|
Name |
Accession |
Description |
Interval |
E-value |
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
27-434 |
3.38e-45 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 168.96 E-value: 3.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 27 SNLRQLTLTAAGACPGAGADALESPASPQLVLPANLGDIEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRFARLPPAV 106
Cdd:COG4886 12 LLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 107 AELGHHLTELDVSHNRLtalgaevVSALRELRKLNLSHNQLPALPAQLGALAHLEELDVSFNRLAHLPDSLSCLSRLRTL 186
Cdd:COG4886 92 LGDLTNLTELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 187 DVDHNQLTAFPRQLLQLVALEELDVSSNRLRGLPEDISALRALKILWLSGAELGTLPAGFCELASLESLMLDNNGLQALP 266
Cdd:COG4886 165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 267 aQFSCLQRLKMLNLSSNLFEEFPaALLPLAGLEELYLSRNQLTSVP----SLISGLGRLLTLWLDNNRIRYLPDSIVELT 342
Cdd:COG4886 245 -ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 343 GLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPLIQPPYEVCMKGIPYIAAYQKELAHSQPAVQPRLKLLLMGHKAAGK 422
Cdd:COG4886 323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
|
410
....*....|..
gi 296437367 423 TLLRHCLTEERV 434
Cdd:COG4886 403 LTLALLDAVNTE 414
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
92-343 |
9.81e-22 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 101.70 E-value: 9.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 92 LVLRRNRFARLPPAVAElghHLTELDVSHNRLTALGAEVVSALRELrklNLSHNQLPALPAQLGALahLEELDVSFNRLA 171
Cdd:PRK15370 183 LRLKILGLTTIPACIPE---QITTLILDNNELKSLPENLQGNIKTL---YANSNQLTSIPATLPDT--IQEMELSINRIT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 172 HLPDSLSclSRLRTLDVDHNQLTAFPRQLLQlvALEELDVSSNRLRGLPEDI-SALRALKILWLSGAEL-GTLPAGfcel 249
Cdd:PRK15370 255 ELPERLP--SALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLpSGITHLNVQSNSLTALpETLPPG---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 250 asLESLMLDNNGLQALPAqfSCLQRLKMLNLSSNLFEEFPAALLPLagLEELYLSRNQLTSVPSLISglGRLLTLWLDNN 329
Cdd:PRK15370 327 --LKTLEAGENALTSLPA--SLPPELQVLDVSKNQITVLPETLPPT--ITTLDVSRNALTNLPENLP--AALQIMQASRN 398
|
250
....*....|....
gi 296437367 330 RIRYLPDSIVELTG 343
Cdd:PRK15370 399 NLVRLPESLPHFRG 412
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
68-236 |
1.69e-16 |
|
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: 79.44 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 68 LNLGNNGLEEVpEGLgSALGSLRVLVLRRNRFARLPPavaeLGH--HLTELDVSHNRLTALgaEVVSALRELRKLNLSHN 145
Cdd:cd21340 7 LYLNDKNITKI-DNL-SLCKNLKVLYLYDNKITKIEN----LEFltNLTHLYLQNNQIEKI--ENLENLVNLKKLYLGGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 146 QLPALpAQLGALAHLEELDVSFNRLAH------LPDSLSCLSR-LRTLDVDHNQLTAfPRQLLQLVALEELDVSSNRLRG 218
Cdd:cd21340 79 RISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALSNsLRVLNISGNNIDS-LEPLAPLRNLEQLDASNNQISD 156
|
170 180
....*....|....*....|.
gi 296437367 219 LPE---DISALRALKILWLSG 236
Cdd:cd21340 157 LEElldLLSSWPSLRELDLTG 177
|
|
| RocCOR |
cd09914 |
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ... |
409-552 |
3.51e-14 |
|
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.
Pssm-ID: 206741 [Multi-domain] Cd Length: 161 Bit Score: 71.21 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 409 RLKLLLMGHKAAGKTLLRHCLTEERVEGcpgggDKEKcyppspppvSKGIEVTSWT--ADASRGLRFIVYDLAGDESYEV 486
Cdd:cd09914 1 EAKLMLVGQGGVGKTSLCKQLIGEKFDG-----DESS---------THGINVQDWKipAPERKKIRLNVWDFGGQEIYHA 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296437367 487 IQPFFLSPGALYVLVVNLATYEprhFPTTVGSFLHRVGARVPHAVVCIVGTHADLCGERELEEKCL 552
Cdd:cd09914 67 THQFFLTSRSLYLLVFDLRTGD---EVSRVPYWLRQIKAFGGVSPVILVGTHIDESCDEDILKKAL 129
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
251-308 |
2.93e-09 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 54.07 E-value: 2.93e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 251 SLESLMLDNNGLQAL-PAQFSCLQRLKMLNLSSNLFEEF-PAALLPLAGLEELYLSRNQL 308
Cdd:pfam13855 2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| Roc |
pfam08477 |
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ... |
411-540 |
3.66e-08 |
|
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.
Pssm-ID: 462490 [Multi-domain] Cd Length: 114 Bit Score: 52.51 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 411 KLLLMGHKAAGKT--LLRHClteervegcpgGGDKEKCYPPSPppvskGIEVTSWTA----DASRGLRFIVYDLAGDESY 484
Cdd:pfam08477 1 KVVLLGDSGVGKTslLKRFV-----------DDTFDPKYKSTI-----GVDFKTKTVlendDNGKKIKLNIWDTAGQERF 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 296437367 485 EVIQPFFLSPGALYVLVVNLATYEprhfptTVGSFLHRVGARVPHAVVCIVGTHAD 540
Cdd:pfam08477 65 RSLHPFYYRGAAAALLVYDSRTFS------NLKYWLRELKKYAGNSPVILVGNKID 114
|
|
| COR |
pfam16095 |
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ... |
660-727 |
1.83e-04 |
|
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.
Pssm-ID: 406489 Cd Length: 196 Bit Score: 43.77 E-value: 1.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296437367 660 PRSWQVLEElHFQPPQAQRLWLSWWDSARLGLQAGLT-EDRLQSALSYLHESGKLLYFEDSPALKEHVF 727
Cdd:pfam16095 1 PKSWLAVRE-ALEKERQKKPYISYEEYRKICAENGIDdEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVI 68
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
27-434 |
3.38e-45 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 168.96 E-value: 3.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 27 SNLRQLTLTAAGACPGAGADALESPASPQLVLPANLGDIEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRFARLPPAV 106
Cdd:COG4886 12 LLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 107 AELGHHLTELDVSHNRLtalgaevVSALRELRKLNLSHNQLPALPAQLGALAHLEELDVSFNRLAHLPDSLSCLSRLRTL 186
Cdd:COG4886 92 LGDLTNLTELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 187 DVDHNQLTAFPRQLLQLVALEELDVSSNRLRGLPEDISALRALKILWLSGAELGTLPAGFCELASLESLMLDNNGLQALP 266
Cdd:COG4886 165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 267 aQFSCLQRLKMLNLSSNLFEEFPaALLPLAGLEELYLSRNQLTSVP----SLISGLGRLLTLWLDNNRIRYLPDSIVELT 342
Cdd:COG4886 245 -ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 343 GLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPLIQPPYEVCMKGIPYIAAYQKELAHSQPAVQPRLKLLLMGHKAAGK 422
Cdd:COG4886 323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
|
410
....*....|..
gi 296437367 423 TLLRHCLTEERV 434
Cdd:COG4886 403 LTLALLDAVNTE 414
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
92-343 |
9.81e-22 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 101.70 E-value: 9.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 92 LVLRRNRFARLPPAVAElghHLTELDVSHNRLTALGAEVVSALRELrklNLSHNQLPALPAQLGALahLEELDVSFNRLA 171
Cdd:PRK15370 183 LRLKILGLTTIPACIPE---QITTLILDNNELKSLPENLQGNIKTL---YANSNQLTSIPATLPDT--IQEMELSINRIT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 172 HLPDSLSclSRLRTLDVDHNQLTAFPRQLLQlvALEELDVSSNRLRGLPEDI-SALRALKILWLSGAEL-GTLPAGfcel 249
Cdd:PRK15370 255 ELPERLP--SALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLpSGITHLNVQSNSLTALpETLPPG---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 250 asLESLMLDNNGLQALPAqfSCLQRLKMLNLSSNLFEEFPAALLPLagLEELYLSRNQLTSVPSLISglGRLLTLWLDNN 329
Cdd:PRK15370 327 --LKTLEAGENALTSLPA--SLPPELQVLDVSKNQITVLPETLPPT--ITTLDVSRNALTNLPENLP--AALQIMQASRN 398
|
250
....*....|....
gi 296437367 330 RIRYLPDSIVELTG 343
Cdd:PRK15370 399 NLVRLPESLPHFRG 412
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
58-243 |
6.41e-21 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 99.00 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 58 LPANLGD-IEALNLGNNGLEEVPEGLGSALGSlrvLVLRRNRFARLPPAVAElghHLTELDVSHNRLTALGAEVVSALRE 136
Cdd:PRK15370 235 IPATLPDtIQEMELSINRITELPERLPSALQS---LDLFHNKISCLPENLPE---ELRYLSVYDNSIRTLPAHLPSGITH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 137 lrkLNLSHNQLPALPAQLGalAHLEELDVSFNRLAHLPDSLSclSRLRTLDVDHNQLTAFPRQLLQlvALEELDVSSNRL 216
Cdd:PRK15370 309 ---LNVQSNSLTALPETLP--PGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLPP--TITTLDVSRNAL 379
|
170 180
....*....|....*....|....*..
gi 296437367 217 RGLPEDISAlrALKILWLSGAELGTLP 243
Cdd:PRK15370 380 TNLPENLPA--ALQIMQASRNNLVRLP 404
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
68-377 |
4.98e-19 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 92.92 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 68 LNLGNNGLEEVPEGLgsalgslrvlvlrrnrfarlpPAvaelghHLTELDVSHNRLTALGAevvsALRELRKLNLSHNQL 147
Cdd:PRK15387 206 LNVGESGLTTLPDCL---------------------PA------HITTLVIPDNNLTSLPA----LPPELRTLEVSGNQL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 148 PALPAQLGALAhleELDVSFNRLAHLPDSLSCLSRLRTLDvdhNQLTAFPrqlLQLVALEELDVSSNRLRGLPEDISALR 227
Cdd:PRK15387 255 TSLPVLPPGLL---ELSIFSNPLTHLPALPSGLCKLWIFG---NQLTSLP---VLPPGLQELSVSDNQLASLPALPSELC 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 228 ALKILWLSGAELGTLPAGfcelasLESLMLDNNGLQALPAQFSCLQRLKMLNlssNLFEEFPAalLPlAGLEELYLSRNQ 307
Cdd:PRK15387 326 KLWAYNNQLTSLPTLPSG------LQELSVSDNQLASLPTLPSELYKLWAYN---NRLTSLPA--LP-SGLKELIVSGNR 393
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 308 LTSVPSLISGLGRLLtlwLDNNRIRYLPdsiVELTGLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPL 377
Cdd:PRK15387 394 LTSLPVLPSELKELM---VSGNRLTSLP---MLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPL 457
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
89-331 |
4.56e-17 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 86.83 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 89 LRVLVLRRNRFA-RLPPAVAELGHHLTELDVSHNRLTalGAEVVSALRELRKLNLSHNQLPA-LPAQLGALAHLEELDVS 166
Cdd:PLN00113 95 IQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNNFT--GSIPRGSIPNLETLDLSNNMLSGeIPNDIGSFSSLKVLDLG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 167 FNRL-AHLPDSLSCLSRLRTLDVDHNQLTA-FPRQLLQLVALEELDVSSNRLRG-LPEDISALRALKILWLSGAEL-GTL 242
Cdd:PLN00113 173 GNVLvGKIPNSLTNLTSLEFLTLASNQLVGqIPRELGQMKSLKWIYLGYNNLSGeIPYEIGGLTSLNHLDLVYNNLtGPI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 243 PAGFCELASLESLMLDNNGLQA-LPAQFSCLQRLKMLNLSSN-LFEEFPAALLPLAGLEELYLSRNQLT-SVPSLISGLG 319
Cdd:PLN00113 253 PSSLGNLKNLQYLFLYQNKLSGpIPPSIFSLQKLISLDLSDNsLSGEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLP 332
|
250
....*....|..
gi 296437367 320 RLLTLWLDNNRI 331
Cdd:PLN00113 333 RLQVLQLWSNKF 344
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
54-285 |
8.08e-17 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 86.06 E-value: 8.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 54 PQLVlpANLGDIEALNL-GNNGLEEVPEGLGSaLGSLRVLVLRRNRFARLPPAvaELGHH--LTELDVSHNRLT------ 124
Cdd:PLN00113 301 PELV--IQLQNLEILHLfSNNFTGKIPVALTS-LPRLQVLQLWSNKFSGEIPK--NLGKHnnLTVLDLSTNNLTgeipeg 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 125 ---------------ALGAEV---VSALRELRKLNLSHNQLPA-LPAQLGALAHLEELDVSFNRL--------------- 170
Cdd:PLN00113 376 lcssgnlfklilfsnSLEGEIpksLGACRSLRRVRLQDNSFSGeLPSEFTKLPLVYFLDISNNNLqgrinsrkwdmpslq 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 171 ----------AHLPDSLSClSRLRTLDVDHNQLT-AFPRQLLQLVALEELDVSSNRLRG-LPEDISALRALKILWLSGAE 238
Cdd:PLN00113 456 mlslarnkffGGLPDSFGS-KRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLDLSHNQ 534
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 296437367 239 L-GTLPAGFCELASLESLMLDNNGLQA-LPAQFSCLQRLKMLNLSSNLF 285
Cdd:PLN00113 535 LsGQIPASFSEMPVLSQLDLSQNQLSGeIPKNLGNVESLVQVNISHNHL 583
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
68-236 |
1.69e-16 |
|
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: 79.44 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 68 LNLGNNGLEEVpEGLgSALGSLRVLVLRRNRFARLPPavaeLGH--HLTELDVSHNRLTALgaEVVSALRELRKLNLSHN 145
Cdd:cd21340 7 LYLNDKNITKI-DNL-SLCKNLKVLYLYDNKITKIEN----LEFltNLTHLYLQNNQIEKI--ENLENLVNLKKLYLGGN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 146 QLPALpAQLGALAHLEELDVSFNRLAH------LPDSLSCLSR-LRTLDVDHNQLTAfPRQLLQLVALEELDVSSNRLRG 218
Cdd:cd21340 79 RISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALSNsLRVLNISGNNIDS-LEPLAPLRNLEQLDASNNQISD 156
|
170 180
....*....|....*....|.
gi 296437367 219 LPE---DISALRALKILWLSG 236
Cdd:cd21340 157 LEElldLLSSWPSLRELDLTG 177
|
|
| RocCOR |
cd09914 |
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ... |
409-552 |
3.51e-14 |
|
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.
Pssm-ID: 206741 [Multi-domain] Cd Length: 161 Bit Score: 71.21 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 409 RLKLLLMGHKAAGKTLLRHCLTEERVEGcpgggDKEKcyppspppvSKGIEVTSWT--ADASRGLRFIVYDLAGDESYEV 486
Cdd:cd09914 1 EAKLMLVGQGGVGKTSLCKQLIGEKFDG-----DESS---------THGINVQDWKipAPERKKIRLNVWDFGGQEIYHA 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296437367 487 IQPFFLSPGALYVLVVNLATYEprhFPTTVGSFLHRVGARVPHAVVCIVGTHADLCGERELEEKCL 552
Cdd:cd09914 67 THQFFLTSRSLYLLVFDLRTGD---EVSRVPYWLRQIKAFGGVSPVILVGTHIDESCDEDILKKAL 129
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
124-354 |
1.68e-12 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 69.69 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 124 TALGAEVVSALRELRKLNLSHNQL-----PALPAQLGALAHLEELDVSFNRLAHLPDSLSCL-------SRLRTLDVDHN 191
Cdd:cd00116 12 TERATELLPKLLCLQVLRLEGNTLgeeaaKALASALRPQPSLKELCLSLNETGRIPRGLQSLlqgltkgCGLQELDLSDN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 192 QLT----AFPRQLLQLVALEELDVSSNRL---------RGLPEDISALRALkILW---LSGAELGTLPAGFCELASLESL 255
Cdd:cd00116 92 ALGpdgcGVLESLLRSSSLQELKLNNNGLgdrglrllaKGLKDLPPALEKL-VLGrnrLEGASCEALAKALRANRDLKEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 256 MLDNNGL---------QALPAQfsclQRLKMLNLSSNLFEE-----FPAALLPLAGLEELYLSRNQLTSV------PSLI 315
Cdd:cd00116 171 NLANNGIgdagiralaEGLKAN----CNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAgaaalaSALL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 296437367 316 SGLGRLLTLWLDNNRI---------RYLPDSIVeltgLEELVLQGNQI 354
Cdd:cd00116 247 SPNISLLTLSLSCNDItddgakdlaEVLAEKES----LLELDLRGNKF 290
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
65-210 |
2.40e-11 |
|
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: 64.42 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 65 IEALNLGNNGLEEVpEGLGSaLGSLRVLVLRRNRFARlppaVAELG--HHLTELDVSHNRLtALGAEV------VSALRE 136
Cdd:cd21340 48 LTHLYLQNNQIEKI-ENLEN-LVNLKKLYLGGNRISV----VEGLEnlTNLEELHIENQRL-PPGEKLtfdprsLAALSN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 137 -LRKLNLSHNQLPALpAQLGALAHLEELDVSFNRLAHLPD---SLSCLSRLRTLDVDHNQLTAFPRQLLQLVA----LEE 208
Cdd:cd21340 121 sLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNPVCKKPKYRDKIILasksLEV 199
|
..
gi 296437367 209 LD 210
Cdd:cd21340 200 LD 201
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
157-355 |
2.49e-10 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 64.87 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 157 LAHLEELDVSFNRLA-HLPDSLSCLS-RLRTLDVDHNQLT-AFPRQLLQLvaLEELDVSSNRLRG-LPEDISALRALKIL 232
Cdd:PLN00113 92 LPYIQTINLSNNQLSgPIPDDIFTTSsSLRYLNLSNNNFTgSIPRGSIPN--LETLDLSNNMLSGeIPNDIGSFSSLKVL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 233 WLSGAEL-GTLPAGFCELASLESLMLDNNGLQAlpaqfsclqrlkmlnlssnlfeEFPAALLPLAGLEELYLSRNQLT-S 310
Cdd:PLN00113 170 DLGGNVLvGKIPNSLTNLTSLEFLTLASNQLVG----------------------QIPRELGQMKSLKWIYLGYNNLSgE 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296437367 311 VPSLISGLGRLLTLWL-DNNRIRYLPDSIVELTGLEELVLQGNQIA 355
Cdd:PLN00113 228 IPYEIGGLTSLNHLDLvYNNLTGPIPSSLGNLKNLQYLFLYQNKLS 273
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
113-312 |
5.30e-10 |
|
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: 60.57 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 113 LTELDVSHNRLTALgaEVVSALRELRKLNLSHNQLPALPaQLGALAHLEELDVSFNRLAHLpDSLSCLSRLRTLDVDHNQ 192
Cdd:cd21340 4 ITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 193 LTafpR--QLLQLVALEELDVSSNRLRglPEDISALRALKILWLSGaelgtlpagfcelaSLESLMLDNNGLQALpAQFS 270
Cdd:cd21340 80 IS---VveGLENLTNLEELHIENQRLP--PGEKLTFDPRSLAALSN--------------SLRVLNISGNNIDSL-EPLA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 296437367 271 CLQRLKMLNLSSNLFEEFPAALLPLAG---LEELYLSRNQLTSVP 312
Cdd:cd21340 140 PLRNLEQLDASNNQISDLEELLDLLSSwpsLRELDLTGNPVCKKP 184
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
251-308 |
2.93e-09 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 54.07 E-value: 2.93e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 251 SLESLMLDNNGLQAL-PAQFSCLQRLKMLNLSSNLFEEF-PAALLPLAGLEELYLSRNQL 308
Cdd:pfam13855 2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
88-147 |
3.04e-09 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 54.07 E-value: 3.04e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 88 SLRVLVLRRNRFARLPPAVAELGHHLTELDVSHNRLTALGAEVVSALRELRKLNLSHNQL 147
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
112-170 |
8.42e-09 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 52.53 E-value: 8.42e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 112 HLTELDVSHNRLTALGAEVVSALRELRKLNLSHNQLPAL-PAQLGALAHLEELDVSFNRL 170
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
68-308 |
3.66e-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: 56.21 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 68 LNLGNNGL-EEVPEGLGSAL--GSLRVLVLRRNRFARLP-----PAVAELGHHLTELDVSHNRLTALG----AEVVSALR 135
Cdd:cd00116 86 LDLSDNALgPDGCGVLESLLrsSSLQELKLNNNGLGDRGlrllaKGLKDLPPALEKLVLGRNRLEGAScealAKALRANR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 136 ELRKLNLSHNQL--PALPAQLGALAHleeldvsfnrlahlpdslscLSRLRTLDVDHNQLT-----AFPRQLLQLVALEE 208
Cdd:cd00116 166 DLKELNLANNGIgdAGIRALAEGLKA--------------------NCNLEVLDLNNNGLTdegasALAETLASLKSLEV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 209 LDVSSNRLRGlpEDISALraLKILWLSGAELGTLPAGFCELASLESLMLdnngLQALPAQfsclQRLKMLNLSSNLF--- 285
Cdd:cd00116 226 LNLGDNNLTD--AGAAAL--ASALLSPNISLLTLSLSCNDITDDGAKDL----AEVLAEK----ESLLELDLRGNKFgee 293
|
250 260
....*....|....*....|....*.
gi 296437367 286 ---EEFPAALLPLAGLEELYLSRNQL 308
Cdd:cd00116 294 gaqLLAESLLEPGNELESLWVKDDSF 319
|
|
| Roc |
pfam08477 |
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ... |
411-540 |
3.66e-08 |
|
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.
Pssm-ID: 462490 [Multi-domain] Cd Length: 114 Bit Score: 52.51 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 411 KLLLMGHKAAGKT--LLRHClteervegcpgGGDKEKCYPPSPppvskGIEVTSWTA----DASRGLRFIVYDLAGDESY 484
Cdd:pfam08477 1 KVVLLGDSGVGKTslLKRFV-----------DDTFDPKYKSTI-----GVDFKTKTVlendDNGKKIKLNIWDTAGQERF 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 296437367 485 EVIQPFFLSPGALYVLVVNLATYEprhfptTVGSFLHRVGARVPHAVVCIVGTHAD 540
Cdd:pfam08477 65 RSLHPFYYRGAAAALLVYDSRTFS------NLKYWLRELKKYAGNSPVILVGNKID 114
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
159-216 |
1.93e-07 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 48.67 E-value: 1.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 159 HLEELDVSFNRLAHL-PDSLSCLSRLRTLDVDHNQLTAF-PRQLLQLVALEELDVSSNRL 216
Cdd:pfam13855 2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
297-354 |
3.99e-07 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 47.90 E-value: 3.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 297 GLEELYLSRNQLTSV-PSLISGLGRLLTLWLDNNRIRYL-PDSIVELTGLEELVLQGNQI 354
Cdd:pfam13855 2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
131-194 |
8.67e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 52.90 E-value: 8.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296437367 131 VSALRELRKLNLSHNQLP-ALPAQLGALAHLEELDVSFNRL-AHLPDSLSCLSRLRTLDVDHNQLT 194
Cdd:PLN03150 438 ISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFnGSIPESLGQLTSLRILNLNGNSLS 503
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
57-193 |
1.03e-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: 51.97 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 57 VLPANlGDIEALNLGNNGLEEvpEGL------GSALGSLRVLVLRRNRFAR-----LPPAVAELgHHLTELDVSHNRLTA 125
Cdd:cd00116 160 ALRAN-RDLKELNLANNGIGD--AGIralaegLKANCNLEVLDLNNNGLTDegasaLAETLASL-KSLEVLNLGDNNLTD 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 126 LG-AEVVSALRE----LRKLNLSHNQLPALPAQ-----LGALAHLEELDVSFNRLAHLPDSLSCLSR------LRTLDVD 189
Cdd:cd00116 236 AGaAALASALLSpnisLLTLSLSCNDITDDGAKdlaevLAEKESLLELDLRGNKFGEEGAQLLAESLlepgneLESLWVK 315
|
....
gi 296437367 190 HNQL 193
Cdd:cd00116 316 DDSF 319
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
221-381 |
5.47e-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: 48.63 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 221 EDISALRALKILWLSGAELGTLPaGFCELASLESLMLDNNGLQALPaQFSCLQRLKMLNLSSNLFEEfpaallpLAGLE- 299
Cdd:cd21340 18 DNLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISV-------VEGLEn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 300 -----ELYLSRNQL------TSVPSLISGLGRLLTLwLD--NNRIRYLpDSIVELTGLEELVLQGNQIAVLPDHFGQLSR 366
Cdd:cd21340 89 ltnleELHIENQRLppgeklTFDPRSLAALSNSLRV-LNisGNNIDSL-EPLAPLRNLEQLDASNNQISDLEELLDLLSS 166
|
170
....*....|....*...
gi 296437367 367 VG-LWKI--KDNPLIQPP 381
Cdd:cd21340 167 WPsLRELdlTGNPVCKKP 184
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
205-355 |
5.88e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 50.20 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 205 ALEELDVSSNRLRGLPEDISALRALKilwlsgAELGtLPAGF------------------CELAS------LESLMLDNN 260
Cdd:PLN03150 356 AIEVFEIITAESKTLLEEVSALQTLK------SSLG-LPLRFgwngdpcvpqqhpwsgadCQFDStkgkwfIDGLGLDNQ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 261 GLQA-LPAQFSCLQRLKMLNLSSNLFE-EFPAALLPLAGLEELYLSRNQLtsvpsliSGLgrlltlwldnnriryLPDSI 338
Cdd:PLN03150 429 GLRGfIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSF-------NGS---------------IPESL 486
|
170
....*....|....*..
gi 296437367 339 VELTGLEELVLQGNQIA 355
Cdd:PLN03150 487 GQLTSLRILNLNGNSLS 503
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
249-355 |
1.44e-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: 47.47 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 249 LASLESLMLDNNGLQALPAqFSCLQRLKMLNLSSNLFEEFPAaLLPLAGLEELYLSRNQLTSVPSLiSGLGRLLTLWLDN 328
Cdd:cd21340 1 LKRITHLYLNDKNITKIDN-LSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIENL-ENLVNLKKLYLGG 77
|
90 100 110
....*....|....*....|....*....|.
gi 296437367 329 NRIrylpdSIVE----LTGLEELVLQGNQIA 355
Cdd:cd21340 78 NRI-----SVVEglenLTNLEELHIENQRLP 103
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
273-331 |
2.37e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 42.90 E-value: 2.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296437367 273 QRLKMLNLSSNLFEEF-PAALLPLAGLEELYLSRNQLTSV-PSLISGLGRLLTLWLDNNRI 331
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
65-157 |
4.20e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 47.50 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 65 IEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRF-ARLPPAVAELGHhLTELDVSHNRLTALGAEVVSALRELRKLNLS 143
Cdd:PLN03150 420 IDGLGLDNQGLRGFIPNDISKLRHLQSINLSGNSIrGNIPPSLGSITS-LEVLDLSYNSFNGSIPESLGQLTSLRILNLN 498
|
90
....*....|....*
gi 296437367 144 HNQLPA-LPAQLGAL 157
Cdd:PLN03150 499 GNSLSGrVPAALGGR 513
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
234-364 |
4.72e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 47.54 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 234 LSGAEL-GTLPAGFCELASLESLMLDNNGLQA-LPAQ-FSCLQRLKMLNLSSNLFE-EFPAALLPlaGLEELYLSRNQLT 309
Cdd:PLN00113 76 LSGKNIsGKISSAIFRLPYIQTINLSNNQLSGpIPDDiFTTSSSLRYLNLSNNNFTgSIPRGSIP--NLETLDLSNNMLS 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 296437367 310 -SVPSLISGLGRLLTLWLDNNRIR-YLPDSIVELTGLEELVLQGNQ-IAVLPDHFGQL 364
Cdd:PLN00113 154 gEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQlVGQIPRELGQM 211
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
58-202 |
1.19e-04 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 46.31 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 58 LPANLGDIEALNLGNNGLEEVPeglgSALGSLRVLVLRRNRFARLPPavaeLGHHLTELDVSHNRLTALgaEVVSAlrEL 137
Cdd:PRK15387 337 LPTLPSGLQELSVSDNQLASLP----TLPSELYKLWAYNNRLTSLPA----LPSGLKELIVSGNRLTSL--PVLPS--EL 404
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296437367 138 RKLNLSHNQLPALPAQLGALAhleELDVSFNRLAHLPDSLSCLSRLRTLDVDHNQLTAFPRQLLQ 202
Cdd:PRK15387 405 KELMVSGNRLTSLPMLPSGLL---SLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALR 466
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
181-236 |
1.32e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 40.97 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 296437367 181 SRLRTLDVDHNQLTAFPRQLLQ-LVALEELDVSSNRLRGL-PEDISALRALKILWLSG 236
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSG 58
|
|
| COR |
pfam16095 |
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ... |
660-727 |
1.83e-04 |
|
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.
Pssm-ID: 406489 Cd Length: 196 Bit Score: 43.77 E-value: 1.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296437367 660 PRSWQVLEElHFQPPQAQRLWLSWWDSARLGLQAGLT-EDRLQSALSYLHESGKLLYFEDSPALKEHVF 727
Cdd:pfam16095 1 PKSWLAVRE-ALEKERQKKPYISYEEYRKICAENGIDdEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVI 68
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
206-285 |
3.86e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 39.43 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 206 LEELDVSSNRLRGLPEDisalralkilWLSGaelgtlpagfceLASLESLMLDNNGLQAL-PAQFSCLQRLKMLNLSSNL 284
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDG----------AFKG------------LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNR 60
|
.
gi 296437367 285 F 285
Cdd:pfam13855 61 L 61
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
150-218 |
5.59e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 44.04 E-value: 5.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296437367 150 LPAQLGALAHLEELDVSFNRL-AHLPDSLSCLSRLRTLDVDHNQLT-AFPRQLLQLVALEELDVSSNRLRG 218
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSG 504
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
140-354 |
6.70e-04 |
|
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: 43.24 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 140 LNLSHN-QLPALPAQLGALAHLEELDVSFNRLAHLPD-SLSCLSRLRTLDVDHNQLTAFPRQLLQLVALEELDVSSNRLR 217
Cdd:COG5238 119 LRRIMAkTLEDSLILYLALPRRINLIQVLKDPLGGNAvHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 218 GLPEDISALRALKILWLSGAELGTLPAGF-----CELASLESLMLDNN--GLQALPAQFSCLQ---RLKMLNLSSNLFEE 287
Cdd:COG5238 199 ELAEALTQNTTVTTLWLKRNPIGDEGAEIlaealKGNKSLTTLDLSNNqiGDEGVIALAEALKnntTVETLYLSGNQIGA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 288 FPAALLP--LAG---LEELYLSRNQLT--SVPSLISGLGR---LLTLWLDNNRI-----RYLPDSIVELTGLEELVLQGN 352
Cdd:COG5238 279 EGAIALAkaLQGnttLTSLDLSVNRIGdeGAIALAEGLQGnktLHTLNLAYNGIgaqgaIALAKALQENTTLHSLDLSDN 358
|
..
gi 296437367 353 QI 354
Cdd:COG5238 359 QI 360
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
129-267 |
8.13e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 43.27 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 129 EVVSALRELRK-----LNLSHNQLPALPAQlgalaH-LEELDVSFnrlahlpDSLSCLSRLRTLDVDHNQLTAF-PRQLL 201
Cdd:PLN03150 372 EEVSALQTLKSslglpLRFGWNGDPCVPQQ-----HpWSGADCQF-------DSTKGKWFIDGLGLDNQGLRGFiPNDIS 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296437367 202 QLVALEELDVSSNRLRG-LPEDISALRALKILWLSGAEL-GTLPAGFCELASLESLMLDNNGLQA-LPA 267
Cdd:PLN03150 440 KLRHLQSINLSGNSIRGnIPPSLGSITSLEVLDLSYNSFnGSIPESLGQLTSLRILNLNGNSLSGrVPA 508
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
68-240 |
1.52e-03 |
|
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: 42.08 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 68 LNLGNNGL-EEVPEGLGSALG---SLRVLVLRRNRFArlPPAVAELGHHLTE------LDVSHNRLTALGAE-VVSALR- 135
Cdd:COG5238 213 LWLKRNPIgDEGAEILAEALKgnkSLTTLDLSNNQIG--DEGVIALAEALKNnttvetLYLSGNQIGAEGAIaLAKALQg 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296437367 136 --ELRKLNLSHNQLP-----ALPAQLGALAHLEELDVSFNRLAH-----LPDSLSCLSRLRTLDVDHNQLT-----AFPR 198
Cdd:COG5238 291 ntTLTSLDLSVNRIGdegaiALAEGLQGNKTLHTLNLAYNGIGAqgaiaLAKALQENTTLHSLDLSDNQIGdegaiALAK 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296437367 199 QLLQLVALEELDVSSNRL--RGLPEDISALRA--LKILWLSGAELG 240
Cdd:COG5238 371 YLEGNTTLRELNLGKNNIgkQGAEALIDALQTnrLHTLILDGNLIG 416
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
298-336 |
6.87e-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: 35.30 E-value: 6.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 296437367 298 LEELYLSRNQLTSVPSLiSGLGRLLTLWL-DNNRIRYLPD 336
Cdd:pfam12799 3 LEVLDLSNNQITDIPPL-AKLPNLETLDLsGNNKITDLSD 41
|
|
|