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Conserved domains on  [gi|15229383|ref|NP_191872|]
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RAN GTPase activating protein 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WPP pfam13943
WPP domain;
15-110 2.68e-42

WPP domain;


:

Pssm-ID: 433596  Cd Length: 101  Bit Score: 146.42  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383    15 VKMWPPSKSTRLMLVERMTKNITTPSIFSRKYGLLSVEEAEQDAKRIEDLAFATANKHFqnEPDG-------DGTSAVHV 87
Cdd:pfam13943   1 IKLWPPSQRTRDAVVERLTENLSTPSILSKRYGTLSKEEAEENAKRIEEEAFAAANQHY--EPDGssgssddDGISALQL 78

                          90       100
                  ....*....|....*....|...
gi 15229383    88 YAKESSKLMLDVIKRGPQEESEV 110
Cdd:pfam13943  79 YSKEISKRMLEVVKRRPAAAAAK 101
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 176-456 8.65e-42

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: 155.33  E-value: 8.65e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 176 DQLTEVDLSDFVAGRPEAEALEVmnmfSSALEGSKLRYLNLSDNALGEKGIRAFASLINSQHDLEELYLMNDGISEDAAR 255
Cdd:COG5238 151 LGGNAVHLLGLAARLGLLAAISM----AKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAE 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 256 AVRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRECPSLEDFRCSSTRIGSEGGVALAEALEHCSHLKKLDLRDNMFGV 335
Cdd:COG5238 227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGD 306

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 336 EGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSEAlLKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSE 415
Cdd:COG5238 307 EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA-LQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGK 385

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15229383 416 NELKDEGTILIAKAVEgHDQLVEVDLSTNMIRRAGARALAQ 456
Cdd:COG5238 386 NNIGKQGAEALIDALQ-TNRLHTLILDGNLIGAEAQQRLEQ 425
 
Name Accession Description Interval E-value
WPP pfam13943
WPP domain;
15-110 2.68e-42

WPP domain;


Pssm-ID: 433596  Cd Length: 101  Bit Score: 146.42  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383    15 VKMWPPSKSTRLMLVERMTKNITTPSIFSRKYGLLSVEEAEQDAKRIEDLAFATANKHFqnEPDG-------DGTSAVHV 87
Cdd:pfam13943   1 IKLWPPSQRTRDAVVERLTENLSTPSILSKRYGTLSKEEAEENAKRIEEEAFAAANQHY--EPDGssgssddDGISALQL 78

                          90       100
                  ....*....|....*....|...
gi 15229383    88 YAKESSKLMLDVIKRGPQEESEV 110
Cdd:pfam13943  79 YSKEISKRMLEVVKRRPAAAAAK 101
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 176-456 8.65e-42

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: 155.33  E-value: 8.65e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 176 DQLTEVDLSDFVAGRPEAEALEVmnmfSSALEGSKLRYLNLSDNALGEKGIRAFASLINSQHDLEELYLMNDGISEDAAR 255
Cdd:COG5238 151 LGGNAVHLLGLAARLGLLAAISM----AKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAE 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 256 AVRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRECPSLEDFRCSSTRIGSEGGVALAEALEHCSHLKKLDLRDNMFGV 335
Cdd:COG5238 227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGD 306

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 336 EGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSEAlLKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSE 415
Cdd:COG5238 307 EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA-LQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGK 385

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15229383 416 NELKDEGTILIAKAVEgHDQLVEVDLSTNMIRRAGARALAQ 456
Cdd:COG5238 386 NNIGKQGAEALIDALQ-TNRLHTLILDGNLIGAEAQQRLEQ 425
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 133-446 1.48e-40

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: 149.04  E-value: 1.48e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 133 EEARDLLRPLADprnsYTKIRFSNRSFGSEAAKFAASVLSSiKDQLTEVDLSDFVAGRPEAEALEVMNMFSSaleGSKLR 212
Cdd:cd00116  13 ERATELLPKLLC----LQVLRLEGNTLGEEAAKALASALRP-QPSLKELCLSLNETGRIPRGLQSLLQGLTK---GCGLQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 213 YLNLSDNALGEKGIRAFASLINSQhDLEELYLMNDGISEDAARAV-RELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRE 291
Cdd:cd00116  85 ELDLSDNALGPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLaKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 292 CPSLEDFRCSSTRIGSEGGVALAEALEHCSHLKKLDLRDNMFGVEGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSE 371
Cdd:cd00116 164 NRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229383 372 ALLKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSENELKDEGTILIAKAVEG-HDQLVEVDLSTNMI 446
Cdd:cd00116 244 ALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEpGNELESLWVKDDSF 319
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
321-346 2.11e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.85  E-value: 2.11e-03
                           10        20
                   ....*....|....*....|....*.
gi 15229383    321 SHLKKLDLRDNMFGVEGGIALAKTLS 346
Cdd:smart00368   2 PSLRELDLSNNKLGDEGARALAEALK 27
 
Name Accession Description Interval E-value
WPP pfam13943
WPP domain;
15-110 2.68e-42

WPP domain;


Pssm-ID: 433596  Cd Length: 101  Bit Score: 146.42  E-value: 2.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383    15 VKMWPPSKSTRLMLVERMTKNITTPSIFSRKYGLLSVEEAEQDAKRIEDLAFATANKHFqnEPDG-------DGTSAVHV 87
Cdd:pfam13943   1 IKLWPPSQRTRDAVVERLTENLSTPSILSKRYGTLSKEEAEENAKRIEEEAFAAANQHY--EPDGssgssddDGISALQL 78

                          90       100
                  ....*....|....*....|...
gi 15229383    88 YAKESSKLMLDVIKRGPQEESEV 110
Cdd:pfam13943  79 YSKEISKRMLEVVKRRPAAAAAK 101
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 176-456 8.65e-42

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: 155.33  E-value: 8.65e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 176 DQLTEVDLSDFVAGRPEAEALEVmnmfSSALEGSKLRYLNLSDNALGEKGIRAFASLINSQHDLEELYLMNDGISEDAAR 255
Cdd:COG5238 151 LGGNAVHLLGLAARLGLLAAISM----AKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAE 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 256 AVRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRECPSLEDFRCSSTRIGSEGGVALAEALEHCSHLKKLDLRDNMFGV 335
Cdd:COG5238 227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGD 306

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 336 EGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSEAlLKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSE 415
Cdd:COG5238 307 EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA-LQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGK 385

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15229383 416 NELKDEGTILIAKAVEgHDQLVEVDLSTNMIRRAGARALAQ 456
Cdd:COG5238 386 NNIGKQGAEALIDALQ-TNRLHTLILDGNLIGAEAQQRLEQ 425
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 133-446 1.48e-40

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: 149.04  E-value: 1.48e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 133 EEARDLLRPLADprnsYTKIRFSNRSFGSEAAKFAASVLSSiKDQLTEVDLSDFVAGRPEAEALEVMNMFSSaleGSKLR 212
Cdd:cd00116  13 ERATELLPKLLC----LQVLRLEGNTLGEEAAKALASALRP-QPSLKELCLSLNETGRIPRGLQSLLQGLTK---GCGLQ 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 213 YLNLSDNALGEKGIRAFASLINSQhDLEELYLMNDGISEDAARAV-RELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRE 291
Cdd:cd00116  85 ELDLSDNALGPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLaKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 292 CPSLEDFRCSSTRIGSEGGVALAEALEHCSHLKKLDLRDNMFGVEGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSE 371
Cdd:cd00116 164 NRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229383 372 ALLKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSENELKDEGTILIAKAVEG-HDQLVEVDLSTNMI 446
Cdd:cd00116 244 ALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEpGNELESLWVKDDSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 234-499 9.67e-37

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: 141.47  E-value: 9.67e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 234 NSQHDLEELYLMNDGISEDAARAVRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRECPSLEDFRCSSTRIGSEGGVAL 313
Cdd:COG5238 177 LQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 314 AEALEHCSHLKKLDLRDNMFGVEGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSEALLKSAPslevlelagnditvk 393
Cdd:COG5238 257 AEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKT--------------- 321

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 394 stgnlaaciaskqsLAKLNLSENELKDEGTILIAKAVEGHDQLVEVDLSTNMIRRAGARALAQTVVKKNTFKLLNINGNF 473
Cdd:COG5238 322 --------------LHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNN 387

                       250       260
                ....*....|....*....|....*.
gi 15229383 474 ISEEGIDEVNDMFKDCLDKLVPLDDN 499
Cdd:COG5238 388 IGKQGAEALIDALQTNRLHTLILDGN 413
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 214-482 2.02e-31

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: 123.62  E-value: 2.02e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 214 LNLSDNALGEKGIRAFASLINSQHDLEELYL--MNDGISEDAARAVRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRE 291
Cdd:cd00116  28 LRLEGNTLGEEAAKALASALRPQPSLKELCLslNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRS 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 292 cPSLEDFRCSSTRIGSEGGVALAEALEHCSH-LKKLDLRDNMFGVEGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALS 370
Cdd:cd00116 108 -SSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALA 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 371 EALlKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSENELKDEGTILIAKAV-EGHDQLVEVDLSTNMIRRA 449
Cdd:cd00116 187 EGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNDITDD 265

                       250       260       270
                ....*....|....*....|....*....|...
gi 15229383 450 GARALAQTVVKKNTFKLLNINGNFISEEGIDEV 482
Cdd:cd00116 266 GAKDLAEVLAEKESLLELDLRGNKFGEEGAQLL 298
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 257-497 4.01e-23

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: 100.12  E-value: 4.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 257 VRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRECPSLE--DFRCSSTRIGSEGGVALAEALEHCSHLKKLDLRDNMFG 334
Cdd:cd00116  15 ATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKelCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 335 VEGGIALAKTLSVLThLTEIYMSYLNLEDEGTEALSEALLKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLS 414
Cdd:cd00116  95 PDGCGVLESLLRSSS-LQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 415 ENELKDEGTILIAKAVEGHDQLVEVDLSTNMIRRAGARALAQTVVKKNTFKLLNINGNFISEEGIDEVNDMFKDCLDKLV 494
Cdd:cd00116 174 NNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLL 253


                ...
gi 15229383 495 PLD 497
Cdd:cd00116 254 TLS 256
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
209-420 6.48e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 67.65  E-value: 6.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 209 SKLRYLNLSDNALGEKGIrAFASLINsqhdLEELYLMNDGISEdaaraVRELLPSTDKIRVLQFHNNmtgdeGATAIAEI 288
Cdd:COG4886 113 TNLESLDLSGNQLTDLPE-ELANLTN----LKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNN-----QLTDLPEE 177

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 289 VRECPSLEDFRCSSTRIGSeggvaLAEALEHCSHLKKLDLRDNMFGveggiALAKTLSVLTHLTEIYMSYLNLEDegtea 368
Cdd:COG4886 178 LGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD----- 242

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15229383 369 LSEalLKSAPSLEVLELAGNDIT-VKSTGNLaaciaskQSLAKLNLSENELKD 420
Cdd:COG4886 243 LPE--LGNLTNLEELDLSNNQLTdLPPLANL-------TNLKTLDLSNNQLTD 286
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 311-488 1.30e-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: 57.11  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 311 VALAEALEHCsHLKKLDLRDNMFGV-EGGIALAKTLSVLTHLTEIYMSYLNLEDEG----------TEALSEALLKSAPS 379
Cdd:COG5238 103 VALAETATAV-ATPPPDLRRIMAKTlEDSLILYLALPRRINLIQVLKDPLGGNAVHllglaarlglLAAISMAKALQNNS 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 380 LEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSENELKDEGTILIAKAVEGHDQLVEVDLSTNMIRRAGARALAQTVV 459
Cdd:COG5238 182 VETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALK 261

                       170       180
                ....*....|....*....|....*....
gi 15229383 460 KKNTFKLLNINGNFISEEGIDEVNDMFKD 488
Cdd:COG5238 262 NNTTVETLYLSGNQIGAEGAIALAKALQG 290
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 315-420 8.41e-06

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: 47.09  E-value: 8.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 315 EALEHCSHLKKLDLRDNMFGV-EGgialaktLSVLTHLTEIYMSYLNLEDEGTEALSEALLKS-APSLEVLELAGNDITv 392
Cdd:cd21340  62 ENLENLVNLKKLYLGGNRISVvEG-------LENLTNLEELHIENQRLPPGEKLTFDPRSLAAlSNSLRVLNISGNNID- 133

                        90       100
                ....*....|....*....|....*...
gi 15229383 393 kstgNLAaCIASKQSLAKLNLSENELKD 420
Cdd:cd21340 134 ----SLE-PLAPLRNLEQLDASNNQISD 156
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
315-476 1.55e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.24  E-value: 1.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 315 EALEHCSHLKKLDLRDNmfgveggialaKTLSVLTHLTEIYMSYLNLEDEGTEalsealLKSAPSLEVLELAGNDITvks 394
Cdd:COG4886  90 TDLGDLTNLTELDLSGN-----------EELSNLTNLESLDLSGNQLTDLPEE------LANLTNLKELDLSNNQLT--- 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229383 395 tgNLAACIASKQSLAKLNLSENELKDegtilIAKAVEGHDQLVEVDLSTNMIrragaRALAQTVVKKNTFKLLNINGNFI 474
Cdd:COG4886 150 --DLPEPLGNLTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQI-----TDLPEPLGNLTNLEELDLSGNQL 217


                ..
gi 15229383 475 SE 476
Cdd:COG4886 218 TD 219
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
321-346 2.11e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.85  E-value: 2.11e-03
                           10        20
                   ....*....|....*....|....*.
gi 15229383    321 SHLKKLDLRDNMFGVEGGIALAKTLS 346
Cdd:smart00368   2 PSLRELDLSNNKLGDEGARALAEALK 27
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
209-233 4.11e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.69  E-value: 4.11e-03
                           10        20
                   ....*....|....*....|....*
gi 15229383    209 SKLRYLNLSDNALGEKGIRAFASLI 233
Cdd:smart00368   2 PSLRELDLSNNKLGDEGARALAEAL 26
 
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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