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Conserved domains on  [gi|254588006|ref|NP_083162|]
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leucine-rich repeat and guanylate kinase domain-containing protein isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 416-537 9.52e-42

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


:

Pssm-ID: 238026  Cd Length: 137  Bit Score: 148.83  E-value: 9.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 416 MLILTGPAACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNR 495
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 254588006 496 DTIEGIARDGLASCIHMELEGVRSLKYSYFEPRYILVVPMDK 537
Cdd:cd00071   81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPPDY 122
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 176-371 1.13e-33

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.


The actual alignment was detected with superfamily member cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 128.75  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 176 LNASQNKLTTFFNFKPPQNLKKVDFSSNLISEMYDLSAYHTLTQLILDNNEIEEITGLENCISLTHLSLAGNKITTIKGL 255
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 256 GTLP-IKVLSLSNNMI----------ETITGLeeLKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIKELSEI-EYI 323
Cdd:cd21340   87 ENLTnLEELHIENQRLppgekltfdpRSLAAL--SNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 254588006 324 ENLPILRVLNLLRNPIQTKPEYWFFVIYMLLRLTELDQQKIKVEEKVF 371
Cdd:cd21340  165 SSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQF 212
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 132-185 1.71e-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.


The actual alignment was detected with superfamily member cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 46.70  E-value: 1.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254588006 132 LNLSHCELVDISILCGYVHLQKLNLSGNRIEDLSCV----SCMPYLLELNASQNKLTT 185
Cdd:cd21340  125 LNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELldllSSWPSLRELDLTGNPVCK 182
 
Name Accession Description Interval E-value
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 416-537 9.52e-42

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 148.83  E-value: 9.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 416 MLILTGPAACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNR 495
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 254588006 496 DTIEGIARDGLASCIHMELEGVRSLKYSYFEPRYILVVPMDK 537
Cdd:cd00071   81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPPDY 122
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 176-371 1.13e-33

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: 128.75  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 176 LNASQNKLTTFFNFKPPQNLKKVDFSSNLISEMYDLSAYHTLTQLILDNNEIEEITGLENCISLTHLSLAGNKITTIKGL 255
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 256 GTLP-IKVLSLSNNMI----------ETITGLeeLKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIKELSEI-EYI 323
Cdd:cd21340   87 ENLTnLEELHIENQRLppgekltfdpRSLAAL--SNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 254588006 324 ENLPILRVLNLLRNPIQTKPEYWFFVIYMLLRLTELDQQKIKVEEKVF 371
Cdd:cd21340  165 SSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQF 212
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
97-340 5.42e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 132.36  E-value: 5.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  97 NLEDKYDGILREETVAEAITGLGWSGRGTEQVYLNLNLSHCELVDISILCGYVHLQKLNLSGNRIEDL-SCVSCMPYLLE 175
Cdd:COG4886   61 LLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLpEELANLTNLKE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 176 LNASQNKLTT----FFNFKppqNLKKVDFSSNLISEM-YDLSAYHTLTQLILDNNEIEEI-TGLENCISLTHLSLAGNKI 249
Cdd:COG4886  141 LDLSNNQLTDlpepLGNLT---NLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQL 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 250 TTI-KGLGTLP-IKVLSLSNNMIETITGLEELKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIKELSeIEYIENLP 327
Cdd:COG4886  218 TDLpEPLANLTnLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLK-LKELELLL 296

                        250
                 ....*....|...
gi 254588006 328 ILRVLNLLRNPIQ 340
Cdd:COG4886  297 GLNSLLLLLLLLN 309
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 426-599 2.48e-23

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 97.75  E-value: 2.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006   426 GKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNRDTIEGIARDG 505
Cdd:smart00072   4 GKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006   506 LASCIHMELEGVRSLKYSYFEPRYILVVPMDKEKyegylRRKGLFSRAEIEIAVSRVDLYV-KVNQKYPGYFDAVINADD 584
Cdd:smart00072  84 KHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEE-----LERRLRQRGTETSERIQKRLAAaQKEAQEYHLFDYVIVNDD 158

                          170
                   ....*....|....*
gi 254588006   585 MDIAYQKLSELIREY 599
Cdd:smart00072 159 LEDAYEELKEILEAE 173
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 416-598 1.18e-22

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 95.64  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  416 MLILTGPAACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNR 495
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  496 DTIEGIARDGLASCIHMELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEIE--IAVSRVDLyvkvnqKYP 573
Cdd:TIGR03263  81 SPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIErrLAKAKKEI------AHA 154

                         170       180
                  ....*....|....*....|....*
gi 254588006  574 GYFDAVINADDMDIAYQKLSELIRE 598
Cdd:TIGR03263 155 DEFDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
417-599 7.70e-22

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 93.60  E-value: 7.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  417 LILTGPAACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNRD 496
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  497 TIEGIARDGLASCIHMELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEI--EIAVSRVDLyvkvnQKYPg 574
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKInkRMAAAEQEF-----QHYE- 158

                         170       180
                  ....*....|....*....|....*
gi 254588006  575 yFDAVINADDMDIAYQKLSELIREY 599
Cdd:pfam00625 159 -FDVIIVNDDLEEAYKKLKEALEAE 182
PLN02772 PLN02772
guanylate kinase
 411-615 3.06e-19

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 90.67  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 411 DAPYPMLIlTGPAACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHN 490
Cdd:PLN02772 133 NAEKPIVI-SGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNL 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 491 YGLNRDTIEGIArDGLASCI-HMELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEIEIAVSRVDLYVKVN 569
Cdd:PLN02772 212 YGTSIEAVEVVT-DSGKRCIlDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQG 290

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 254588006 570 QKyPGYFDAVINADDMDIAYQKLSELireyLGLTETAAKTLAPTAD 615
Cdd:PLN02772 291 KS-SGIFDHILYNDNLEECYKNLKKL----LGLDGLAAVNGVEAPE 331
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
416-597 1.56e-18

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 84.35  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 416 MLILTGPAACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFI-LTFNYGNHnYGLN 494
Cdd:COG0194    4 LIVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLeWAEVHGNY-YGTP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 495 RDTIEgiarDGLASCIHM----ELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEIE--IAVSRVDLyvkv 568
Cdd:COG0194   82 KAEVE----EALAAGKDVlleiDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIErrLAKAREEL---- 153

                        170       180
                 ....*....|....*....|....*....
gi 254588006 569 nqKYPGYFDAVINADDMDIAYQKLSELIR 597
Cdd:COG0194  154 --AHADEFDYVVVNDDLDRAVEELKAIIR 180
LRR_9 pfam14580
Leucine-rich repeat;
235-369 8.01e-15

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 73.26  E-value: 8.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  235 NCISLTHLSLAGNKITTIKGLG-TL-PIKVLSLSNNMIETITGLEELKALQNLDLSHNQISSL-QGLENH--DLLEVInL 309
Cdd:pfam14580  17 NPVRERELDLRGYKIPIIENLGaTLdQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIgEGLGEAlpNLTELI-L 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  310 EDNKIKELSEIEYIENLPILRVLNLLRNPIQTKPEYWFFVIYMLLRLTELDQQKIKVEEK 369
Cdd:pfam14580  96 TNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKER 155
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
217-344 3.33e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 50.85  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 217 LTQLILDNNEIEEITglENC-ISLTHLSLAGNKITTIKGlgTLP--IKVLSLS-NNMIETITGLEElkALQNLDLSHNQI 292
Cdd:PRK15370 201 ITTLILDNNELKSLP--ENLqGNIKTLYANSNQLTSIPA--TLPdtIQEMELSiNRITELPERLPS--ALQSLDLFHNKI 274

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254588006 293 SSLQglEN-HDLLEVINLEDNKIKELSeieyiENLPI-LRVLNLLRNPIQTKPE 344
Cdd:PRK15370 275 SCLP--ENlPEELRYLSVYDNSIRTLP-----AHLPSgITHLNVQSNSLTALPE 321
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 132-185 1.71e-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: 46.70  E-value: 1.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254588006 132 LNLSHCELVDISILCGYVHLQKLNLSGNRIEDLSCV----SCMPYLLELNASQNKLTT 185
Cdd:cd21340  125 LNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELldllSSWPSLRELDLTGNPVCK 182
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 132-168 2.99e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.07  E-value: 2.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 254588006  132 LNLSHCELVDISILCGYVHLQKLNLSGN-RIEDLSCVS 168
Cdd:pfam12799   6 LDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLA 43
 
Name Accession Description Interval E-value
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
 416-537 9.52e-42

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.


Pssm-ID: 238026  Cd Length: 137  Bit Score: 148.83  E-value: 9.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 416 MLILTGPAACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNR 495
Cdd:cd00071    1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 254588006 496 DTIEGIARDGLASCIHMELEGVRSLKYSYFEPRYILVVPMDK 537
Cdd:cd00071   81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPPDY 122
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 176-371 1.13e-33

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: 128.75  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 176 LNASQNKLTTFFNFKPPQNLKKVDFSSNLISEMYDLSAYHTLTQLILDNNEIEEITGLENCISLTHLSLAGNKITTIKGL 255
Cdd:cd21340    7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 256 GTLP-IKVLSLSNNMI----------ETITGLeeLKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIKELSEI-EYI 323
Cdd:cd21340   87 ENLTnLEELHIENQRLppgekltfdpRSLAAL--SNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 254588006 324 ENLPILRVLNLLRNPIQTKPEYWFFVIYMLLRLTELDQQKIKVEEKVF 371
Cdd:cd21340  165 SSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTERQF 212
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
97-340 5.42e-33

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 132.36  E-value: 5.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  97 NLEDKYDGILREETVAEAITGLGWSGRGTEQVYLNLNLSHCELVDISILCGYVHLQKLNLSGNRIEDL-SCVSCMPYLLE 175
Cdd:COG4886   61 LLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLpEELANLTNLKE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 176 LNASQNKLTT----FFNFKppqNLKKVDFSSNLISEM-YDLSAYHTLTQLILDNNEIEEI-TGLENCISLTHLSLAGNKI 249
Cdd:COG4886  141 LDLSNNQLTDlpepLGNLT---NLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQL 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 250 TTI-KGLGTLP-IKVLSLSNNMIETITGLEELKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIKELSeIEYIENLP 327
Cdd:COG4886  218 TDLpEPLANLTnLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLK-LKELELLL 296

                        250
                 ....*....|...
gi 254588006 328 ILRVLNLLRNPIQ 340
Cdd:COG4886  297 GLNSLLLLLLLLN 309
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
173-360 1.32e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 104.25  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 173 LLELNASQNKLTTFFNFKPPQNLKKVDFSSNLisemyDLSAYHTLTQLILDNNEIEEI-TGLENCISLTHLSLAGNKITT 251
Cdd:COG4886   76 LLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-----ELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTD 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 252 I-KGLGTLP-IKVLSLSNNMIETIT-GLEELKALQNLDLSHNQISSL-QGLENHDLLEVINLEDNKIKELSEIeyIENLP 327
Cdd:COG4886  151 LpEPLGNLTnLKSLDLSNNQLTDLPeELGNLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEP--LANLT 228

                        170       180       190
                 ....*....|....*....|....*....|...
gi 254588006 328 ILRVLNLLRNPIQTKPEywffvIYMLLRLTELD 360
Cdd:COG4886  229 NLETLDLSNNQLTDLPE-----LGNLTNLEELD 256
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
 426-599 2.48e-23

Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to GDP. Structure resembles that of adenylate kinase. So-called membrane-associated guanylate kinase homologues (MAGUKs) do not possess guanylate kinase activities; instead at least some possess protein-binding functions.


Pssm-ID: 214504 [Multi-domain]  Cd Length: 174  Bit Score: 97.75  E-value: 2.48e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006   426 GKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNRDTIEGIARDG 505
Cdd:smart00072   4 GKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006   506 LASCIHMELEGVRSLKYSYFEPRYILVVPMDKEKyegylRRKGLFSRAEIEIAVSRVDLYV-KVNQKYPGYFDAVINADD 584
Cdd:smart00072  84 KHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEE-----LERRLRQRGTETSERIQKRLAAaQKEAQEYHLFDYVIVNDD 158

                          170
                   ....*....|....*
gi 254588006   585 MDIAYQKLSELIREY 599
Cdd:smart00072 159 LEDAYEELKEILEAE 173
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
 416-598 1.18e-22

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 213788  Cd Length: 179  Bit Score: 95.64  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  416 MLILTGPAACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNR 495
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  496 DTIEGIARDGLASCIHMELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEIE--IAVSRVDLyvkvnqKYP 573
Cdd:TIGR03263  81 SPVEEALAAGKDVLLEIDVQGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIErrLAKAKKEI------AHA 154

                         170       180
                  ....*....|....*....|....*
gi 254588006  574 GYFDAVINADDMDIAYQKLSELIRE 598
Cdd:TIGR03263 155 DEFDYVIVNDDLEKAVEELKSIILA 179
Guanylate_kin pfam00625
Guanylate kinase;
417-599 7.70e-22

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 93.60  E-value: 7.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  417 LILTGPAACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNRD 496
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  497 TIEGIARDGLASCIHMELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEI--EIAVSRVDLyvkvnQKYPg 574
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGKEQEEKInkRMAAAEQEF-----QHYE- 158

                         170       180
                  ....*....|....*....|....*
gi 254588006  575 yFDAVINADDMDIAYQKLSELIREY 599
Cdd:pfam00625 159 -FDVIIVNDDLEEAYKKLKEALEAE 182
PLN02772 PLN02772
guanylate kinase
 411-615 3.06e-19

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 90.67  E-value: 3.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 411 DAPYPMLIlTGPAACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHN 490
Cdd:PLN02772 133 NAEKPIVI-SGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNL 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 491 YGLNRDTIEGIArDGLASCI-HMELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEIEIAVSRVDLYVKVN 569
Cdd:PLN02772 212 YGTSIEAVEVVT-DSGKRCIlDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQG 290

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 254588006 570 QKyPGYFDAVINADDMDIAYQKLSELireyLGLTETAAKTLAPTAD 615
Cdd:PLN02772 291 KS-SGIFDHILYNDNLEECYKNLKKL----LGLDGLAAVNGVEAPE 331
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
132-374 9.18e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 89.61  E-value: 9.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 132 LNLSHCELVDISI-LCGYVHLQKLNLSGNRIEDLSC-VSCMPYLLELNASQNKLTTF-FNFKPPQNLKKVDFSSNLISEM 208
Cdd:COG4886  164 LDLSNNQLTDLPEeLGNLTNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDL 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 209 YDLSAYHTLTQLILDNNEIEEITGLENCISLTHLSLAGNKITTIKG---LGTLPIKVLSLSNNMIETITGLEELKALQNL 285
Cdd:COG4886  244 PELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLkelELLLGLNSLLLLLLLLNLLELLILLLLLTTL 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 286 DLSHNQISSLQGLENHDLLEVINLEDNKIKELSEIEYIENLPILRVLNLLRNPIQTKPEYWFFVIYMLLRLTELDQQKIK 365
Cdd:COG4886  324 LLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLL 403


                 ....*....
gi 254588006 366 VEEKVFAVN 374
Cdd:COG4886  404 TLALLDAVN 412
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
416-597 1.56e-18

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 84.35  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 416 MLILTGPAACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFI-LTFNYGNHnYGLN 494
Cdd:COG0194    4 LIVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLeWAEVHGNY-YGTP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 495 RDTIEgiarDGLASCIHM----ELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEIE--IAVSRVDLyvkv 568
Cdd:COG0194   82 KAEVE----EALAAGKDVlleiDVQGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIErrLAKAREEL---- 153

                        170       180
                 ....*....|....*....|....*....
gi 254588006 569 nqKYPGYFDAVINADDMDIAYQKLSELIR 597
Cdd:COG0194  154 --AHADEFDYVVVNDDLDRAVEELKAIIR 180
LRR_9 pfam14580
Leucine-rich repeat;
235-369 8.01e-15

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 73.26  E-value: 8.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  235 NCISLTHLSLAGNKITTIKGLG-TL-PIKVLSLSNNMIETITGLEELKALQNLDLSHNQISSL-QGLENH--DLLEVInL 309
Cdd:pfam14580  17 NPVRERELDLRGYKIPIIENLGaTLdQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIgEGLGEAlpNLTELI-L 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006  310 EDNKIKELSEIEYIENLPILRVLNLLRNPIQTKPEYWFFVIYMLLRLTELDQQKIKVEEK 369
Cdd:pfam14580  96 TNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKER 155
gmk PRK00300
guanylate kinase; Provisional
 416-597 3.35e-14

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 72.04  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 416 MLILTGPAACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFI--LTFnYGNHnYGL 493
Cdd:PRK00300   7 LIVLSGPSGAGKSTLVKALLERDPN-LQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLewAEV-FGNY-YGT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 494 NRDTIEgiarDGLASCIHM----ELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGL---------FSRAEIEIA-V 559
Cdd:PRK00300  84 PRSPVE----EALAAGKDVlleiDWQGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTdseeviarrLAKAREEIAhA 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 254588006 560 SRVDlYVkvnqkypgyfdaVINaDDMDIAYQKLSELIR 597
Cdd:PRK00300 160 SEYD-YV------------IVN-DDLDTALEELKAIIR 183
gmk PRK14738
guanylate kinase; Provisional
 412-597 2.80e-12

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 66.68  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 412 APYPMLI-LTGPAACGKRELAHRLcRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFN-YGNH 489
Cdd:PRK14738  10 PAKPLLVvISGPSGVGKDAVLARM-RERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEvYGNY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 490 nYGLNRDTIegiaRDGLAS----CIHMELEGVRSLKYSYFEPRYILVVPMDKEKYEGYLRRKGLFSRAEIE--IAVSRVD 563
Cdd:PRK14738  89 -YGVPKAPV----RQALASgrdvIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELErrLATAPLE 163

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 254588006 564 LyvkvnQKYPGYFDAVIN-ADDMDIAYQKLSELIR 597
Cdd:PRK14738 164 L-----EQLPEFDYVVVNpEDRLDEAVAQIMAIIS 193
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
173-360 6.27e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.42  E-value: 6.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 173 LLELNASQNKLTTFFNFKPPQNLKKVDFSSNLISEMYDLSAYHTLTQLILDNNEIEEITGLENCISLTHLSLAGNKITTI 252
Cdd:COG4886   11 KLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 253 KGLGTLPIKVLSLSNNmietiTGLEELKALQNLDLSHNQISSL-QGLENHDLLEVINLEDNKIKELSeiEYIENLPILRV 331
Cdd:COG4886   91 DLGDLTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLP--EPLGNLTNLKS 163

                        170       180
                 ....*....|....*....|....*....
gi 254588006 332 LNLLRNPIQTKPEywffVIYMLLRLTELD 360
Cdd:COG4886  164 LDLSNNQLTDLPE----ELGNLTNLKELD 188
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
131-312 4.36e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.56  E-value: 4.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 131 NLNLSHCELVDISILCGYVHLQKLNLSGNRIEDLSCVSCMPYLLELNASQNKLTTFfnfkppqNLKKVDFSSNLISEMYD 210
Cdd:COG4886  232 TLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDL-------KLKELELLLGLNSLLLL 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 211 LSAYHTLTQLILDNNEI----EEITGLENCISLTHLSLAGNKITTIKGLGTLPIKVLSLSNNMIETITGLEELKALQNLD 286
Cdd:COG4886  305 LLLLNLLELLILLLLLTtlllLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLAL 384

                        170       180
                 ....*....|....*....|....*.
gi 254588006 287 LSHNQISSLQGLENHDLLEVINLEDN 312
Cdd:COG4886  385 LLLTLLLLLLTTTAGVLLLTLALLDA 410
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 215-351 2.43e-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: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 215 HTLTQLILDNNEIEE------ITGLENCISLTHLSLAGNKITT------IKGL-GTLPIKVLSLSNNMIET------ITG 275
Cdd:COG5238  264 TTVETLYLSGNQIGAegaialAKALQGNTTLTSLDLSVNRIGDegaialAEGLqGNKTLHTLNLAYNGIGAqgaialAKA 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 276 LEELKALQNLDLSHNQISS------LQGLENHDLLEVINLEDNKIKELSEIEYIENLPI--LRVLNLLRNPIQTKPEYWF 347
Cdd:COG5238  344 LQENTTLHSLDLSDNQIGDegaialAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTnrLHTLILDGNLIGAEAQQRL 423


                 ....
gi 254588006 348 FVIY 351
Cdd:COG5238  424 EQLL 427
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 129-339 4.27e-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: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 129 YLNLNLSHCELVDISILCGYVHLQKLNLSGNRIE--DLSCVSCMPYLLELNASQnklttffnFKPPQNLKKVDFSSNLIS 206
Cdd:COG5238  150 PLGGNAVHLLGLAARLGLLAAISMAKALQNNSVEtvYLGCNQIGDEGIEELAEA--------LTQNTTVTTLWLKRNPIG 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 207 E--MYD----LSAYHTLTQLILDNNEIEE------ITGLENCISLTHLSLAGNKITtikglgtlpikvlslSNNMIETIT 274
Cdd:COG5238  222 DegAEIlaeaLKGNKSLTTLDLSNNQIGDegvialAEALKNNTTVETLYLSGNQIG---------------AEGAIALAK 286

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254588006 275 GLEELKALQNLDLSHNQISS------LQGLENHDLLEVINLEDNKIKELSEIEYIENL---PILRVLNLLRNPI 339
Cdd:COG5238  287 ALQGNTTLTSLDLSVNRIGDegaialAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALqenTTLHSLDLSDNQI 360
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 260-300 5.40e-07

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 46.85  E-value: 5.40e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 254588006  260 IKVLSLSNNMIETITGLEELKALQNLDLSHN-QISSLQGLEN 300
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLAN 44
gmk PRK14737
guanylate kinase; Provisional
 416-596 1.82e-06

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 49.22  E-value: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 416 MLILTGPAACGKRELAHRLCRQFSTYFRYGAChTTRPPYFGEGDRVDYHFISQEVFDEMLNMGKFILTFNYGNHNYGLNR 495
Cdd:PRK14737   6 LFIISSVAGGGKSTIIQALLEEHPDFLFSISC-TTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTPK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 496 DTIEGIARDGLASCIHMELEGVRSLKYSYFEPRY-ILVVPMDKEKYEGYLRRKGLFSRAEIEiavSRVDLYVKVNQKYPG 574
Cdd:PRK14737  85 AFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVtIFIEPPSEEEWEERLIHRGTDSEESIE---KRIENGIIELDEANE 161

                        170       180
                 ....*....|....*....|..
gi 254588006 575 yFDAVINADDMDIAYQKLSELI 596
Cdd:PRK14737 162 -FDYKIINDDLEDAIADLEAII 182
LRR_8 pfam13855
Leucine rich repeat;
282-339 2.87e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.21  E-value: 2.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254588006  282 LQNLDLSHNQISSL-----QGLENhdlLEVINLEDNKIKELSEIEyIENLPILRVLNLLRNPI 339
Cdd:pfam13855   3 LRSLDLSNNRLTSLddgafKGLSN---LKVLDLSNNLLTTLSPGA-FSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
217-344 3.33e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 50.85  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 217 LTQLILDNNEIEEITglENC-ISLTHLSLAGNKITTIKGlgTLP--IKVLSLS-NNMIETITGLEElkALQNLDLSHNQI 292
Cdd:PRK15370 201 ITTLILDNNELKSLP--ENLqGNIKTLYANSNQLTSIPA--TLPdtIQEMELSiNRITELPERLPS--ALQSLDLFHNKI 274

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 254588006 293 SSLQglEN-HDLLEVINLEDNKIKELSeieyiENLPI-LRVLNLLRNPIQTKPE 344
Cdd:PRK15370 275 SCLP--ENlPEELRYLSVYDNSIRTLP-----AHLPSgITHLNVQSNSLTALPE 321
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 150-339 5.83e-06

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: 49.28  E-value: 5.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 150 HLQKLNLSGNRIEDLSC--VSCM----PYLLELNASQNKLTTFF--------NFKPPQNLKKVDFSSNLISE-----MYD 210
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAkaLASAlrpqPSLKELCLSLNETGRIPrglqsllqGLTKGCGLQELDLSDNALGPdgcgvLES 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 211 LSAYHTLTQLILDNNEIEEITGLENCISLTHLSLAgnkittikglgtlpIKVLSLSNNMIE---TITGLEELKA---LQN 284
Cdd:cd00116  104 LLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPA--------------LEKLVLGRNRLEgasCEALAKALRAnrdLKE 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254588006 285 LDLSHNQISS------LQGLENHDLLEVINLEDNKI-----KELSEIeyIENLPILRVLNLLRNPI 339
Cdd:cd00116  170 LNLANNGIGDagiralAEGLKANCNLEVLDLNNNGLtdegaSALAET--LASLKSLEVLNLGDNNL 233
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 151-206 8.99e-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: 47.47  E-value: 8.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 151 LQKLNLSGNRIEDLSCVSCMPYLLELNASQNKLTTFFNFKPP----QNLKKVDFSSNLIS 206
Cdd:cd21340  122 LRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELLDLlsswPSLRELDLTGNPVC 181
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 155-293 9.49e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.46  E-value: 9.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 155 NLSGnRIEDLSCVscMPYLLELNASQNKlttFFNFKP----PQNLKKVDFSSNLISEMY--DLSAYHTLTQLILDNNEIE 228
Cdd:PLN00113 439 NLQG-RINSRKWD--MPSLQMLSLARNK---FFGGLPdsfgSKRLENLDLSRNQFSGAVprKLGSLSELMQLKLSENKLS 512

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254588006 229 -EITG-LENCISLTHLSLAGNKITtikglGTLPikvlslsnnmietiTGLEELKALQNLDLSHNQIS 293
Cdd:PLN00113 513 gEIPDeLSSCKKLVSLDLSHNQLS-----GQIP--------------ASFSEMPVLSQLDLSQNQLS 560
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 238-278 1.64e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 42.62  E-value: 1.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 254588006  238 SLTHLSLAGNKITTIKGLGTLP-IKVLSLS-NNMIETITGLEE 278
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPnLETLDLSgNNKITDLSDLAN 44
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 132-185 1.71e-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: 46.70  E-value: 1.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254588006 132 LNLSHCELVDISILCGYVHLQKLNLSGNRIEDLSCV----SCMPYLLELNASQNKLTT 185
Cdd:cd21340  125 LNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELldllSSWPSLRELDLTGNPVCK 182
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 280-321 3.14e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 41.85  E-value: 3.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 254588006  280 KALQNLDLSHNQISSLQGLENHDLLEVINLEDN-KIKELSEIE 321
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLA 43
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 217-255 9.53e-05

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 40.31  E-value: 9.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 254588006  217 LTQLILDNNEIEEITGLENCISLTHLSLAGN-KITTIKGL 255
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDL 42
LRR_8 pfam13855
Leucine rich repeat;
216-292 1.61e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 1.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254588006  216 TLTQLILDNNEIEEITG--LENCISLTHLSLAGNKITTIkglgtlpikvlslSNNMietitgLEELKALQNLDLSHNQI 292
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTL-------------SPGA------FSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 151-334 4.22e-04

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: 43.11  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 151 LQKLNLSGNRIED----LSCVS---CMPYLLELNASQNKLTtffnfkppqnlkkvDFSSNLISEmyDLSAYHTLTQLILD 223
Cdd:cd00116  110 LQELKLNNNGLGDrglrLLAKGlkdLPPALEKLVLGRNRLE--------------GASCEALAK--ALRANRDLKELNLA 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 224 NNEIEE--ITGLenCISLTHLSLagnkittikglgtlpIKVLSLSNNMIETITG------LEELKALQNLDLSHNQISSL 295
Cdd:cd00116  174 NNGIGDagIRAL--AEGLKANCN---------------LEVLDLNNNGLTDEGAsalaetLASLKSLEVLNLGDNNLTDA 236

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 254588006 296 -------QGLENHDLLEVINLEDNKIKEL---SEIEYIENLPILRVLNL 334
Cdd:cd00116  237 gaaalasALLSPNISLLTLSLSCNDITDDgakDLAEVLAEKESLLELDL 285
LRR_8 pfam13855
Leucine rich repeat;
261-314 1.36e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.50  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254588006  261 KVLSLSNNMIETITG--LEELKALQNLDLSHNQISSL-----QGLENhdlLEVINLEDNKI 314
Cdd:pfam13855   4 RSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLspgafSGLPS---LRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 145-293 2.79e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 41.37  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 145 LCGYVHLQKLNLSGNRIE-----DLS-CVSCMPYLLELNASQNKLTTFFNFKPPQNLkkVDFSSNLISEMYDLSAYH--T 216
Cdd:PLN00113 376 LCSSGNLFKLILFSNSLEgeipkSLGaCRSLRRVRLQDNSFSGELPSEFTKLPLVYF--LDISNNNLQGRINSRKWDmpS 453

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254588006 217 LTQLILDNN----EIEEITGLENcisLTHLSLAGNKITTI--KGLGTLP-IKVLSLSNNMI--ETITGLEELKALQNLDL 287
Cdd:PLN00113 454 LQMLSLARNkffgGLPDSFGSKR---LENLDLSRNQFSGAvpRKLGSLSeLMQLKLSENKLsgEIPDELSSCKKLVSLDL 530


                 ....*.
gi 254588006 288 SHNQIS 293
Cdd:PLN00113 531 SHNQLS 536
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 132-168 2.99e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 36.07  E-value: 2.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 254588006  132 LNLSHCELVDISILCGYVHLQKLNLSGN-RIEDLSCVS 168
Cdd:pfam12799   6 LDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLA 43
 
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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