding but also for deadenylase binding.


Pssm-ID: 188955  Cd Length: 69  Bit Score: 37.28  E-value: 2.77e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 50400170 782 LKKLSLEKYQPIFEEqeVDMEAFLTLTDGDLQELGIKTDGSRQQILAA 829
Cdd:cd09556  13 LRSLRLHKYTDNLKD--LSWKELIELDDEDLEDKGVSALGARRKLLKA 58
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 776-833 3.13e-03

SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK-delta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. In particular DGK-delta is involved in the regulation of clathrin-dependent endocytosis. The SAM domain of DGK-delta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-eta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it inhibits the translocation of the protein to the plasma membrane from the cytoplasm. The SAM domain also can bind Zn at multiple (not conserved) sites driving the formation of highly ordered large sheets of polymers, thus suggesting that Zn may play important role in the function of DCK-delta.


Pssm-ID: 188974  Cd Length: 65  Bit Score: 36.85  E-value: 3.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50400170 776 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:cd09575   8 EEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_DGK-eta cd09576
SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ...
 776-833 3.38e-03

SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases. The SAM domain is located at the C-terminus of two out of three isoforms of DGK-eta protein. DGK-eta proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DCK-eta proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers with the SAM domain of DGK-delta proteins. The oligomerization plays a role in the regulation of the DGK-delta intracellular localization: it is responsible for sustained endosomal localization of the protein and resulted in negative regulation of DCK-eta catalytic activity.


Pssm-ID: 188975  Cd Length: 65  Bit Score: 36.87  E-value: 3.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50400170 776 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:cd09576   8 DEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL 65
SAM_USH1G cd09586
SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) ...
 774-846 3.66e-03

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.


Pssm-ID: 188985  Cd Length: 66  Bit Score: 36.69  E-value: 3.66e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50400170 774 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTdGSRQQILAAISelnagkgRERQILQE 846
Cdd:cd09586   1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPL-GPRKKILDACQ-------RRRQTIER 65
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 772-835 4.67e-03

SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 proteins is a protein-protein interaction domain. Caskin has two tandem SAM domains. Caskin protein is known to interact with membrane-associated guanylate kinase CASK, and apparently may play a role in neural development, synaptic protein targeting, and regulation of gene expression.


Pssm-ID: 188896  Cd Length: 66  Bit Score: 36.47  E-value: 4.67e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50400170 772 ITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNA 835
Cdd:cd09497   1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQI 64
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 294-379 4.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170  294 GNFQLVKEIADEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMNKQDSvHGWTALMQATYHGNKEIVKYLLNQ 373
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINT-KIPHPLLTAIKIGAHDIIKLLIDN 90


                 ....*.
gi 50400170  374 GADVTL 379
Cdd:PHA02874  91 GVDTSI 96
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-243 4.91e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 4.91e-03
                           10        20
                   ....*....|....*....|....*...
gi 50400170    216 GWSPLMLAALLGKLSVVQQLVEKGANPD 243
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-142 5.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50400170   62 VDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTV 141
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229


                 .
gi 50400170  142 A 142
Cdd:PHA02874 230 A 230
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 776-833 5.40e-03

SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 family proteins is a protein-protein interaction domain. Shank1,2,3 proteins are scaffold proteins that are known to interact with a variety of cytoplasmic and membrane proteins. SAM domains of the Shank1,2,3 family are prone to homooligomerization. They are highly enriched in the postsynaptic density, acting as scaffolds to organize assembly of postsynaptic proteins. SAM domains of Shank3 proteins can form large sheets of helical fibers. Shank genes show distinct patterns of expression, in rat Shank1 mRNA is found almost exclusively in brain, Shank2 in brain, kidney and liver, and Shank3 in heart, brain and spleen.


Pssm-ID: 188905  Cd Length: 66  Bit Score: 36.14  E-value: 5.40e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50400170 776 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:cd09506   8 DDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 776-833 7.85e-03

SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain of DGK-eta-delta subfamily proteins is a protein-protein interaction domain. Proteins of this subfamily are multidomain diacylglycerol kinases with a SAM domain located at the C-terminus. DGK proteins participate in signal transduction. They regulate the level of second messengers such as diacylglycerol and phosphatidic acid. The SAM domain of DGK proteins can form high molecular weight homooligomers through head-to-tail interactions as well as heterooligomers between the SAM domains of DGK delta and eta proteins. The oligomerization plays a role in the regulation of DGK intracellular localization.


Pssm-ID: 188906  Cd Length: 65  Bit Score: 35.85  E-value: 7.85e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50400170 776 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISEL 833
Cdd:cd09507   8 EEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
 
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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