|
Name |
Accession |
Description |
Interval |
E-value |
| PP2C |
pfam00481 |
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ... |
1374-1617 |
1.74e-73 |
|
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.
Pssm-ID: 395385 Cd Length: 252 Bit Score: 245.71 E-value: 1.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1374 DVTFERFRGNDDECLLCLHDSKNQNADyGHNISRIVRDIYDKILIRQLERYGDETDDNIkTALRFSFLQLNKEINGMLNS 1453
Cdd:pfam00481 2 DLGGPRMQGWRKSMEDAHIDLPNLNSS-SGKDSWSFFAVFDGHGGSEAAKYCGKHLHTI-LALRRSFLEGEKLEDALRKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1454 VDNGADVANLSY--ADLLSGACSTVIYIRGKKLFAANLGDCMAILSKNNGDYQTLTKQHLPTKREEYERIRISGGYV-NN 1530
Cdd:pfam00481 80 FLEDTDEVLRSAekEDLDSGCTAVVALISGNKLYVANVGDSRAVLCRNGNAIKRLTKDHKPSDEDERRRIRAAGGFVsRN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1531 GKLDGVVDVSRAVGFFDLLP---HIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIARENS---TDPLRAAAEL 1604
Cdd:pfam00481 160 GRVNGVLAVSRAFGDFELKPgeqAVSAEPDITSHTITEDDEFLILACDGLWDVLSDQEVVDLVRSELsdgGSPMEAAEEL 239
|
250
....*....|...
gi 398364701 1605 KDHAMAYGCTENI 1617
Cdd:pfam00481 240 RDEAIAYGSEDNI 252
|
|
| PP2Cc |
cd00143 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1356-1624 |
6.45e-62 |
|
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 238083 [Multi-domain] Cd Length: 254 Bit Score: 212.57 E-value: 6.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1356 MRYGVADTLGQR----DYVSSRdvtfeRFRGNDDECLLCLHDSKNqnadyGHNISRIVRDIYDKILIRQLERYGDETDDN 1431
Cdd:cd00143 1 FSAGVSDKGGDRktneDAVVIK-----PNLNNEDGGLFGVFDGHG-----GHAAGEFASKLLVEELLEELEETLTLSEED 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1432 IKTALRFSFLQLNKEINGMLNSVDNGADvanlsyadllSGACSTVIYIRGKKLFAANLGDCMAILSKNnGDYQTLTKQHL 1511
Cdd:cd00143 71 IEEALRKAFLRADEEILEEAQDEPDDAR----------SGTTAVVALIRGNKLYVANVGDSRAVLCRN-GEAVQLTKDHK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1512 PTKREEYERIRISGGYVNNGKLDGVVDVSRAVGFFDLLPHIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIAR 1591
Cdd:cd00143 140 PVNEEERERIEKAGGRVSNGRVPGVLAVTRALGDFDLKPGVSAEPDVTVVKLTEDDDFLILASDGLWDVLSNQEAVDIVR 219
|
250 260 270
....*....|....*....|....*....|....*
gi 398364701 1592 E--NSTDPLRAAAELKDHAMAYGCTENITILCLAL 1624
Cdd:cd00143 220 SelAKEDLQEAAQELVDLALRRGSHDNITVVVVRL 254
|
|
| PP2Cc |
smart00332 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1354-1622 |
6.61e-57 |
|
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 214625 [Multi-domain] Cd Length: 252 Bit Score: 198.37 E-value: 6.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1354 NGMRYGVADTLGQRdyVSSRDVTFERFRGNDDECLLCLHDSKNqnadyGHNISRIVRDIYDKILIRQLERYGDETDDnIK 1433
Cdd:smart00332 7 LGLRYGLSSMQGVR--KPMEDAHVITPDLSDSGGFFGVFDGHG-----GSEAAKFLSKNLPEILAEELIKEKDELED-VE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1434 TALRFSFLQLNKEINGMLNSvdngadvanlsyadlLSGACSTVIYIRGKKLFAANLGDCMAILSKNNGDYQtLTKQHLPT 1513
Cdd:smart00332 79 EALRKAFLSTDEEILEELEA---------------LSGSTAVVALISGNKLYVANVGDSRAVLCRNGKAVQ-LTEDHKPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1514 KREEYERIRISGGYVNNGKLDGVVDVSRAVGFFDLLPHIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIAREN 1593
Cdd:smart00332 143 NEDERARIEAAGGFVINGRVNGVLALSRAIGDFFLKPYVSAEPDVTVVELTEKDDFLILASDGLWDVLSNQEVVDIVRKH 222
|
250 260 270
....*....|....*....|....*....|
gi 398364701 1594 -STDPLRAAAELKDHAMAYGCTENITILCL 1622
Cdd:smart00332 223 lSKDPKEAAKRLIDLALARGSKDNITVVVV 252
|
|
| CYCc |
smart00044 |
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ... |
1613-1825 |
2.83e-53 |
|
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.
Pssm-ID: 214485 Cd Length: 194 Bit Score: 185.54 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1613 CTENITILCLALYENIQQQNRftlnknslmtrrstfedttlRRLQPEISPPTGNLAMVFTDIKSSTFLWE-LFPNAMRTA 1691
Cdd:smart00044 3 KKKTDRLLDQLLPASVAEQLK--------------------RGGSPVPAESYDNVTILFSDIVGFTSLCStSTPEQVVNL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1692 IKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSGLtwclsVQLKLLDAQWPEEITSVQDGCQVTDRngniiYQGLSV 1771
Cdd:smart00044 63 LNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAL-----VDHAELIADEALDMVEELKTVLVQHR-----EEGLRV 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398364701 1772 RMGIHWGCPVPELDLVTQ-RMDYLGPMVNKAARVQGVADGGQIAMSSDFYSEFNK 1825
Cdd:smart00044 133 RIGIHTGPVVAGVVGIRMpRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLAR 187
|
|
| RA_PHLPP_like |
cd01775 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
678-776 |
5.90e-43 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatases, fungal adenylate cyclase, and similar proteins; PHLPP represents a novel family of Ser/Thr protein phosphatases, which is involved in two key signaling pathways, the phosphatidylinositol 3-kinase and diacylglycerol signaling pathways, by directly dephosphorylating and inactivating Akt serine-threonine kinases (Akt1, Akt2, Akt3) and protein kinase C (PKC) isoforms. PHLPP contains a putative Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain. Fungal adenylate cyclase regulates developmental processes such as hyphal growth, biofilm formation, and phenotypic switching. It plays an essential role in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. Fungal adenylate cyclase has at least four domains, including an N-terminal adenylate cyclase G-alpha binding domain, a Ras-associating (RA) domain, a middle leucine-rich repeat region, and a catalytic domain. The RA domain of adenylate cyclase post-translationally modifies a small GTPase called Ras, which is involved in cellular signal transduction. The activity of adenylate cyclase is stimulated directly by regulatory proteins (Ras1 and Gpa2), peptidoglycan fragments and carbon dioxide.
Pssm-ID: 340473 Cd Length: 99 Bit Score: 152.25 E-value: 5.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 678 YAIRIFNTDDTFTTLSCTPATTVEEIIPALKRKFNITAQGNFQISLKVGKLSKILRPTSKPILIERKLLLLNGYRKSDPL 757
Cdd:cd01775 1 GSIRVYKADSKFTTVSCTINTTVSEIIAGLGRKSFLNANEDYRILLKHGGLVRRLRPDEKPLRIQRDLLLLLGYTDPDRQ 80
|
90
....*....|....*....
gi 398364701 758 HIMGIEDLSFVFKFLFHPV 776
Cdd:cd01775 81 EEATNPDLSYVIKFVFEKP 99
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
818-1252 |
4.17e-36 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 143.15 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 818 IESLDVSNNANIFLPLEFIESSIKLLSLRMVNIRASKFPSNITKAYKLVSLELQRNFIRKVPNSIMKLSNLTILNLQCNE 897
Cdd:COG4886 5 LLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 898 LESLPAGFVELKNLQLLDLSSNKFmhypevINYCTNLLQIDLSYNKIQSLPQSTKYLVKLAKMNLSHNKLNFIGD-LSEM 976
Cdd:COG4886 85 LLLGLTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEpLGNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 977 TDLRTLNLRYNRISSIKTNASNLQNL---FLTDNRISNFEDTLPKLraleiqenpitsisfkdfypKNMTSLTLNKAQLS 1053
Cdd:COG4886 159 TNLKSLDLSNNQLTDLPEELGNLTNLkelDLSNNQITDLPEPLGNL--------------------TNLEELDLSGNQLT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1054 SIPGElLTKLSFLEKLELNQNNLTRLPqEISKLTKLVFLSVARNKLEYIPPeLSQLKSLRTLDLHSNNIRDFVDGMENLE 1133
Cdd:COG4886 219 DLPEP-LANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELELL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1134 LTSLNISSNAFGNSSLENSFYHNMSYGSKLSKSLMFFIAADNQFDDAMWPLFNCFVNLKVLNLSYNNFSDVSHMKLESIT 1213
Cdd:COG4886 296 LGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLL 375
|
410 420 430
....*....|....*....|....*....|....*....
gi 398364701 1214 ELYLSGNKLTTLSGDTVLKWSSLKTLMLNSNQMLSLPAE 1252
Cdd:COG4886 376 EATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
|
|
| Guanylate_cyc |
pfam00211 |
Adenylate and Guanylate cyclase catalytic domain; |
1661-1837 |
1.42e-27 |
|
Adenylate and Guanylate cyclase catalytic domain;
Pssm-ID: 425528 Cd Length: 183 Bit Score: 111.18 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1661 SPPTGNLAMVFTDIKSSTFLWE-LFPNAMRTAIKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSG---LTWCLSVQ 1736
Cdd:pfam00211 3 AQPYDNVTILFADIVGFTALSSrHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSpahARKIAEMA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1737 LKLLDAqwpeeITSVqdgcQVTDRNgniiyqGLSVRMGIHWGCPVPELD-LVTQRMDYLGPMVNKAARVQGVADGGQIAM 1815
Cdd:pfam00211 83 LDMLEA-----IGEV----NVESSE------GLRVRVGIHTGPVVAGVIgARMPRYDLWGNTVNLASRMESTGVPGKIHV 147
|
170 180
....*....|....*....|....*.
gi 398364701 1816 SSDFYSEFNKIMKYHERV----VKGK 1837
Cdd:pfam00211 148 SEETYRLLKTEGFEFTERgeieVKGK 173
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
792-1273 |
1.43e-23 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 109.17 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 792 SEFVHVDL--RNMDLTTPPIIFyqHTSEIESLDVSNNANIF-LPLEFIESSIkllSLRMVNIRASKFPSNITKAY--KLV 866
Cdd:PLN00113 69 SRVVSIDLsgKNISGKISSAIF--RLPYIQTINLSNNQLSGpIPDDIFTTSS---SLRYLNLSNNNFTGSIPRGSipNLE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 867 SLELQRNFIR-KVPNSIMKLSNLTILNLQCNELES-LPAGFVELKNLQLLDLSSNKFM-HYPEVINYCTNLLQIDLSYNk 943
Cdd:PLN00113 144 TLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYN- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 944 iqslpqstkylvklakmNLSHNKLNFIGDLsemTDLRTLNLRYN----RISSIKTNASNLQNLFLTDNRISnfeDTLPKl 1019
Cdd:PLN00113 223 -----------------NLSGEIPYEIGGL---TSLNHLDLVYNnltgPIPSSLGNLKNLQYLFLYQNKLS---GPIPP- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1020 raleiqenpitSIsfkdFYPKNMTSLTLNKAQLSSIPGELLTKLSFLEKLELNQNNLT-RLPQEISKLTKLVFLSVARNK 1098
Cdd:PLN00113 279 -----------SI----FSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1099 LE-YIPPELSQLKSLRTLDLHSNNIR-DFVDGM-ENLELTSLNISSNAFGN---------SSLENSFYHNMSYGSKLSKS 1166
Cdd:PLN00113 344 FSgEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLcSSGNLFKLILFSNSLEGeipkslgacRSLRRVRLQDNSFSGELPSE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1167 LM------FFIAADNQF----DDAMWPL---------FNCFV----------NLKVLNLSYNNFSDV---SHMKLESITE 1214
Cdd:PLN00113 424 FTklplvyFLDISNNNLqgriNSRKWDMpslqmlslaRNKFFgglpdsfgskRLENLDLSRNQFSGAvprKLGSLSELMQ 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1215 LYLSGNKLTTLSGDTVLKWSSLKTLMLNSNQML-SLPAELSNLSQLSVFDVGANQLKYNI 1273
Cdd:PLN00113 504 LKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSGEI 563
|
|
| CHD |
cd07302 |
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ... |
1666-1844 |
3.19e-22 |
|
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.
Pssm-ID: 143636 [Multi-domain] Cd Length: 177 Bit Score: 95.72 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1666 NLAMVFTDIKSSTFLWE-LFPNAMRTAIKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSG-------LTWCLSVQL 1737
Cdd:cd07302 1 EVTVLFADIVGFTALSErLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHedhaeraVRAALEMQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1738 KLLDAQWPEEitsvqdgcqvtdrngniIYQGLSVRMGIHWGcPVPELDLVTQRMDY--LGPMVNKAARVQGVADGGQIAM 1815
Cdd:cd07302 81 ALAELNAERE-----------------GGPPLRLRIGIHTG-PVVAGVVGSERPEYtvIGDTVNLAARLESLAKPGQILV 142
|
170 180 190
....*....|....*....|....*....|...
gi 398364701 1816 SSDFY----SEFNKIMKYHERVVKGKESLKEVY 1844
Cdd:cd07302 143 SEATYellgDAGFEFEELGEVELKGKSGPVRVY 175
|
|
| AcyC |
COG2114 |
Adenylate cyclase, class 3 [Signal transduction mechanisms]; |
1657-1844 |
8.37e-20 |
|
Adenylate cyclase, class 3 [Signal transduction mechanisms];
Pssm-ID: 441717 [Multi-domain] Cd Length: 407 Bit Score: 94.10 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1657 QPEISPPTGNLAMVFTDIKSSTFLWE-LFPNAMRTAIKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSG------- 1728
Cdd:COG2114 213 ELRLGGERREVTVLFADIVGFTALSErLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVARedhaera 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1729 LTWCLSVQ--LKLLDAQWPEEitsvqdgcqvtdrngniIYQGLSVRMGIHWGcPVpeldLV-----TQRMDY--LGPMVN 1799
Cdd:COG2114 293 VRAALAMQeaLAELNAELPAE-----------------GGPPLRVRIGIHTG-EV----VVgnigsEDRLDYtvIGDTVN 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398364701 1800 KAARVQGVADGGQIAMSSDFYSEFNKIMKYHER---VVKGKESLKEVY 1844
Cdd:COG2114 351 LAARLESLAKPGEILVSEATYDLLRDRFEFRELgevRLKGKAEPVEVY 398
|
|
| PLN03145 |
PLN03145 |
Protein phosphatase 2c; Provisional |
1445-1657 |
1.24e-17 |
|
Protein phosphatase 2c; Provisional
Pssm-ID: 215603 [Multi-domain] Cd Length: 365 Bit Score: 86.89 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1445 KEINGMLNS----VDNG-ADVANLSyADLLSGACSTVIYIRGKKLFAANLGDCMAILSKNnGDYQTLTKQHLPTKREEYE 1519
Cdd:PLN03145 137 REIEKVVSSaflqTDTAfAEACSLD-ASLASGTTALAALVVGRSLVVANAGDCRAVLCRR-GKAIEMSRDHKPMCSKERK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1520 RIRISGGYVNNGKLDGVVDVSRAVGFF--------DLLPhIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIAR 1591
Cdd:PLN03145 215 RIEASGGYVYDGYLNGQLNVARALGDWhmegmkgsDGGP-LSAEPELMTTQLTEEDEFLIIGCDGIWDVFRSQNAVDFAR 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364701 1592 ---ENSTDPLRAAAELKDHAMAYGCTENITILCLALyeniQQQNRFTLNKNSLMTRRStFEDTTLRRLQ 1657
Cdd:PLN03145 294 rrlQEHNDPVMCSKELVDEALKRKSGDNLAVVVVCF----QSQPPPNLVAPRPRVQRS-ISAEGLRELQ 357
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
864-1070 |
5.67e-15 |
|
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: 75.98 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 864 KLVSLELQRNFIRKVPNsIMKLSNLTILNLQCNELESLPaGFVELKNLQLLDLSSNKFmhypEVI---NYCTNLLQIDLS 940
Cdd:cd21340 25 NLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRI----SVVeglENLTNLEELHIE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 941 YNKI---QSL---PQSTKYLVK-LAKMNLSHNKLNFIGDLSEMTDLRTLNLRYNRISSIKtnasnlqnlfltdnRISNFE 1013
Cdd:cd21340 99 NQRLppgEKLtfdPRSLAALSNsLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLE--------------ELLDLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398364701 1014 DTLPKLRALEIQENPITSIsfkdfyPKNMTSLTLNKAQLSSIPGELLTKLS--FLEKLE 1070
Cdd:cd21340 165 SSWPSLRELDLTGNPVCKK------PKYRDKIILASKSLEVLDGKEITDTErqFLKRLK 217
|
|
| Ad_cyc_g-alpha |
pfam08509 |
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and ... |
368-418 |
7.82e-11 |
|
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and interacts with the alpha subunit of heterotrimeric G proteins.
Pssm-ID: 430040 Cd Length: 48 Bit Score: 58.85 E-value: 7.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 398364701 368 EATTPTIETPiscKPSLFRLDTNLEDVTDITKTVPPTAVNSTLNSTHGTET 418
Cdd:pfam08509 1 EAIGPTDRTD---GGTVFHLDTNLNDMEGILSKPPPLTPMDTDFSINGVEF 48
|
|
| Ad_cyc_g-alpha |
smart00789 |
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and ... |
367-420 |
1.91e-07 |
|
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and interacts with the alpha subunit of heterotrimeric G proteins.
Pssm-ID: 129025 Cd Length: 51 Bit Score: 49.29 E-value: 1.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 398364701 367 REATTPTIETPisckPSLFRLDTNLEDVTDI-TKTVPPTAVNSTLNSTHGTETAS 420
Cdd:smart00789 1 DEAIGPTDREG----GSVFHLDTNLNDMEGIlTKPPPLTPMDGSFINTGESEKHN 51
|
|
| RA |
smart00314 |
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ... |
676-755 |
4.73e-07 |
|
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)
Pssm-ID: 214612 Cd Length: 90 Bit Score: 49.60 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 676 RHYAIRIFNTD---DTFTTLSCTPATTVEEIIPALKRKFNITAQGN-FQISLKV--GKLSKILRPTSKPILIER----KL 745
Cdd:smart00314 1 DTFVLRVYVDDlpgGTYKTLRVSSRTTARDVIQQLLEKFHLTDDPEeYVLVEVLpdGKERVLPDDENPLQLQKLwprrGP 80
|
90
....*....|
gi 398364701 746 LLLNGYRKSD 755
Cdd:smart00314 81 NLRFVLRKRD 90
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
864-921 |
5.50e-07 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 48.29 E-value: 5.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 864 KLVSLELQRNFIRKV-PNSIMKLSNLTILNLQCNELESL-PAGFVELKNLQLLDLSSNKF 921
Cdd:pfam13855 2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
188-366 |
3.47e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 42.59 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 188 SGKESKVANLSLSTVNPApANRKPSKDSTLSNhladNVPSTLRRKVSSLVRGSsvhDINNGIADKQIRPkavAQSENTLH 267
Cdd:NF033609 33 SSKEADASENSVTQSDSA-SNESKSNDSSSVS----AAPKTDDTNVSDTKTSS---NTNNGETSVAQNP---AQQETTQS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 268 SSDVPNSKRSHRKSFLLGSTSSSSSRRGSNVSSMTNSDSASMATSgSHVLQHNVSNVSPTTKSKDSVNSESADHTNNKSE 347
Cdd:NF033609 102 ASTNATTEETPVTGEATTTATNQANTPATTQSSNTNAEELVNQTS-NETTSNDTNTVSSVNSPQNSTNAENVSTTQDTST 180
|
170
....*....|....*....
gi 398364701 348 KVTPEYNENIPENSNSDNK 366
Cdd:NF033609 181 EATPSNNESAPQSTDASNK 199
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PP2C |
pfam00481 |
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ... |
1374-1617 |
1.74e-73 |
|
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.
Pssm-ID: 395385 Cd Length: 252 Bit Score: 245.71 E-value: 1.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1374 DVTFERFRGNDDECLLCLHDSKNQNADyGHNISRIVRDIYDKILIRQLERYGDETDDNIkTALRFSFLQLNKEINGMLNS 1453
Cdd:pfam00481 2 DLGGPRMQGWRKSMEDAHIDLPNLNSS-SGKDSWSFFAVFDGHGGSEAAKYCGKHLHTI-LALRRSFLEGEKLEDALRKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1454 VDNGADVANLSY--ADLLSGACSTVIYIRGKKLFAANLGDCMAILSKNNGDYQTLTKQHLPTKREEYERIRISGGYV-NN 1530
Cdd:pfam00481 80 FLEDTDEVLRSAekEDLDSGCTAVVALISGNKLYVANVGDSRAVLCRNGNAIKRLTKDHKPSDEDERRRIRAAGGFVsRN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1531 GKLDGVVDVSRAVGFFDLLP---HIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIARENS---TDPLRAAAEL 1604
Cdd:pfam00481 160 GRVNGVLAVSRAFGDFELKPgeqAVSAEPDITSHTITEDDEFLILACDGLWDVLSDQEVVDLVRSELsdgGSPMEAAEEL 239
|
250
....*....|...
gi 398364701 1605 KDHAMAYGCTENI 1617
Cdd:pfam00481 240 RDEAIAYGSEDNI 252
|
|
| PP2Cc |
cd00143 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1356-1624 |
6.45e-62 |
|
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 238083 [Multi-domain] Cd Length: 254 Bit Score: 212.57 E-value: 6.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1356 MRYGVADTLGQR----DYVSSRdvtfeRFRGNDDECLLCLHDSKNqnadyGHNISRIVRDIYDKILIRQLERYGDETDDN 1431
Cdd:cd00143 1 FSAGVSDKGGDRktneDAVVIK-----PNLNNEDGGLFGVFDGHG-----GHAAGEFASKLLVEELLEELEETLTLSEED 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1432 IKTALRFSFLQLNKEINGMLNSVDNGADvanlsyadllSGACSTVIYIRGKKLFAANLGDCMAILSKNnGDYQTLTKQHL 1511
Cdd:cd00143 71 IEEALRKAFLRADEEILEEAQDEPDDAR----------SGTTAVVALIRGNKLYVANVGDSRAVLCRN-GEAVQLTKDHK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1512 PTKREEYERIRISGGYVNNGKLDGVVDVSRAVGFFDLLPHIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIAR 1591
Cdd:cd00143 140 PVNEEERERIEKAGGRVSNGRVPGVLAVTRALGDFDLKPGVSAEPDVTVVKLTEDDDFLILASDGLWDVLSNQEAVDIVR 219
|
250 260 270
....*....|....*....|....*....|....*
gi 398364701 1592 E--NSTDPLRAAAELKDHAMAYGCTENITILCLAL 1624
Cdd:cd00143 220 SelAKEDLQEAAQELVDLALRRGSHDNITVVVVRL 254
|
|
| PP2Cc |
smart00332 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1354-1622 |
6.61e-57 |
|
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 214625 [Multi-domain] Cd Length: 252 Bit Score: 198.37 E-value: 6.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1354 NGMRYGVADTLGQRdyVSSRDVTFERFRGNDDECLLCLHDSKNqnadyGHNISRIVRDIYDKILIRQLERYGDETDDnIK 1433
Cdd:smart00332 7 LGLRYGLSSMQGVR--KPMEDAHVITPDLSDSGGFFGVFDGHG-----GSEAAKFLSKNLPEILAEELIKEKDELED-VE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1434 TALRFSFLQLNKEINGMLNSvdngadvanlsyadlLSGACSTVIYIRGKKLFAANLGDCMAILSKNNGDYQtLTKQHLPT 1513
Cdd:smart00332 79 EALRKAFLSTDEEILEELEA---------------LSGSTAVVALISGNKLYVANVGDSRAVLCRNGKAVQ-LTEDHKPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1514 KREEYERIRISGGYVNNGKLDGVVDVSRAVGFFDLLPHIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIAREN 1593
Cdd:smart00332 143 NEDERARIEAAGGFVINGRVNGVLALSRAIGDFFLKPYVSAEPDVTVVELTEKDDFLILASDGLWDVLSNQEVVDIVRKH 222
|
250 260 270
....*....|....*....|....*....|
gi 398364701 1594 -STDPLRAAAELKDHAMAYGCTENITILCL 1622
Cdd:smart00332 223 lSKDPKEAAKRLIDLALARGSKDNITVVVV 252
|
|
| CYCc |
smart00044 |
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ... |
1613-1825 |
2.83e-53 |
|
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.
Pssm-ID: 214485 Cd Length: 194 Bit Score: 185.54 E-value: 2.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1613 CTENITILCLALYENIQQQNRftlnknslmtrrstfedttlRRLQPEISPPTGNLAMVFTDIKSSTFLWE-LFPNAMRTA 1691
Cdd:smart00044 3 KKKTDRLLDQLLPASVAEQLK--------------------RGGSPVPAESYDNVTILFSDIVGFTSLCStSTPEQVVNL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1692 IKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSGLtwclsVQLKLLDAQWPEEITSVQDGCQVTDRngniiYQGLSV 1771
Cdd:smart00044 63 LNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAL-----VDHAELIADEALDMVEELKTVLVQHR-----EEGLRV 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 398364701 1772 RMGIHWGCPVPELDLVTQ-RMDYLGPMVNKAARVQGVADGGQIAMSSDFYSEFNK 1825
Cdd:smart00044 133 RIGIHTGPVVAGVVGIRMpRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLAR 187
|
|
| RA_PHLPP_like |
cd01775 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
678-776 |
5.90e-43 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatases, fungal adenylate cyclase, and similar proteins; PHLPP represents a novel family of Ser/Thr protein phosphatases, which is involved in two key signaling pathways, the phosphatidylinositol 3-kinase and diacylglycerol signaling pathways, by directly dephosphorylating and inactivating Akt serine-threonine kinases (Akt1, Akt2, Akt3) and protein kinase C (PKC) isoforms. PHLPP contains a putative Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain. Fungal adenylate cyclase regulates developmental processes such as hyphal growth, biofilm formation, and phenotypic switching. It plays an essential role in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. Fungal adenylate cyclase has at least four domains, including an N-terminal adenylate cyclase G-alpha binding domain, a Ras-associating (RA) domain, a middle leucine-rich repeat region, and a catalytic domain. The RA domain of adenylate cyclase post-translationally modifies a small GTPase called Ras, which is involved in cellular signal transduction. The activity of adenylate cyclase is stimulated directly by regulatory proteins (Ras1 and Gpa2), peptidoglycan fragments and carbon dioxide.
Pssm-ID: 340473 Cd Length: 99 Bit Score: 152.25 E-value: 5.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 678 YAIRIFNTDDTFTTLSCTPATTVEEIIPALKRKFNITAQGNFQISLKVGKLSKILRPTSKPILIERKLLLLNGYRKSDPL 757
Cdd:cd01775 1 GSIRVYKADSKFTTVSCTINTTVSEIIAGLGRKSFLNANEDYRILLKHGGLVRRLRPDEKPLRIQRDLLLLLGYTDPDRQ 80
|
90
....*....|....*....
gi 398364701 758 HIMGIEDLSFVFKFLFHPV 776
Cdd:cd01775 81 EEATNPDLSYVIKFVFEKP 99
|
|
| RA_CYR1_like |
cd17214 |
Ras-associating (RA) domain found in Saccharomyces cerevisiae adenylate cyclase and similar ... |
678-775 |
5.38e-38 |
|
Ras-associating (RA) domain found in Saccharomyces cerevisiae adenylate cyclase and similar proteins; CYR1, also termed ATP pyrophosphate-lyase, or adenylyl cyclase, is a fungal adenylate cyclase that regulates developmental processes such as hyphal growth, biofilm formation, and phenotypic switching. CYR1 plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. It acts as a scaffold protein keeping Ras2 available for its regulatory factors, the Ira proteins. CYR1 has at least four domains, including an N-terminal adenylate cyclase G-alpha binding domain, a Ras-associating (RA) domain, a middle leucine-rich repeat region, and a catalytic domain. The RA domain has the beta-grasp ubiquitin-like fold with low sequence similarity to ubiquitin; ubiquitin is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. The RA domain of CYR1 post-translationally modifies a small GTPase called Ras, which is involved in cellular signal transduction. CYR1 activity is stimulated directly by regulatory proteins (Ras1 and Gpa2), peptidoglycan fragments and carbon dioxide.
Pssm-ID: 340734 Cd Length: 99 Bit Score: 138.12 E-value: 5.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 678 YAIRIFNTDDTFTTLSCTPATTVEEIIPALKRKFNITAQGNFQISLKVGKLSKILRPTSKPILIERKLLLLNGYRKSDPL 757
Cdd:cd17214 1 YRIRVYRPDGTFHTLSCPLNTTTSELLSMLAKKFFLPDSANYRLYLRERGLERILRSNEKPLLIQKRLLLQAGYTELDGL 80
|
90
....*....|....*...
gi 398364701 758 HIMGIEDLSFVFKFLFHP 775
Cdd:cd17214 81 EEIGREDNSYLCRFIFRP 98
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
818-1252 |
4.17e-36 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 143.15 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 818 IESLDVSNNANIFLPLEFIESSIKLLSLRMVNIRASKFPSNITKAYKLVSLELQRNFIRKVPNSIMKLSNLTILNLQCNE 897
Cdd:COG4886 5 LLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 898 LESLPAGFVELKNLQLLDLSSNKFmhypevINYCTNLLQIDLSYNKIQSLPQSTKYLVKLAKMNLSHNKLNFIGD-LSEM 976
Cdd:COG4886 85 LLLGLTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEpLGNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 977 TDLRTLNLRYNRISSIKTNASNLQNL---FLTDNRISNFEDTLPKLraleiqenpitsisfkdfypKNMTSLTLNKAQLS 1053
Cdd:COG4886 159 TNLKSLDLSNNQLTDLPEELGNLTNLkelDLSNNQITDLPEPLGNL--------------------TNLEELDLSGNQLT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1054 SIPGElLTKLSFLEKLELNQNNLTRLPqEISKLTKLVFLSVARNKLEYIPPeLSQLKSLRTLDLHSNNIRDFVDGMENLE 1133
Cdd:COG4886 219 DLPEP-LANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELELL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1134 LTSLNISSNAFGNSSLENSFYHNMSYGSKLSKSLMFFIAADNQFDDAMWPLFNCFVNLKVLNLSYNNFSDVSHMKLESIT 1213
Cdd:COG4886 296 LGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLL 375
|
410 420 430
....*....|....*....|....*....|....*....
gi 398364701 1214 ELYLSGNKLTTLSGDTVLKWSSLKTLMLNSNQMLSLPAE 1252
Cdd:COG4886 376 EATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
789-1146 |
2.26e-35 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 141.22 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 789 IMRSEFVHVDLRNMDLTTPPIIFYQHTSEIESLDVSNNANIFLPLEFIESSIKLLSLR--MVNIRASKFPSNITKAYKLV 866
Cdd:COG4886 20 LLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLslLLLSLLLLGLTDLGDLTNLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 867 SLELQRNfirkvpNSIMKLSNLTILNLQCNELESLPAGFVELKNLQLLDLSSNKFMHYPEVINYCTNLLQIDLSYNKIQS 946
Cdd:COG4886 100 ELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 947 LPQSTKYLVKLAKMNLSHNKLNFIGD-LSEMTDLRTLNLRYNRISSIK---TNASNLQNLFLTDNRISNFED--TLPKLR 1020
Cdd:COG4886 174 LPEELGNLTNLKELDLSNNQITDLPEpLGNLTNLEELDLSGNQLTDLPeplANLTNLETLDLSNNQLTDLPElgNLTNLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1021 ALEIQENPITSISfKDFYPKNMTSLTLNKAQLSSIPGELLTKLSFLEKLELNQNNLTRLPQEISKLTKLVFLSVARNKLE 1100
Cdd:COG4886 254 ELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398364701 1101 YIPPELSQLKSLRTLDLHSNNIRDFVDGMENLELTSLNISSNAFGN 1146
Cdd:COG4886 333 LLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEAT 378
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
816-1139 |
1.06e-31 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 130.05 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 816 SEIESLDVSNNaniflplEFIESSIKLLSLRMVNIRASKFPSNITKAYKLVSLELQRNFIRKVPNSIMKLSNLTILNLQC 895
Cdd:COG4886 96 TNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 896 NELESLPAGFVELKNLQLLDLSSNKFMHYPEVINYCTNLLQIDLSYNKIQSLPQSTKYLVKLAKMNLSHNKLNFIGDLSE 975
Cdd:COG4886 169 NQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 976 MTDLRTLNLRYNRISSIKTNA--SNLQNLFLTDNRISNFEDTLPKLRALEIQENPITSISFKDFYPKNMTSLTLNKAQLS 1053
Cdd:COG4886 249 LTNLEELDLSNNQLTDLPPLAnlTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1054 SIPGELLTKLSFLEKLELNQNNLTRLPQEISKLTKLVFLSVARNKLEYIPPELSQLKSLRTLDLHSNNIRDFVDGMENLE 1133
Cdd:COG4886 329 LLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALL 408
|
....*.
gi 398364701 1134 LTSLNI 1139
Cdd:COG4886 409 DAVNTE 414
|
|
| Guanylate_cyc |
pfam00211 |
Adenylate and Guanylate cyclase catalytic domain; |
1661-1837 |
1.42e-27 |
|
Adenylate and Guanylate cyclase catalytic domain;
Pssm-ID: 425528 Cd Length: 183 Bit Score: 111.18 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1661 SPPTGNLAMVFTDIKSSTFLWE-LFPNAMRTAIKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSG---LTWCLSVQ 1736
Cdd:pfam00211 3 AQPYDNVTILFADIVGFTALSSrHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSpahARKIAEMA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1737 LKLLDAqwpeeITSVqdgcQVTDRNgniiyqGLSVRMGIHWGCPVPELD-LVTQRMDYLGPMVNKAARVQGVADGGQIAM 1815
Cdd:pfam00211 83 LDMLEA-----IGEV----NVESSE------GLRVRVGIHTGPVVAGVIgARMPRYDLWGNTVNLASRMESTGVPGKIHV 147
|
170 180
....*....|....*....|....*.
gi 398364701 1816 SSDFYSEFNKIMKYHERV----VKGK 1837
Cdd:pfam00211 148 SEETYRLLKTEGFEFTERgeieVKGK 173
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
981-1396 |
3.61e-27 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 116.57 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 981 TLNLRYNRISSIKTNASNLQNLFLTDNRISNFEDTLPKLRALEIQENPITSISFKDFYPKNMTSLTLNKAQLSSIPGELL 1060
Cdd:COG4886 13 LLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1061 TKLSFLEKLELNQNNltrlpqEISKLTKLVFLSVARNKLEYIPPELSQLKSLRTLDLHSNNIRDFVDGMENLE-LTSLNI 1139
Cdd:COG4886 93 GDLTNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTnLKSLDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1140 SSNAFgnSSLENSFyhnmsygSKLsKSLMFFIAADNQFDDAMWPLFNCfVNLKVLNLSYNNFSDVSH--MKLESITELYL 1217
Cdd:COG4886 167 SNNQL--TDLPEEL-------GNL-TNLKELDLSNNQITDLPEPLGNL-TNLEELDLSGNQLTDLPEplANLTNLETLDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1218 SGNKLTTLSGdtVLKWSSLKTLMLNSNQMLSLPaELSNLSQLSVFDVGANQLKYNISNYHYDWNWRNNKELKYLNFSGNR 1297
Cdd:COG4886 236 SNNQLTDLPE--LGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1298 RFEIKSFISHDIDADLSDLTVLPQLKVLGLMDVTLNTTKVPDENVNFRLRTTASIINGMRYGVADTLGQRDYVSSRDVTF 1377
Cdd:COG4886 313 LLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLL 392
|
410
....*....|....*....
gi 398364701 1378 ERFRGNDDECLLCLHDSKN 1396
Cdd:COG4886 393 LLTTTAGVLLLTLALLDAV 411
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
792-1273 |
1.43e-23 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 109.17 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 792 SEFVHVDL--RNMDLTTPPIIFyqHTSEIESLDVSNNANIF-LPLEFIESSIkllSLRMVNIRASKFPSNITKAY--KLV 866
Cdd:PLN00113 69 SRVVSIDLsgKNISGKISSAIF--RLPYIQTINLSNNQLSGpIPDDIFTTSS---SLRYLNLSNNNFTGSIPRGSipNLE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 867 SLELQRNFIR-KVPNSIMKLSNLTILNLQCNELES-LPAGFVELKNLQLLDLSSNKFM-HYPEVINYCTNLLQIDLSYNk 943
Cdd:PLN00113 144 TLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYN- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 944 iqslpqstkylvklakmNLSHNKLNFIGDLsemTDLRTLNLRYN----RISSIKTNASNLQNLFLTDNRISnfeDTLPKl 1019
Cdd:PLN00113 223 -----------------NLSGEIPYEIGGL---TSLNHLDLVYNnltgPIPSSLGNLKNLQYLFLYQNKLS---GPIPP- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1020 raleiqenpitSIsfkdFYPKNMTSLTLNKAQLSSIPGELLTKLSFLEKLELNQNNLT-RLPQEISKLTKLVFLSVARNK 1098
Cdd:PLN00113 279 -----------SI----FSLQKLISLDLSDNSLSGEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLPRLQVLQLWSNK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1099 LE-YIPPELSQLKSLRTLDLHSNNIR-DFVDGM-ENLELTSLNISSNAFGN---------SSLENSFYHNMSYGSKLSKS 1166
Cdd:PLN00113 344 FSgEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLcSSGNLFKLILFSNSLEGeipkslgacRSLRRVRLQDNSFSGELPSE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1167 LM------FFIAADNQF----DDAMWPL---------FNCFV----------NLKVLNLSYNNFSDV---SHMKLESITE 1214
Cdd:PLN00113 424 FTklplvyFLDISNNNLqgriNSRKWDMpslqmlslaRNKFFgglpdsfgskRLENLDLSRNQFSGAvprKLGSLSELMQ 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1215 LYLSGNKLTTLSGDTVLKWSSLKTLMLNSNQML-SLPAELSNLSQLSVFDVGANQLKYNI 1273
Cdd:PLN00113 504 LKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSGEI 563
|
|
| CHD |
cd07302 |
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ... |
1666-1844 |
3.19e-22 |
|
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.
Pssm-ID: 143636 [Multi-domain] Cd Length: 177 Bit Score: 95.72 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1666 NLAMVFTDIKSSTFLWE-LFPNAMRTAIKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSG-------LTWCLSVQL 1737
Cdd:cd07302 1 EVTVLFADIVGFTALSErLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHedhaeraVRAALEMQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1738 KLLDAQWPEEitsvqdgcqvtdrngniIYQGLSVRMGIHWGcPVPELDLVTQRMDY--LGPMVNKAARVQGVADGGQIAM 1815
Cdd:cd07302 81 ALAELNAERE-----------------GGPPLRLRIGIHTG-PVVAGVVGSERPEYtvIGDTVNLAARLESLAKPGQILV 142
|
170 180 190
....*....|....*....|....*....|...
gi 398364701 1816 SSDFY----SEFNKIMKYHERVVKGKESLKEVY 1844
Cdd:cd07302 143 SEATYellgDAGFEFEELGEVELKGKSGPVRVY 175
|
|
| AcyC |
COG2114 |
Adenylate cyclase, class 3 [Signal transduction mechanisms]; |
1657-1844 |
8.37e-20 |
|
Adenylate cyclase, class 3 [Signal transduction mechanisms];
Pssm-ID: 441717 [Multi-domain] Cd Length: 407 Bit Score: 94.10 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1657 QPEISPPTGNLAMVFTDIKSSTFLWE-LFPNAMRTAIKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPTPTSG------- 1728
Cdd:COG2114 213 ELRLGGERREVTVLFADIVGFTALSErLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVARedhaera 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1729 LTWCLSVQ--LKLLDAQWPEEitsvqdgcqvtdrngniIYQGLSVRMGIHWGcPVpeldLV-----TQRMDY--LGPMVN 1799
Cdd:COG2114 293 VRAALAMQeaLAELNAELPAE-----------------GGPPLRVRIGIHTG-EV----VVgnigsEDRLDYtvIGDTVN 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398364701 1800 KAARVQGVADGGQIAMSSDFYSEFNKIMKYHER---VVKGKESLKEVY 1844
Cdd:COG2114 351 LAARLESLAKPGEILVSEATYDLLRDRFEFRELgevRLKGKAEPVEVY 398
|
|
| PLN03145 |
PLN03145 |
Protein phosphatase 2c; Provisional |
1445-1657 |
1.24e-17 |
|
Protein phosphatase 2c; Provisional
Pssm-ID: 215603 [Multi-domain] Cd Length: 365 Bit Score: 86.89 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1445 KEINGMLNS----VDNG-ADVANLSyADLLSGACSTVIYIRGKKLFAANLGDCMAILSKNnGDYQTLTKQHLPTKREEYE 1519
Cdd:PLN03145 137 REIEKVVSSaflqTDTAfAEACSLD-ASLASGTTALAALVVGRSLVVANAGDCRAVLCRR-GKAIEMSRDHKPMCSKERK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1520 RIRISGGYVNNGKLDGVVDVSRAVGFF--------DLLPhIHASPDISVVTLTKADEMLIVATHKLWEYMDVDTVCDIAR 1591
Cdd:PLN03145 215 RIEASGGYVYDGYLNGQLNVARALGDWhmegmkgsDGGP-LSAEPELMTTQLTEEDEFLIIGCDGIWDVFRSQNAVDFAR 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364701 1592 ---ENSTDPLRAAAELKDHAMAYGCTENITILCLALyeniQQQNRFTLNKNSLMTRRStFEDTTLRRLQ 1657
Cdd:PLN03145 294 rrlQEHNDPVMCSKELVDEALKRKSGDNLAVVVVCF----QSQPPPNLVAPRPRVQRS-ISAEGLRELQ 357
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
864-1070 |
5.67e-15 |
|
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: 75.98 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 864 KLVSLELQRNFIRKVPNsIMKLSNLTILNLQCNELESLPaGFVELKNLQLLDLSSNKFmhypEVI---NYCTNLLQIDLS 940
Cdd:cd21340 25 NLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRI----SVVeglENLTNLEELHIE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 941 YNKI---QSL---PQSTKYLVK-LAKMNLSHNKLNFIGDLSEMTDLRTLNLRYNRISSIKtnasnlqnlfltdnRISNFE 1013
Cdd:cd21340 99 NQRLppgEKLtfdPRSLAALSNsLRVLNISGNNIDSLEPLAPLRNLEQLDASNNQISDLE--------------ELLDLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398364701 1014 DTLPKLRALEIQENPITSIsfkdfyPKNMTSLTLNKAQLSSIPGELLTKLS--FLEKLE 1070
Cdd:cd21340 165 SSWPSLRELDLTGNPVCKK------PKYRDKIILASKSLEVLDGKEITDTErqFLKRLK 217
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
1666-1813 |
5.15e-14 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 70.85 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1666 NLAMVFTDIKSSTFLWELF-PNAMRTAIKTHNDIMRRQLRIYGGYEVKTEGDAFMVAFPT--PTSGLTWCLSVQLKLLDA 1742
Cdd:cd07556 1 PVTILFADIVGFTSLADALgPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLdhPAAAVAFAEDMREAVSAL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364701 1743 QWPEeitsvqdgcqvtdrngniiYQGLSVRMGIHWGCPVPELDLVTQRMDYLGPMVNKAARVQGVADGGQI 1813
Cdd:cd07556 81 NQSE-------------------GNPVRVRIGIHTGPVVVGVIGSRPQYDVWGALVNLASRMESQAKAGQV 132
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
961-1142 |
1.47e-12 |
|
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: 69.04 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 961 NLSHNKLNFIGDLSEMTDLRTLNLRYNRISSIK--TNASNLQNLFLTDNRISNFE--DTLPKLRALEIQENPITSIsfkd 1036
Cdd:cd21340 8 YLNDKNITKIDNLSLCKNLKVLYLYDNKITKIEnlEFLTNLTHLYLQNNQIEKIEnlENLVNLKKLYLGGNRISVV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1037 fypknmtsltlnkaqlssipgELLTKLSFLEKLEL-NQNN-----LTRLPQEISKLTK-LVFLSVARNKLEYIPPeLSQL 1109
Cdd:cd21340 84 ---------------------EGLENLTNLEELHIeNQRLppgekLTFDPRSLAALSNsLRVLNISGNNIDSLEP-LAPL 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 398364701 1110 KSLRTLDLHSNNIRDFVDgMENL-----ELTSLNISSN 1142
Cdd:cd21340 142 RNLEQLDASNNQISDLEE-LLDLlsswpSLRELDLTGN 178
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
855-1124 |
1.14e-11 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 70.19 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 855 FPSNITkayklvSLELQRNFIRKVPNSIMKLSNLTILNLQCNELESLPAGFVELKnlqlldLSSNKFMHYPEVInycTNL 934
Cdd:PRK15387 220 LPAHIT------TLVIPDNNLTSLPALPPELRTLEVSGNQLTSLPVLPPGLLELS------IFSNPLTHLPALP---SGL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 935 LQIDLSYNKIQSLPQSTKylvKLAKMNLSHNKLNFIGDL-SEMTDLRTLNlryNRISSIKTNASNLQNLFLTDNRISNFE 1013
Cdd:PRK15387 285 CKLWIFGNQLTSLPVLPP---GLQELSVSDNQLASLPALpSELCKLWAYN---NQLTSLPTLPSGLQELSVSDNQLASLP 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1014 DTLPKLRALEIQENPITSISFkdfYPKNMTSLTLNKAQLSSIPgellTKLSFLEKLELNQNNLTRLPQEISKLTKLvflS 1093
Cdd:PRK15387 359 TLPSELYKLWAYNNRLTSLPA---LPSGLKELIVSGNRLTSLP----VLPSELKELMVSGNRLTSLPMLPSGLLSL---S 428
|
250 260 270
....*....|....*....|....*....|.
gi 398364701 1094 VARNKLEYIPPELSQLKSLRTLDLHSNNIRD 1124
Cdd:PRK15387 429 VYRNQLTRLPESLIHLSSETTVNLEGNPLSE 459
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
1041-1253 |
1.92e-11 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 69.34 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1041 NMTSLTLNKAQLSSIPGELLTKLsflEKLELNQNNLTRLPQEISklTKLVFLSVARNKLEYIPPELSQlkSLRTLDLHSN 1120
Cdd:PRK15370 221 NIKTLYANSNQLTSIPATLPDTI---QEMELSINRITELPERLP--SALQSLDLFHNKISCLPENLPE--ELRYLSVYDN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1121 NIRDFVDGMENlELTSLNISSNAFgnsslensfyhnMSYGSKLSKSLMFFIAADNQFD---DAMWPlfncfvNLKVLNLS 1197
Cdd:PRK15370 294 SIRTLPAHLPS-GITHLNVQSNSL------------TALPETLPPGLKTLEAGENALTslpASLPP------ELQVLDVS 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 398364701 1198 YNNFSDVSHMKLESITELYLSGNKLTTLSGDTVlkwSSLKTLMLNSNQMLSLPAEL 1253
Cdd:PRK15370 355 KNQITVLPETLPPTITTLDVSRNALTNLPENLP---AALQIMQASRNNLVRLPESL 407
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1040-1226 |
2.36e-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: 65.58 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1040 KNMTSLTLNKAQLSSIPgelltKLSFLEKLE---LNQNNLTRLPQeISKLTKLVFLSVARNKLEYIPPeLSQLKSLRTLD 1116
Cdd:cd21340 2 KRITHLYLNDKNITKID-----NLSLCKNLKvlyLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1117 LHSNNIRdFVDGMENLE-LTSLNISSNafgNSSLENSF---YHNMSYgskLSKSLMFFIAADNQFDDaMWPLfNCFVNLK 1192
Cdd:cd21340 75 LGGNRIS-VVEGLENLTnLEELHIENQ---RLPPGEKLtfdPRSLAA---LSNSLRVLNISGNNIDS-LEPL-APLRNLE 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 398364701 1193 VLNLSYNNFSDVSHM-----KLESITELYLSGNKLTTLS 1226
Cdd:cd21340 146 QLDASNNQISDLEELldllsSWPSLRELDLTGNPVCKKP 184
|
|
| Ad_cyc_g-alpha |
pfam08509 |
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and ... |
368-418 |
7.82e-11 |
|
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and interacts with the alpha subunit of heterotrimeric G proteins.
Pssm-ID: 430040 Cd Length: 48 Bit Score: 58.85 E-value: 7.82e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 398364701 368 EATTPTIETPiscKPSLFRLDTNLEDVTDITKTVPPTAVNSTLNSTHGTET 418
Cdd:pfam08509 1 EAIGPTDRTD---GGTVFHLDTNLNDMEGILSKPPPLTPMDTDFSINGVEF 48
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
886-1168 |
1.43e-10 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 66.64 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 886 SNLTILNLQCNELESLPAGFVElkNLQLLDLSSNKFMHYPEviNYCTNLLQIDLSYNKIQSLPQSTKYLVKLakMNLSHN 965
Cdd:PRK15370 178 NNKTELRLKILGLTTIPACIPE--QITTLILDNNELKSLPE--NLQGNIKTLYANSNQLTSIPATLPDTIQE--MELSIN 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 966 KlnfIGDLSEMTdlrtlnlrynrissiktnASNLQNLFLTDNRISNFEDTLPK-LRALEIQENPITSISfkDFYPKNMTS 1044
Cdd:PRK15370 252 R---ITELPERL------------------PSALQSLDLFHNKISCLPENLPEeLRYLSVYDNSIRTLP--AHLPSGITH 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1045 LTLNKAQLSSIPGELLTKlsfLEKLELNQNNLTRLPQEISKltKLVFLSVARNKLEYIPPELSqlKSLRTLDLHSNNIRD 1124
Cdd:PRK15370 309 LNVQSNSLTALPETLPPG---LKTLEAGENALTSLPASLPP--ELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTN 381
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 398364701 1125 FVdgmENLElTSLNISSNAFGN-SSLENSFYHNMSYGSKLSKSLM 1168
Cdd:PRK15370 382 LP---ENLP-AALQIMQASRNNlVRLPESLPHFRGEGPQPTRIIV 422
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
997-1269 |
4.77e-08 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 58.25 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 997 SNLQNLFLTDNRISNFEDTLPKLRALEIQENPITSISfkdFYPKNMTSLTLNKAQLSSIPGelltKLSFLEKLELNQNNL 1076
Cdd:PRK15387 222 AHITTLVIPDNNLTSLPALPPELRTLEVSGNQLTSLP---VLPPGLLELSIFSNPLTHLPA----LPSGLCKLWIFGNQL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1077 TRLPQEISKLTKlvfLSVARNKLEYIPPELSQLKSLRTLDLHSNNIRDFVDGMENLELTSLNISSnafgNSSLENSFYHN 1156
Cdd:PRK15387 295 TSLPVLPPGLQE---LSVSDNQLASLPALPSELCKLWAYNNQLTSLPTLPSGLQELSVSDNQLAS----LPTLPSELYKL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1157 MSYGSKLSkSLMFFIAAdnqfddamwplfncfvnLKVLNLSYNNFSDVSHMKLEsITELYLSGNKLTTLSgdtvLKWSSL 1236
Cdd:PRK15387 368 WAYNNRLT-SLPALPSG-----------------LKELIVSGNRLTSLPVLPSE-LKELMVSGNRLTSLP----MLPSGL 424
|
250 260 270
....*....|....*....|....*....|...
gi 398364701 1237 KTLMLNSNQMLSLPAELSNLSQLSVFDVGANQL 1269
Cdd:PRK15387 425 LSLSVYRNQLTRLPESLIHLSSETTVNLEGNPL 457
|
|
| Ad_cyc_g-alpha |
smart00789 |
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and ... |
367-420 |
1.91e-07 |
|
Adenylate cyclase G-alpha binding domain; This fungal domain is found in adenylate cyclase and interacts with the alpha subunit of heterotrimeric G proteins.
Pssm-ID: 129025 Cd Length: 51 Bit Score: 49.29 E-value: 1.91e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 398364701 367 REATTPTIETPisckPSLFRLDTNLEDVTDI-TKTVPPTAVNSTLNSTHGTETAS 420
Cdd:smart00789 1 DEAIGPTDREG----GSVFHLDTNLNDMEGIlTKPPPLTPMDGSFINTGESEKHN 51
|
|
| RA |
smart00314 |
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ... |
676-755 |
4.73e-07 |
|
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)
Pssm-ID: 214612 Cd Length: 90 Bit Score: 49.60 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 676 RHYAIRIFNTD---DTFTTLSCTPATTVEEIIPALKRKFNITAQGN-FQISLKV--GKLSKILRPTSKPILIER----KL 745
Cdd:smart00314 1 DTFVLRVYVDDlpgGTYKTLRVSSRTTARDVIQQLLEKFHLTDDPEeYVLVEVLpdGKERVLPDDENPLQLQKLwprrGP 80
|
90
....*....|
gi 398364701 746 LLLNGYRKSD 755
Cdd:smart00314 81 NLRFVLRKRD 90
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
864-921 |
5.50e-07 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 48.29 E-value: 5.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 864 KLVSLELQRNFIRKV-PNSIMKLSNLTILNLQCNELESL-PAGFVELKNLQLLDLSSNKF 921
Cdd:pfam13855 2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
884-1145 |
1.57e-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: 52.36 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 884 KLSNLTILNLQCNELESLPAGFVElKNLQlldlssnkfmHYPEV--INYCTNLLQIDLSYnkIQSLPQSTKYLVKLAKMN 961
Cdd:cd00116 21 KLLCLQVLRLEGNTLGEEAAKALA-SALR----------PQPSLkeLCLSLNETGRIPRG--LQSLLQGLTKGCGLQELD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 962 LSHNKLNFIG-----DLSEMTDLRTLNLRYNRIS---------SIKTNASNLQNLFLTDNRISN--FEDT------LPKL 1019
Cdd:cd00116 88 LSDNALGPDGcgvleSLLRSSSLQELKLNNNGLGdrglrllakGLKDLPPALEKLVLGRNRLEGasCEALakalraNRDL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1020 RALEIQENPITS-------ISFKDFypKNMTSLTLNKAQL----SSIPGELLTKLSFLEKLELNQNNLTRLPqeISKLTK 1088
Cdd:cd00116 168 KELNLANNGIGDagiralaEGLKAN--CNLEVLDLNNNGLtdegASALAETLASLKSLEVLNLGDNNLTDAG--AAALAS 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364701 1089 LVflsvarnkleyippeLSQLKSLRTLDLHSNNI-----RDFVDGM-ENLELTSLNISSNAFG 1145
Cdd:cd00116 244 AL---------------LSPNISLLTLSLSCNDItddgaKDLAEVLaEKESLLELDLRGNKFG 291
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
937-989 |
1.60e-06 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 47.13 E-value: 1.60e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 398364701 937 IDLSYNKIQSLPQST-KYLVKLAKMNLSHNKLNFI--GDLSEMTDLRTLNLRYNRI 989
Cdd:pfam13855 6 LDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLspGAFSGLPSLRYLDLSGNRL 61
|
|
| PLN03210 |
PLN03210 |
Resistant to P. syringae 6; Provisional |
864-1138 |
2.58e-06 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 52.95 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 864 KLVSLELQRNFIRKVPnSIMKLSNLTILNLQCNELESLPAGFVELKNLQLLDLSSNKFMHYPEVINYCTNLLQIDLS-YN 942
Cdd:PLN03210 590 KLRLLRWDKYPLRCMP-SNFRPENLVKLQMQGSKLEKLWDGVHSLTGLRNIDLRGSKNLKEIPDLSMATNLETLKLSdCS 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 943 KIQSLPQSTKYLVKLAKMNLSH-NKLNFIGDLSEMTDLRTLNLR-YNRISSIKTNASNLQNLFLTDNRISNFEDTLP--- 1017
Cdd:PLN03210 669 SLVELPSSIQYLNKLEDLDMSRcENLEILPTGINLKSLYRLNLSgCSRLKSFPDISTNISWLDLDETAIEEFPSNLRlen 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1018 ---------KLRALEIQENPITSIsfkdfypKNMTSLTLNKAQLSSIPgelltklsfleklelnqnNLTRLPQEISKLTK 1088
Cdd:PLN03210 749 ldelilcemKSEKLWERVQPLTPL-------MTMLSPSLTRLFLSDIP------------------SLVELPSSIQNLHK 803
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 398364701 1089 LVFLSVARNK-LEYIPPELSqLKSLRTLDL-HSNNIRDFVDGMENLELTSLN 1138
Cdd:PLN03210 804 LEHLEIENCInLETLPTGIN-LESLESLDLsGCSRLRTFPDISTNISDLNLS 854
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1066-1122 |
3.54e-06 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 45.98 E-value: 3.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 398364701 1066 LEKLELNQNNLTRLPQEI-SKLTKLVFLSVARNKLEYIPPE-LSQLKSLRTLDLHSNNI 1122
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
|
|
| PLN03210 |
PLN03210 |
Resistant to P. syringae 6; Provisional |
842-1116 |
5.51e-06 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 51.80 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 842 LLSLRMVNIRASK----FPsNITKAYKLVSLELQR-NFIRKVPNSIMKLSNLTILNLQ-CNELESLPAGfVELKNLQLLD 915
Cdd:PLN03210 633 LTGLRNIDLRGSKnlkeIP-DLSMATNLETLKLSDcSSLVELPSSIQYLNKLEDLDMSrCENLEILPTG-INLKSLYRLN 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 916 LSS-NKFMHYPEVinyCTNLLQIDLSYNKIQSLPqSTKYLVKLAKMNLSHNKlnfIGDLSEMTDLRTLNLRYNRISSIKT 994
Cdd:PLN03210 711 LSGcSRLKSFPDI---STNISWLDLDETAIEEFP-SNLRLENLDELILCEMK---SEKLWERVQPLTPLMTMLSPSLTRL 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 995 NASNLQNLFLTDNRISNFEdtlpKLRALEIQ-----ENPITSISFKDFYPKNMTSLTlnkaQLSSIPgELLTKLSfleKL 1069
Cdd:PLN03210 784 FLSDIPSLVELPSSIQNLH----KLEHLEIEncinlETLPTGINLESLESLDLSGCS----RLRTFP-DISTNIS---DL 851
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 398364701 1070 ELNQNNLTRLPQEISKLTKLVFLSVAR-NKLEYIPPELSQLKSLRTLD 1116
Cdd:PLN03210 852 NLSRTGIEEVPWWIEKFSNLSFLDMNGcNNLQRVSLNISKLKHLETVD 899
|
|
| PTZ00224 |
PTZ00224 |
protein phosphatase 2C; Provisional |
1487-1620 |
5.72e-06 |
|
protein phosphatase 2C; Provisional
Pssm-ID: 240318 [Multi-domain] Cd Length: 381 Bit Score: 50.93 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1487 ANLGDCMAILSKNnGDYQTLTKQHLPTKREEYERIRISGGYVNNGKLDGVVDVSRAVGFFD---------LLPHIHASPD 1557
Cdd:PTZ00224 122 GNVGDSRVLVCRD-GKLVFATEDHKPNNPGERQRIEACGGRVVSNRVDGDLAVSRAFGDRSfkvkgtgdyLEQKVIAVPD 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364701 1558 ISVVTLTKADeMLIVATHKLWE-YMDVDTVCDIARE---NSTDPLRAAAELKDHAMAYGCTENITIL 1620
Cdd:PTZ00224 201 VTHLTCQSND-FIILACDGVFEgNFSNEEVVAFVKEqleTCDDLAVVAGRVCDEAIRRGSKDNISCL 266
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
855-919 |
5.96e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 48.27 E-value: 5.96e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364701 855 FPSNITKAYKLVSLELQRNFIR-KVPNSIMKLSNLTILNLQCNELE-SLPAGFVELKNLQLLDLSSN 919
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGN 500
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1190-1246 |
6.86e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 42.51 E-value: 6.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1190 NLKVLNLSYNNFSDVSH---MKLESITELYLSGNKLTTLSGDTVLKWSSLKTLMLNSNQM 1246
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDgafKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1211-1269 |
6.86e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 42.51 E-value: 6.86e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1211 SITELYLSGNKLTTLSGDTVLKWSSLKTLMLNSNQMLSL-PAELSNLSQLSVFDVGANQL 1269
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
886-967 |
7.43e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 42.51 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 886 SNLTILNLQCNELESLPAG-FVELKNLQLLDLSsnkfmhypevinyctnllqidlsYNKIQSL-PQSTKYLVKLAKMNLS 963
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLS-----------------------NNLLTTLsPGAFSGLPSLRYLDLS 57
|
....
gi 398364701 964 HNKL 967
Cdd:pfam13855 58 GNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
956-1009 |
1.23e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.74 E-value: 1.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 956 KLAKMNLSHNKLNFIGD--LSEMTDLRTLNLRYNRISSIKTNA----SNLQNLFLTDNRI 1009
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSPGAfsglPSLRYLDLSGNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1041-1099 |
1.66e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.36 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1041 NMTSLTLNKAQLSSIPGELLTKLSFLEKLELNQNNLTRL-PQEISKLTKLVFLSVARNKL 1099
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
803-1087 |
1.90e-04 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 46.69 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 803 DLTTPPIIfyqhTSEIESLDVSNNANIFLPLefieSSIKLLSLRMVNIRASKFPSNITKAYKLVSLELQRNFIRKVPNSI 882
Cdd:PRK15387 233 NLTSLPAL----PPELRTLEVSGNQLTSLPV----LPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 883 MKLSnltilnLQCNELESLPAGFVELKNLQLLDlssNKFMHYPEVInycTNLLQIDLSYNKIQSLPQSTKYLVKLAKMNl 962
Cdd:PRK15387 305 QELS------VSDNQLASLPALPSELCKLWAYN---NQLTSLPTLP---SGLQELSVSDNQLASLPTLPSELYKLWAYN- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 963 shNKLNFIGDLSemTDLRTLNLRYNRISSIKTNASNLQNLFLTDNRISnfedTLPKLraleiqenpitsisfkdfyPKNM 1042
Cdd:PRK15387 372 --NRLTSLPALP--SGLKELIVSGNRLTSLPVLPSELKELMVSGNRLT----SLPML-------------------PSGL 424
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 398364701 1043 TSLTLNKAQLSSIPgELLTKLSFLEKLELNQNNLT-RLPQEISKLT 1087
Cdd:PRK15387 425 LSLSVYRNQLTRLP-ESLIHLSSETTVNLEGNPLSeRTLQALREIT 469
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1066-1269 |
3.30e-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: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1066 LEKLELNQNNLTRLPQEISKLTKLVFLSVARNK-----LEYIPPELSQLKSLRTLDLHSNNIRDfvDGMENL-------- 1132
Cdd:COG5238 187 LGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPigdegAEILAEALKGNKSLTTLDLSNNQIGD--EGVIALaealknnt 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 1133 ELTSLNISSNAFGNSSLEnsfyhnmsygsKLSKSLmffiaADNQfddamwplfncfvNLKVLNLSYNNFSDVSHMKL--- 1209
Cdd:COG5238 265 TVETLYLSGNQIGAEGAI-----------ALAKAL-----QGNT-------------TLTSLDLSVNRIGDEGAIALaeg 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364701 1210 ----ESITELYLSGNKLTT----LSGDTVLKWSSLKTLMLNSNQ-----MLSLPAELSNLSQLSVFDVGANQL 1269
Cdd:COG5238 316 lqgnKTLHTLNLAYNGIGAqgaiALAKALQENTTLHSLDLSDNQigdegAIALAKYLEGNTTLRELNLGKNNI 388
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
188-366 |
3.47e-03 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 42.59 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 188 SGKESKVANLSLSTVNPApANRKPSKDSTLSNhladNVPSTLRRKVSSLVRGSsvhDINNGIADKQIRPkavAQSENTLH 267
Cdd:NF033609 33 SSKEADASENSVTQSDSA-SNESKSNDSSSVS----AAPKTDDTNVSDTKTSS---NTNNGETSVAQNP---AQQETTQS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364701 268 SSDVPNSKRSHRKSFLLGSTSSSSSRRGSNVSSMTNSDSASMATSgSHVLQHNVSNVSPTTKSKDSVNSESADHTNNKSE 347
Cdd:NF033609 102 ASTNATTEETPVTGEATTTATNQANTPATTQSSNTNAEELVNQTS-NETTSNDTNTVSSVNSPQNSTNAENVSTTQDTST 180
|
170
....*....|....*....
gi 398364701 348 KVTPEYNENIPENSNSDNK 366
Cdd:NF033609 181 EATPSNNESAPQSTDASNK 199
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
1087-1131 |
6.14e-03 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 36.45 E-value: 6.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398364701 1087 TKLVFLSVARNKLEYIPPeLSQLKSLRTLDLHSNNIRDFVDGMEN 1131
Cdd:pfam12799 1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKITDLSDLAN 44
|
|
| |
