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Conserved domains on  [gi|194474010|ref|NP_001124044|]
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tonsoku-like protein [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-635 8.28e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 8.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
                          90       100       110
                  ....*....|....*....|....*....|...
gi 194474010  603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
1055-1331 3.50e-19

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: 92.16  E-value: 3.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTafqNVEELDLSMNPL 1134
Cdd:COG5238   200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT---TVETLYLSGNQI 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPvlrtlrlqacgfspsfflshqaalgsafkdaeHLKTLSLSYNTLGAP---ALARVLQSLPTCTL 1211
Cdd:COG5238   277 GAEGAIALAKALQGNT--------------------------------TLTSLDLSVNRIGDEgaiALAEGLQGNKTLHT 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHLELSSVAASKSnssliEPVIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLEELL 1291
Cdd:COG5238   325 LNLAYNGIGAQGA-----IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALI 397
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 194474010 1292 SALQErpQGLSFFDLSGcsiqGPLNSDLWDKILSQLQELQ 1331
Cdd:COG5238   398 DALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
197-450 1.37e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKP 276
Cdd:COG0457     3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL---DP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  277 NQRVAICQslkyvLAVVRLQQ-QLQEAEgNDLQGAMAI-------CEQLGDLFSKADDFPKASEAYQKQLHFaellnrpD 348
Cdd:COG0457    74 DDAEALNN-----LGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  349 LELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQ 428
Cdd:COG0457   141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
                         250       260
                  ....*....|....*....|..
gi 194474010  429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457   221 ELLLLALALLLALRLAALALYQ 242
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
25-234 1.62e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.08  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010   25 EEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457     6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  105 ELQRAWATIGRTHLDVYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTAQCNNY 184
Cdd:COG0457    74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 194474010  185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457   133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-635 8.28e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 8.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
                          90       100       110
                  ....*....|....*....|....*....|...
gi 194474010  603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-627 8.47e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 8.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010   533 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 612
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 194474010   613 VAELLIERGASVTLR 627
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
1055-1331 3.50e-19

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: 92.16  E-value: 3.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTafqNVEELDLSMNPL 1134
Cdd:COG5238   200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT---TVETLYLSGNQI 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPvlrtlrlqacgfspsfflshqaalgsafkdaeHLKTLSLSYNTLGAP---ALARVLQSLPTCTL 1211
Cdd:COG5238   277 GAEGAIALAKALQGNT--------------------------------TLTSLDLSVNRIGDEgaiALAEGLQGNKTLHT 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHLELSSVAASKSnssliEPVIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLEELL 1291
Cdd:COG5238   325 LNLAYNGIGAQGA-----IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALI 397
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 194474010 1292 SALQErpQGLSFFDLSGcsiqGPLNSDLWDKILSQLQELQ 1331
Cdd:COG5238   398 DALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1055-1311 2.28e-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: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGdPCATELLATLGTMPNLVLLDLSSNHLGPEGLRqLVEGSLGQTAfQNVEELDLSMNPL 1134
Cdd:cd00116    73 LLQGLTKGCGLQELDLSDNALG-PDGCGVLESLLRSSSLQELKLNNNGLGDRGLR-LLAKGLKDLP-PALEKLVLGRNRL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPVLRTLRLQACGFSPSFFlshqAALGSAFKDAEHLKTLSLSYNTL---GAPALARVLQSLPTCTL 1211
Cdd:cd00116   150 EGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtdeGASALAETLASLKSLEV 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHL---ELSSVAASKSNSSLIEPVIKYLTkegcalahLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLE 1288
Cdd:cd00116   226 LNLgdnNLTDAGAAALASALLSPNISLLT--------LSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN-KFGEEGAQ 296
                         250       260
                  ....*....|....*....|...
gi 194474010 1289 ELLSALQERPQGLSFFDLSGCSI 1311
Cdd:cd00116   297 LLAESLLEPGNELESLWVKDDSF 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
544-667 2.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  544 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 623
Cdd:PHA03100  174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 194474010  624 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAASMERRLQMA 667
Cdd:PHA03100  251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
197-450 1.37e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKP 276
Cdd:COG0457     3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL---DP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  277 NQRVAICQslkyvLAVVRLQQ-QLQEAEgNDLQGAMAI-------CEQLGDLFSKADDFPKASEAYQKQLHFaellnrpD 348
Cdd:COG0457    74 DDAEALNN-----LGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  349 LELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQ 428
Cdd:COG0457   141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
                         250       260
                  ....*....|....*....|..
gi 194474010  429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457   221 ELLLLALALLLALRLAALALYQ 242
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
562-590 5.14e-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: 5.14e-07
                            10        20
                    ....*....|....*....|....*....
gi 194474010    562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
1065-1319 7.29e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 50.62  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1065 LRELRLSGNRLgdpcATELLATLGTMPNLVLLDLSSNHLG---PEGLrqlveGSLGqtafqNVEELDLSMNPLGDGCAQA 1141
Cdd:PLN00113  334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTgeiPEGL-----CSSG-----NLFKLILFSNSLEGEIPKS 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1142 LAsllrTCPVLRTLRLQACGFS---PS--------FFL-----SHQAALGSAFKDAEHLKTLSLSYNTLgapaLARVLQS 1205
Cdd:PLN00113  400 LG----ACRSLRRVRLQDNSFSgelPSeftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDS 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1206 LPTCTLLHLELS----SVAASKSNSSLIEpvikyltkegcaLAHLTLSANCLSDKAVRELSrclpSCPSLTSLDLSANpe 1281
Cdd:PLN00113  472 FGSKRLENLDLSrnqfSGAVPRKLGSLSE------------LMQLKLSENKLSGEIPDELS----SCKKLVSLDLSHN-- 533
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 194474010 1282 vSCAGleELLSALQERPQgLSFFDLSGCSIQGPLNSDL 1319
Cdd:PLN00113  534 -QLSG--QIPASFSEMPV-LSQLDLSQNQLSGEIPKNL 567
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
25-234 1.62e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.08  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010   25 EEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457     6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  105 ELQRAWATIGRTHLDVYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTAQCNNY 184
Cdd:COG0457    74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 194474010  185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457   133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
525-638 4.00e-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: 48.09  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  525 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 591
Cdd:cd22192    47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 194474010  592 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 638
Cdd:cd22192   125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
TPR_12 pfam13424
Tetratricopeptide repeat;
316-383 2.70e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.14  E-value: 2.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010   316 QLGDLFSKADDFPKASEAYQKQL-HFAELLNRPDLELAVIHESLATTLGDMKDYHKAVHHYEEELRLRK 383
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALeIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-635 8.28e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 8.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNA---RDNDGETPL 190
                          90       100       110
                  ....*....|....*....|....*....|...
gi 194474010  603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-635 8.66e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 8.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPL 602
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA---QDNDGNTPL 157
                          90       100       110
                  ....*....|....*....|....*....|...
gi 194474010  603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-658 6.53e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPL 602
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTAL 223
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010  603 HDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAA 658
Cdd:COG0666   224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
533-627 8.47e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 8.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010   533 LHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggqgCDGITPLHDALNCGHFE 612
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-----DNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*
gi 194474010   613 VAELLIERGASVTLR 627
Cdd:pfam12796   76 IVKLLLEKGADINVK 90
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
1055-1331 3.50e-19

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: 92.16  E-value: 3.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQTafqNVEELDLSMNPL 1134
Cdd:COG5238   200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT---TVETLYLSGNQI 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPvlrtlrlqacgfspsfflshqaalgsafkdaeHLKTLSLSYNTLGAP---ALARVLQSLPTCTL 1211
Cdd:COG5238   277 GAEGAIALAKALQGNT--------------------------------TLTSLDLSVNRIGDEgaiALAEGLQGNKTLHT 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHLELSSVAASKSnssliEPVIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLEELL 1291
Cdd:COG5238   325 LNLAYNGIGAQGA-----IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN-NIGKQGAEALI 397
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 194474010 1292 SALQErpQGLSFFDLSGcsiqGPLNSDLWDKILSQLQELQ 1331
Cdd:COG5238   398 DALQT--NRLHTLILDG----NLIGAEAQQRLEQLLERIK 431
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
518-635 3.57e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  518 KINKWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGqgcD 597
Cdd:COG0666    43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK---D 119
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 194474010  598 GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1055-1311 2.28e-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: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1055 LLRALKLHTALRELRLSGNRLGdPCATELLATLGTMPNLVLLDLSSNHLGPEGLRqLVEGSLGQTAfQNVEELDLSMNPL 1134
Cdd:cd00116    73 LLQGLTKGCGLQELDLSDNALG-PDGCGVLESLLRSSSLQELKLNNNGLGDRGLR-LLAKGLKDLP-PALEKLVLGRNRL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1135 GDGCAQALASLLRTCPVLRTLRLQACGFSPSFFlshqAALGSAFKDAEHLKTLSLSYNTL---GAPALARVLQSLPTCTL 1211
Cdd:cd00116   150 EGASCEALAKALRANRDLKELNLANNGIGDAGI----RALAEGLKANCNLEVLDLNNNGLtdeGASALAETLASLKSLEV 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1212 LHL---ELSSVAASKSNSSLIEPVIKYLTkegcalahLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANpEVSCAGLE 1288
Cdd:cd00116   226 LNLgdnNLTDAGAAALASALLSPNISLLT--------LSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN-KFGEEGAQ 296
                         250       260
                  ....*....|....*....|...
gi 194474010 1289 ELLSALQERPQGLSFFDLSGCSI 1311
Cdd:cd00116   297 LLAESLLEPGNELESLWVKDDSF 319
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1059-1311 3.94e-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: 87.03  E-value: 3.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1059 LKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLG--PEGLRQLVEGsLGQTAfqNVEELDLSMNPLGD 1136
Cdd:cd00116    19 LPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQG-LTKGC--GLQELDLSDNALGP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1137 GCAQALASLLRTcPVLRTLRLQACGFSPSfflsHQAALGSAFKD-AEHLKTLSLSYNTL---GAPALARVLQSLPTCTLL 1212
Cdd:cd00116    96 DGCGVLESLLRS-SSLQELKLNNNGLGDR----GLRLLAKGLKDlPPALEKLVLGRNRLegaSCEALAKALRANRDLKEL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1213 HLelssvaaskSNSSLIEPVIKYLT---KEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSANPeVSCAGLEE 1289
Cdd:cd00116   171 NL---------ANNGIGDAGIRALAeglKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN-LTDAGAAA 240
                         250       260
                  ....*....|....*....|..
gi 194474010 1290 LLSALQERPQGLSFFDLSGCSI 1311
Cdd:cd00116   241 LASALLSPNISLLTLSLSCNDI 262
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
1052-1196 6.33e-12

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: 68.54  E-value: 6.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1052 LTPLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGQtafQNVEELDLSM 1131
Cdd:cd00116   154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASL---KSLEVLNLGD 230
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010 1132 NPLGDGCAQALAS-LLRTCPVLRTLRLQACGFSPSFFLShqaaLGSAFKDAEHLKTLSLSYNTLGA 1196
Cdd:cd00116   231 NNLTDAGAAALASaLLSPNISLLTLSLSCNDITDDGAKD----LAEVLAEKESLLELDLRGNKFGE 292
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1049-1345 1.77e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.04  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1049 QAQLTPLLRALKLHTALRELRLSGNRlgdpcatellaTLGTMPNLVLLDLSSNHLG--PEGLRQLvegslgqtafQNVEE 1126
Cdd:COG4886    82 LSLLLLGLTDLGDLTNLTELDLSGNE-----------ELSNLTNLESLDLSGNQLTdlPEELANL----------TNLKE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1127 LDLSMNPLGDgcaqaLASLLRTCPVLRTLRLQACGFSpsfflshqaALGSAFKDAEHLKTLSLSYNTLgapalarvlQSL 1206
Cdd:COG4886   141 LDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLT---------DLPEELGNLTNLKELDLSNNQI---------TDL 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1207 PtctllhlelssvaasksnssliePVIKYLTKegcaLAHLTLSANCLSDkavreLSRCLPSCPSLTSLDLSANPEVSCAG 1286
Cdd:COG4886   198 P-----------------------EPLGNLTN----LEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTDLPE 245
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1287 LEELLSalqerpqgLSFFDLSGCSIQG-PLNSDlwdkiLSQLQELQLCSKDLTTKDRDTL 1345
Cdd:COG4886   246 LGNLTN--------LEELDLSNNQLTDlPPLAN-----LTNLKTLDLSNNQLTDLKLKEL 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
523-586 6.50e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 6.50e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194474010   523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHpLNPRDYcGWTPLHEACNYGHLEIVRFLLDHGA 586
Cdd:pfam12796   24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN-GRTALHYAARSGHLEIVKLLLEKGA 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
531-582 2.43e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 2.43e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 194474010   531 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLL 582
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
544-667 2.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  544 RVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGAS 623
Cdd:PHA03100  174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA---NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 194474010  624 VtlrtrkglsplETLQQWVkLYFRDLDLETRQKAASMERRLQMA 667
Cdd:PHA03100  251 I-----------KTIIETL-LYFKDKDLNTITKIKMLKKSIMYM 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
531-653 2.71e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  531 TLLHRACiEGQLRRVQDLVKQGHPLNPRDYCGWTPLH-EACNYGHLEIVRFLLDHGAAVDDPGGQGcdgITPLHDALN-- 607
Cdd:PHA03095   53 LYLHYSS-EKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVG---RTPLHVYLSgf 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 194474010  608 CGHFEVAELLIERGASVTLRTRKGLSPLETLqqwvkLYFRDLDLET 653
Cdd:PHA03095  129 NINPKVIRLLLRKGADVNALDLYGMTPLAVL-----LKSRNANVEL 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
562-618 1.02e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 194474010   562 GWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNCGHFEVAELLI 618
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE---TALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
521-637 1.80e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  521 KWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGA--AVDDPGGQgcdg 598
Cdd:PHA02874  116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGE---- 191
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 194474010  599 iTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLET 637
Cdd:PHA02874  192 -SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
197-450 1.37e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKP 276
Cdd:COG0457     3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYE------KALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALEL---DP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  277 NQRVAICQslkyvLAVVRLQQ-QLQEAEgNDLQGAMAI-------CEQLGDLFSKADDFPKASEAYQKQLHFaellnrpD 348
Cdd:COG0457    74 DDAEALNN-----LGLALQALgRYEEAL-EDYDKALELdpddaeaLYNLGLALLELGRYDEAIEAYERALEL-------D 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  349 LELAVIHESLATTLGDMKDYHKAVHHYEEELRLRKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAFGCAQQAQRYQ 428
Cdd:COG0457   141 PDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALA 220
                         250       260
                  ....*....|....*....|..
gi 194474010  429 LQRQILQHLYTVQLKLQPQEAR 450
Cdd:COG0457   221 ELLLLALALLLALRLAALALYQ 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
531-628 4.26e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  531 TLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgITPLHDALNCGH 610
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC--VAALCYAIENNK 214
                          90
                  ....*....|....*...
gi 194474010  611 FEVAELLIERGASVTLRT 628
Cdd:PHA02875  215 IDIVRLFIKRGADCNIMF 232
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
1050-1349 9.13e-08

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: 56.34  E-value: 9.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1050 AQLTPLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVL-----------LDLSSNHLGPEGLRQLVEGSLGQ 1118
Cdd:COG5238   101 SPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQVlkdplggnavhLLGLAARLGLLAAISMAKALQNN 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1119 tafqNVEELDLSMNPLGDGCAQALASLLRTCPVLRTLRLQACGFSPSfflshqaalgsafkdaehlktlslsyntlGAPA 1198
Cdd:COG5238   181 ----SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDE-----------------------------GAEI 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1199 LARVLQSLPTCTllHLELSSVAASKSNSSLIepvIKYLtKEGCALAHLTLSANCLSDKAVRELSRCLPSCPSLTSLDLSA 1278
Cdd:COG5238   228 LAEALKGNKSLT--TLDLSNNQIGDEGVIAL---AEAL-KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSV 301
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194474010 1279 NPeVSCAGLEELLSALQeRPQGLSFFDLSGCSI--QG--PLNSDLWDkiLSQLQELQLCSKDLTTKDRDTLCQRL 1349
Cdd:COG5238   302 NR-IGDEGAIALAEGLQ-GNKTLHTLNLAYNGIgaQGaiALAKALQE--NTTLHSLDLSDNQIGDEGAIALAKYL 372
PHA03100 PHA03100
ankyrin repeat protein; Provisional
523-636 9.74e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRACIE--GQLRRVQDLVKQGHPLNPRDYCGWTPLHEA--CNYGHLEIVRFLLDHGAAVDdpggqGCD- 597
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDIN-----AKNr 174
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010  598 -----------------GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:PHA03100  175 vnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
526-617 1.05e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  526 NDMGETLLHRACIE-------GQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDG 598
Cdd:PTZ00322   72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA---DPTLLDKDG 148
                          90
                  ....*....|....*....
gi 194474010  599 ITPLHDALNCGHFEVAELL 617
Cdd:PTZ00322  149 KTPLELAEENGFREVVQLL 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
530-635 1.33e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  530 ETLLHRACIEGQLRRVQDLVKQGHPLNPRDYC-GWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNC 608
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGA---DPDIPNTDKFSPLHLAVMM 145
                          90       100
                  ....*....|....*....|....*..
gi 194474010  609 GHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPL 172
PHA02874 PHA02874
ankyrin repeat protein; Provisional
523-642 3.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQG------- 595
Cdd:PHA02874  151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGftplhna 230
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  596 ---------------------CDGITPLHDALN--CGhFEVAELLIERGASVTLRTRKGLSPLETLQQWV 642
Cdd:PHA02874  231 iihnrsaiellinnasindqdIDGSTPLHHAINppCD-IDIIDILLYHKADISIKDNKGENPIDTAFKYI 299
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
561-589 5.09e-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: 47.25  E-value: 5.09e-07
                           10        20
                   ....*....|....*....|....*....
gi 194474010   561 CGWTPLHEACNYGHLEIVRFLLDHGAAVD 589
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
562-590 5.14e-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: 5.14e-07
                            10        20
                    ....*....|....*....|....*....
gi 194474010    562 GWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
519-635 7.93e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 7.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  519 INKWNRrnDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDdpgGQGCDG 598
Cdd:PHA02878  160 INMKDR--HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---ARDKCG 234
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 194474010  599 ITPLHDALN-CGHFEVAELLIERGASVTLR-TRKGLSPL 635
Cdd:PHA02878  235 NTPLHISVGyCKDYDILKLLLEHGVDVNAKsYILGLTAL 273
PHA02874 PHA02874
ankyrin repeat protein; Provisional
514-635 1.53e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  514 VGRRKINKWNRRNDMGETLLHRACIEGQLrrVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGG 593
Cdd:PHA02874   78 IGAHDIIKLLIDNGVDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 194474010  594 QGCdgiTPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02874  156 NGC---YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1045-1157 1.53e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.24  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1045 LALCQAQLTPLLRALKLHTALRELRLSGNRLGDpcatelLATLGTMPNLVLLDLSSNHLgpEGLRQLVEgslgqtaFQNV 1124
Cdd:COG4886   210 LDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQL--TDLPPLAN-------LTNL 274
                          90       100       110
                  ....*....|....*....|....*....|...
gi 194474010 1125 EELDLSMNPLGDGCAQALASLLRTCPVLRTLRL 1157
Cdd:COG4886   275 KTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
562-589 1.54e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 1.54e-06
                           10        20
                   ....*....|....*....|....*....
gi 194474010   562 GWTPLHEAC-NYGHLEIVRFLLDHGAAVD 589
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
1054-1146 1.85e-06

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: 52.10  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1054 PLLRALKLHTALRELRLSGNRLGDPCATELLATLGTMPNLVLLDLSSNHLGPEGLRQLVEGSLGqtafQNVEELDLSMNP 1133
Cdd:COG5238   339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQT----NRLHTLILDGNL 414
                          90
                  ....*....|...
gi 194474010 1134 LGDGCAQALASLL 1146
Cdd:COG5238   415 IGAEAQQRLEQLL 427
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
44-355 2.14e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 52.30  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010   44 QEALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDVYDH 123
Cdd:COG3914     2 AAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  124 CQsRDSLLQAQAAFEKSLAIVDEKLEgmltqreLSEMRTRLYLNLGLTCESLQQTAQCNNYFKKSIFLAEqnhlyeDLFR 203
Cdd:COG3914    82 EL-AALLLQALGRYEEALALYRRALA-------LNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP------DFAE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  204 ARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLgsqKPNQRVAIC 283
Cdd:COG3914   148 AYLNLGEALRRLGRLEEAIAALR------RALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL---DPDNADAHS 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010  284 QslkyvlavvRLQQQLQEAEGNDLQGAMAICEQLGDLFSKADDF-----PKASEAYQKQLH--FAELLNRPDLELAVIH 355
Cdd:COG3914   219 N---------LLFALRQACDWEVYDRFEELLAALARGPSELSPFallylPDDDPAELLALAraWAQLVAAAAAPELPPP 288
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
1065-1319 7.29e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 50.62  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1065 LRELRLSGNRLgdpcATELLATLGTMPNLVLLDLSSNHLG---PEGLrqlveGSLGqtafqNVEELDLSMNPLGDGCAQA 1141
Cdd:PLN00113  334 LQVLQLWSNKF----SGEIPKNLGKHNNLTVLDLSTNNLTgeiPEGL-----CSSG-----NLFKLILFSNSLEGEIPKS 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1142 LAsllrTCPVLRTLRLQACGFS---PS--------FFL-----SHQAALGSAFKDAEHLKTLSLSYNTLgapaLARVLQS 1205
Cdd:PLN00113  400 LG----ACRSLRRVRLQDNSFSgelPSeftklplvYFLdisnnNLQGRINSRKWDMPSLQMLSLARNKF----FGGLPDS 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1206 LPTCTLLHLELS----SVAASKSNSSLIEpvikyltkegcaLAHLTLSANCLSDKAVRELSrclpSCPSLTSLDLSANpe 1281
Cdd:PLN00113  472 FGSKRLENLDLSrnqfSGAVPRKLGSLSE------------LMQLKLSENKLSGEIPDELS----SCKKLVSLDLSHN-- 533
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 194474010 1282 vSCAGleELLSALQERPQgLSFFDLSGCSIQGPLNSDL 1319
Cdd:PLN00113  534 -QLSG--QIPASFSEMPV-LSQLDLSQNQLSGEIPKNL 567
Ank_5 pfam13857
Ankyrin repeats (many copies);
581-636 1.11e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.11e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 194474010   581 LLDHGAAvdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:pfam13857    1 LLEHGPI--DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
25-234 1.62e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.08  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010   25 EEAVCCHQLGELLASHGRFQEALEEHQQELHLLESVqdtlgcAVAHRKIGERLAEMENYSAALKHQHLYLDLagslsnHT 104
Cdd:COG0457     6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD------AEALYNLGLAYLRLGRYEEALADYEQALEL------DP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  105 ELQRAWATIGRTHLDVYDHcqsrdslLQAQAAFEKSLAIVDEKLEgmltqrelsemrtrLYLNLGLTCESLQQTAQCNNY 184
Cdd:COG0457    74 DDAEALNNLGLALQALGRY-------EEALEDYDKALELDPDDAE--------------ALYNLGLALLELGRYDEAIEA 132
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 194474010  185 FKKSIFLAeqnhlyEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARA 234
Cdd:COG0457   133 YERALELD------PDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
578-636 2.15e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 2.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010  578 VRFLLDHGAavdDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLE 636
Cdd:PTZ00322   98 ARILLTGGA---DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
Ank_5 pfam13857
Ankyrin repeats (many copies);
548-603 3.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 194474010   548 LVKQGHP-LNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLH 603
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL---TALD 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
525-638 4.00e-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: 48.09  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  525 RNDMGETLLHRACIEGQ-------LRRVQDLVKQghPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDP------ 591
Cdd:cd22192    47 RGALGETALHVAALYDNleaavvlMEAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPratgtf 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 194474010  592 --GGQGCD---GITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETL 638
Cdd:cd22192   125 frPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
197-436 4.07e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.03  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  197 LYEDLFRARYNLGAIHWRGGQHSQAMRCLEgarecaRAMKMRFMESECCMLVSQVLQDLGDFLAAKRALKKAYRLGSQKP 276
Cdd:COG2956    37 LDPETVEAHLALGNLYRRRGEYDRAIRIHQ------KLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  277 N---QRVAICQSLKYVLAVVRLQQQLQEAEGNDlqgAMAICEqLGDLFSKADDFPKASEAYQKQLHFAELLNRPDLELAV 353
Cdd:COG2956   111 EalrLLAEIYEQEGDWEKAIEVLERLLKLGPEN---AHAYCE-LAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAE 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  354 IHESLattlgdmKDYHKAVHHYEEELRL---------------RKGNALEEAKTWFNIGLAREEAGDAYELLAPCFQKAF 418
Cdd:COG2956   187 LYLEQ-------GDYEEAIAALERALEQdpdylpalprlaelyEKLGDPEEALELLRKALELDPSDDLLLALADLLERKE 259
                         250
                  ....*....|....*...
gi 194474010  419 GcAQQAQRYqLQRQILQH 436
Cdd:COG2956   260 G-LEAALAL-LERQLRRH 275
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
1063-1158 4.35e-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: 46.32  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1063 TALRELRLSGNRLG-------DPCATELLAtlgtmPNLVLLDLSSNHLgpEGLRQLVegslgqtAFQNVEELDLSMNPLG 1135
Cdd:cd21340    90 TNLEELHIENQRLPpgekltfDPRSLAALS-----NSLRVLNISGNNI--DSLEPLA-------PLRNLEQLDASNNQIS 155
                          90       100
                  ....*....|....*....|...
gi 194474010 1136 DgcAQALASLLRTCPVLRTLRLQ 1158
Cdd:cd21340   156 D--LEELLDLLSSWPSLRELDLT 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
523-635 4.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  523 NRRNDMGETLLHRAcieGQLRRVQD----LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQ-Gcd 597
Cdd:PHA02876  335 NAADRLYITPLHQA---STLDRNKDivitLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKiG-- 409
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 194474010  598 giTPLHDALnCGH--FEVAELLIERGASVTLRTRKGLSPL 635
Cdd:PHA02876  410 --TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPL 446
PHA02875 PHA02875
ankyrin repeat protein; Provisional
529-631 5.29e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  529 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCdgiTPLHDALNC 608
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC---TPLIIAMAK 178
                          90       100
                  ....*....|....*....|...
gi 194474010  609 GHFEVAELLIERGASVTLRTRKG 631
Cdd:PHA02875  179 GDIAICKMLLDSGANIDYFGKNG 201
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
597-629 1.07e-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: 40.74  E-value: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 194474010   597 DGITPLHDA-LNCGHFEVAELLIERGASVTLRTR 629
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
530-624 1.94e-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: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  530 ETLLHRACIEGQLRRVQDLVKQGH-PLNPRDYCGWTPLHEACNYGHLEIVRFLLDhgAA---VDDP-GGQGCDGITPLHD 604
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVLME--AApelVNEPmTSDLYQGETALHI 95
                          90       100
                  ....*....|....*....|
gi 194474010  605 ALNCGHFEVAELLIERGASV 624
Cdd:cd22192    96 AVVNQNLNLVRELIARGADV 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
597-626 2.47e-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: 39.49  E-value: 2.47e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 194474010    597 DGITPLHDALNCGHFEVAELLIERGASVTL 626
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
529-639 3.52e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  529 GETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRfLLDHGAAVDDPGGQG---C--------- 596
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDPHAAGdllCtaakrndlt 636
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194474010  597 -----------------DGITPLHDALNCGHFEVAELLIERGASVT-LRTRKGLSPLETLQ 639
Cdd:PLN03192  637 amkellkqglnvdsedhQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTELRE 697
PHA03100 PHA03100
ankyrin repeat protein; Provisional
523-590 3.82e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 3.82e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
529-635 5.48e-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: 44.23  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  529 GETLLHRACIEGQLRRVQDLVKQG-HPLNPRD-------------YCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQ 594
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGaDVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGA---DIRAQ 165
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194474010  595 GCDGITPLH-------DALNCGHFEVAELLIERGASVTL---RTRKGLSPL 635
Cdd:cd22192   166 DSLGNTVLHilvlqpnKTFACQMYDLILSYDKEDDLQPLdlvPNNQGLTPF 216
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
294-452 5.53e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.21  E-value: 5.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  294 RLQQQLQEAEGNDLQGAMAICEQLGDLFSKADDFPKASEAYQKQLHFAEllnrpdlELAVIHESLATTLGDMKDYHKAVH 373
Cdd:COG3914    61 ALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNP-------DNAEALFNLGNLLLALGRLEEALA 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  374 HYEEELRLRKGNALeeakTWFNIGLAREEAGDayellapcFQKAFGCAQQAQRYQLQR-QILQHLYTVQLKL-QPQEARD 451
Cdd:COG3914   134 ALRRALALNPDFAE----AYLNLGEALRRLGR--------LEEAIAALRRALELDPDNaEALNNLGNALQDLgRLEEAIA 201

                  .
gi 194474010  452 T 452
Cdd:COG3914   202 A 202
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
1183-1280 7.37e-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: 42.47  E-value: 7.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010 1183 HLKTLSLSYNtlgapALARV--LQSLPTCTLLHLE----------------LSSVA-------ASKSNSSLIEPvIKYLT 1237
Cdd:cd21340    69 NLKKLYLGGN-----RISVVegLENLTNLEELHIEnqrlppgekltfdprsLAALSnslrvlnISGNNIDSLEP-LAPLR 142
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 194474010 1238 kegcALAHLTLSANCLSDkaVRELSRCLPSCPSLTSLDLSANP 1280
Cdd:cd21340   143 ----NLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNP 179
PHA03100 PHA03100
ankyrin repeat protein; Provisional
548-635 7.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  548 LVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAavdDPGGQGCDGITPLHDALNCGH-----FEVAELLIERGA 622
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGA---DINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGA 97
                          90
                  ....*....|...
gi 194474010  623 SVTLRTRKGLSPL 635
Cdd:PHA03100   98 NVNAPDNNGITPL 110
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
32-339 9.73e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 42.79  E-value: 9.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010   32 QLGELLASHGRFQEALEEHQQelhLLESVQDTlgcAVAHRKIGERLAEMENYSAALKhqhLYLDLAGSLSNHTELQRAWA 111
Cdd:COG2956    47 ALGNLYRRRGEYDRAIRIHQK---LLERDPDR---AEALLELAQDYLKAGLLDRAEE---LLEKLLELDPDDAEALRLLA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  112 TIgrthldvydhcqsrdslLQAQAAFEKSLAIVdEKLEgmltqrELSEMRTRLYLNLGLTCESLQQTAQCNNYFKKSIFL 191
Cdd:COG2956   118 EI-----------------YEQEGDWEKAIEVL-ERLL------KLGPENAHAYCELAELYLEQGDYDEAIEALEKALKL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  192 AEQNhlyedlFRARYNLGAIHWRGGQHSQAMRCLEgarecaramkmrfmeseccmlvsQVLQDLGDFLAAKRALKKAYRL 271
Cdd:COG2956   174 DPDC------ARALLLLAELYLEQGDYEEAIAALE-----------------------RALEQDPDYLPALPRLAELYEK 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474010  272 GSQKPNqrvaicqslkyvlAVVRLQQQLQEAEGNDLQGAmaiceqLGDLFSKADDFPKASEAYQKQLH 339
Cdd:COG2956   225 LGDPEE-------------ALELLRKALELDPSDDLLLA------LADLLERKEGLEAALALLERQLR 273
PHA02876 PHA02876
ankyrin repeat protein; Provisional
539-653 2.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194474010  539 EGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDpggQGCDGITPLHDALNCGHFEVAELLI 618
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI---IALDDLSVLECAVDSKNIDTIKAII 231
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 194474010  619 ERGASVtlrTRKGLSPLETLqqwvklyfRDLDLET 653
Cdd:PHA02876  232 DNRSNI---NKNDLSLLKAI--------RNEDLET 255
TPR_12 pfam13424
Tetratricopeptide repeat;
316-383 2.70e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 38.14  E-value: 2.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194474010   316 QLGDLFSKADDFPKASEAYQKQL-HFAELLNRPDLELAVIHESLATTLGDMKDYHKAVHHYEEELRLRK 383
Cdd:pfam13424    8 NLAAVLRRLGRYDEALELLEKALeIARRLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAE 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
523-590 6.39e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 6.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194474010  523 NRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDD 590
Cdd:COG0666   213 NAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
 
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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