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Conserved domains on  [gi|40255285|ref|NP_954600|]
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protein phosphatase 1 regulatory subunit 37 [Mus musculus]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 10061432)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
117-435 1.51e-89

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: 282.71  E-value: 1.51e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 117 CLDLKGEKLdyKTCEALEEVFKRLQFKVVDLEQTNLDEDGASALFDMIEYYESATHLNISFNKHIG-TRGWQAAAHMMRK 195
Cdd:cd00116   2 QLSLKGELL--KTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 196 TSCLQYLDARNTPLLDHSAPFVARALRIrSSLAVLHLENASLSGRPLMLLATALKMN-MNLRELYLADNKLNGlQDSAQL 274
Cdd:cd00116  80 GCGLQELDLSDNALGPDGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEG-ASCEAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 275 GNLLKFNCSLQILDLRNNHVLDSGLAYICEGLKEQrKGLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNE 354
Cdd:cd00116 158 AKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 355 GVRNLKNGLIS-NRSVLRLGLASTKLTCEGAVAVAEFIAESPRLLRLDLRENEIKTGG--LMALSLALKVNhSLLRLDLD 431
Cdd:cd00116 237 GAAALASALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGaqLLAESLLEPGN-ELESLWVK 315

                ....
gi 40255285 432 REPK 435
Cdd:cd00116 316 DDSF 319
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
117-435 1.51e-89

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: 282.71  E-value: 1.51e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 117 CLDLKGEKLdyKTCEALEEVFKRLQFKVVDLEQTNLDEDGASALFDMIEYYESATHLNISFNKHIG-TRGWQAAAHMMRK 195
Cdd:cd00116   2 QLSLKGELL--KTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 196 TSCLQYLDARNTPLLDHSAPFVARALRIrSSLAVLHLENASLSGRPLMLLATALKMN-MNLRELYLADNKLNGlQDSAQL 274
Cdd:cd00116  80 GCGLQELDLSDNALGPDGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEG-ASCEAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 275 GNLLKFNCSLQILDLRNNHVLDSGLAYICEGLKEQrKGLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNE 354
Cdd:cd00116 158 AKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 355 GVRNLKNGLIS-NRSVLRLGLASTKLTCEGAVAVAEFIAESPRLLRLDLRENEIKTGG--LMALSLALKVNhSLLRLDLD 431
Cdd:cd00116 237 GAAALASALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGaqLLAESLLEPGN-ELESLWVK 315

                ....
gi 40255285 432 REPK 435
Cdd:cd00116 316 DDSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
226-430 1.61e-32

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: 131.07  E-value: 1.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 226 SLAVLHLENASLSGRPLMLLATALKMNMNLRELYLADNKLnGLQDSAQLGNLLKFNCSLQILDLRNNHVLDSGLAYICEG 305
Cdd:COG5238 181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPI-GDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEA 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 306 LKEQRKgLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNEGVRNLKNGLISNRSVLRLGLASTKLTCEGAV 385
Cdd:COG5238 260 LKNNTT-VETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAI 338
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 40255285 386 AVAEFIAESPRLLRLDLRENEIKTGGLMALSLALKVNHSLLRLDL 430
Cdd:COG5238 339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNL 383
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
281-308 9.62e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.70  E-value: 9.62e-05
                           10        20
                   ....*....|....*....|....*...
gi 40255285    281 NCSLQILDLRNNHVLDSGLAYICEGLKE 308
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
117-435 1.51e-89

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: 282.71  E-value: 1.51e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 117 CLDLKGEKLdyKTCEALEEVFKRLQFKVVDLEQTNLDEDGASALFDMIEYYESATHLNISFNKHIG-TRGWQAAAHMMRK 195
Cdd:cd00116   2 QLSLKGELL--KTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 196 TSCLQYLDARNTPLLDHSAPFVARALRIrSSLAVLHLENASLSGRPLMLLATALKMN-MNLRELYLADNKLNGlQDSAQL 274
Cdd:cd00116  80 GCGLQELDLSDNALGPDGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEG-ASCEAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 275 GNLLKFNCSLQILDLRNNHVLDSGLAYICEGLKEQrKGLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNE 354
Cdd:cd00116 158 AKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 355 GVRNLKNGLIS-NRSVLRLGLASTKLTCEGAVAVAEFIAESPRLLRLDLRENEIKTGG--LMALSLALKVNhSLLRLDLD 431
Cdd:cd00116 237 GAAALASALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGaqLLAESLLEPGN-ELESLWVK 315

                ....
gi 40255285 432 REPK 435
Cdd:cd00116 316 DDSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
226-430 1.61e-32

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: 131.07  E-value: 1.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 226 SLAVLHLENASLSGRPLMLLATALKMNMNLRELYLADNKLnGLQDSAQLGNLLKFNCSLQILDLRNNHVLDSGLAYICEG 305
Cdd:COG5238 181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPI-GDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEA 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 306 LKEQRKgLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNEGVRNLKNGLISNRSVLRLGLASTKLTCEGAV 385
Cdd:COG5238 260 LKNNTT-VETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAI 338
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 40255285 386 AVAEFIAESPRLLRLDLRENEIKTGGLMALSLALKVNHSLLRLDL 430
Cdd:COG5238 339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNL 383
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
218-446 2.97e-27

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: 115.27  E-value: 2.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 218 ARALRIRSSLAVLHLENASLSGRPLMLLATALKMNMNLRELYLADNKLnGLQDSAQLGNLLKFNCSLQILDLRNNHVLDS 297
Cdd:COG5238 201 AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI-GDEGVIALAEALKNNTTVETLYLSGNQIGAE 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 298 GLAYICEGLKEQrKGLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNEGVRNLKNGLISNRSVLRLGLAST 377
Cdd:COG5238 280 GAIALAKALQGN-TTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDN 358
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40255285 378 KLTCEGAVAVAEFIAESPRLLRLDLRENEIKTGGLMALSLALKVNhSLLRLDLDREPKKEPVKSFIETQ 446
Cdd:COG5238 359 QIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLEQL 426
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
146-455 3.15e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.11  E-value: 3.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 146 DLEQTNLDEDGASALFDMIEYYESATHLNISFNKHIGtrgwqaaahmmrKTSCLQYLDARNTPLLDhsapfvaralrIRS 225
Cdd:COG4886  74 LLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELS------------NLTNLESLDLSGNQLTD-----------LPE 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 226 SLAVL-HLENASLSGRPLMLLATALKMNMNLRELYLADNKLNGLqdSAQLGNLLKfncsLQILDLRNNHV--LDSGLAyi 302
Cdd:COG4886 131 ELANLtNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDL--PEELGNLTN----LKELDLSNNQItdLPEPLG-- 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 303 ceglkeQRKGLVTLVLWNNQLTHtgmafLGMALPHTQSLETLNLGHNPIGN-EGVRNLKNgLISnrsvlrLGLASTKLTC 381
Cdd:COG4886 203 ------NLTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTDlPELGNLTN-LEE------LDLSNNQLTD 264
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40255285 382 egavavAEFIAESPRLLRLDLRENEIKTGGLMALSLALKVNHSLLRLDLDREPKKEPVKSFIETQKALLAEIQN 455
Cdd:COG4886 265 ------LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-431 5.37e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.55  E-value: 5.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285  92 KLNCRQIPKLLRQLQEFTDLEQRINCLDLKGEKLDYKTCEALEEVFKRLQFKVVDLEQTNLDEDGASALFDMIEYYESAT 171
Cdd:COG4886  60 LLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLK 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 172 HLNISFNK--HIGTrgwqaaahMMRKTSCLQYLDARNTPLLDhsapfvaralrIRSSLAVL-HLENASLSGRPLMLLATA 248
Cdd:COG4886 140 ELDLSNNQltDLPE--------PLGNLTNLKSLDLSNNQLTD-----------LPEELGNLtNLKELDLSNNQITDLPEP 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 249 LKMNMNLRELYLADNKLNGLQDS-AQLGNLLKFNCS---------------LQILDLRNNHVldsglayicEGLKE--QR 310
Cdd:COG4886 201 LGNLTNLEELDLSGNQLTDLPEPlANLTNLETLDLSnnqltdlpelgnltnLEELDLSNNQL---------TDLPPlaNL 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 311 KGLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNEGVRNLKNGLISNRSVLRLGLASTKLTCEGAVAVAEF 390
Cdd:COG4886 272 TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLT 351
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 40255285 391 IAESPRLLRLDLRENEIKTGGLMALSLALKVNHSLLRLDLD 431
Cdd:COG4886 352 LLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLL 392
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
281-308 9.62e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.70  E-value: 9.62e-05
                           10        20
                   ....*....|....*....|....*...
gi 40255285    281 NCSLQILDLRNNHVLDSGLAYICEGLKE 308
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
254-351 2.01e-03

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: 40.15  E-value: 2.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 254 NLRELYLADNKLnglqdsaQLGNLLKFNC--------SLQILDLRNNHVLD-SGLAYIceglkeqrKGLVTLVLWNNQLT 324
Cdd:cd21340  91 NLEELHIENQRL-------PPGEKLTFDPrslaalsnSLRVLNISGNNIDSlEPLAPL--------RNLEQLDASNNQIS 155
                        90       100
                ....*....|....*....|....*..
gi 40255285 325 HtgMAFLGMALPHTQSLETLNLGHNPI 351
Cdd:cd21340 156 D--LEELLDLLSSWPSLRELDLTGNPV 180
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
199-404 2.81e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 2.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 199 LQYLDARNTPLldHSAPFVARALrirSSLAVLHLENASLSGRPlmllatALKMNMNLRELYLADNKLNGLQDSAQLGNll 278
Cdd:COG4886 207 LEELDLSGNQL--TDLPEPLANL---TNLETLDLSNNQLTDLP------ELGNLTNLEELDLSNNQLTDLPPLANLTN-- 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40255285 279 kfncsLQILDLRNNHVLDSGLAYIcEGLKEQRKGLVTLVLWNNQLTHTGMAFLGMALPHTQSLETLNLGHNPIGNEGVRN 358
Cdd:COG4886 274 -----LKTLDLSNNQLTDLKLKEL-ELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLL 347
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 40255285 359 LKNGLISNRSVLRLGLASTKLTCEGAVAVAEFIAESPRLLRLDLRE 404
Cdd:COG4886 348 ALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLL 393
 
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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