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Conserved domains on  [gi|1370509528|ref|XP_024302429|]
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leucine-rich repeat and guanylate kinase domain-containing protein isoform X4 [Homo sapiens]

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), ...
416-592 6.70e-43

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: 151.92  E-value: 6.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNR 495
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 496 DTVEGIARDGLASCIHMEIEGVRSLKYSYFEPRYILVVPMnkekyegylrrkglfsraeiefavsrvdlyikinqnfpgy 575
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120
                         170
                  ....*....|....*..
gi 1370509528 576 fDEVINADDLDVAYQKL 592
Cdd:cd00071   121 -DYVIVNDDLEKAYEEL 136
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
176-369 3.52e-32

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: 124.51  E-value: 3.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 176 LNASQNNLTTFFNFKPPKNLKKADFSHNQISEICDLSAYHALTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTINGL 255
Cdd:cd21340     7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 256 NKLP-IKILCLSNNQI----------EMITGLedLKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIAELREI-EYI 323
Cdd:cd21340    87 ENLTnLEELHIENQRLppgekltfdpRSLAAL--SNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLL 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370509528 324 KNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKKIKVEEK 369
Cdd:cd21340   165 SSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTER 210
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
132-181 2.71e-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: 45.93  E-value: 2.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370509528 132 LTLSGCNLIDVSILCGYVHLQKLDLSANKIEDLSCV----SCMPYLLELNASQN 181
Cdd:cd21340   125 LNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELldllSSWPSLRELDLTGN 178
 
Name Accession Description Interval E-value
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
416-592 6.70e-43

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: 151.92  E-value: 6.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNR 495
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 496 DTVEGIARDGLASCIHMEIEGVRSLKYSYFEPRYILVVPMnkekyegylrrkglfsraeiefavsrvdlyikinqnfpgy 575
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120
                         170
                  ....*....|....*..
gi 1370509528 576 fDEVINADDLDVAYQKL 592
Cdd:cd00071   121 -DYVIVNDDLEKAYEEL 136
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
176-369 3.52e-32

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: 124.51  E-value: 3.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 176 LNASQNNLTTFFNFKPPKNLKKADFSHNQISEICDLSAYHALTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTINGL 255
Cdd:cd21340     7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 256 NKLP-IKILCLSNNQI----------EMITGLedLKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIAELREI-EYI 323
Cdd:cd21340    87 ENLTnLEELHIENQRLppgekltfdpRSLAAL--SNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLL 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370509528 324 KNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKKIKVEEK 369
Cdd:cd21340   165 SSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTER 210
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
132-377 1.58e-29

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 121.96  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 132 LTLSGCNLIDV-SILCGYVHLQKLDLSANKIEDL-SCVSCMPYLLELNASQNNLTTF-FNFKPPKNLKKADFSHNQISEI 208
Cdd:COG4886   118 LDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDL 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 209 -CDLSAYHALTKLILDGNEIEEIS-GLEMCNNLIHLSLANNKITTINGLNKLP-IKILCLSNNQIEMITGLEDLKALQNL 285
Cdd:COG4886   198 pEPLGNLTNLEELDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNLTnLEELDLSNNQLTDLPPLANLTNLKTL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 286 DLSHNQISS--LQGLENHDLLEVINLEDNKIAELREIEYIKNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKK 363
Cdd:COG4886   278 DLSNNQLTDlkLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLN 357
                         250
                  ....*....|....
gi 1370509528 364 IKVEEKVSAVNKYD 377
Cdd:COG4886   358 LLSLLLTLLLTLGL 371
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
426-599 1.65e-22

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: 95.05  E-value: 1.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528  426 GKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNRDTVEGIARDG 505
Cdd:smart00072   4 GKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528  506 LASCIHMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGlfsrAEIEFAVSRVDLYIKINQNFPGYFDEVINADDL 585
Cdd:smart00072  84 KHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRG----TETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159
                          170
                   ....*....|....
gi 1370509528  586 DVAYQKLSQLIREY 599
Cdd:smart00072 160 EDAYEELKEILEAE 173
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
416-598 2.19e-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: 94.87  E-value: 2.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNR 495
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 496 DTVEGIARDGLaSCIhMEIE--GVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIE--FAVSRVDL-YIKinq 570
Cdd:TIGR03263  81 SPVEEALAAGK-DVL-LEIDvqGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIErrLAKAKKEIaHAD--- 155
                         170       180
                  ....*....|....*....|....*...
gi 1370509528 571 nfpgYFDEVINADDLDVAYQKLSQLIRE 598
Cdd:TIGR03263 156 ----EFDYVIVNDDLEKAVEELKSIILA 179
PLN02772 PLN02772
guanylate kinase
411-637 1.01e-21

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 98.37  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 411 DAPYPMLIlAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHK 490
Cdd:PLN02772  133 NAEKPIVI-SGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 491 YGLNRDTVEGIArDGLASCI-HMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIEFAVSRVDLYIKIN 569
Cdd:PLN02772  212 YGTSIEAVEVVT-DSGKRCIlDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQG 290
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509528 570 QNfPGYFDEVINADDLDVAYQKLSQLireyLGLTeepakslATTADVKTSHLKPEAHPTKYISSNMGD 637
Cdd:PLN02772  291 KS-SGIFDHILYNDNLEECYKNLKKL----LGLD-------GLAAVNGVEAPEGINLPKEHSVSKMDD 346
Guanylate_kin pfam00625
Guanylate kinase;
417-599 2.18e-21

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 92.06  E-value: 2.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 417 LILAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNRD 496
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 497 TVEGIARDGLASCIHMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKG------LFSRAEiefavsrvdlyiKINQ 570
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGkeqeekINKRMA------------AAEQ 152
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370509528 571 NFPGY-FDEVINADDLDVAYQKLSQLIREY 599
Cdd:pfam00625 153 EFQHYeFDVIIVNDDLEEAYKKLKEALEAE 182
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
416-597 2.49e-17

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 80.88  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFI-LTFSYGNHkYGLN 494
Cdd:COG0194     4 LIVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLeWAEVHGNY-YGTP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 495 RDTVEgiarDGLASCIH--MEIE--GVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIE--FAVSRVDLyiki 568
Cdd:COG0194    82 KAEVE----EALAAGKDvlLEIDvqGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIErrLAKAREEL---- 153
                         170       180
                  ....*....|....*....|....*....
gi 1370509528 569 nqNFPGYFDEVINADDLDVAYQKLSQLIR 597
Cdd:COG0194   154 --AHADEFDYVVVNDDLDRAVEELKAIIR 180
LRR_9 pfam14580
Leucine-rich repeat;
242-376 6.67e-09

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 55.93  E-value: 6.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 242 LSLANNKITTINGLNKL--PIKILCLSNNQIEMITGLEDLKALQNLDLSHNQISSL-QGLENH-DLLEVINLEDNKIAEL 317
Cdd:pfam14580  24 LDLRGYKIPIIENLGATldQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIgEGLGEAlPNLTELILTNNNLQEL 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509528 318 REIEYIKNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKKIKVEEKVSAVNKY 376
Cdd:pfam14580 104 GDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMF 162
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
154-293 4.72e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.70  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 154 LDLSANKIEDL--SCVSCMPYLLELNASQNNlttFFNFKP----PKNLKKADFSHNQISEIC--DLSAYHALTKLILDGN 225
Cdd:PLN00113  433 LDISNNNLQGRinSRKWDMPSLQMLSLARNK---FFGGLPdsfgSKRLENLDLSRNQFSGAVprKLGSLSELMQLKLSEN 509
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 226 EIE-EI-SGLEMCNNLIHLSLANNKITTinglnklpikilclsnnqiEMITGLEDLKALQNLDLSHNQIS 293
Cdd:PLN00113  510 KLSgEIpDELSSCKKLVSLDLSHNQLSG-------------------QIPASFSEMPVLSQLDLSQNQLS 560
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
132-181 2.71e-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: 45.93  E-value: 2.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370509528 132 LTLSGCNLIDVSILCGYVHLQKLDLSANKIEDLSCV----SCMPYLLELNASQN 181
Cdd:cd21340   125 LNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELldllSSWPSLRELDLTGN 178
 
Name Accession Description Interval E-value
GMPK cd00071
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...
416-592 6.70e-43

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: 151.92  E-value: 6.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNR 495
Cdd:cd00071     1 LIVLSGPSGVGKSTLLKRLLEEFDPNFGFSVSHTTRKPRPGEVDGVDYHFVSKEEFERLIENGEFLEWAEFHGNYYGTSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 496 DTVEGIARDGLASCIHMEIEGVRSLKYSYFEPRYILVVPMnkekyegylrrkglfsraeiefavsrvdlyikinqnfpgy 575
Cdd:cd00071    81 AAVEEALAEGKIVILEIDVQGARQVKKSYPDAVSIFILPP---------------------------------------- 120
                         170
                  ....*....|....*..
gi 1370509528 576 fDEVINADDLDVAYQKL 592
Cdd:cd00071   121 -DYVIVNDDLEKAYEEL 136
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
176-369 3.52e-32

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: 124.51  E-value: 3.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 176 LNASQNNLTTFFNFKPPKNLKKADFSHNQISEICDLSAYHALTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTINGL 255
Cdd:cd21340     7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRISVVEGL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 256 NKLP-IKILCLSNNQI----------EMITGLedLKALQNLDLSHNQISSLQGLENHDLLEVINLEDNKIAELREI-EYI 323
Cdd:cd21340    87 ENLTnLEELHIENQRLppgekltfdpRSLAAL--SNSLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLL 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370509528 324 KNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKKIKVEEK 369
Cdd:cd21340   165 SSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDGKEITDTER 210
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
132-377 1.58e-29

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 121.96  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 132 LTLSGCNLIDV-SILCGYVHLQKLDLSANKIEDL-SCVSCMPYLLELNASQNNLTTF-FNFKPPKNLKKADFSHNQISEI 208
Cdd:COG4886   118 LDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDL 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 209 -CDLSAYHALTKLILDGNEIEEIS-GLEMCNNLIHLSLANNKITTINGLNKLP-IKILCLSNNQIEMITGLEDLKALQNL 285
Cdd:COG4886   198 pEPLGNLTNLEELDLSGNQLTDLPePLANLTNLETLDLSNNQLTDLPELGNLTnLEELDLSNNQLTDLPPLANLTNLKTL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 286 DLSHNQISS--LQGLENHDLLEVINLEDNKIAELREIEYIKNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKK 363
Cdd:COG4886   278 DLSNNQLTDlkLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLN 357
                         250
                  ....*....|....
gi 1370509528 364 IKVEEKVSAVNKYD 377
Cdd:COG4886   358 LLSLLLTLLLTLGL 371
GuKc smart00072
Guanylate kinase homologues; Active enzymes catalyze ATP-dependent phosphorylation of GMP to ...
426-599 1.65e-22

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: 95.05  E-value: 1.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528  426 GKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNRDTVEGIARDG 505
Cdd:smart00072   4 GKGTLLAELIQEIPDAFERVVSHTTRPPRPGEVNGVDYHFVSKEEFEDDIKSGLFLEWGEYEGNYYGTSKETIRQVAEKG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528  506 LASCIHMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGlfsrAEIEFAVSRVDLYIKINQNFPGYFDEVINADDL 585
Cdd:smart00072  84 KHCLLDIDPQGVKQLRKAQLYPIVIFIAPPSSEELERRLRQRG----TETSERIQKRLAAAQKEAQEYHLFDYVIVNDDL 159
                          170
                   ....*....|....
gi 1370509528  586 DVAYQKLSQLIREY 599
Cdd:smart00072 160 EDAYEELKEILEAE 173
guanyl_kin TIGR03263
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...
416-598 2.19e-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: 94.87  E-value: 2.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNR 495
Cdd:TIGR03263   2 LIVISGPSGAGKSTLVKALLEEDPN-LKFSISATTRKPRPGEVDGVDYFFVSKEEFEEMIKAGEFLEWAEVHGNYYGTPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 496 DTVEGIARDGLaSCIhMEIE--GVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIE--FAVSRVDL-YIKinq 570
Cdd:TIGR03263  81 SPVEEALAAGK-DVL-LEIDvqGARQVKKKFPDAVSIFILPPSLEELERRLRKRGTDSEEVIErrLAKAKKEIaHAD--- 155
                         170       180
                  ....*....|....*....|....*...
gi 1370509528 571 nfpgYFDEVINADDLDVAYQKLSQLIRE 598
Cdd:TIGR03263 156 ----EFDYVIVNDDLEKAVEELKSIILA 179
PLN02772 PLN02772
guanylate kinase
411-637 1.01e-21

guanylate kinase


Pssm-ID: 215414 [Multi-domain]  Cd Length: 398  Bit Score: 98.37  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 411 DAPYPMLIlAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHK 490
Cdd:PLN02772  133 NAEKPIVI-SGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRAPREMEKDGVHYHFTERSVMEKEIKDGKFLEFASVHGNL 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 491 YGLNRDTVEGIArDGLASCI-HMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIEFAVSRVDLYIKIN 569
Cdd:PLN02772  212 YGTSIEAVEVVT-DSGKRCIlDIDVQGARSVRASSLEAIFIFICPPSMEELEKRLRARGTETEEQIQKRLRNAEAELEQG 290
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509528 570 QNfPGYFDEVINADDLDVAYQKLSQLireyLGLTeepakslATTADVKTSHLKPEAHPTKYISSNMGD 637
Cdd:PLN02772  291 KS-SGIFDHILYNDNLEECYKNLKKL----LGLD-------GLAAVNGVEAPEGINLPKEHSVSKMDD 346
Guanylate_kin pfam00625
Guanylate kinase;
417-599 2.18e-21

Guanylate kinase;


Pssm-ID: 395500  Cd Length: 182  Bit Score: 92.06  E-value: 2.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 417 LILAGPEACGKRELAHRLCRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNRD 496
Cdd:pfam00625   5 VVLSGPSGVGKSHIKKALLSEYPDKFGYSVPHTTRPPRKGEVDGKDYYFVSKEEMERDISANEFLEYAQFSGNMYGTSVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 497 TVEGIARDGLASCIHMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKG------LFSRAEiefavsrvdlyiKINQ 570
Cdd:pfam00625  85 TIEQIHEQGKIVILDVDPQGVKQLRKAELSPISVFIKPPSLKVLQRRLKGRGkeqeekINKRMA------------AAEQ 152
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370509528 571 NFPGY-FDEVINADDLDVAYQKLSQLIREY 599
Cdd:pfam00625 153 EFQHYeFDVIIVNDDLEEAYKKLKEALEAE 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
132-374 6.87e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 89.99  E-value: 6.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 132 LTLSGCNLIDVSI-LCGYVHLQKLDLSANKIEDLSC-VSCMPYLLELNASQNNLTTF-FNFKPPKNLKKADFSHNQISEI 208
Cdd:COG4886   164 LDLSNNQLTDLPEeLGNLTNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 209 CDLSAYHALTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTING---LNKLPIKILCLSNNQIEMITGLEDLKALQNL 285
Cdd:COG4886   244 PELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLkelELLLGLNSLLLLLLLLNLLELLILLLLLTTL 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 286 DLSHNQISSLQGLENHDLLEVINLEDNKIAELREIEYIKNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKKIK 365
Cdd:COG4886   324 LLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLL 403

                  ....*....
gi 1370509528 366 VEEKVSAVN 374
Cdd:COG4886   404 TLALLDAVN 412
Gmk COG0194
Guanylate kinase [Nucleotide transport and metabolism];
416-597 2.49e-17

Guanylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 439964  Cd Length: 190  Bit Score: 80.88  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFI-LTFSYGNHkYGLN 494
Cdd:COG0194     4 LIVLSGPSGAGKTTLVKALLERDPD-LRFSVSATTRPPRPGEVDGVDYHFVSREEFERMIENGEFLeWAEVHGNY-YGTP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 495 RDTVEgiarDGLASCIH--MEIE--GVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIE--FAVSRVDLyiki 568
Cdd:COG0194    82 KAEVE----EALAAGKDvlLEIDvqGARQVKKKFPDAVSIFILPPSLEELERRLRGRGTDSEEVIErrLAKAREEL---- 153
                         170       180
                  ....*....|....*....|....*....
gi 1370509528 569 nqNFPGYFDEVINADDLDVAYQKLSQLIR 597
Cdd:COG0194   154 --AHADEFDYVVVNDDLDRAVEELKAIIR 180
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
153-341 1.10e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 79.98  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 153 KLDLSANKIEDLSCVSCMPYLLELNASQNNLTTFFNFKPPKNLKKADFSHNQISEICDLSAYHALTKLILDGNEieEISG 232
Cdd:COG4886    34 LLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE--ELSN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 233 LEmcnNLIHLSLANNKITTI-NGLNKLP-IKILCLSNNQIEMI-TGLEDLKALQNLDLSHNQISSL-QGLENHDLLEVIN 308
Cdd:COG4886   112 LT---NLESLDLSGNQLTDLpEELANLTnLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKELD 188
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370509528 309 LEDNKIAELREIeyIKNLPILRVLNLLENPIQE 341
Cdd:COG4886   189 LSNNQITDLPEP--LGNLTNLEELDLSGNQLTD 219
gmk PRK00300
guanylate kinase; Provisional
416-597 4.66e-14

guanylate kinase; Provisional


Pssm-ID: 234719  Cd Length: 205  Bit Score: 71.66  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTyFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFI--LTFsYGNHkYGL 493
Cdd:PRK00300    7 LIVLSGPSGAGKSTLVKALLERDPN-LQLSVSATTRAPRPGEVDGVDYFFVSKEEFEEMIENGEFLewAEV-FGNY-YGT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 494 NRDTVEgiarDGLASCIHM--EIE--GVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIE--FAVSRVDLyik 567
Cdd:PRK00300   84 PRSPVE----EALAAGKDVllEIDwqGARQVKKKMPDAVSIFILPPSLEELERRLRGRGTDSEEVIArrLAKAREEI--- 156
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370509528 568 inqNFPGYFDEVINADDLDVAYQKLSQLIR 597
Cdd:PRK00300  157 ---AHASEYDYVIVNDDLDTALEELKAIIR 183
gmk PRK14738
guanylate kinase; Provisional
412-597 1.58e-11

guanylate kinase; Provisional


Pssm-ID: 237809  Cd Length: 206  Bit Score: 64.37  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 412 APYPMLI-LAGPEACGKRELAHRLcRQFSTYFRYGACHTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFS-YGNH 489
Cdd:PRK14738   10 PAKPLLVvISGPSGVGKDAVLARM-RERKLPFHFVVTATTRPKRPGEIDGVDYHFVTPEEFREMISQNELLEWAEvYGNY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 490 kYGLNRDTVegiaRDGLAS----CIHMEIEGVRSLKYSYFEPRYILVVPMNKEKYEGYLRRKGLFSRAEIEFAVSRVDLY 565
Cdd:PRK14738   89 -YGVPKAPV----RQALASgrdvIVKVDVQGAASIKRLVPEAVFIFLAPPSMDELTRRLELRRTESPEELERRLATAPLE 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370509528 566 IKINQNFpGYFdeVIN-ADDLDVAYQKLSQLIR 597
Cdd:PRK14738  164 LEQLPEF-DYV--VVNpEDRLDEAVAQIMAIIS 193
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
132-336 3.52e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.11  E-value: 3.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 132 LTLSGCNLIDVSI-LCGYVHLQKLDLSANKIEDLSCVSCMPYLLELNASQNNLTTFFNFKPPKNLKKADFSHNQISEICd 210
Cdd:COG4886   210 LDLSGNQLTDLPEpLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLK- 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 211 LSAYHALTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTINGLNKLPIKILCLSNNQIEMITGLEDLKALQNLDLSHN 290
Cdd:COG4886   289 LKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLT 368
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370509528 291 QISSLQGLENHDLLEVINLEDNKIAELREIEYIKNLPILRVLNLLE 336
Cdd:COG4886   369 LGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
109-344 2.50e-09

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 60.19  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 109 EAVAKALH--------HLGRSGSGTEQVYlnltlsgcnlIDVSILCGYVHLQKLDLSANKIEDLSCVScmpyLLELNASQ 180
Cdd:COG5238   198 EELAEALTqnttvttlWLKRNPIGDEGAE----------ILAEALKGNKSLTTLDLSNNQIGDEGVIA----LAEALKNN 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 181 NNLTTFfnfkppknlkkaDFSHNQISE------ICDLSAYHALTKLILDGNEIEE------ISGLEMCNNLIHLSLANNK 248
Cdd:COG5238   264 TTVETL------------YLSGNQIGAegaialAKALQGNTTLTSLDLSVNRIGDegaialAEGLQGNKTLHTLNLAYNG 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 249 ITTINGlnklpikilclsnnqIEMITGLEDLKALQNLDLSHNQISS------LQGLENHDLLEVINLEDNKIAELREIEY 322
Cdd:COG5238   332 IGAQGA---------------IALAKALQENTTLHSLDLSDNQIGDegaialAKYLEGNTTLRELNLGKNNIGKQGAEAL 396
                         250       260
                  ....*....|....*....|....
gi 1370509528 323 IKNLPI--LRVLNLLENPIQEKSE 344
Cdd:COG5238   397 IDALQTnrLHTLILDGNLIGAEAQ 420
LRR_9 pfam14580
Leucine-rich repeat;
242-376 6.67e-09

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 55.93  E-value: 6.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 242 LSLANNKITTINGLNKL--PIKILCLSNNQIEMITGLEDLKALQNLDLSHNQISSL-QGLENH-DLLEVINLEDNKIAEL 317
Cdd:pfam14580  24 LDLRGYKIPIIENLGATldQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIgEGLGEAlPNLTELILTNNNLQEL 103
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370509528 318 REIEYIKNLPILRVLNLLENPIQEKSEYWFFVIFMLLRLTELDQKKIKVEEKVSAVNKY 376
Cdd:pfam14580 104 GDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMF 162
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
193-343 8.19e-09

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 58.65  E-value: 8.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 193 KNLKKADFSHNQI-----SEICD-LSAYHALTKLILDGNEIEE------ISGLEMCNNLIHLSLANNKI----------- 249
Cdd:COG5238   180 NSVETVYLGCNQIgdegiEELAEaLTQNTTVTTLWLKRNPIGDegaeilAEALKGNKSLTTLDLSNNQIgdegvialaea 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 250 ----TTINGLNklpikilcLSNNQIE------MITGLEDLKALQNLDLSHNQISS------LQGLENHDLLEVINLEDNK 313
Cdd:COG5238   260 lknnTTVETLY--------LSGNQIGaegaiaLAKALQGNTTLTSLDLSVNRIGDegaialAEGLQGNKTLHTLNLAYNG 331
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370509528 314 IAE---LREIEYIKNLPILRVLNLLENPIQEKS 343
Cdd:COG5238   332 IGAqgaIALAKALQENTTLHSLDLSDNQIGDEG 364
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
95-345 8.98e-08

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: 54.67  E-value: 8.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528  95 MLNLEEEFDGVLREEAVAKALH------HLGRSGSGTEQVYLNLTLSGCNLIDvsiLCGyvhLQKLDLSANKIEDLSCvs 168
Cdd:cd00116    27 VLRLEGNTLGEEAAKALASALRpqpslkELCLSLNETGRIPRGLQSLLQGLTK---GCG---LQELDLSDNALGPDGC-- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 169 cmpyllelnasqnnlTTFFNFKPPKNLKKADFSHNQISE-----ICD--LSAYHALTKLILDGNEIEEISGLEMCNNLIH 241
Cdd:cd00116    99 ---------------GVLESLLRSSSLQELKLNNNGLGDrglrlLAKglKDLPPALEKLVLGRNRLEGASCEALAKALRA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 242 ------LSLANNKI------TTINGLNKLP-IKILCLSNNQIE------MITGLEDLKALQNLDLSHNQISSL------- 295
Cdd:cd00116   164 nrdlkeLNLANNGIgdagirALAEGLKANCnLEVLDLNNNGLTdegasaLAETLASLKSLEVLNLGDNNLTDAgaaalas 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370509528 296 QGLENHDLLEVINLEDNKI---AELREIEYIKNLPILRVLNLLENPIQEKSEY 345
Cdd:cd00116   244 ALLSPNISLLTLSLSCNDItddGAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
154-293 4.72e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.70  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 154 LDLSANKIEDL--SCVSCMPYLLELNASQNNlttFFNFKP----PKNLKKADFSHNQISEIC--DLSAYHALTKLILDGN 225
Cdd:PLN00113  433 LDISNNNLQGRinSRKWDMPSLQMLSLARNK---FFGGLPdsfgSKRLENLDLSRNQFSGAVprKLGSLSELMQLKLSEN 509
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 226 EIE-EI-SGLEMCNNLIHLSLANNKITTinglnklpikilclsnnqiEMITGLEDLKALQNLDLSHNQIS 293
Cdd:PLN00113  510 KLSgEIpDELSSCKKLVSLDLSHNQLSG-------------------QIPASFSEMPVLSQLDLSQNQLS 560
LRR_8 pfam13855
Leucine rich repeat;
217-292 1.43e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.98  E-value: 1.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509528 217 LTKLILDGNEIEEISG--LEMCNNLIHLSLANNKITTINGlnklpikilclsnnqiemiTGLEDLKALQNLDLSHNQI 292
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSP-------------------GAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
131-310 1.46e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.47  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 131 NLTLSGCNLIDVSILCGYVHLQKLDLSANKIEDLSCVSCMPYLLELNASQNNLTTF--FNFKPPKNLKKADFSHNQISEI 208
Cdd:COG4886   232 TLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLklKELELLLGLNSLLLLLLLLNLL 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 209 CDLSAYHALTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTINGLNKLPIKILCLSN-NQIEMITGLEDLKALQNLDL 287
Cdd:COG4886   312 ELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGlLGLLEATLLTLALLLLTLLL 391
                         170       180
                  ....*....|....*....|...
gi 1370509528 288 SHNQISSLQGLENHDLLEVINLE 310
Cdd:COG4886   392 LLLTTTAGVLLLTLALLDAVNTE 414
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
260-300 1.97e-06

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: 44.93  E-value: 1.97e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370509528 260 IKILCLSNNQIEMITGLEDLKALQNLDLSHN-QISSLQGLEN 300
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLAN 44
gmk PRK14737
guanylate kinase; Provisional
416-596 6.54e-06

guanylate kinase; Provisional


Pssm-ID: 173199  Cd Length: 186  Bit Score: 47.29  E-value: 6.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 416 MLILAGPEACGKRELAHRLCRQFSTYFRYGAChTTRPPYFGEGDRVDYHFISQDVFDEMVNMGKFILTFSYGNHKYGLNR 495
Cdd:PRK14737    6 LFIISSVAGGGKSTIIQALLEEHPDFLFSISC-TTRAPRPGDEEGKTYFFLTIEEFKKGIADGEFLEWAEVHDNYYGTPK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 496 DTVEGIARDGLASCIHMEIEGVRSLKYSYFEPRY-ILVVPMNKEKYEGYLRRKGLFSRAEIEFAVSRVdlyiKINQNFPG 574
Cdd:PRK14737   85 AFIEDAFKEGRSAIMDIDVQGAKIIKEKFPERIVtIFIEPPSEEEWEERLIHRGTDSEESIEKRIENG----IIELDEAN 160
                         170       180
                  ....*....|....*....|..
gi 1370509528 575 YFDEVINADDLDVAYQKLSQLI 596
Cdd:PRK14737  161 EFDYKIINDDLEDAIADLEAII 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
217-360 9.30e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 217 LTKLILDGNEIEEISGLEMCNNLIHLSLANNKITTINGLNKLPIKILCLSNNQIEMITGLEDLKALQNLDLSHNQisSLQ 296
Cdd:COG4886    33 LLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE--ELS 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370509528 297 GLENhdlLEVINLEDNKIAELreIEYIKNLPILRVLNLLENPIQEKSEywffVIFMLLRLTELD 360
Cdd:COG4886   111 NLTN---LESLDLSGNQLTDL--PEELANLTNLKELDLSNNQLTDLPE----PLGNLTNLKSLD 165
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
238-277 1.51e-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: 1.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370509528 238 NLIHLSLANNKITTINGLNKLP-IKILCLS-NNQIEMITGLE 277
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPnLETLDLSgNNKITDLSDLA 43
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
167-326 1.85e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 48.31  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 167 VSCMPYLLELNASQNNLTTffnfKPPKNLKKA------DFSHNQIS-EICD-LSAYHALTKLILDGNEIE-EI-SGLEMC 236
Cdd:PLN00113  328 LTSLPRLQVLQLWSNKFSG----EIPKNLGKHnnltvlDLSTNNLTgEIPEgLCSSGNLFKLILFSNSLEgEIpKSLGAC 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 237 NNLIHLSLANNKIT--TINGLNKLP-IKILCLSNN--------------QIEMIT--------GLEDL---KALQNLDLS 288
Cdd:PLN00113  404 RSLRRVRLQDNSFSgeLPSEFTKLPlVYFLDISNNnlqgrinsrkwdmpSLQMLSlarnkffgGLPDSfgsKRLENLDLS 483
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370509528 289 HNQISSL--QGLENHDLLEVINLEDNKIAEL--REIEYIKNL 326
Cdd:PLN00113  484 RNQFSGAvpRKLGSLSELMQLKLSENKLSGEipDELSSCKKL 525
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
217-257 2.09e-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: 42.23  E-value: 2.09e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370509528 217 LTKLILDGNEIEEISGLEMCNNLIHLSLA-NNKITTINGLNK 257
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSgNNKITDLSDLAN 44
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
132-181 2.71e-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: 45.93  E-value: 2.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370509528 132 LTLSGCNLIDVSILCGYVHLQKLDLSANKIEDLSCV----SCMPYLLELNASQN 181
Cdd:cd21340   125 LNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEELldllSSWPSLRELDLTGN 178
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
280-321 2.86e-04

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: 39.15  E-value: 2.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370509528 280 KALQNLDLSHNQISSLQGLENHDLLEVINLEDN-KIAELREIE 321
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLA 43
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
151-227 5.44e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 42.08  E-value: 5.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370509528 151 LQKLDLSANKIEDLSCVSCMPYLLELNASQNNLttffnfkppknlkkadfshNQISEICD-LSAYHALTKLILDGNEI 227
Cdd:cd21340   122 LRVLNISGNNIDSLEPLAPLRNLEQLDASNNQI-------------------SDLEELLDlLSSWPSLRELDLTGNPV 180
LRR_8 pfam13855
Leucine rich repeat;
261-314 6.43e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.66  E-value: 6.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370509528 261 KILCLSNNQIEMITG--LEDLKALQNLDLSHNQISSL-----QGLENhdlLEVINLEDNKI 314
Cdd:pfam13855   4 RSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLspgafSGLPS---LRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
282-339 2.45e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.73  E-value: 2.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370509528 282 LQNLDLSHNQISSL-----QGLENhdlLEVINLEDNKIAELREIEyIKNLPILRVLNLLENPI 339
Cdd:pfam13855   3 LRSLDLSNNRLTSLddgafKGLSN---LKVLDLSNNLLTTLSPGA-FSGLPSLRYLDLSGNRL 61
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
193-234 4.84e-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: 35.68  E-value: 4.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370509528 193 KNLKKADFSHNQISEICDLSAYHALTKLILDGN-EIEEISGLE 234
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNnKITDLSDLA 43
LRR_8 pfam13855
Leucine rich repeat;
150-205 7.61e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.58  E-value: 7.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370509528 150 HLQKLDLSANKIEDL--SCVSCMPYLLELNASQNNLTTFFN--FKPPKNLKKADFSHNQI 205
Cdd:pfam13855   2 NLRSLDLSNNRLTSLddGAFKGLSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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