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Conserved domains on  [gi|1622871988|ref|XP_028690863|]
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ankyrin repeat and SAM domain-containing protein 6 isoform X3 [Macaca mulatta]

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];
74-277 7.92e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 7.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  74 SDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASR 153
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 154 GGHLGVVKLLLEAGAFVDHHHPSGEqlglggnrdepldiTALMAAIQHGHEAVVRLLMEWGADPNRAARTvGWSPLMLAA 233
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGN--------------TPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAA 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622871988 234 LTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRDLVDYL 277
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 773-837 2.58e-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: 136.54  E-value: 2.58e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622871988 773 TITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNA 837
Cdd:cd09518     1 TITEEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
296-389 3.67e-20

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 296 IFHALKMGNFQLVKEIADEdPSHVNLVNGDGATPLMLAAVTGQLALVQLLVErHADVDKQDsvHGWTALMQATYHGNKEI 375
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD--NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 1622871988 376 VKYLLNQGADVTLR 389
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
364-427 1.23e-07

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 1.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 364 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAfdLVMLLNDPDTELVRLLASVCMQVNKDKGR 427
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA--LHLAAKNGHLEIVKLLLEHADVNLKDNGR 62
Ank_4 pfam13637
Ankyrin repeats (many copies);
12-98 1.19e-03

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  12 LLLRACDQGDTETARRLLEPGAaepaergaepeagaepvgaeaagpgaaaaaavgapvPVDCSDEAGNTALQFAAAGGHE 91
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGA------------------------------------DINAVDGNGETALHFAASNGNV 47


                  ....*..
gi 1622871988  92 PLVRFLL 98
Cdd:pfam13637  48 EVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-277 7.92e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 7.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  74 SDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASR 153
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 154 GGHLGVVKLLLEAGAFVDHHHPSGEqlglggnrdepldiTALMAAIQHGHEAVVRLLMEWGADPNRAARTvGWSPLMLAA 233
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGN--------------TPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAA 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622871988 234 LTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRDLVDYL 277
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 773-837 2.58e-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: 136.54  E-value: 2.58e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622871988 773 TITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNA 837
Cdd:cd09518     1 TITEEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-405 4.83e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 4.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  94 VRFLLRRGASVNSRNHYGWSALMQAARFGH---VSVAHLLLDHGADVNAQNRLGASVL-TVASRGGHLGVVKLLLEAGAF 169
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 170 VDHHHpsgeqlglgGNRDEPLDITALMAAIqhgHEAVVRLLMEWGADPNrAARTVGWSPLmlAALtgrlgvaqqLVEKGA 249
Cdd:PHA03095  110 VNAKD---------KVGRTPLHVYLSGFNI---NPKVIRLLLRKGADVN-ALDLYGMTPL--AVL---------LKSRNA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 250 NPDHLSVL-EKTAFEVALDCKHRDLVDYLdpMTTVRPktdeekrRPDIFHALKMgnfqlvkeiADEDPSHVNLVngdGAT 328
Cdd:PHA03095  166 NVELLRLLiDAGADVYAVDDRFRSLLHHH--LQSFKP-------RARIVRELIR---------AGCDPAATDML---GNT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 329 PLMLAAVTGQLA--LVQLLVERHADVDKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLvMLLND 405
Cdd:PHA03095  225 PLHSMATGSSCKrsLVLPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL-MVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
296-389 3.67e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 296 IFHALKMGNFQLVKEIADEdPSHVNLVNGDGATPLMLAAVTGQLALVQLLVErHADVDKQDsvHGWTALMQATYHGNKEI 375
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD--NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 1622871988 376 VKYLLNQGADVTLR 389
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-219 1.00e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 115 LMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEagafvdhhHPSGEQLGLGGnrdepldiTA 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--------HADVNLKDNGR--------TA 64

                          90       100
                  ....*....|....*....|....*
gi 1622871988 195 LMAAIQHGHEAVVRLLMEWGADPNR 219
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 301-395 8.69e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 8.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 301 KMGNFQLVKEIADEDpSHVNLVNGDGATPLMLAA--VTGQLALVQLLVERHADVDKQDSV---------------HGWTA 363
Cdd:PHA03100  117 KSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVnyllsygvpinikdvYGFTP 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622871988 364 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYT 395
Cdd:PHA03100  196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 776-835 3.59e-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: 56.54  E-value: 3.59e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622871988  776 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDG-DLKELGIKTDGSRQQILAAISEL 835
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGITKLGHRKKILKAIQKL 65
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 784-835 2.75e-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: 53.81  E-value: 2.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622871988 784 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:pfam00536  12 LESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-247 2.45e-08

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: 57.72  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  77 AGNTALQFAAAGGHEPLVRFLLRRGASVNS------------RN--HYGWSALMQAARFGHVSVAHLLLDHGADVNAQNR 142
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 143 LGASVLtvasrgghlgvvkllleagafvdHHhpsgeqLGLGGNRD---EPLDItaLMAAIQHGHEAVVRLLmewgadPNR 219
Cdd:cd22192   168 LGNTVL-----------------------HI------LVLQPNKTfacQMYDL--ILSYDKEDDLQPLDLV------PNN 210

                         170       180
                  ....*....|....*....|....*...
gi 1622871988 220 AartvGWSPLMLAALTGRLGVAQQLVEK 247
Cdd:cd22192   211 Q----GLTPFKLAAKEGNIVMFQHLVQK 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
364-427 1.23e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 1.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 364 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAfdLVMLLNDPDTELVRLLASVCMQVNKDKGR 427
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA--LHLAAKNGHLEIVKLLLEHADVNLKDNGR 62
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 298-411 1.19e-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: 52.32  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 298 HALKMGNFQLVKEIADEDPSHVNL-VNGD---GATPLMLAAVTGQLALVQLLVERHADVDK-----------QDSV--HG 360
Cdd:cd22192    57 VAALYDNLEAAVVLMEAAPELVNEpMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyYG 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 361 WTALMQATYHGNKEIVKYLLNQGADvtLRAKNGYTAFDLVMLLNDPDTELV 411
Cdd:cd22192   137 EHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLGNTVLHILVLQPNKTFA 185
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-139 1.91e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.91e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622871988  110 YGWSALMQAARFGHVSVAHLLLDHGADVNA 139
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 359-388 2.10e-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: 2.10e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622871988  359 HGWTALMQATYHGNKEIVKYLLNQGADVTL 388
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
12-98 1.19e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  12 LLLRACDQGDTETARRLLEPGAaepaergaepeagaepvgaeaagpgaaaaaavgapvPVDCSDEAGNTALQFAAAGGHE 91
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGA------------------------------------DINAVDGNGETALHFAASNGNV 47


                  ....*..
gi 1622871988  92 PLVRFLL 98
Cdd:pfam13637  48 EVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 73-148 2.06e-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: 41.99  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  73 CSDE--AGNTALQFAAAGGHEPLVRFLLRRGASVNSRNH--------------YGWSALMQAARFGHVSVAHLLLDHGAD 136
Cdd:TIGR00870 121 YTSEftPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPAD 200

                          90
                  ....*....|..
gi 1622871988 137 VNAQNRLGASVL 148
Cdd:TIGR00870 201 ILTADSLGNTLL 212
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-277 7.92e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 7.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  74 SDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASR 153
Cdd:COG0666    50 ADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 154 GGHLGVVKLLLEAGAFVDHHHPSGEqlglggnrdepldiTALMAAIQHGHEAVVRLLMEWGADPNRAARTvGWSPLMLAA 233
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGN--------------TPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAA 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622871988 234 LTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRDLVDYL 277
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
72-415 9.07e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 9.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  72 DCSDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVA 151
Cdd:COG0666    15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 152 SRGGHLGVVKLLLEAGAFVDHHHPSGEqlglggnrdepldiTALMAAIQHGHEAVVRLLMEWGADPNRAARTvGWSPLML 231
Cdd:COG0666    95 ARNGDLEIVKLLLEAGADVNARDKDGE--------------TPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 232 AALTGRLGVAQQLVEKGANpdhlsvlektafevaldckhrdlvdyldpmttvrpktdeekrrpdifhalkmgnfqlvkei 311
Cdd:COG0666   160 AAANGNLEIVKLLLEAGAD------------------------------------------------------------- 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 312 adedpshVNLVNGDGATPLMLAAVTGQLALVQLLVERHADVDKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAK 391
Cdd:COG0666   179 -------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         330       340
                  ....*....|....*....|....
gi 1622871988 392 NGYTAFDLVMLLNDPDTELVRLLA 415
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-250 4.46e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 4.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  12 LLLRACDQGDTETARRLLEpgaaepaeRGAEPEAgaepvgaeaagpgaaaaaavgapvpvdcSDEAGNTALQFAAAGGHE 91
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLE--------AGADVNA----------------------------RDKDGETPLHLAAYNGNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  92 PLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVD 171
Cdd:COG0666   134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 172 HHHPSGEqlglggnrdepldiTALMAAIQHGHEAVVRLLMEWGADPNRAARTvGWSPLMLAALTGRLGVAQQLVEKGAN 250
Cdd:COG0666   214 AKDNDGK--------------TALDLAAENGNLEIVKLLLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-415 3.24e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 3.24e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  93 LVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVdh 172
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI-- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 173 hhpsgeqlglggNRDEPLDITALMAAIQHGHEAVVRLLMEWGADPNrAARTVGWSPLMLAALTGRLGVAQQLVEKGANpd 252
Cdd:COG0666    81 ------------NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGAD-- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 253 hlsvlektafevaldckhrdlvdyldpmttvrpktdeekrrpdifhalkmgnfqlvkeiadedpshVNLVNGDGATPLML 332
Cdd:COG0666   146 ------------------------------------------------------------------VNAQDNDGNTPLHL 159

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 333 AAVTGQLALVQLLVERHADVDKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVR 412
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238


                  ...
gi 1622871988 413 LLA 415
Cdd:COG0666   239 LEA 241
SAM_ANKS6 cd09518
SAM domain of ANKS6 (or SamCystin) subfamily; SAM (sterile alpha motif) domain of ANKS6 (or ...
 773-837 2.58e-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: 136.54  E-value: 2.58e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622871988 773 TITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNA 837
Cdd:cd09518     1 TITEEDELSGILRKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGPRQQILAAISELNA 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-405 4.83e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 4.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  94 VRFLLRRGASVNSRNHYGWSALMQAARFGH---VSVAHLLLDHGADVNAQNRLGASVL-TVASRGGHLGVVKLLLEAGAF 169
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 170 VDHHHpsgeqlglgGNRDEPLDITALMAAIqhgHEAVVRLLMEWGADPNrAARTVGWSPLmlAALtgrlgvaqqLVEKGA 249
Cdd:PHA03095  110 VNAKD---------KVGRTPLHVYLSGFNI---NPKVIRLLLRKGADVN-ALDLYGMTPL--AVL---------LKSRNA 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 250 NPDHLSVL-EKTAFEVALDCKHRDLVDYLdpMTTVRPktdeekrRPDIFHALKMgnfqlvkeiADEDPSHVNLVngdGAT 328
Cdd:PHA03095  166 NVELLRLLiDAGADVYAVDDRFRSLLHHH--LQSFKP-------RARIVRELIR---------AGCDPAATDML---GNT 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 329 PLMLAAVTGQLA--LVQLLVERHADVDKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLvMLLND 405
Cdd:PHA03095  225 PLHSMATGSSCKrsLVLPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL-MVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
296-389 3.67e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 296 IFHALKMGNFQLVKEIADEdPSHVNLVNGDGATPLMLAAVTGQLALVQLLVErHADVDKQDsvHGWTALMQATYHGNKEI 375
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD--NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 1622871988 376 VKYLLNQGADVTLR 389
Cdd:pfam12796  77 VKLLLEKGADINVK 90
SAM_BICC1 cd09520
SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) ...
 778-837 5.36e-20

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: 84.27  E-value: 5.36e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 778 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNA 837
Cdd:cd09520     5 SDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGITAFGARRKMLLAISELNK 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-219 1.00e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 115 LMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEagafvdhhHPSGEQLGLGGnrdepldiTA 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--------HADVNLKDNGR--------TA 64

                          90       100
                  ....*....|....*....|....*
gi 1622871988 195 LMAAIQHGHEAVVRLLMEWGADPNR 219
Cdd:pfam12796  65 LHYAARSGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-171 1.16e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  82 LQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHgADVNAQNRlGASVLTVASRGGHLGVVK 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 1622871988 162 LLLEAGAFVD 171
Cdd:pfam12796  79 LLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-252 9.00e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 9.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 148 LTVASRGGHLGVVKLLLEAGAFVDHHHPSGEqlglggnrdepldiTALMAAIQHGHEAVVRLLMEwGADPNraARTVGWS 227
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR--------------TALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRT 63

                          90       100
                  ....*....|....*....|....*
gi 1622871988 228 PLMLAALTGRLGVAQQLVEKGANPD 252
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-141 2.06e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  13 LLRACDQGDTETARRLLEPGAAepaergaepeagaepvgaeaagpgaaaaaavgapvpVDCSDEAGNTALQFAAAGGHEP 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------------------------------------ANLQDKNGRTALHLAAKNGHLE 44

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622871988  93 LVRFLLRRgASVNSRNhYGWSALMQAARFGHVSVAHLLLDHGADVNAQN 141
Cdd:pfam12796  45 IVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 779-837 3.02e-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: 65.21  E-value: 3.02e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 779 ELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNA 837
Cdd:cd09519     6 DLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGITLFGPKRKMTSAIARWHS 64
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 784-834 3.62e-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: 3.62e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 784 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISE 834
Cdd:cd09487     6 LESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGHRKKILRAIQR 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-254 1.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  75 DEAGNTALQFAAAG--GHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHV--SVAHLLLDHGADVNAQNRlgasvltv 150
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-------- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 151 asrgghlgvVKLLLEAGAFVDhhhpsgeqlglggNRDEpLDITALMAAIQHGHEAVVRLLMEWGADPNraARTV-GWSPL 229
Cdd:PHA03100  175 ---------VNYLLSYGVPIN-------------IKDV-YGFTPLHYAVYNNNPEFVKYLLDLGANPN--LVNKyGDTPL 229

                         170       180
                  ....*....|....*....|....*
gi 1622871988 230 MLAALTGRLGVAQQLVEKGANPDHL 254
Cdd:PHA03100  230 HIAILNNNKEIFKLLLNNGPSIKTI 254
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 78-252 2.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  78 GNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVA-SRGGH 156
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKD 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 157 LGVVKLLLEAGAFVDhhhpsgeqlglggNRDEPLDITALMAAIQhgHEAVVRLLMEWGADPNraarTVGW---SPLMLAA 233
Cdd:PHA02878  248 YDILKLLLEHGVDVN-------------AKSYILGLTALHSSIK--SERKLKLLLEYGADIN----SLNSyklTPLSSAV 308

                         170       180
                  ....*....|....*....|....*
gi 1622871988 234 LT------GRLGVAQQLVEKGANPD 252
Cdd:PHA02878  309 KQylciniGRILISNICLLKRIKPD 333
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 72-231 3.01e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  72 DCSDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQnrLGASVLTVA 151
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTA 629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 152 SRGGHLGVVKLLLEAGAFVDHHHPSGeqlglggnrdepldITALMAAIQHGHEAVVRLLMEWGADPNRAARTVGWSPLML 231
Cdd:PLN03192  630 AKRNDLTAMKELLKQGLNVDSEDHQG--------------ATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-356 5.38e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 5.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 229 LMLAALTGRLGVAQQLVEKGANPDHLSVLEKTAfevaldckhrdlvdyldpmttvrpktdeekrrpdIFHALKMGNFQLV 308
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA----------------------------------LHLAAKNGHLEIV 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622871988 309 KEIADedpsHVNL-VNGDGATPLMLAAVTGQLALVQLLVERHADVDKQD 356
Cdd:pfam12796  47 KLLLE----HADVnLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-131 6.86e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 6.86e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622871988  78 GNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLL 131
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-164 8.67e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 8.67e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 111 GWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLL 164
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 91-275 1.88e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  91 EPLVRFLLRRGASVNSRNHYGWSALMQAAR--FGHVSVAHLLLDHGADVNAQNRLGASVLTV--ASRGGHLGVVKLLLEA 166
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 167 GAF---VD-------HHH-----PSGE------QLGLGGNRDEPLDITAL--MAAIQHGHEAVVRLLMEWGADPNRAART 223
Cdd:PHA03095  177 GADvyaVDdrfrsllHHHlqsfkPRARivreliRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRY 256

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622871988 224 vGWSPLMLAALTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRDLVD 275
Cdd:PHA03095  257 -GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 114-427 2.41e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 114 ALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVDHHHPSGEqlglggnrdepldiT 193
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE--------------S 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 194 ALMAAIQHGHEAVVRLLMEWGADPNRAARTVGWSPLMLAALTGRLGVAQQLVEKGANPDhlsvlektafevaldckhrdl 273
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD--------------------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 274 vdyldpmttvRPKTDeekRRPDIFHALKMGNFQLVKEIADEDPShVNLVNGDGATPLMLAAVTGQLALVQLLVERHADVD 353
Cdd:PHA02875  130 ----------IPNTD---KFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 354 KQDSVHGWTALMQATYHGNKEIVKYLLNQGAD---VTLRAKNGYTAFDLV--MLLNdPDTELV-RLLASVCMQVNKDKGR 427
Cdd:PHA02875  196 YFGKNGCVAALCYAIENNKIDIVRLFIKRGADcniMFMIEGEECTILDMIcnMCTN-LESEAIdALIADIAIRIHKKTIR 274
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 192-411 3.33e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 192 ITALMAAIQHGHEAVVRLLMEWGADPNRAARTVGwSPLMLAALTGRLGVAQQLVEKGANPDHLSV--LEKTAFEVALDCK 269
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIP-HPLLTAIKIGAHDIIKLLIDNGVDTSILPIpcIEKDMIKTILDCG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 270 hrdlvdyldpmttVRPKTDEEKRRPDIFHALKMGNFQLVKEIAdEDPSHVNLVNGDGATPLMLAAVTGQLALVQLLVERH 349
Cdd:PHA02874  115 -------------IDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622871988 350 ADVDKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELV 411
Cdd:PHA02874  181 AYANVKDN-NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELL 241
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-425 3.93e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 3.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 113 SALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGafVDHHH---PSGEQLGLGGNRDEP 189
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDTSIlpiPCIEKDMIKTILDCG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 190 LDI--------TALMAAIQHGHEAVVRLLMEWGADPNrAARTVGWSPLMLAALTGRLGVAQQLVEKGAnpdHLSVlekta 261
Cdd:PHA02874  115 IDVnikdaelkTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGA---YANV----- 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 262 fevaldckhrdlvdyldpmttvrpkTDEEKRRPdIFHALKMGNFQLVKEIADeDPSHVNLVNGDGATPLMLAAVTGQlAL 341
Cdd:PHA02874  186 -------------------------KDNNGESP-LHNAAEYGDYACIKLLID-HGNHIMNKCKNGFTPLHNAIIHNR-SA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 342 VQLLVErHADVDKQDsVHGWTALMQA-TYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMQ 420
Cdd:PHA02874  238 IELLIN-NASINDQD-IDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLI 315


                  ....*
gi 1622871988 421 VNKDK 425
Cdd:PHA02874  316 KEADK 320
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 301-395 8.69e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 8.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 301 KMGNFQLVKEIADEDpSHVNLVNGDGATPLMLAA--VTGQLALVQLLVERHADVDKQDSV---------------HGWTA 363
Cdd:PHA03100  117 KSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVnyllsygvpinikdvYGFTP 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622871988 364 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYT 395
Cdd:PHA03100  196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 776-835 3.59e-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: 56.54  E-value: 3.59e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622871988  776 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDG-DLKELGIKTDGSRQQILAAISEL 835
Cdd:smart00454   5 SPESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGITKLGHRKKILKAIQKL 65
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 78-218 5.67e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 5.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  78 GNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHL 157
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 158 GVVKLLLEAGAFVDHHHPSGeqlglggnrdeplDITALMAAIQHGHEAVVRLLMEWGADPN 218
Cdd:PHA02875  182 AICKMLLDSGANIDYFGKNG-------------CVAALCYAIENNKIDIVRLFIKRGADCN 229
SAM_sec23ip-like cd09516
SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 ...
 776-834 1.25e-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: 55.11  E-value: 1.25e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 776 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTdGSRQQILAAISE 834
Cdd:cd09516     8 EPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPM-GPRKKLLGFLKD 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 93-274 1.54e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  93 LVRFLLRRGASVNSRNHYGWSALMQAARFGHVS-----VAHLLLDHGADVNAQNRLGASVLTVAS--RGGHLGVVKLLLE 165
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 166 AGAFVDHHHPSGEQL---GLGGNRDEpLDITALMaaIQHGH----EAVVRLLMEWGADPNrAARTVGWSPLMLAALTGRL 238
Cdd:PHA03100  130 NGANVNIKNSDGENLlhlYLESNKID-LKILKLL--IDKGVdinaKNRVNYLLSYGVPIN-IKDVYGFTPLHYAVYNNNP 205

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622871988 239 GVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRDLV 274
Cdd:PHA03100  206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
328-380 1.55e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 328 TPLMLAAVTGQLALVQLLVERHADVDKQDSvHGWTALMQATYHGNKEIVKYLL 380
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 784-835 2.75e-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: 53.81  E-value: 2.75e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622871988 784 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:pfam00536  12 LESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLGHRKKILYAIQRL 63
SAM_DDHD2 cd09585
SAM domain of DDHD2; SAM (sterile alpha motif) domain of DDHD2 group is a potential ...
 776-833 3.15e-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: 3.15e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622871988 776 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTdGSRQQILAAIS 833
Cdd:cd09585     8 DTPTLEETLKKLGLSEYCDVFEKEKIDLEALALCQERDLKDLGIPL-GPRKKILNYIR 64
SAM_TAL cd09523
SAM domain of TAL subfamily; SAM (sterile alpha motif) domain of TAL (Tsg101-associated ligase) ...
 777-835 4.59e-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: 53.45  E-value: 4.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 777 EDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:cd09523     5 DPQLVNLLNELSAEHYLPVFARHRITMETLSTMTDEDLKKIGIHEIGLRKEILRAAQEL 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-247 2.45e-08

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: 57.72  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  77 AGNTALQFAAAGGHEPLVRFLLRRGASVNS------------RN--HYGWSALMQAARFGHVSVAHLLLDHGADVNAQNR 142
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgpKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 143 LGASVLtvasrgghlgvvkllleagafvdHHhpsgeqLGLGGNRD---EPLDItaLMAAIQHGHEAVVRLLmewgadPNR 219
Cdd:cd22192   168 LGNTVL-----------------------HI------LVLQPNKTfacQMYDL--ILSYDKEDDLQPLDLV------PNN 210

                         170       180
                  ....*....|....*....|....*...
gi 1622871988 220 AartvGWSPLMLAALTGRLGVAQQLVEK 247
Cdd:cd22192   211 Q----GLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 86-164 2.90e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 2.90e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988  86 AAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLL 164
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-469 3.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  93 LVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVK----------- 161
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsnink 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 162 ------------------LLLEAGAFVDH---------HH----PSGEQL-------GLGGNRDEPLDITALMAAIQHGH 203
Cdd:PHA02876  240 ndlsllkairnedletslLLYDAGFSVNSiddckntplHHasqaPSLSRLvpkllerGADVNAKNIKGETPLYLMAKNGY 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 204 EAV-VRLLMEWGADPNrAARTVGWSPLMLAALTGRL-GVAQQLVEKGANPDHLSVLEKTAFEVALDCKH----RDLVDYL 277
Cdd:PHA02876  320 DTEnIRTLIMLGADVN-AADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNvviiNTLLDYG 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 278 DPMTTVRPKTDEekrrpdIFHALKMGN--FQLVKEIADEDpSHVNLVNGDGATPLMLAAVTG-QLALVQLLVERHADVDK 354
Cdd:PHA02876  399 ADIEALSQKIGT------ALHFALCGTnpYMSVKTLIDRG-ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 355 QDSVHGWTALMQATYHGnkeIVKYLLNQGADvtLRAKNgytafDLVMLLNDPDTELVRLLASVCMQ--VNKD---KGRPS 429
Cdd:PHA02876  472 INIQNQYPLLIALEYHG---IVNILLHYGAE--LRDSR-----VLHKSLNDNMFSFRYIIAHICIQdfIRHDirnEVNPL 541

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622871988 430 HQLPLPHSKVRQPWSIPVLPDDKggLKSWWNRMSNRFRKL 469
Cdd:PHA02876  542 KRVPTRFTSLRESFKEIIQSDDT--FKRIWLRCKEELKDI 579
SAM_Ste11_fungal cd09534
SAM domain of Ste11_fungal subfamily; SAM (sterile alpha motif) domain of Ste11 subfamily is a ...
 776-836 3.67e-08

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: 50.67  E-value: 3.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 776 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELN 836
Cdd:cd09534     2 DEEFVEEWLNELNCGQYLDIFEKNLITGDLLLELDKEALKELGITKVGDRIRLLRAIKSLR 62
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 93-266 4.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 4.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  93 LVRFLLRRGASVNSRN-HYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVD 171
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 172 HHHPSGeqlglggnrDEPLDItALMAAIQHgheAVVRLLMEWGADPNRAARTVGWSPLMLAALTGRlgVAQQLVEKGANP 251
Cdd:PHA02878  229 ARDKCG---------NTPLHI-SVGYCKDY---DILKLLLEHGVDVNAKSYILGLTALHSSIKSER--KLKLLLEYGADI 293

                         170
                  ....*....|....*
gi 1622871988 252 DHLSVLEKTAFEVAL 266
Cdd:PHA02878  294 NSLNSYKLTPLSSAV 308
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-348 6.35e-08

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: 56.17  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 113 SALMQAARFGHV-SVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAgAFVDHHHPSGEQLGLGgnrdepld 191
Cdd:cd22192    19 SPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA-APELVNEPMTSDLYQG-------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 192 ITALMAAIQHGHEAVVRLLMEWGADPN--RAARTV-----------GWSPLMLAALTGRLGVAQQLVEKGANPDHLSVLE 258
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVspRATGTFfrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 259 KTAFEValdckhrdLVdyLDPMTTVrpktdeekrrpdifhALKMGNFQLVKEIADEDPSHVNLVNGDGATPLMLAAVTGQ 338
Cdd:cd22192   170 NTVLHI--------LV--LQPNKTF---------------ACQMYDLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGN 224

                         250
                  ....*....|
gi 1622871988 339 LALVQLLVER 348
Cdd:cd22192   225 IVMFQHLVQK 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
364-427 1.23e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 1.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 364 LMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAfdLVMLLNDPDTELVRLLASVCMQVNKDKGR 427
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA--LHLAAKNGHLEIVKLLLEHADVNLKDNGR 62
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-168 2.54e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  75 DEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSAL-MQAARFGHVSVAHLLLDHGADVNAQNR-LGASVLTVAS 152
Cdd:PHA02878  198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI 277

                          90
                  ....*....|....*.
gi 1622871988 153 RGGHlgVVKLLLEAGA 168
Cdd:PHA02878  278 KSER--KLKLLLEYGA 291
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-165 5.36e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  75 DEAGNTALQFAAAGG--HEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVAS 152
Cdd:PHA03095  219 DMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298

                          90
                  ....*....|...
gi 1622871988 153 RGGHLGVVKLLLE 165
Cdd:PHA03095  299 RNNNGRAVRAALA 311
PHA03095 PHA03095
ankyrin-like protein; Provisional
 298-417 5.60e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 298 HALKMGNFQLVKEIAD---EDPSHVNLVNGDGATPL---MLAAVTgqLALVQLLVERHADVDKQDSVhGWTALmqATYHG 371
Cdd:PHA03095   52 HLYLHYSSEKVKDIVRlllEAGADVNAPERCGFTPLhlyLYNATT--LDVIKLLIKAGADVNAKDKV-GRTPL--HVYLS 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622871988 372 NKEI----VKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLLASV 417
Cdd:PHA03095  127 GFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDA 176
SAM_sec23ip cd09584
SAM domain of sec23ip; SAM (sterile alpha motif) domain of Sec23ip (Sec23 interacting protein) ...
 780-828 5.92e-07

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: 47.50  E-value: 5.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622871988 780 LTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTdGSRQQI 828
Cdd:cd09584    12 LQSVLEALSLSEYKSTFEKEKIDMESLLMCTVDDLKEMGIPL-GPRKKI 59
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 206-386 1.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 206 VVRLLMEWGADPNRAARTVGWSPLMLAALTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALdckhrdlvdyldpmttvrp 285
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV------------------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 286 ktdeEKRRPDIFHALKmgnfqlvkeiadEDPSHVNLVNGDGATPLMLAavTGQL---ALVQLLVERHADVDKQDSVHGWT 362
Cdd:PHA02878  210 ----KHYNKPIVHILL------------ENGASTDARDKCGNTPLHIS--VGYCkdyDILKLLLEHGVDVNAKSYILGLT 271

                         170       180
                  ....*....|....*....|....
gi 1622871988 363 ALMQATYhgNKEIVKYLLNQGADV 386
Cdd:PHA02878  272 ALHSSIK--SERKLKLLLEYGADI 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 298-411 1.19e-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: 52.32  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 298 HALKMGNFQLVKEIADEDPSHVNL-VNGD---GATPLMLAAVTGQLALVQLLVERHADVDK-----------QDSV--HG 360
Cdd:cd22192    57 VAALYDNLEAAVVLMEAAPELVNEpMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyYG 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 361 WTALMQATYHGNKEIVKYLLNQGADvtLRAKNGYTAFDLVMLLNDPDTELV 411
Cdd:cd22192   137 EHPLSFAACVGNEEIVRLLIEHGAD--IRAQDSLGNTVLHILVLQPNKTFA 185
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 778-836 1.58e-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: 46.13  E-value: 1.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 778 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELN 836
Cdd:cd09521     6 DDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPGDQKKILDAIKEVH 64
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-142 1.68e-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: 45.36  E-value: 1.68e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622871988 110 YGWSALMQAA-RFGHVSVAHLLLDHGADVNAQNR 142
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
344-400 1.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622871988 344 LLVERHADVDKQDSvHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLV 400
Cdd:pfam13857   1 LLEHGPIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 93-237 2.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  93 LVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVDH 172
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622871988 173 HHPSGEqlglggnrdepldiTALMAAIQHGHEAVVRLLMEWGAD-PNRAARtvGWSPLMLAALTGR 237
Cdd:PHA02874  186 KDNNGE--------------SPLHNAAEYGDYACIKLLIDHGNHiMNKCKN--GFTPLHNAIIHNR 235
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 207-277 2.47e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 207 VRLLMEWGADPNrAARTVGWSPLMLAALTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRDLVDYL 277
Cdd:PTZ00322   98 ARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 208-277 2.73e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 47.95  E-value: 2.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 208 RLLMEWGADPNRAARTVGWSPLMLAALTGRLGVAQQLVEK-GANPDHLSVLEKTAFEVALDCKHRDLVDYL 277
Cdd:PHA02736   75 KLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
SAM_USH1G_HARP cd09517
SAM domain of USH1G_HARP family; SAM (sterile alpha motif) domain of USH1G/HARP (Usher ...
 784-834 3.10e-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: 45.41  E-value: 3.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 784 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTdGSRQQILAAISE 834
Cdd:cd09517     9 LTSNHLEEYLPVFEREKIDLEALMLLTDEDLQSLKLPL-GPRRKLLNAIAK 58
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-139 5.72e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.40  E-value: 5.72e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622871988 110 YGWSALMQAARFGHVSVAHLLLDHGADVNA 139
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 269-414 7.50e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 7.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 269 KHRDLVDYLDPMTTVRPKTDEEKRRPDIF-HALKMGnfqlvkeiadedpSHVNLVNGDGATPLMLAAV-----TGQLALV 342
Cdd:PHA03100   23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVkILLDNG-------------ADINSSTKNNSTPLHYLSNikynlTDVKEIV 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 343 QLLVERHADVDKQDSVHGWTALMQATYH-GNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLL 414
Cdd:PHA03100   90 KLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLL 162
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
784-835 1.30e-05

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 43.41  E-value: 1.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 784 LKKLSLEKYQPIFEEQEVD-MEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:pfam07647  13 LRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
Ank_4 pfam13637
Ankyrin repeats (many copies);
193-245 1.65e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 193 TALMAAIQHGHEAVVRLLMEWGADPNRAARTvGWSPLMLAALTGRLGVAQQLV 245
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-139 1.91e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.91e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622871988  110 YGWSALMQAARFGHVSVAHLLLDHGADVNA 139
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 359-388 2.10e-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: 2.10e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622871988  359 HGWTALMQATYHGNKEIVKYLLNQGADVTL 388
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_Ste50-like_fungal cd09533
SAM domain of Ste50_like (ubc2) subfamily; SAM (sterile alpha motif) domain of Ste50-like (or ...
 784-835 3.04e-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: 42.30  E-value: 3.04e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622871988 784 LKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:cd09533     6 LSSLGLPQYEDQFIENGITGDVLVALDHEDLKEMGITSVGHRLTILKAVYEL 57
Ank_5 pfam13857
Ankyrin repeats (many copies);
311-364 3.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 311 IADEDPSHVNLVNGDGATPLMLAAVTGQLALVQLLVERHADVDKQDSvHGWTAL 364
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 271-422 3.54e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 271 RDLVDYLDPMTTVRPKTDEEK--RRPDIfhalkmgNFQLVKEIADEDpSHVNLVNGDGATPL--MLAAV---TGQLALVQ 343
Cdd:PHA02798   22 KLLIKSCNPNEIVNEYSIFQKylQRDSP-------STDIVKLFINLG-ANVNGLDNEYSTPLctILSNIkdyKHMLDIVK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 344 LLVERHADVDKQDSvHGWT---ALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDP-DTELVRLLASVCM 419
Cdd:PHA02798   94 ILIENGADINKKNS-DGETplyCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHiDIEIIKLLLEKGV 172


                  ...
gi 1622871988 420 QVN 422
Cdd:PHA02798  173 DIN 175
SAM_HARP cd09587
SAM domain of HARP subfamily; SAM (sterile alpha motif) domain of HARP (Harmonin-interacting ...
 776-848 3.93e-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: 42.12  E-value: 3.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 776 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTdGSRQQILAAISelnagkgRERQILQE 848
Cdd:cd09587     1 DATPLEVFLSSQHLEEFLPIFMREQIDLEALMLCSDEDLQNIQMQL-GPRKKILSAVA-------RRKQVLQQ 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 359-386 4.10e-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: 4.10e-05
                          10        20
                  ....*....|....*....|....*...
gi 1622871988 359 HGWTALMQATYHGNKEIVKYLLNQGADV 386
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
97-151 5.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622871988  97 LLRRG-ASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVA 151
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-109 5.25e-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: 5.25e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622871988  78 GNTALQFAAA-GGHEPLVRFLLRRGASVNSRNH 109
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 359-391 5.73e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 5.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622871988 359 HGWTALMQATYH-GNKEIVKYLLNQGADVTLRAK 391
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 325-356 7.55e-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: 7.55e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622871988 325 DGATPLMLAAV-TGQLALVQLLVERHADVDKQD 356
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
SAM_WDSUB1 cd09505
SAM domain of WDSUB1 proteins; SAM (sterile alpha motif) domain of WDSUB1 subfamily proteins ...
 777-835 8.99e-05

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: 41.53  E-value: 8.99e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 777 EDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDL-KELGIKTDGSRQQILAAISEL 835
Cdd:cd09505     7 EEDVCTWLRSIGLEQYVEVFRANNIDGKELLNLTKESLsKDLKIESLGHRNKILRKIEEL 66
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 113-277 1.31e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 113 SALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVDHHHPSGEqlglggnrdepldi 192
Cdd:PLN03192  527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN-------------- 592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 193 TALMAAIQHGHEAVVRLLMEWGADPNRAArtvGWSPLMLAALTGRLGVAQQLVEKGANPDHLSVLEKTAFEVALDCKHRD 272
Cdd:PLN03192  593 TALWNAISAKHHKIFRILYHFASISDPHA---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669


                  ....*
gi 1622871988 273 LVDYL 277
Cdd:PLN03192  670 MVRLL 674
SAM_ZCCH14 cd09558
SAM domain of ZCCH14 subfamily; SAM (sterile alpha motif) domain of ZCCH14 (Zinc finger CCHC ...
 779-828 1.72e-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: 40.45  E-value: 1.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 779 ELTGIL---KKLSLEKYQPIFeeQEVDMEAFLTLTDGDLKELGIKTDGSRQQI 828
Cdd:cd09558     4 EQNGILdwlRKLRLHKYYPVF--KQLTMEKFLSLTEEDLNKFESLTMGAKKKL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-142 1.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 1.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622871988  75 DEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNR 142
Cdd:PHA03100  189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
SAM_Smaug-like cd09489
SAM (Sterile alpha motif ); SAM (sterile alpha motif) domain of Smaug-like subfamily proteins ...
 784-832 2.06e-04

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: 39.84  E-value: 2.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622871988 784 LKKLSLEKYQPIFeeQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAI 832
Cdd:cd09489     6 LKSLRLHKYSDAF--KGTTWEELLYLTEETLEKKGVLTLGARRKLLKAF 52
SAM_tankyrase1,2 cd09524
SAM domain of tankyrase1,2 subfamily; SAM (sterile alpha motif) domain of Tankyrase1,2 ...
 780-838 2.32e-04

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: 40.00  E-value: 2.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622871988 780 LTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNAG 838
Cdd:cd09524     8 ISQFLSSLGLEHLREIFEREQITLDVLAEMGHEELKEIGINAYGHRHKLIKGVERLISG 66
Ank_5 pfam13857
Ankyrin repeats (many copies);
72-115 3.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622871988  72 DCSDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSAL 115
Cdd:pfam13857  10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
360-414 4.39e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622871988 360 GWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVmLLNDpDTELVRLL 414
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA-ASNG-NVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 72-168 5.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  72 DCSDEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLG-ASVLTV 150
Cdd:PHA02875  129 DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCY 208

                          90
                  ....*....|....*...
gi 1622871988 151 ASRGGHLGVVKLLLEAGA 168
Cdd:PHA02875  209 AIENNKIDIVRLFIKRGA 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-210 6.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622871988 146 SVLTVASRGGHLGVVKLLLEAGAFVDHhhpsgeqlglggnRDEpLDITALMAAIQHGHEAVVRLL 210
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINA-------------VDG-NGETALHFAASNGNVEVLKLL 53
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 73-247 6.14e-04

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: 43.33  E-value: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  73 CSDE--AGNTALQFAAAGGHEPLVRFLLRRGASVNSRN-------------HYGWSALMQAARFGHVSVAHLLLDHGAD- 136
Cdd:cd21882    66 CTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQp 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 137 --VNAQNRLGASVLtvasrggHLGVVKL--LLEAGAFVDHHHPSGEQLGLGGNRDEPLDITalmaaiqhgheavvrllme 212
Cdd:cd21882   146 aaLEAQDSLGNTVL-------HALVLQAdnTPENSAFVCQMYNLLLSYGAHLDPTQQLEEI------------------- 199

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622871988 213 wgadPNRAartvGWSPLMLAALTGRLGVAQQLVEK 247
Cdd:cd21882   200 ----PNHQ----GLTPLKLAAVEGKIVMFQHILQR 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
296-346 6.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 296 IFHALKMGNFQLVKEIAdEDPSHVNLVNGDGATPLMLAAVTGQLALVQLLV 346
Cdd:pfam13637   5 LHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02741 PHA02741
hypothetical protein; Provisional
 295-399 7.79e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.18  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 295 DIFH-ALKMGNFQLVKEIA-----DEDPSHVNLVNGDGATPLMLAAVT--GQLA--LVQLLVERHADVDKQDSVHGWTAL 364
Cdd:PHA02741   23 NFFHeAARCGCFDIIARFTpfirgDCHAAALNATDDAGQMCIHIAAEKheAQLAaeIIDHLIELGADINAQEMLEGDTAL 102

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622871988 365 MQATYHGNKEIVKYLLNQ-GADVTLRAKNGYTAFDL 399
Cdd:PHA02741  103 HLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFEL 138
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 193-218 7.83e-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: 37.65  E-value: 7.83e-04
                          10        20
                  ....*....|....*....|....*..
gi 1622871988 193 TALM-AAIQHGHEAVVRLLMEWGADPN 218
Cdd:pfam00023   4 TPLHlAAGRRGNLEIVKLLLSKGADVN 30
SAM_DGK-delta cd09575
SAM domain of diacylglycerol kinase delta; SAM (sterile alpha motif) domain of DGK-delta ...
 778-835 8.11e-04

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: 38.39  E-value: 8.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622871988 778 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:cd09575     8 EEVAAWLEHLSLCEYKDIFTRHDVRGSELLHLERRDLKDLGVTKVGHMKRILCGIKEL 65
SAM_BOI-like_fungal cd09535
SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal ...
 795-835 8.46e-04

SAM domain of BOI-like fungal subfamily; SAM (sterile alpha motif) domain of BOI-like fungal subfamily is a potential protein-protein interaction domain. Proteins of this subfamily are apparently scaffold proteins, since most contain SH3 and PH domains, which are also protein-protein interaction domains, in addition to SAM domain. BOI-like proteins participate in cell cycle regulation. In particular BOI1 and BOI2 proteins of budding yeast S.cerevisiae are involved in bud formation, and POB1 protein of fission yeast S.pombe plays a role in cell elongation and separation. Among binding partners of BOI-like fungal subfamily members are such proteins as Bem1 and Cdc42 (they are known to be involved in cell polarization and bud formation).


Pssm-ID: 188934  Cd Length: 65  Bit Score: 38.31  E-value: 8.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622871988 795 IFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:cd09535    24 KFRENEITGDILLELDLEDLKELDIGSFGKRFKLWNEIKSL 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-168 9.15e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 9.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 115 LMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGA 168
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA 139
SAM_USH1G cd09586
SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) ...
 776-848 9.37e-04

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: 38.24  E-value: 9.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 776 DEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTdGSRQQILAAISelnagkgRERQILQE 848
Cdd:cd09586     1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPL-GPRKKILDACQ-------RRRQTIER 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-105 1.12e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|....*...
gi 1622871988  78 GNTALQFAAAGGHEPLVRFLLRRGASVN 105
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
SAM_DGK-delta-eta cd09507
SAM domain of diacylglycerol kinase delta and eta subunits; SAM (sterile alpha motif) domain ...
 778-835 1.15e-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: 38.16  E-value: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622871988 778 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:cd09507     8 EEVGAWLESLQLGEYRDIFARNDIRGSELLHLERRDLKDLGITKVGHVKRILQAIKDL 65
Ank_4 pfam13637
Ankyrin repeats (many copies);
12-98 1.19e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  12 LLLRACDQGDTETARRLLEPGAaepaergaepeagaepvgaeaagpgaaaaaavgapvPVDCSDEAGNTALQFAAAGGHE 91
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGA------------------------------------DINAVDGNGETALHFAASNGNV 47


                  ....*..
gi 1622871988  92 PLVRFLL 98
Cdd:pfam13637  48 EVLKLLL 54
SAM_Neurabin-like cd09512
SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like ...
 787-837 1.22e-03

SAM domain of SAM_Neurabin-like subfamily; SAM (sterile alpha motif) domain of Neurabin-like (Neural actin-binding) subfamily is a putative protein-protein interaction domain. This group currently includes the SAM domains of neurobin-I, SAMD14 and neurobin-I/SAMD14-like proteins. Most are multidomain proteins and in addition to SAM domain they contain other protein-binding domains such as PDZ and actin-binding domains. Members of this subfamily participate in signal transduction. Neurabin-I is involved in the regulation of Ca signaling intensity in alpha-adrenergic receptors; it forms a functional pair of opposing regulators with neurabin-II. Neurabins are expressed almost exclusively in neuronal cells. They are known to interact with protein phosphatase 1 and inhibit its activity; they also can bind actin filaments; however, the exact role of the SAM domain is unclear, since SAM doesn't participate in these interactions.


Pssm-ID: 188911 [Multi-domain]  Cd Length: 70  Bit Score: 38.02  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 787 LSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNA 837
Cdd:cd09512    19 LGLEQYIPEFTANNIDGQQLLQLDSSKLKALGITSSSDRSLLKKKLKELKA 69
SAM_DGK-eta cd09576
SAM domain of diacylglycerol kinase eta; SAM (sterile alpha motif) domain of DGK-eta subfamily ...
 778-835 1.23e-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: 38.03  E-value: 1.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622871988 778 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:cd09576     8 DEVAAWLDLLSLGEYKEIFIRHDIRGSELLHLERRDLKDLGIPKVGHMKRILQGIKEL 65
SAM_Smaug cd09557
SAM domain of Smaug subfamily; SAM (sterile alpha motif) domain of Smaug proteins is an RNA ...
 784-835 1.44e-03

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: 37.69  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622871988 784 LKKLSLEKYQPIFeeQEVDMEAFLTLTDGDLKELGIkTDGSRQQILAAISEL 835
Cdd:cd09557    13 LKSLRLHKYASLF--SQMTYEEMLNLTEEQLEAQGV-TKGARHKIALSIQKL 61
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 111-258 1.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 111 GWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGAFVDHHHPSGeqlglggnrdepl 190
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG------------- 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622871988 191 dITALMAAIQHGHEAVVRLLMEWGADPNRAARTVGWSPLMLAALTGRLGVAQQLVEKGANPDHLSVLE 258
Cdd:PHA02875  169 -CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIE 235
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 325-354 1.58e-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: 36.80  E-value: 1.58e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622871988  325 DGATPLMLAAVTGQLALVQLLVERHADVDK 354
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 310-418 2.02e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 310 EIADEDPSHvNLVNGDGATPL---MLAAVTGQLAL------VQLLVERHADVDKQDsVHGWTALMQATYHGNKEIVKYLL 380
Cdd:PTZ00322   58 ENKDATPDH-NLTTEEVIDPVvahMLTVELCQLAAsgdavgARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLL 135

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622871988 381 NQGADVTLRAKNGYTAFDLVMllNDPDTELVRLLASVC 418
Cdd:PTZ00322  136 EFGADPTLLDKDGKTPLELAE--ENGFREVVQLLSRHS 171
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 73-148 2.06e-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: 41.99  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988  73 CSDE--AGNTALQFAAAGGHEPLVRFLLRRGASVNSRNH--------------YGWSALMQAARFGHVSVAHLLLDHGAD 136
Cdd:TIGR00870 121 YTSEftPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPAD 200

                          90
                  ....*....|..
gi 1622871988 137 VNAQNRLGASVL 148
Cdd:TIGR00870 201 ILTADSLGNTLL 212
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 145-280 2.40e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622871988 145 ASVLTV-----ASRGGHLGVvKLLLEAGA---FVDHHHPSgeqlglggnrdePLDITALMaaiqhGHEAVVRLLMEWGAD 216
Cdd:PTZ00322   79 AHMLTVelcqlAASGDAVGA-RILLTGGAdpnCRDYDGRT------------PLHIACAN-----GHVQVVRVLLEFGAD 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622871988 217 PNRAARTvGWSPLMLAALTGRLGVAQQLV-------EKGAN--PDHLSVLEKTAFEVALDCKHRDLVDYLDPM 280
Cdd:PTZ00322  141 PTLLDKD-GKTPLELAEENGFREVVQLLSrhsqchfELGANakPDSFTGKPPSLEDSPISSHHPDFSAVPQPM 212
Ank_5 pfam13857
Ankyrin repeats (many copies);
130-168 2.41e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622871988 130 LLDHG-ADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGA 168
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGV 40
SAM_caskin1,2_repeat2 cd09498
SAM domain of caskin protein repeat 2; SAM (sterile alpha motif) domain repeat 2 of caskin1,2 ...
 784-836 2.46e-03

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: 37.27  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 784 LKKLSLEKYQPIFEEQEVD-MEAFLTLTDGDLKELGIKTDGSRQQILAAISELN 836
Cdd:cd09498    14 LSLLGLPQYHKVLVENGYDsIDFVTDLTWEDLQDIGITKLGHQKKLMLAIKKLK 67
SAM_SGMS1-like cd09515
SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of ...
 784-835 2.82e-03

SAM domain of sphingomyelin synthase related subfamily; SAM (sterile alpha motif) domain of SGMS-like (sphingomyelin synthase) subfamily is a potential protein-protein interaction domain. This group of proteins is related to sphingomyelin synthase 1, and contains an N-terminal SAM domain. The function of SGMS1-like proteins is unknown; they may play a role in sphingolipid metabolism.


Pssm-ID: 188914  Cd Length: 70  Bit Score: 37.23  E-value: 2.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622871988 784 LKKLSLEKY-QPIFEEQEVDMEAFLTLTDGDLKE--LGIKTDGSRQQILAAISEL 835
Cdd:cd09515    13 LKKEGFSKYvDLLCNKHRIDGKVLLSLTEEDLRSppLEIKVLGDIKRLWLAIRKL 67
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 225-252 3.00e-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: 36.03  E-value: 3.00e-03
                           10        20
                   ....*....|....*....|....*...
gi 1622871988  225 GWSPLMLAALTGRLGVAQQLVEKGANPD 252
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 225-253 3.69e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 3.69e-03
                          10        20
                  ....*....|....*....|....*....
gi 1622871988 225 GWSPLMLAALTGRLGVAQQLVEKGANPDH 253
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 75-151 4.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 4.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622871988  75 DEAGNTALQFAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARFGHVSVAHLLLDHGADVNAQNRLGASVLTVA 151
Cdd:PHA02874  154 DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
SAM_caskin1,2_repeat1 cd09497
SAM domain of caskin protein repeat 1; SAM (sterile alpha motif) domain repeat 1 of caskin1,2 ...
 774-837 4.71e-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: 4.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622871988 774 ITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISELNA 837
Cdd:cd09497     1 NPDAEAIFDWLREFGLEEYTPNFIKAGYDLPTISRMTPEDLTAIGITKPGHRKKLKSEIAQLQI 64
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 338-408 5.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 5.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622871988 338 QLALVQLLVERHADVDKQDsVHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDT 408
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 325-354 6.79e-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: 34.93  E-value: 6.79e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622871988 325 DGATPLMLAAVTGQLALVQLLVERHADVDK 354
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
SAM_Shank1,2,3 cd09506
SAM domain of Shank1,2,3 family proteins; SAM (sterile alpha motif) domain of Shank1,2,3 ...
 778-835 7.24e-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: 35.76  E-value: 7.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622871988 778 DELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLKELGIKTDGSRQQILAAISEL 835
Cdd:cd09506     8 DDVGDWLESLNLGEHRERFMDNEIDGSHLPNLDKEDLTELGVTRVGHRMNIERALKKL 65
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 193-218 8.35e-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: 34.54  E-value: 8.35e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622871988 193 TALMAAIQHGHEAVVRLLMEWGADPN 218
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 225-252 9.63e-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: 34.57  E-value: 9.63e-03
                          10        20
                  ....*....|....*....|....*....
gi 1622871988 225 GWSPLMLAAL-TGRLGVAQQLVEKGANPD 252
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVN 30
 
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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