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Conserved domains on  [gi|767953026|ref|XP_011515351|]
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tonsoku-like protein isoform X2 [Homo sapiens]

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];
181-299 8.46e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 8.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  181 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 260
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953026  261 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 299
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 688-1002 1.10e-20

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: 96.01  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  688 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 767
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  768 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 847
Cdd:COG5238   242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  848 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 924
Cdd:COG5238   289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953026  925 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1002
Cdd:COG5238   361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 332-586 2.57e-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: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  332 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 411
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  412 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 491
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  492 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 561
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834

                         250       260
                  ....*....|....*....|....*
gi 767953026  562 LASEPPGSPSTPRVSEPSGDSSAAG 586
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-299 8.46e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 8.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  181 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 260
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953026  261 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 299
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
197-291 9.89e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 9.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026   197 LHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCEGITPLHDALNCGHFE 276
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*
gi 767953026   277 VAELLLERGASVTLR 291
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 688-1002 1.10e-20

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: 96.01  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  688 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 767
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  768 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 847
Cdd:COG5238   242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  848 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 924
Cdd:COG5238   289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953026  925 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1002
Cdd:COG5238   361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 709-970 1.69e-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: 87.80  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  709 LSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAeLVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPG 788
Cdd:cd00116    56 LCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCG-VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  789 QAtlQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFlshqTALGSAFQDAEHLKTLSLSYNAL--- 865
Cdd:cd00116   135 LP--PALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtde 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  866 GAPALARTLQSLPAgtLLHLELSS-VAAGKGDSDLMEPvfryLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLIS 944
Cdd:cd00116   209 GASALAETLASLKS--LEVLNLGDnNLTDAGAAALASA----LLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLE 282

                         250       260
                  ....*....|....*....|....*..
gi 767953026  945 LDLSANpEISCASLEEL-LSTLQKRPQ 970
Cdd:cd00116   283 LDLRGN-KFGEEGAQLLaESLLEPGNE 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 181-317 3.63e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  181 RKGSKWNRRNDMGETLLH---RACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPG 256
Cdd:PHA03095   35 AAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953026  257 GQGcegITPLHDALN--CGHFEVAELLLERGASVTLRTRKGLSPLETLqqwvkLYRRDLDLET 317
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 ...
 226-254 3.81e-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: 3.81e-07
                            10        20
                    ....*....|....*....|....*....
gi 767953026    226 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 254
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 193-299 7.56e-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: 7.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  193 GETLLHRACIEGQLRRVQDLVRQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 258
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767953026  259 GCEGITPLH-------DALNCghfEVAELLL-----ERGASV-TLRTRKGLSPL 299
Cdd:cd22192   166 DSLGNTVLHilvlqpnKTFAC---QMYDLILsydkeDDLQPLdLVPNNQGLTPF 216
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 187-291 2.24e-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: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026   187 NRRNDMGETLLHRACIEgqlrrvqdlvrqghplnprdycgwtpLHEACNyghlEIVRFLLDHGA-------AVDDPGGQG 259
Cdd:TIGR00870   76 SCRGAVGDTLLHAISLE--------------------------YVDAVE----AILLHLLAAFRksgplelANDQYTSEF 125

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767953026   260 CEGITPLHDALNCGHFEVAELLLERGASVTLR 291
Cdd:TIGR00870  126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA03247 PHA03247
large tegument protein UL36; Provisional
 332-586 2.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  332 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 411
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  412 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 491
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  492 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 561
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834

                         250       260
                  ....*....|....*....|....*
gi 767953026  562 LASEPPGSPSTPRVSEPSGDSSAAG 586
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
LRR_8 pfam13855
Leucine rich repeat;
736-805 8.57e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.58  E-value: 8.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953026   736 LRELRLAGNRLGDKCVAelvaALGTMPSLALLDLSSN---HLGPEGLRQLAmglpgqatlqSLEELDLSMNPL 805
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNlltTLSPGAFSGLP----------SLRYLDLSGNRL 61
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-299 8.46e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 8.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  181 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGC 260
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDN 184

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953026  261 EGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 299
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
158-299 1.48e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 1.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  158 EDDTDGLTPQLEEDEELQGHLGRRKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYG 237
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767953026  238 HLEIVRFLLDHGAAVDDpggQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPL 299
Cdd:COG0666   132 NLEIVKLLLEAGADVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-323 2.12e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 2.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  187 NRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPL 266
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953026  267 HDALNCGHFEVAELLLERGASVTLRTRKGLSPLETLQQWVKLYRRDLDLETRQKARA 323
Cdd:COG0666   224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
197-291 9.89e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 9.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026   197 LHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCEGITPLHDALNCGHFE 276
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75

                           90
                   ....*....|....*
gi 767953026   277 VAELLLERGASVTLR 291
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 688-1002 1.10e-20

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: 96.01  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  688 QSLGQGEHQQVLQAVELQGLGLSfsacSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 767
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLG----CNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  768 DLSSNHLGPEGLRQLAMGLPGQATlqsLEELDLSMNPLGDGCGQSLASLLhacpllstlrlqacgfgpsfflshqtalgs 847
Cdd:COG5238   242 DLSNNQIGDEGVIALAEALKNNTT---VETLYLSGNQIGAEGAIALAKAL------------------------------ 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  848 afQDAEHLKTLSLSYNALGAP---ALARTLQSLPAGTLLHLelssvAAGKGDSDLMEPVFRYLaKEGCALAHLTLSANHL 924
Cdd:COG5238   289 --QGNTTLTSLDLSVNRIGDEgaiALAEGLQGNKTLHTLNL-----AYNGIGAQGAIALAKAL-QENTTLHSLDLSDNQI 360

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767953026  925 GDKAVRDLCRCLSLCPSLISLDLSANpEISCASLEELLSTLQKrpQGLSFLGLSGcavqGPLGLGLWDKIAAQLRELQ 1002
Cdd:COG5238   361 GDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALIDALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 709-970 1.69e-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: 87.80  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  709 LSFSACSLALDQAQLTPLLRALKLHTALRELRLAGNRLGDKCVAeLVAALGTMPSLALLDLSSNHLGPEGLRQLAMGLPG 788
Cdd:cd00116    56 LCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCG-VLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKD 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  789 QAtlQSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSFFlshqTALGSAFQDAEHLKTLSLSYNAL--- 865
Cdd:cd00116   135 LP--PALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtde 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  866 GAPALARTLQSLPAgtLLHLELSS-VAAGKGDSDLMEPvfryLAKEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLIS 944
Cdd:cd00116   209 GASALAETLASLKS--LEVLNLGDnNLTDAGAAALASA----LLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLE 282

                         250       260
                  ....*....|....*....|....*..
gi 767953026  945 LDLSANpEISCASLEEL-LSTLQKRPQ 970
Cdd:cd00116   283 LDLRGN-KFGEEGAQLLaESLLEPGNE 308
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 730-980 2.87e-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: 83.94  E-value: 2.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  730 LKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALLDLSSNHLG--PEGLRQLAMGLPGQATLQsleELDLSMNPLGD 807
Cdd:cd00116    19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTKGCGLQ---ELDLSDNALGP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  808 GCGQSLASLLHAcPLLSTLRLQACGFGPSFFLSHQTALGSAfqdAEHLKTLSLSYNALGAPALARTLQSLPAGTLLH-LE 886
Cdd:cd00116    96 DGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDL---PPALEKLVLGRNRLEGASCEALAKALRANRDLKeLN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  887 LSsvaagkgDSDLMEPVFRYLA---KEGCALAHLTLSANHLGDKAVRDLCRCLSLCPSLISLDLSANPeISCASLEELLS 963
Cdd:cd00116   172 LA-------NNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAALAS 243

                         250
                  ....*....|....*..
gi 767953026  964 TLQKRPQGLSFLGLSGC 980
Cdd:cd00116   244 ALLSPNISLLTLSLSCN 260
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 703-867 9.26e-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: 70.46  E-value: 9.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  703 ELQGLGLSFSACSL--------ALDQAQ-------LTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLALL 767
Cdd:cd00116   119 GLGDRGLRLLAKGLkdlppaleKLVLGRnrlegasCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVL 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  768 DLSSNHLGPEGLRQLAMGLPgqaTLQSLEELDLSMNPLGDGCGQSLAS-LLHACPLLSTLRLQACGFGPSFFLSHQTALg 846
Cdd:cd00116   199 DLNNNGLTDEGASALAETLA---SLKSLEVLNLGDNNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGAKDLAEVL- 274

                         170       180
                  ....*....|....*....|.
gi 767953026  847 safQDAEHLKTLSLSYNALGA 867
Cdd:cd00116   275 ---AEKESLLELDLRGNKFGE 292
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-299 5.32e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 5.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  187 NRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGqgcEGITPL 266
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK---DGLTAL 256

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767953026  267 HDALNCGHFEVAELLLERGASVTLRTRKGLSPL 299
Cdd:COG0666   257 LLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-250 5.98e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 5.98e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767953026   182 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 250
Cdd:pfam12796   19 NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 181-317 3.63e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  181 RKGSKWNRRNDMGETLLH---RACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPG 256
Cdd:PHA03095   35 AAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKD 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953026  257 GQGcegITPLHDALN--CGHFEVAELLLERGASVTLRTRKGLSPLETLqqwvkLYRRDLDLET 317
Cdd:PHA03095  115 KVG---RTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
226-282 5.87e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.87e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953026   226 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDALNCGHFEVAELLL 282
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
195-246 7.72e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 7.72e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767953026   195 TLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 246
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
703-887 7.82e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 62.26  E-value: 7.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  703 ELQGLGLSFSACS----LALDQAQLTPLLRALKLHTALRELRLAGNRLGDkcvaelVAALGTMPSLALLDLSSNHLGpeg 778
Cdd:COG4886   193 QITDLPEPLGNLTnleeLDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLT--- 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  779 lrqlamGLPGQATLQSLEELDLSMNPLGDGCGQSLASLLhacPLLSTLRLQACGFGPSFFLSHQTALGSAFQDAEHLKTL 858
Cdd:COG4886   264 ------DLPPLANLTNLKTLDLSNNQLTDLKLKELELLL---GLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLL 334

                         170       180
                  ....*....|....*....|....*....
gi 767953026  859 SLSYNALGAPALARTLQSLPAGTLLHLEL 887
Cdd:COG4886   335 VTLTTLALSLSLLALLTLLLLLNLLSLLL 363
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 183-301 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  183 GSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgc 260
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE-- 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767953026  261 egiTPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLET 301
Cdd:PHA02874  192 ---SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 208-288 2.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  208 RVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNCGHFEVAELLLERGAS 287
Cdd:PHA03100  174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                  .
gi 767953026  288 V 288
Cdd:PHA03100  251 I 251
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 695-1025 5.18e-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: 59.80  E-value: 5.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  695 HQQVLQAVELQGLGLSfsacslaldqaQLTPLLRALKLHTALRELRLAGNRLGDKCVAELVAALGTMPSLAL-------- 766
Cdd:COG5238    86 PTQLLVVDWEGAEEVS-----------PVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQVlkdplggn 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  767 ---LDLSSNHLGPEGLRQLAMGLPGQatlqSLEELDLSMNPLGDGCGQSLASLLHACPLLSTLRLQACGFGPSfflshqt 843
Cdd:COG5238   155 avhLLGLAARLGLLAAISMAKALQNN----SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDE------- 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  844 algsafqdaehlktlslsynalGAPALARTLQSLPagTLLHLELSSVAAGkgDSDLMEpVFRYLaKEGCALAHLTLSANH 923
Cdd:COG5238   224 ----------------------GAEILAEALKGNK--SLTTLDLSNNQIG--DEGVIA-LAEAL-KNNTTVETLYLSGNQ 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  924 LGDKAVRDLCRCLSLCPSLISLDLSANPeISCASLEELLSTLQKRpQGLSFLGLSGCAV--QGPLGLGLWDKIAAQLREL 1001
Cdd:COG5238   276 IGAEGAIALAKALQGNTTLTSLDLSVNR-IGDEGAIALAEGLQGN-KTLHTLNLAYNGIgaQGAIALAKALQENTTLHSL 353

                         330       340
                  ....*....|....*....|....
gi 767953026 1002 QLCSRRLCAEDRDALRQLQPSRPG 1025
Cdd:COG5238   354 DLSDNQIGDEGAIALAKYLEGNTT 377
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
607-877 1.94e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  607 LFLIPVPHSSDTHSVAWLAEQAAQRYYQTCGLLPRLTLRKEGALLAPQDLIPDVLQSNDEVLAEVTSWDLPPLTDRYRRA 686
Cdd:COG4886    26 LLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  687 CQSLGQGEHQQVL--QAVELQGLGLSFSAC----SLALDQAQLTPLLRALKLHTALRELRLAGNRLGDkcvaeLVAALGT 760
Cdd:COG4886   106 NEELSNLTNLESLdlSGNQLTDLPEELANLtnlkELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTD-----LPEELGN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  761 MPSLALLDLSSNHLG--PEGLRQlamglpgqatLQSLEELDLSMNPLGDgcgqsLASLLHACPLLSTLRLQACGFgpsff 838
Cdd:COG4886   181 LTNLKELDLSNNQITdlPEPLGN----------LTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQL----- 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767953026  839 lshqTALgSAFQDAEHLKTLSLSYNALGAPALARTLQSL 877
Cdd:COG4886   241 ----TDL-PELGNLTNLEELDLSNNQLTDLPPLANLTNL 274
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
718-1003 3.00e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  718 LDQAQLTPLLRALKLHTALRELRLAGNRlgdkcvaelvaALGTMPSLALLDLSSNHLG--PEGLRQLamglpgqatlQSL 795
Cdd:COG4886    80 LLLSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTdlPEELANL----------TNL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  796 EELDLSMNPLGDgcgqsLASLLHACPLLSTLRLQACGFgpsfflshqTALGSAFQDAEHLKTLSLSYNALGApaLARTLQ 875
Cdd:COG4886   139 KELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQL---------TDLPEELGNLTNLKELDLSNNQITD--LPEPLG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  876 SLPAgtllhlelssvaagkgdsdlmepvfrylakegcaLAHLTLSANHLgdkavRDLCRCLSLCPSLISLDLSANPeisc 955
Cdd:COG4886   203 NLTN----------------------------------LEELDLSGNQL-----TDLPEPLANLTNLETLDLSNNQ---- 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767953026  956 asLEEL--LSTLQKrpqgLSFLGLSGCAVQG-PLGLGLwdkiaAQLRELQL 1003
Cdd:COG4886   240 --LTDLpeLGNLTN----LEELDLSNNQLTDlPPLANL-----TNLKTLDL 279
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 195-292 8.58e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  195 TLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegITPLHDALNCGH 274
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214

                          90
                  ....*....|....*...
gi 767953026  275 FEVAELLLERGASVTLRT 292
Cdd:PHA02875  215 IDIVRLFIKRGADCNIMF 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 183-282 1.32e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  183 GSKWNR--RNDMGETLLHRACIE-------GQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavd 253
Cdd:PTZ00322   63 TPDHNLttEEVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA--- 139

                          90       100
                  ....*....|....*....|....*....
gi 767953026  254 DPGGQGCEGITPLHDALNCGHFEVAELLL 282
Cdd:PTZ00322  140 DPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 191-299 2.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  191 DMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCEGITPLHDAL 270
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCGNTPLHISV 242

                          90       100       110
                  ....*....|....*....|....*....|.
gi 767953026  271 N-CGHFEVAELLLERGASVTLR-TRKGLSPL 299
Cdd:PHA02878  243 GyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 225-253 2.18e-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: 47.64  E-value: 2.18e-07
                           10        20
                   ....*....|....*....|....*....
gi 767953026   225 CGWTPLHEACNYGHLEIVRFLLDHGAAVD 253
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 182-300 2.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  182 KGSKWNRRNDMGETLLHRACIE--GQLRRVQDLVRQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpgg 257
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN---- 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  258 QGCE-----------------GITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 300
Cdd:PHA03100  171 AKNRvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 183-306 3.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  183 GSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG--- 259
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftp 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953026  260 -------------------------CEGITPLHDALN--CGhFEVAELLLERGASVTLRTRKGLSPLETLQQWV 306
Cdd:PHA02874  227 lhnaiihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 226-254 3.81e-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: 3.81e-07
                            10        20
                    ....*....|....*....|....*....
gi 767953026    226 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 254
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 182-299 4.30e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  182 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNY-GHLEIVRFLLDHGAAVDdpGGQGC 260
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVN--AKSYI 267

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767953026  261 EGITPLHDALNCGhfEVAELLLERGASVTLRTRKGLSPL 299
Cdd:PHA02878  268 LGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPL 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 194-299 5.73e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 5.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  194 ETLLHRACIEGQLRRVQDLVRQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNC 272
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145

                          90       100
                  ....*....|....*....|....*..
gi 767953026  273 GHFEVAELLLERGASVTLRTRKGLSPL 299
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 226-253 9.39e-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: 9.39e-07
                           10        20
                   ....*....|....*....|....*....
gi 767953026   226 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 253
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
245-300 1.53e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.53e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767953026   245 LLDHGAAvdDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 300
Cdd:pfam13857    1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 190-299 4.46e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  190 NDMGETLLHRACIEGQLrrVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDA 269
Cdd:PHA02874   90 NGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC---YPIHIA 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 767953026  270 LNCGHFEVAELLLERGASVTLRTRKGLSPL 299
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_5 pfam13857
Ankyrin repeats (many copies);
212-267 2.47e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767953026   212 LVRQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLH 267
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 242-300 2.98e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 2.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767953026  242 VRFLLDHGAavdDPGGQGCEGITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLE 300
Cdd:PTZ00322   98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 193-295 3.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 3.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  193 GETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCegiTPLHDALNC 272
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178

                          90       100
                  ....*....|....*....|...
gi 767953026  273 GHFEVAELLLERGASVTLRTRKG 295
Cdd:PHA02875  179 GDIAICKMLLDSGANIDYFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 182-299 3.98e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  182 KGSKWNRRNDMGETLLHRAcieGQLRRVQD----LVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 257
Cdd:PHA02876  330 LGADVNAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQ 406

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767953026  258 Q-GcegiTPLHDALnCGH--FEVAELLLERGASVTLRTRKGLSPL 299
Cdd:PHA02876  407 KiG----TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 181-254 5.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 5.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767953026  181 RKGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 254
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 193-299 7.56e-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: 7.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  193 GETLLHRACIEGQLRRVQDLVRQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 258
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767953026  259 GCEGITPLH-------DALNCghfEVAELLL-----ERGASV-TLRTRKGLSPL 299
Cdd:cd22192   166 DSLGNTVLHilvlqpnKTFAC---QMYDLILsydkeDDLQPLdLVPNNQGLTPF 216
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 734-829 8.90e-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: 44.78  E-value: 8.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  734 TALRELRLAGNRL--GDK-CVA-ELVAALGtmPSLALLDLSSNHLgpEGLRQLAmglpgqaTLQSLEELDLSMNPLGDgc 809
Cdd:cd21340    90 TNLEELHIENQRLppGEKlTFDpRSLAALS--NSLRVLNISGNNI--DSLEPLA-------PLRNLEQLDASNNQISD-- 156

                          90       100
                  ....*....|....*....|
gi 767953026  810 GQSLASLLHACPLLSTLRLQ 829
Cdd:cd21340   157 LEELLDLLSSWPSLRELDLT 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 189-302 1.02e-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: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  189 RNDMGETLLHRACIEGQ-------LRRVQDLVRQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 255
Cdd:cd22192    47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767953026  256 --GGQGCE---GITPLHDALNCGHFEVAELLLERGASVTLRTRKGLSPLETL 302
Cdd:cd22192   125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 261-293 1.26e-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: 1.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767953026   261 EGITPLHDA-LNCGHFEVAELLLERGASVTLRTR 293
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 194-288 1.47e-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: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  194 ETLLHRACIEGQLRRVQDLVRQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDDP-GGQGCEGITPLHD 268
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNEPmTSDLYQGETALHI 95

                          90       100
                  ....*....|....*....|
gi 767953026  269 ALNCGHFEVAELLLERGASV 288
Cdd:cd22192    96 AVVNQNLNLVRELIARGADV 115
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 872-961 3.09e-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: 43.24  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  872 RTLQSLpAGTLLHLELSsvaaGKGDSDLMEpvFRYLakegCALAHLTLSANHLGDkaVRDLCRCLSLCPSLISLDLSANP 951
Cdd:cd21340   113 RSLAAL-SNSLRVLNIS----GNNIDSLEP--LAPL----RNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNP 179

                          90       100
                  ....*....|....*....|.
gi 767953026  952 --------E---ISCASLEEL 961
Cdd:cd21340   180 vckkpkyrDkiiLASKSLEVL 200
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 261-290 4.06e-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: 4.06e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 767953026    261 EGITPLHDALNCGHFEVAELLLERGASVTL 290
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
182-254 1.08e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.25  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953026  182 KGSKWNRRNDMGETLLHRACIEGQLRRVQDLVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 254
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 187-291 2.24e-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: 2.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026   187 NRRNDMGETLLHRACIEgqlrrvqdlvrqghplnprdycgwtpLHEACNyghlEIVRFLLDHGA-------AVDDPGGQG 259
Cdd:TIGR00870   76 SCRGAVGDTLLHAISLE--------------------------YVDAVE----AILLHLLAAFRksgplelANDQYTSEF 125

                           90       100       110
                   ....*....|....*....|....*....|..
gi 767953026   260 CEGITPLHDALNCGHFEVAELLLERGASVTLR 291
Cdd:TIGR00870  126 TPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA03247 PHA03247
large tegument protein UL36; Provisional
 332-586 2.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  332 ASGQDPHSSQAFHTPSSLLFDPETSPPLSPCPEPPSNSTRLPEASQAHVRVSPgQAAPAMARPRRSRHGPASSSSSSEGE 411
Cdd:PHA03247 2600 APVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERP-RDDPAPGRVSRPRRARRLGRAAQASS 2678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  412 DSAGPARPSQKRPRCSATAQRVAAWTPGPASNREAATASTSRAAYQAAIRGVGSAQSRLGPGPPRGHSKALAPQAALIPE 491
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  492 EECLAGDWLELDMPLTRSRRPRPRGTgdnrRPSSTSGSDSEESRPRAR----------AKQVRLTCMQSCSAPVNAGPSS 561
Cdd:PHA03247 2759 RPPTTAGPPAPAPPAAPAAGPPRRLT----RPAVASLSESRESLPSPWdpadppaavlAPAAALPPAASPAGPLPPPTSA 2834

                         250       260
                  ....*....|....*....|....*
gi 767953026  562 LASEPPGSPSTPRVSEPSGDSSAAG 586
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPG 2859
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 212-299 3.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767953026  212 LVRQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCEGITPLHDALNCGH-----FEVAELLLERGA 286
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97

                          90
                  ....*....|...
gi 767953026  287 SVTLRTRKGLSPL 299
Cdd:PHA03100   98 NVNAPDNNGITPL 110
LRR_8 pfam13855
Leucine rich repeat;
736-805 8.57e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.58  E-value: 8.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767953026   736 LRELRLAGNRLGDKCVAelvaALGTMPSLALLDLSSN---HLGPEGLRQLAmglpgqatlqSLEELDLSMNPL 805
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.
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