NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767953024|ref|XP_011515350|]
View 

tonsoku-like protein isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
193-311 3.86e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 3.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  193 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 272
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953024  273 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 311
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 700-1014 8.59e-21

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 96.40  E-value: 8.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  700 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 779
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  780 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 859
Cdd:COG5238   242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  860 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 936
Cdd:COG5238   289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953024  937 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1014
Cdd:COG5238   361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 344-598 2.58e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  344 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 423
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  424 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 503
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  504 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 573
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834

                         250       260
                  ....*....|....*....|....*
gi 767953024  574 LASEPPGSPSTPRVSEPSGDSSAAG 598
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
193-311 3.86e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 3.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  193 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 272
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953024  273 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 311
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-303 7.19e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 7.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024   209 LHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCEGITPLHDALNCGHFE 288
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*
gi 767953024   289 VAELLLERGASVTLR 303
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 700-1014 8.59e-21

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 96.40  E-value: 8.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  700 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 779
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  780 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 859
Cdd:COG5238   242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  860 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 936
Cdd:COG5238   289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953024  937 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1014
Cdd:COG5238   361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 721-982 1.07e-18

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 88.18  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  721 LSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAeLVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPG 800
Cdd:cd00116    56 LCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCG-VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  801 QAtlQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFlshqTALGSAFQDAEHLKTLSLSYNAL--- 877
Cdd:cd00116   135 LP--PALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtde 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  878 GAPALARTLQSLPAgtLLHLELSS-VAAGKGDSDLMEPvfryLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLIS 956
Cdd:cd00116   209 GASALAETLASLKS--LEVLNLGDnNLTDAGAAALASA----LLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLE 282

                         250       260
                  ....*....|....*....|....*..
gi 767953024  957 LDLSANpEISCASLEEL-LSTLQKRPQ 982
Cdd:cd00116   283 LDLRGN-KFGEEGAQLLaESLLEPGNE 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 193-329 3.69e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  193 RKGSKWNRRNDMGETLLH---RACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPG 268
Cdd:PHA03095   35 AAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953024  269 GQGcegITPLHDALN--CGHFEVAELLLERGASVTLRTRKGLSPLETLqqwvkLYRRDLDLET 329
Cdd:PHA03095  115 KVG---RTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 3.86e-07

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: 47.20  E-value: 3.86e-07
                            10        20
                    ....*....|....*....|....*....
gi 767953024    238 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 266
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-311 7.67e-05

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: 46.54  E-value: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  205 GETLLHRACIEGQLRRVQDLVRQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 270
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767953024  271 GCEGITPLH-------DALNCghfEVAELLL-----ERGASV-TLRTRKGLSPL 311
Cdd:cd22192   166 DSLGNTVLHilvlqpnKTFAC---QMYDLILsydkeDDLQPLdLVPNNQGLTPF 216
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 199-303 2.27e-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: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024   199 NRRNDMGETLLHRACIEgqlrrvqdlvrqghplnprdycgwtpLHEACNyghlEIVRFLLDHGA-------AVDDPGGQG 271
Cdd:TIGR00870   76 SCRGAVGDTLLHAISLE--------------------------YVDAVE----AILLHLLAAFRksgplelANDQYTSEF 125

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767953024   272 CEGITPLHDALNCGHFEVAELLLERGASVTLR 303
Cdd:TIGR00870  126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA03247 PHA03247
large tegument protein UL36; Provisional
 344-598 2.58e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  344 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 423
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  424 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 503
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  504 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 573
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834

                         250       260
                  ....*....|....*....|....*
gi 767953024  574 LASEPPGSPSTPRVSEPSGDSSAAG 598
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
LRR_8 pfam13855
Leucine rich repeat;
748-817 7.40e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.96  E-value: 7.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953024   748 LRELRLAGNRLGDKCVAelvaALGTMPSLALLDLSSN---HLGPEGLRQLAmglpgqatlqSLEELDLSMNPL 817
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNlltTLSPGAFSGLP----------SLRYLDLSGNRL 61
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
193-311 3.86e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 3.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  193 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 272
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953024  273 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 311
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
170-311 7.09e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 7.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  170 EDDTDGLTPQLEEDEELQGHLGRRKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYG 249
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953024  250 HLEIVRFLLDHGAAVDDpggQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 311
Cdd:COG0666   132 NLEIVKLLLEAGADVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
199-335 1.07e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.42  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  199 NRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPL 278
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953024  279 HDALNCGHFEVAELLLERGASVTLRTRKGLSPLETLQQWVKLYRRDLDLETRQKARA 335
Cdd:COG0666   224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-303 7.19e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 7.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024   209 LHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCEGITPLHDALNCGHFE 288
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*
gi 767953024   289 VAELLLERGASVTLR 303
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 700-1014 8.59e-21

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 96.40  E-value: 8.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  700 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 779
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  780 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 859
Cdd:COG5238   242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  860 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 936
Cdd:COG5238   289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953024  937 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1014
Cdd:COG5238   361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 721-982 1.07e-18

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 88.18  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  721 LSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAeLVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPG 800
Cdd:cd00116    56 LCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCG-VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  801 QAtlQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFlshqTALGSAFQDAEHLKTLSLSYNAL--- 877
Cdd:cd00116   135 LP--PALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtde 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  878 GAPALARTLQSLPAgtLLHLELSS-VAAGKGDSDLMEPvfryLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLIS 956
Cdd:cd00116   209 GASALAETLASLKS--LEVLNLGDnNLTDAGAAALASA----LLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLE 282

                         250       260
                  ....*....|....*....|....*..
gi 767953024  957 LDLSANpEISCASLEEL-LSTLQKRPQ 982
Cdd:cd00116   283 LDLRGN-KFGEEGAQLLaESLLEPGNE 308
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 742-992 1.90e-17

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 84.71  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  742 LKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALLDLSSNHLG--PEGLRQLAMGLPGQATLQsleELDLSMNPLGD 819
Cdd:cd00116    19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTKGCGLQ---ELDLSDNALGP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  820 GCGQSLASLLHAcPLLSTLRLQACGFGPSFFLSHQTALGSAfqdAEHLKTLSLSYNALGAPALARTLQSLPAGTLLH-LE 898
Cdd:cd00116    96 DGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDL---PPALEKLVLGRNRLEGASCEALAKALRANRDLKeLN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  899 LSsvaagkgDSDLMEPVFRYLA---KEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLISLDLSANPeISCASLEELLS 975
Cdd:cd00116   172 LA-------NNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAALAS 243

                         250
                  ....*....|....*..
gi 767953024  976 TLQKRPQGLSFLGLSGC 992
Cdd:cd00116   244 ALLSPNISLLTLSLSCN 260
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 715-879 6.23e-13

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 70.85  E-value: 6.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  715 ELQGLGLSFSACSL--------ALDQAQ-------LTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 779
Cdd:cd00116   119 GLGDRGLRLLAKGLkdlppaleKLVLGRnrlegasCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  780 DLSSNHLGPEGLRQLAMGLPgqaTLQSLEELDLSMNPLGDGCGQSLAS-LLHACPLLSTLRLQACGFGPSFFLSHQTALg 858
Cdd:cd00116   199 DLNNNGLTDEGASALAETLA---SLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGAKDLAEVL- 274

                         170       180
                  ....*....|....*....|.
gi 767953024  859 safQDAEHLKTLSLSYNALGA 879
Cdd:cd00116   275 ---AEKESLLELDLRGNKFGE 292
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
199-311 3.13e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  199 NRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGqgcEGITPL 278
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK---DGLTAL 256

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767953024  279 HDALNCGHFEVAELLLERGASVTLRTRKGLSPL 311
Cdd:COG0666   257 LLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-262 4.88e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.88e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767953024   194 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 262
Cdd:pfam12796   19 NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 193-329 3.69e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  193 RKGSKWNRRNDMGETLLH---RACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPG 268
Cdd:PHA03095   35 AAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953024  269 GQGcegITPLHDALN--CGHFEVAELLLERGASVTLRTRKGLSPLETLqqwvkLYRRDLDLET 329
Cdd:PHA03095  115 KVG---RTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
715-899 5.26e-10

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 5.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  715 ELQGLGLSFSACS----LALDQAQLTPLLRALKLHTALRELRLAGNRLGDkcvaelVAALGTMPSLALLDLSSNHLGpeg 790
Cdd:COG4886   193 QITDLPEPLGNLTnleeLDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLT--- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  791 lrqlamGLPGQATLQSLEELDLSMNPLGDGCGQSLASLLhacPLLSTLRLQACGFGPSFFLSHQTALGSAFQDAEHLKTL 870
Cdd:COG4886   264 ------DLPPLANLTNLKTLDLSNNQLTDLKLKELELLL---GLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLL 334

                         170       180
                  ....*....|....*....|....*....
gi 767953024  871 SLSYNALGAPALARTLQSLPAGTLLHLEL 899
Cdd:COG4886   335 VTLTTLALSLSLLALLTLLLLLNLLSLLL 363
Ank_4 pfam13637
Ankyrin repeats (many copies);
238-294 5.83e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.83e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953024   238 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDALNCGHFEVAELLL 294
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-258 7.51e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 7.51e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767953024   207 TLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 258
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 195-313 1.15e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  195 GSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgc 272
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE-- 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767953024  273 egiTPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLET 313
Cdd:PHA02874  192 ---SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 220-300 2.54e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  220 RVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNCGHFEVAELLLERGAS 299
Cdd:PHA03100  174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                  .
gi 767953024  300 V 300
Cdd:PHA03100  251 I 251
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 707-1037 3.81e-09

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 60.19  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  707 HQQVLQAVELQGLGLSfsacslaldqaQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLAL-------- 778
Cdd:COG5238    86 PTQLLVVDWEGAEEVS-----------PVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQVlkdplggn 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  779 ---LDLSSNHLGPEGLRQLAMGLPGQatlqSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSfflshqt 855
Cdd:COG5238   155 avhLLGLAARLGLLAAISMAKALQNN----SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDE------- 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  856 algsafqdaehlktlslsynalGAPALARTLQSLPagTLLHLELSSVAAGkgDSDLMEpVFRYLaKEGCALAHLTLSANH 935
Cdd:COG5238   224 ----------------------GAEILAEALKGNK--SLTTLDLSNNQIG--DEGVIA-LAEAL-KNNTTVETLYLSGNQ 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  936 LGDKAVRDLCRCLSLCPSLISLDLSANPeISCASLEELLSTLQKRpQGLSFLGLSGCAV--QGPLGLGLWDKIAAQLREL 1013
Cdd:COG5238   276 IGAEGAIALAKALQGNTTLTSLDLSVNR-IGDEGAIALAEGLQGN-KTLHTLNLAYNGIgaQGAIALAKALQENTTLHSL 353

                         330       340
                  ....*....|....*....|....
gi 767953024 1014 QLCSRRLCAEDRDALRQLQPSRPG 1037
Cdd:COG5238   354 DLSDNQIGDEGAIALAKYLEGNTT 377
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
619-889 1.14e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.79  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  619 LFLIPVPHSSDTHSVAWLAEQAAQRYYQTCGLLPRLTLRKEGALLAPQDLIPDVLQSNDEVLAEVTSWDLPPLTDRYRRA 698
Cdd:COG4886    26 LLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  699 CQSLGQGEHQQVL--QAVELQGLGLSFSAC----SLALDQAQLTPLLRALKLHTALRELRLAGNRLGDkcvaeLVAALGT 772
Cdd:COG4886   106 NEELSNLTNLESLdlSGNQLTDLPEELANLtnlkELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTD-----LPEELGN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  773 MPSLALLDLSSNHLG--PEGLRQlamglpgqatLQSLEELDLSMNPLGDgcgqsLASLLHACPLLSTLRLQACGFgpsff 850
Cdd:COG4886   181 LTNLKELDLSNNQITdlPEPLGN----------LTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQL----- 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767953024  851 lshqTALgSAFQDAEHLKTLSLSYNALGAPALARTLQSL 889
Cdd:COG4886   241 ----TDL-PELGNLTNLEELDLSNNQLTDLPPLANLTNL 274
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
730-1015 1.39e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.41  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  730 LDQAQLTPLLRALKLHTALRELRLAGNRlgdkcvaelvaALGTMPSLALLDLSSNHLG--PEGLRQLamglpgqatlQSL 807
Cdd:COG4886    80 LLLSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTdlPEELANL----------TNL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  808 EELDLSMNPLGDgcgqsLASLLHACPLLSTLRLQACGFgpsfflshqTALGSAFQDAEHLKTLSLSYNALGApaLARTLQ 887
Cdd:COG4886   139 KELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQL---------TDLPEELGNLTNLKELDLSNNQITD--LPEPLG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  888 SLPAgtllhlelssvaagkgdsdlmepvfrylakegcaLAHLTLSANHLgdkavRDLCRCLSLCPSLISLDLSANPeisc 967
Cdd:COG4886   203 NLTN----------------------------------LEELDLSGNQL-----TDLPEPLANLTNLETLDLSNNQ---- 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767953024  968 asLEEL--LSTLQKrpqgLSFLGLSGCAVQG-PLGLGLwdkiaAQLRELQL 1015
Cdd:COG4886   240 --LTDLpeLGNLTN----LEELDLSNNQLTDlPPLANL-----TNLKTLDL 279
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 207-304 8.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  207 TLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegITPLHDALNCGH 286
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214

                          90
                  ....*....|....*...
gi 767953024  287 FEVAELLLERGASVTLRT 304
Cdd:PHA02875  215 IDIVRLFIKRGADCNIMF 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 195-294 1.16e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  195 GSKWNR--RNDMGETLLHRACIE-------GQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavd 265
Cdd:PTZ00322   63 TPDHNLttEEVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--- 139

                          90       100
                  ....*....|....*....|....*....
gi 767953024  266 DPGGQGCEGITPLHDALNCGHFEVAELLL 294
Cdd:PTZ00322  140 DPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 237-265 2.02e-07

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: 48.02  E-value: 2.02e-07
                           10        20
                   ....*....|....*....|....*....
gi 767953024   237 CGWTPLHEACNYGHLEIVRFLLDHGAAVD 265
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 203-311 2.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  203 DMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCEGITPLHDAL 282
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCGNTPLHISV 242

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767953024  283 N-CGHFEVAELLLERGASVTLR-TRKGLSPL 311
Cdd:PHA02878  243 GyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 194-312 2.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  194 KGSKWNRRNDMGETLLHRACIE--GQLRRVQDLVRQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpgg 269
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN---- 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  270 QGCE-----------------GITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 312
Cdd:PHA03100  171 AKNRvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 195-318 3.79e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  195 GSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG--- 271
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftp 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953024  272 -------------------------CEGITPLHDALN--CGhFEVAELLLERGASVTLRTRKGLSPLETLQQWV 318
Cdd:PHA02874  227 lhnaiihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 3.86e-07

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: 47.20  E-value: 3.86e-07
                            10        20
                    ....*....|....*....|....*....
gi 767953024    238 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 266
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 194-311 4.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  194 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNY-GHLEIVRFLLDHGAAVDdpGGQGC 272
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN--AKSYI 267

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953024  273 EGITPLHDALNCGhfEVAELLLERGASVTLRTRKGLSPL 311
Cdd:PHA02878  268 LGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPL 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 206-311 5.81e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  206 ETLLHRACIEGQLRRVQDLVRQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNC 284
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145

                          90       100
                  ....*....|....*....|....*..
gi 767953024  285 GHFEVAELLLERGASVTLRTRKGLSPL 311
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-265 9.04e-07

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: 46.13  E-value: 9.04e-07
                           10        20
                   ....*....|....*....|....*....
gi 767953024   238 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 265
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
257-312 1.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767953024   257 LLDHGAAvdDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 312
Cdd:pfam13857    1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 202-311 4.52e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  202 NDMGETLLHRACIEGQLrrVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDA 281
Cdd:PHA02874   90 NGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC---YPIHIA 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 767953024  282 LNCGHFEVAELLLERGASVTLRTRKGLSPL 311
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_5 pfam13857
Ankyrin repeats (many copies);
224-279 2.11e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 2.11e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953024   224 LVRQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLH 279
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 254-312 2.73e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767953024  254 VRFLLDHGAavdDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 312
Cdd:PTZ00322   98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 205-307 3.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 3.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  205 GETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDALNC 284
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178

                          90       100
                  ....*....|....*....|...
gi 767953024  285 GHFEVAELLLERGASVTLRTRKG 307
Cdd:PHA02875  179 GDIAICKMLLDSGANIDYFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 194-311 4.04e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  194 KGSKWNRRNDMGETLLHRAcieGQLRRVQD----LVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 269
Cdd:PHA02876  330 LGADVNAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767953024  270 Q-GcegiTPLHDALnCGH--FEVAELLLERGASVTLRTRKGLSPL 311
Cdd:PHA02876  407 KiG----TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 193-266 5.77e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 5.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953024  193 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 266
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 746-841 6.97e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 45.16  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  746 TALRELRLAGNRL--GDK-CVA-ELVAALGtmPSLALLDLSSNHLgpEGLRQLAmglpgqaTLQSLEELDLSMNPLGDgc 821
Cdd:cd21340    90 TNLEELHIENQRLppGEKlTFDpRSLAALS--NSLRVLNISGNNI--DSLEPLA-------PLRNLEQLDASNNQISD-- 156

                          90       100
                  ....*....|....*....|
gi 767953024  822 GQSLASLLHACPLLSTLRLQ 841
Cdd:cd21340   157 LEELLDLLSSWPSLRELDLT 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-311 7.67e-05

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: 46.54  E-value: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  205 GETLLHRACIEGQLRRVQDLVRQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 270
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767953024  271 GCEGITPLH-------DALNCghfEVAELLL-----ERGASV-TLRTRKGLSPL 311
Cdd:cd22192   166 DSLGNTVLHilvlqpnKTFAC---QMYDLILsydkeDDLQPLdLVPNNQGLTPF 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 201-314 1.03e-04

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: 46.16  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  201 RNDMGETLLHRACIEGQ-------LRRVQDLVRQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 267
Cdd:cd22192    47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767953024  268 --GGQGCE---GITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLETL 314
Cdd:cd22192   125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 273-305 1.23e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.23e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767953024   273 EGITPLHDA-LNCGHFEVAELLLERGASVTLRTR 305
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 206-300 1.49e-04

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: 45.77  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  206 ETLLHRACIEGQLRRVQDLVRQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDDP-GGQGCEGITPLHD 280
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNEPmTSDLYQGETALHI 95

                          90       100
                  ....*....|....*....|
gi 767953024  281 ALNCGHFEVAELLLERGASV 300
Cdd:cd22192    96 AVVNQNLNLVRELIARGADV 115
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 884-973 2.54e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 43.62  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  884 RTLQSLpAGTLLHLELSsvaaGKGDSDLMEpvFRYLakegCALAHLTLSANHLGDkaVRDLCRCLSLCPSLISLDLSANP 963
Cdd:cd21340   113 RSLAAL-SNSLRVLNIS----GNNIDSLEP--LAPL----RNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNP 179

                          90       100
                  ....*....|....*....|.
gi 767953024  964 --------E---ISCASLEEL 973
Cdd:cd21340   180 vckkpkyrDkiiLASKSLEVL 200
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 273-302 4.11e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 4.11e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 767953024    273 EGITPLHDALNCGHFEVAELLLERGASVTL 302
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
194-266 8.54e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 8.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953024  194 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 266
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 199-303 2.27e-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: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024   199 NRRNDMGETLLHRACIEgqlrrvqdlvrqghplnprdycgwtpLHEACNyghlEIVRFLLDHGA-------AVDDPGGQG 271
Cdd:TIGR00870   76 SCRGAVGDTLLHAISLE--------------------------YVDAVE----AILLHLLAAFRksgplelANDQYTSEF 125

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767953024   272 CEGITPLHDALNCGHFEVAELLLERGASVTLR 303
Cdd:TIGR00870  126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA03247 PHA03247
large tegument protein UL36; Provisional
 344-598 2.58e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  344 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 423
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  424 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 503
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  504 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 573
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834

                         250       260
                  ....*....|....*....|....*
gi 767953024  574 LASEPPGSPSTPRVSEPSGDSSAAG 598
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 224-311 3.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953024  224 LVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNCGH-----FEVAELLLERGA 298
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97

                          90
                  ....*....|...
gi 767953024  299 SVTLRTRKGLSPL 311
Cdd:PHA03100   98 NVNAPDNNGITPL 110
LRR_8 pfam13855
Leucine rich repeat;
748-817 7.40e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.96  E-value: 7.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953024   748 LRELRLAGNRLGDKCVAelvaALGTMPSLALLDLSSN---HLGPEGLRQLAmglpgqatlqSLEELDLSMNPL 817
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNlltTLSPGAFSGLP----------SLRYLDLSGNRL 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH