|
Name |
Accession |
Description |
Interval |
E-value |
| PH_PHLPP-like |
cd13322 |
PH domain leucine-rich repeat protein phosphatase family Pleckstrin homology-like domain; The ... |
491-587 |
2.80e-60 |
|
PH domain leucine-rich repeat protein phosphatase family Pleckstrin homology-like domain; The PHLPP family has members PHLPP1 (also called hSCOP/Suprachiasmatic nucleus circadian oscillatory protein; PLEKHE1/Pleckstrin homology domain-containing family E member 1) and PHLPP2 (PHLPP-like/PHLPPL). The PHLPP family of novel Ser/Thr phosphatases serve as important regulators of cell survival and apoptosis. PHLPP isozymes catalyze the dephosphorylation of a conserved regulatory motif, the hydrophobic motif, on the AGC kinases Akt, PKC, and S6 kinase, as well as an inhibitory site on the kinase Mst1, to inhibit cellular proliferation and induce apoptosis and negatively regulates ERK1/2 activation. Reductions in their expression have been detected in several cancers and linked to cancer progression. PHLPP1 and PHLPP2 both contain an N-terminal PH domain, followed by 21 LRR (leucine-rich) repeats, and a C-terminal PP2C-like domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270131 Cd Length: 95 Bit Score: 201.29 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 491 ERIQLSGMYNVRKGKMQLpvNRWTRRQVILCGTCLIVSSVKDSVSGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTY 570
Cdd:cd13322 1 ERILLSGIYNVRKGKTQL--HKWAERQVILCGTCLIVSSVKDSQTGKMHILPLVGGKVEEVKRRQHCLAFSSAGPQAQTY 78
|
90
....*....|....*..
gi 257467468 571 YICFDTFTEYLRWLRQV 587
Cdd:cd13322 79 YVSFDTLAEYQRWHRQA 95
|
|
| PP2Cc |
smart00332 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1124-1376 |
3.07e-59 |
|
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: 204.53 E-value: 3.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1124 SGAPAVWSHGYTEASGVKNKLCVAALSVNNFRDNrEALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE----EEYM 1199
Cdd:smart00332 3 SGKNLGLRYGLSSMQGVRKPMEDAHVITPDLSDS-GGFFGVFDGHGGSEAAKFLSKNLPEILAEELIKEKDEledvEEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1200 VNTFIVMQRKLGTAGQKLGGA-AVLCHIKPDpvdlggsfTLTSANVGKCQTVLCRNGKPLSLSRSYIMSCEEERKRIKQH 1278
Cdd:smart00332 82 RKAFLSTDEEILEELEALSGStAVVALISGN--------KLYVANVGDSRAVLCRNGKAVQLTEDHKPSNEDERARIEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1279 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNVP--DALAAAK 1356
Cdd:smart00332 154 GGFV-INGRVNGVLALSRAIGDFFLKPYVSAEPDVTVVELTEKDDFLILASDGLWDVLSNQEVVDIVRKHLskDPKEAAK 232
|
250 260
....*....|....*....|
gi 257467468 1357 KLCTLAQSYGCHDSISAVVV 1376
Cdd:smart00332 233 RLIDLALARGSKDNITVVVV 252
|
|
| PP2Cc |
cd00143 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1130-1378 |
4.33e-56 |
|
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: 195.62 E-value: 4.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1130 WSHGYTEASGVKNKLCVAALSVNNFRDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE-----EEYMVNTFI 1204
Cdd:cd00143 1 FSAGVSDKGGDRKTNEDAVVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLseediEEALRKAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1205 VMQRKLGTAGQKL------GGAAVLCHIKPDpvdlggsfTLTSANVGKCQTVLCRNGKPLSLSRSYIMSCEEERKRIKQH 1278
Cdd:cd00143 81 RADEEILEEAQDEpddarsGTTAVVALIRGN--------KLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEEERERIEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1279 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNVP---DALAAA 1355
Cdd:cd00143 153 GGRV-SNGRVPGVLAVTRALGDFDLKPGVSAEPDVTVVKLTEDDDFLILASDGLWDVLSNQEAVDIVRSELakeDLQEAA 231
|
250 260
....*....|....*....|...
gi 257467468 1356 KKLCTLAQSYGCHDSISAVVVQL 1378
Cdd:cd00143 232 QELVDLALRRGSHDNITVVVVRL 254
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
427-484 |
2.69e-33 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase 1 (PHLPP1); PHLPP1, also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP), 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. PHLPP1 also plays critical roles in many cancers, such as gastric cancer, sacral chordoma, gallbladder cancer, hypopharyngeal squamous cell carcinomas, and non-small cell lung cancer. It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role in learning and memory. PHLPP1 contains a Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain.
Pssm-ID: 340760 Cd Length: 90 Bit Score: 124.17 E-value: 2.69e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 257467468 427 LYVQLHGETTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 484
Cdd:cd17240 33 LQLQLHGETVRRLEPHEKPLQIQNDYLFQLGFGDLWRVQEEGMDPEIGCLIRFYAGKP 90
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
593-854 |
2.95e-32 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 131.59 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 593 QRISSVDLSCCSlehlpaNLFYSQDLTHLNLKQNFLRQTPTlpaarglgELQRFTKLKSLNLSNNHLGAFPSAVCSIPTL 672
Cdd:COG4886 96 TNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPE--------ELANLTNLKELDLSNNQLTDLPEPLGNLTNL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 673 AELNVSCNALREVPAAVGDMQNLQTFLLDGNFLQSLPAELESMHQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMAGNCVE 752
Cdd:COG4886 162 KSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 753 TLRlqALRRMPHIKHVDLRLNILRKLmaDEVDFVQHVTQLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTLNVCGYFLKA 832
Cdd:COG4886 242 DLP--ELGNLTNLEELDLSNNQLTDL--PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
|
250 260
....*....|....*....|..
gi 257467468 833 LYASSNELAQLDVYPVPNYLSY 854
Cdd:COG4886 318 LLLTTLLLLLLLLKGLLVTLTT 339
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
907-1110 |
5.94e-32 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 130.82 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 907 RLARLPERLERTSVEVLDVQHNQITELPPNLLmKADSLRFLNASANKLETLPPAtLSEETSsiLQELYLTNNCLTDkcVP 986
Cdd:COG4886 102 DLSGNEELSNLTNLESLDLSGNQLTDLPEELA-NLTNLKELDLSNNQLTDLPEP-LGNLTN--LKSLDLSNNQLTD--LP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 987 L-LTGHPRLKILHMAYNRLQSFPASkMAKLEELEEIDISGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVMQLPEVKC 1065
Cdd:COG4886 176 EeLGNLTNLKELDLSNNQITDLPEP-LGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEE 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 257467468 1066 VDLSCNELSEITLPENLpPKLQELDLTGNPRLALDHKSLELLNNI 1110
Cdd:COG4886 255 LDLSNNQLTDLPPLANL-TNLKTLDLSNNQLTDLKLKELELLLGL 298
|
|
| PP2C |
pfam00481 |
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ... |
1130-1371 |
9.77e-30 |
|
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.
Pssm-ID: 395385 Cd Length: 252 Bit Score: 119.75 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1130 WSHGYTEASGVKNKLCVAALSVNNFR----DNREALYGVFDGDRNVEVPYLLQCTMSDILAE--ELQKTKNEEEYMVNTF 1203
Cdd:pfam00481 1 IDLGGPRMQGWRKSMEDAHIDLPNLNsssgKDSWSFFAVFDGHGGSEAAKYCGKHLHTILALrrSFLEGEKLEDALRKSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1204 I----VMQRKLGTAGQKLGGAAVLCHIKPDpvdlggsfTLTSANVGKCQTVLCRNGKP-LSLSRSYIMSCEEERKRIKQH 1278
Cdd:pfam00481 81 LedtdEVLRSAEKEDLDSGCTAVVALISGN--------KLYVANVGDSRAVLCRNGNAiKRLTKDHKPSDEDERRRIRAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1279 KAIITEDGKVNGVTESTRILGYTFLHPS---VVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNV----PDA 1351
Cdd:pfam00481 153 GGFVSRNGRVNGVLAVSRAFGDFELKPGeqaVSAEPDITSHTITEDDEFLILACDGLWDVLSDQEVVDLVRSElsdgGSP 232
|
250 260
....*....|....*....|
gi 257467468 1352 LAAAKKLCTLAQSYGCHDSI 1371
Cdd:pfam00481 233 MEAAEELRDEAIAYGSEDNI 252
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
595-1082 |
3.07e-24 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 111.09 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 595 ISSVDLSCCSLE-HLPANLFY-SQDLTHLNLKQNFLrqtpTLPAARGLGELqrftkLKSLNLSNNHL-GAFPSAVCSIPT 671
Cdd:PLN00113 95 IQTINLSNNQLSgPIPDDIFTtSSSLRYLNLSNNNF----TGSIPRGSIPN-----LETLDLSNNMLsGEIPNDIGSFSS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 672 LAELNVSCNALR-EVPAAVGDMQNLQTFLLDGN-FLQSLPAELESMHQLSYLGLSFNEFT-DIPEVLEKLTAVDKLCMAG 748
Cdd:PLN00113 166 LKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNqLVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 749 NCVETLRLQALRRMPHIKHVDLRLNILRKLMADEVDFVQHVTQLDLRDNKL-GDLDAMI--FNNIEVLHcernqLVTLNV 825
Cdd:PLN00113 246 NNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLsGEIPELViqLQNLEILH-----LFSNNF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 826 CGYFLKALyASSNELAQLDVYpvpnylsymdvSRNCLESVPEWVCESRKLEVLDIGHNQIC-ELPARLfCNS-SLRKLLA 903
Cdd:PLN00113 321 TGKIPVAL-TSLPRLQVLQLW-----------SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEIPEGL-CSSgNLFKLIL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 904 GHNRL-ARLPERLER-TSVEVLDVQHNQITELPPNLLMKADSLRFLNASANKLETLPPATLSEETSsiLQELYLTNNCLT 981
Cdd:PLN00113 388 FSNSLeGEIPKSLGAcRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPS--LQMLSLARNKFF 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 982 DKcVPLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKLKA-IPTTIMNCRRMHTV-IAHSNCIEVFPEVM- 1058
Cdd:PLN00113 466 GG-LPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLdLSHNQLSGQIPASFs 544
|
490 500
....*....|....*....|....*
gi 257467468 1059 QLPEVKCVDLSCNELS-EItlPENL 1082
Cdd:PLN00113 545 EMPVLSQLDLSQNQLSgEI--PKNL 567
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
848-1094 |
2.90e-19 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 94.38 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 848 VPNYLSYMDVSRNCLESVPEWVceSRKLEVLDIGHNQICELPARLfcNSSLRKLLAGHNRLARLPERLErTSVEVLDVQH 927
Cdd:PRK15370 197 IPEQITTLILDNNELKSLPENL--QGNIKTLYANSNQLTSIPATL--PDTIQEMELSINRITELPERLP-SALQSLDLFH 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 928 NQITELPPNLlmkADSLRFLNASANKLETLPpatlsEETSSILQELYLTNNCLTdkCVPLlTGHPRLKILHMAYNRLQSF 1007
Cdd:PRK15370 272 NKISCLPENL---PEELRYLSVYDNSIRTLP-----AHLPSGITHLNVQSNSLT--ALPE-TLPPGLKTLEAGENALTSL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1008 PASKMAkleELEEIDISGNKLKAIPTTImncrrmhtviahsncievfPevmqlPEVKCVDLSCNELseITLPENLPPKLQ 1087
Cdd:PRK15370 341 PASLPP---ELQVLDVSKNQITVLPETL-------------------P-----PTITTLDVSRNAL--TNLPENLPAALQ 391
|
....*..
gi 257467468 1088 ELDLTGN 1094
Cdd:PRK15370 392 IMQASRN 398
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
177-219 |
1.88e-14 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase 1 (PHLPP1); PHLPP1, also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP), 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. PHLPP1 also plays critical roles in many cancers, such as gastric cancer, sacral chordoma, gallbladder cancer, hypopharyngeal squamous cell carcinomas, and non-small cell lung cancer. It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role in learning and memory. PHLPP1 contains a Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain.
Pssm-ID: 340760 Cd Length: 90 Bit Score: 70.24 E-value: 1.88e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 257467468 177 GCVHVFDRHMaSSYLRPVLCTLDTTAAEVAARLLQLGHKGGGV 219
Cdd:cd17240 1 GCIHVYDRHM-SSYLRPVLCTLDTTASEVAARLLQLQLHGETV 42
|
|
| PLN03145 |
PLN03145 |
Protein phosphatase 2c; Provisional |
1151-1376 |
6.24e-14 |
|
Protein phosphatase 2c; Provisional
Pssm-ID: 215603 [Multi-domain] Cd Length: 365 Bit Score: 75.34 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1151 VNNFRDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNEEEYMVNTFIVMQRKLGTA----GQKLGGAAVLCHI 1226
Cdd:PLN03145 95 LKNSEDGPSAFYGVFDGHGGKHAADFACYHLPRFIVEDEDFPREIEKVVSSAFLQTDTAFAEAcsldASLASGTTALAAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1227 KpdpvdLGGSftLTSANVGKCQTVLCRNGKPLSLSRSYIMSCEEERKRIKQHKAIItEDGKVNGVTESTRILGYTFLH-- 1304
Cdd:PLN03145 175 V-----VGRS--LVVANAGDCRAVLCRRGKAIEMSRDHKPMCSKERKRIEASGGYV-YDGYLNGQLNVARALGDWHMEgm 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1305 -----PSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNV----PDALAAAKKLCTLAQSYGCHDSISAVV 1375
Cdd:PLN03145 247 kgsdgGPLSAEPELMTTQLTEEDEFLIIGCDGIWDVFRSQNAVDFARRRlqehNDPVMCSKELVDEALKRKSGDNLAVVV 326
|
.
gi 257467468 1376 V 1376
Cdd:PLN03145 327 V 327
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
581-885 |
6.55e-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: 68.54 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 581 LRWLRQVSKVasQRISSVDLSCCSL--EHLPA---NLFYSQDLTHLNLKQNFLRQTPTLPAARGLGeLQRFTKLKSLNLS 655
Cdd:cd00116 13 ERATELLPKL--LCLQVLRLEGNTLgeEAAKAlasALRPQPSLKELCLSLNETGRIPRGLQSLLQG-LTKGCGLQELDLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 656 NNHLG----AFPSAVCSIPTLAELNVSCNALREVPAAvgdmqnlqtFLLDGnfLQSLPAELESMhQLSYLGLSFNEFTDI 731
Cdd:cd00116 90 DNALGpdgcGVLESLLRSSSLQELKLNNNGLGDRGLR---------LLAKG--LKDLPPALEKL-VLGRNRLEGASCEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 732 PEVLEKLTAVDKLCMAGNCV-----ETLrLQALRRMPHIKHVDLRLNILR----KLMADEVDFVQHVTQLDLRDNKLGDL 802
Cdd:cd00116 158 AKALRANRDLKELNLANNGIgdagiRAL-AEGLKANCNLEVLDLNNNGLTdegaSALAETLASLKSLEVLNLGDNNLTDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 803 DAMIFNnievlhcerNQLVTLNVCgyfLKALYASSNELAQLDVYPVPNYLS------YMDVSRNCL------ESVPEWVC 870
Cdd:cd00116 237 GAAALA---------SALLSPNIS---LLTLSLSCNDITDDGAKDLAEVLAekesllELDLRGNKFgeegaqLLAESLLE 304
|
330
....*....|....*
gi 257467468 871 ESRKLEVLDIGHNQI 885
Cdd:cd00116 305 PGNELESLWVKDDSF 319
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
245-427 |
1.45e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.42 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 245 GRDVEPPPSSGTVgavrgpARAPPADLPLPGGAWTRCAPRISPAPSDSSPGELFAGGPgsPPRAPRPASDtesfSLSPSA 324
Cdd:PHA03247 2728 ARQASPALPAAPA------PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVA----SLSESR 2795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 325 ESVSDRLDPYSSGGG-GSSSSSEELEADPAMPHRPGRPAQPRPPsPKTSALLQPKAPTGvdstGVIAGEGPGDDKAMAAA 403
Cdd:PHA03247 2796 ESLPSPWDPADPPAAvLAPAAALPPAASPAGPLPPPTSAQPTAP-PPPPGPPPPSLPLG----GSVAPGGDVRRRPPSRS 2870
|
170 180
....*....|....*....|....
gi 257467468 404 APDVPlSTSGRIRetVQKTSPPSL 427
Cdd:PHA03247 2871 PAAKP-AAPARPP--VRRLARPAV 2891
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
906-1109 |
9.61e-09 |
|
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: 57.49 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 906 NRLARLpERLER-TSVEVLDVQHNQITELPPnllmkadslrflnasankLETLPPatlseetssiLQELYLTNNCLTdkC 984
Cdd:cd21340 34 NKITKI-ENLEFlTNLTHLYLQNNQIEKIEN------------------LENLVN----------LKKLYLGGNRIS--V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 985 VPLLTGHPRLKILHMAYNRLQS-----F-PASKMAKLEELEEIDISGNKLKAIpTTIMNCRRMHTVIAHSNCIEVFPEVm 1058
Cdd:cd21340 83 VEGLENLTNLEELHIENQRLPPgekltFdPRSLAALSNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEEL- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 1059 qlpevkCVDLSCNelseitlpenlpPKLQELDLTGNPrLALDHK----------SLELLNN 1109
Cdd:cd21340 161 ------LDLLSSW------------PSLRELDLTGNP-VCKKPKyrdkiilaskSLEVLDG 202
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
746-1066 |
5.20e-06 |
|
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: 50.94 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 746 MAGNCVETLRLQALR-RMPHIKHVDLRLNILRKLMADEVDFVQHVTQLDLR-------DNKLGDLDAMIF--NNIEVLHC 815
Cdd:COG5238 70 DPGLNPVALEKAAEAfPTQLLVVDWEGAEEVSPVALAETATAVATPPPDLRrimaktlEDSLILYLALPRriNLIQVLKD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 816 E---RNQLVTLNVCGyfLKALYASSNELAQLDVYPVPNYLSYMDVSRNCLESVPEWVCESRKLEVLDIGHNQICELPARL 892
Cdd:COG5238 150 PlggNAVHLLGLAAR--LGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 893 FC-----NSSLRKLLAGHNR-----LARLPERLER-TSVEVLDVQHNQITE----LPPNLLMKADSLRFLNASANKLETL 957
Cdd:COG5238 228 LAealkgNKSLTTLDLSNNQigdegVIALAEALKNnTTVETLYLSGNQIGAegaiALAKALQGNTTLTSLDLSVNRIGDE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 958 PPATLSE--ETSSILQELYLTNNCLTDKCVPLLT----GHPRLKILHMAYNRLQSFPASKMAKLEE----LEEIDISGNK 1027
Cdd:COG5238 308 GAIALAEglQGNKTLHTLNLAYNGIGAQGAIALAkalqENTTLHSLDLSDNQIGDEGAIALAKYLEgnttLRELNLGKNN 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 257467468 1028 L---------KAIPTTimncrRMHTVIAHSNCIEVFPE---VMQLPEVKCV 1066
Cdd:COG5238 388 IgkqgaealiDALQTN-----RLHTLILDGNLIGAEAQqrlEQLLERIKSV 433
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
593-659 |
8.41e-06 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 44.82 E-value: 8.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257467468 593 QRISSVDLSCCSLEHLPANLFYS-QDLTHLNLKQNFLRqtpTLPAarglGELQRFTKLKSLNLSNNHL 659
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKGlSNLKVLDLSNNLLT---TLSP----GAFSGLPSLRYLDLSGNRL 61
|
|
| PTC1 |
COG0631 |
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms]; |
1309-1383 |
1.42e-05 |
|
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
Pssm-ID: 440396 [Multi-domain] Cd Length: 247 Bit Score: 48.28 E-value: 1.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 1309 PRPHVQSVLLTPQDeFFILGSKGLWDSLSIDEAVEAVRNVPDALAAAKKLCTLAQSYGCHDSISAVVVQLSVTED 1383
Cdd:COG0631 172 VEPDISPLELEPGD-RLLLCSDGLTDMVSDEEIAEILASAGDPQEAAEALIELALEAGGPDNITVVLVRVEDADA 245
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
242-425 |
3.66e-05 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 48.52 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 242 GEHGRDVEPPPSSGTVGAVRGPARAPPADLP--LPGGAWTRCAPR-----------------ISPAPSDSSPGELFAGGP 302
Cdd:COG5180 286 GSEPQSDAPEAETARPIDVKGVASAPPATRPvrPPGGARDPGTPRpgqpterpagvpeaasdAGQPPSAYPPAEEAVPGK 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 303 GSPPRAPRPASdtesfSLSPSAesvsdrldPYSSGGGGSSSSSEELEA-DPAMPHRPGRPAQPRPPSPKTSALLQPKA-- 379
Cdd:COG5180 366 PLEQGAPRPGS-----SGGDGA--------PFQPPNGAPQPGLGRRGApGPPMGAGDLVQAALDGGGRETASLGGAAGga 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 257467468 380 -----PTGVD------STGVIAGEGPGDDKAMAAAAPDVPLSTSGRIRETVQKTSPP 425
Cdd:COG5180 433 gqgpkADFVPgdaesvSGPAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGVRP 489
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
896-954 |
7.30e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 42.13 E-value: 7.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 896 SSLRKLLAGHNRLARLPERLER--TSVEVLDVQHNQITELPPNLLMKADSLRFLNASANKL 954
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKglSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
511-592 |
6.78e-04 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 40.62 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 511 NRWTRRQVILCGTCLIV--SSVKDSVSGKMHVLPLIGGKVEEV-----KKHQHCLAFSSSGPQ-SQTYYICFDTFTEYLR 582
Cdd:pfam00169 16 KSWKKRYFVLFDGSLLYykDDKSGKSKEPKGSISLSGCEVVEVvasdsPKRKFCFELRTGERTgKRTYLLQAESEEERKD 95
|
90
....*....|
gi 257467468 583 WLRQVSKVAS 592
Cdd:pfam00169 96 WIKAIQSAIR 105
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
250-381 |
8.84e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 44.37 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 250 PPPSSGTVGAVRGPARAPPADLPlpgGAWTRCAPRISPAP----SDSSPGELFAGGPG-SPPRAPRPASDTESFSLSPSA 324
Cdd:pfam03154 182 SPPSPPPPGTTQAATAGPTPSAP---SVPPQGSPATSQPPnqtqSTAAPHTLIQQTPTlHPQRLPSPHPPLQPMTQPPPP 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 257467468 325 ESVSDRLDPYSSGGGGSSSSSEELEADPA-MPHrPGrPAQPRPPSPKTSALLQPKAPT 381
Cdd:pfam03154 259 SQVSPQPLPQPSLHGQMPPMPHSLQTGPShMQH-PV-PPQPFPLTPQSSQSQVPPGPS 314
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
512-592 |
3.54e-03 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 38.68 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 512 RWTRRQVILCGTCLIVSSVKDSVSGKM--HVLPLIGGKVEEV-----KKHQHClaFSSSGPQSQTYYICFDTFTEYLRWL 584
Cdd:smart00233 17 SWKKRYFVLFNSTLLYYKSKKDKKSYKpkGSIDLSGCTVREApdpdsSKKPHC--FEIKTSDRKTLLLQAESEEEREKWV 94
|
....*...
gi 257467468 585 RQVSKVAS 592
Cdd:smart00233 95 EALRKAIA 102
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
250-406 |
4.73e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 41.29 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 250 PPPSSGTVGAVRGPARappaDL--PLPGGAWTRCA--PRISPAPSDSSPGELfaGGPGSPPRAPRPASDTESfSLSPSAE 325
Cdd:NF040712 170 PGAHGGTVTALDDEAR----WLidPDFGRPLRPLAtvPRLAREPADARPEEV--EPAPAAEGAPATDSDPAE-AGTPDDL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 326 SVSDRLDPYSSGGGGSSSSSEELEADPAMPHRPGRPAQPRPPSPKTSALLQPKAPTGVDSTGVIAGEGPGDDKAMAAAAP 405
Cdd:NF040712 243 ASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAP 322
|
.
gi 257467468 406 D 406
Cdd:NF040712 323 K 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PH_PHLPP-like |
cd13322 |
PH domain leucine-rich repeat protein phosphatase family Pleckstrin homology-like domain; The ... |
491-587 |
2.80e-60 |
|
PH domain leucine-rich repeat protein phosphatase family Pleckstrin homology-like domain; The PHLPP family has members PHLPP1 (also called hSCOP/Suprachiasmatic nucleus circadian oscillatory protein; PLEKHE1/Pleckstrin homology domain-containing family E member 1) and PHLPP2 (PHLPP-like/PHLPPL). The PHLPP family of novel Ser/Thr phosphatases serve as important regulators of cell survival and apoptosis. PHLPP isozymes catalyze the dephosphorylation of a conserved regulatory motif, the hydrophobic motif, on the AGC kinases Akt, PKC, and S6 kinase, as well as an inhibitory site on the kinase Mst1, to inhibit cellular proliferation and induce apoptosis and negatively regulates ERK1/2 activation. Reductions in their expression have been detected in several cancers and linked to cancer progression. PHLPP1 and PHLPP2 both contain an N-terminal PH domain, followed by 21 LRR (leucine-rich) repeats, and a C-terminal PP2C-like domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270131 Cd Length: 95 Bit Score: 201.29 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 491 ERIQLSGMYNVRKGKMQLpvNRWTRRQVILCGTCLIVSSVKDSVSGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTY 570
Cdd:cd13322 1 ERILLSGIYNVRKGKTQL--HKWAERQVILCGTCLIVSSVKDSQTGKMHILPLVGGKVEEVKRRQHCLAFSSAGPQAQTY 78
|
90
....*....|....*..
gi 257467468 571 YICFDTFTEYLRWLRQV 587
Cdd:cd13322 79 YVSFDTLAEYQRWHRQA 95
|
|
| PP2Cc |
smart00332 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1124-1376 |
3.07e-59 |
|
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: 204.53 E-value: 3.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1124 SGAPAVWSHGYTEASGVKNKLCVAALSVNNFRDNrEALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE----EEYM 1199
Cdd:smart00332 3 SGKNLGLRYGLSSMQGVRKPMEDAHVITPDLSDS-GGFFGVFDGHGGSEAAKFLSKNLPEILAEELIKEKDEledvEEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1200 VNTFIVMQRKLGTAGQKLGGA-AVLCHIKPDpvdlggsfTLTSANVGKCQTVLCRNGKPLSLSRSYIMSCEEERKRIKQH 1278
Cdd:smart00332 82 RKAFLSTDEEILEELEALSGStAVVALISGN--------KLYVANVGDSRAVLCRNGKAVQLTEDHKPSNEDERARIEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1279 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNVP--DALAAAK 1356
Cdd:smart00332 154 GGFV-INGRVNGVLALSRAIGDFFLKPYVSAEPDVTVVELTEKDDFLILASDGLWDVLSNQEVVDIVRKHLskDPKEAAK 232
|
250 260
....*....|....*....|
gi 257467468 1357 KLCTLAQSYGCHDSISAVVV 1376
Cdd:smart00332 233 RLIDLALARGSKDNITVVVV 252
|
|
| PP2Cc |
cd00143 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1130-1378 |
4.33e-56 |
|
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: 195.62 E-value: 4.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1130 WSHGYTEASGVKNKLCVAALSVNNFRDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE-----EEYMVNTFI 1204
Cdd:cd00143 1 FSAGVSDKGGDRKTNEDAVVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLseediEEALRKAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1205 VMQRKLGTAGQKL------GGAAVLCHIKPDpvdlggsfTLTSANVGKCQTVLCRNGKPLSLSRSYIMSCEEERKRIKQH 1278
Cdd:cd00143 81 RADEEILEEAQDEpddarsGTTAVVALIRGN--------KLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEEERERIEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1279 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNVP---DALAAA 1355
Cdd:cd00143 153 GGRV-SNGRVPGVLAVTRALGDFDLKPGVSAEPDVTVVKLTEDDDFLILASDGLWDVLSNQEAVDIVRSELakeDLQEAA 231
|
250 260
....*....|....*....|...
gi 257467468 1356 KKLCTLAQSYGCHDSISAVVVQL 1378
Cdd:cd00143 232 QELVDLALRRGSHDNITVVVVRL 254
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
427-484 |
2.69e-33 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase 1 (PHLPP1); PHLPP1, also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP), 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. PHLPP1 also plays critical roles in many cancers, such as gastric cancer, sacral chordoma, gallbladder cancer, hypopharyngeal squamous cell carcinomas, and non-small cell lung cancer. It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role in learning and memory. PHLPP1 contains a Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain.
Pssm-ID: 340760 Cd Length: 90 Bit Score: 124.17 E-value: 2.69e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 257467468 427 LYVQLHGETTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 484
Cdd:cd17240 33 LQLQLHGETVRRLEPHEKPLQIQNDYLFQLGFGDLWRVQEEGMDPEIGCLIRFYAGKP 90
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
593-854 |
2.95e-32 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 131.59 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 593 QRISSVDLSCCSlehlpaNLFYSQDLTHLNLKQNFLRQTPTlpaarglgELQRFTKLKSLNLSNNHLGAFPSAVCSIPTL 672
Cdd:COG4886 96 TNLTELDLSGNE------ELSNLTNLESLDLSGNQLTDLPE--------ELANLTNLKELDLSNNQLTDLPEPLGNLTNL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 673 AELNVSCNALREVPAAVGDMQNLQTFLLDGNFLQSLPAELESMHQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMAGNCVE 752
Cdd:COG4886 162 KSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 753 TLRlqALRRMPHIKHVDLRLNILRKLmaDEVDFVQHVTQLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTLNVCGYFLKA 832
Cdd:COG4886 242 DLP--ELGNLTNLEELDLSNNQLTDL--PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
|
250 260
....*....|....*....|..
gi 257467468 833 LYASSNELAQLDVYPVPNYLSY 854
Cdd:COG4886 318 LLLTTLLLLLLLLKGLLVTLTT 339
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
907-1110 |
5.94e-32 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 130.82 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 907 RLARLPERLERTSVEVLDVQHNQITELPPNLLmKADSLRFLNASANKLETLPPAtLSEETSsiLQELYLTNNCLTDkcVP 986
Cdd:COG4886 102 DLSGNEELSNLTNLESLDLSGNQLTDLPEELA-NLTNLKELDLSNNQLTDLPEP-LGNLTN--LKSLDLSNNQLTD--LP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 987 L-LTGHPRLKILHMAYNRLQSFPASkMAKLEELEEIDISGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVMQLPEVKC 1065
Cdd:COG4886 176 EeLGNLTNLKELDLSNNQITDLPEP-LGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEE 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 257467468 1066 VDLSCNELSEITLPENLpPKLQELDLTGNPRLALDHKSLELLNNI 1110
Cdd:COG4886 255 LDLSNNQLTDLPPLANL-TNLKTLDLSNNQLTDLKLKELELLLGL 298
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
874-1110 |
1.81e-30 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 126.20 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 874 KLEVLDIGHNQIcelparLFCNSSLRKLLAGHNRLARLPERLER-TSVEVLDVQHNQITELPPNLlMKADSLRFLNASAN 952
Cdd:COG4886 97 NLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANlTNLKELDLSNNQLTDLPEPL-GNLTNLKSLDLSNN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 953 KLETLPPAtLSEETSsiLQELYLTNNCLTDkcVPL-LTGHPRLKILHMAYNRLQSFPASkMAKLEELEEIDISGNKLKAI 1031
Cdd:COG4886 170 QLTDLPEE-LGNLTN--LKELDLSNNQITD--LPEpLGNLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQLTDL 243
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257467468 1032 PTtIMNCRRMHTVIAHSNCIEVFPEVMQLPEVKCVDLSCNELSEITLpENLPPKLQELDLTGNPRLALDHKSLELLNNI 1110
Cdd:COG4886 244 PE-LGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKL-KELELLLGLNSLLLLLLLLNLLELLILLLLL 320
|
|
| PP2C |
pfam00481 |
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ... |
1130-1371 |
9.77e-30 |
|
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.
Pssm-ID: 395385 Cd Length: 252 Bit Score: 119.75 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1130 WSHGYTEASGVKNKLCVAALSVNNFR----DNREALYGVFDGDRNVEVPYLLQCTMSDILAE--ELQKTKNEEEYMVNTF 1203
Cdd:pfam00481 1 IDLGGPRMQGWRKSMEDAHIDLPNLNsssgKDSWSFFAVFDGHGGSEAAKYCGKHLHTILALrrSFLEGEKLEDALRKSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1204 I----VMQRKLGTAGQKLGGAAVLCHIKPDpvdlggsfTLTSANVGKCQTVLCRNGKP-LSLSRSYIMSCEEERKRIKQH 1278
Cdd:pfam00481 81 LedtdEVLRSAEKEDLDSGCTAVVALISGN--------KLYVANVGDSRAVLCRNGNAiKRLTKDHKPSDEDERRRIRAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1279 KAIITEDGKVNGVTESTRILGYTFLHPS---VVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNV----PDA 1351
Cdd:pfam00481 153 GGFVSRNGRVNGVLAVSRAFGDFELKPGeqaVSAEPDITSHTITEDDEFLILACDGLWDVLSDQEVVDLVRSElsdgGSP 232
|
250 260
....*....|....*....|
gi 257467468 1352 LAAAKKLCTLAQSYGCHDSI 1371
Cdd:pfam00481 233 MEAAEELRDEAIAYGSEDNI 252
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
610-978 |
4.48e-29 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 121.96 E-value: 4.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 610 ANLFYSQDLTHLNLKQNFLRQTPTLPAARGLGELQRFTKLKSLNLSNNhlgafpSAVCSIPTLAELNVSCNALREVPAAV 689
Cdd:COG4886 59 DLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEEL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 690 GDMQNLQTFLLDGNFLQSLPAELESMHQLSYLGLSFNEFTDIPEVLEKLTavdklcmagncvetlrlqalrrmphikhvd 769
Cdd:COG4886 133 ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLT------------------------------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 770 lrlnilrklmadevdfvqHVTQLDLRDNKLGDLDAMIFN--NIEVLHCERNQLVTLnvcgyflkalyasSNELAQLdvyp 847
Cdd:COG4886 183 ------------------NLKELDLSNNQITDLPEPLGNltNLEELDLSGNQLTDL-------------PEPLANL---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 848 vpnylsymdvsrnclesvpewvcesRKLEVLDIGHNQICELPArLFCNSSLRKLLAGHNRLARLPERLERTSVEVLDVQH 927
Cdd:COG4886 228 -------------------------TNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSN 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 257467468 928 NQITELPPNLLMKADSLRFLNASANKLETLPPATLSEETSSILQELYLTNN 978
Cdd:COG4886 282 NQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
|
|
| RA_PHLPP |
cd17213 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
407-484 |
6.14e-29 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase PHLPP1, PHLPP2, 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 targets oncogenic kinases and may act as a tumor suppressor in several types of cancers. Two PHLPP isoforms are included in this family, PHLPP1 and PHLPP2. They regulate Akt activation together when both phosphatases are expressed. PHLPP1 is also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP). It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role for PHLPP1 in learning and memory. PHLPP2 is also termed PH domain leucine-rich repeat-containing protein phosphatase-like (PHLPP-like). Both PHLPP1 and PHLPP2 contain 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.
Pssm-ID: 340733 Cd Length: 97 Bit Score: 112.00 E-value: 6.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 407 VPLSTSGRIRETVQK--TSPPSLYVQLHGETTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 484
Cdd:cd17213 18 VPCTLETTAEDICKKlgISSLYLYVQLGGDHIRRLEPDERPLQIQNEFLASLGYSDPSRIQREGTDPDLGHLIRFYAGRP 97
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
595-1082 |
3.07e-24 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 111.09 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 595 ISSVDLSCCSLE-HLPANLFY-SQDLTHLNLKQNFLrqtpTLPAARGLGELqrftkLKSLNLSNNHL-GAFPSAVCSIPT 671
Cdd:PLN00113 95 IQTINLSNNQLSgPIPDDIFTtSSSLRYLNLSNNNF----TGSIPRGSIPN-----LETLDLSNNMLsGEIPNDIGSFSS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 672 LAELNVSCNALR-EVPAAVGDMQNLQTFLLDGN-FLQSLPAELESMHQLSYLGLSFNEFT-DIPEVLEKLTAVDKLCMAG 748
Cdd:PLN00113 166 LKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNqLVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 749 NCVETLRLQALRRMPHIKHVDLRLNILRKLMADEVDFVQHVTQLDLRDNKL-GDLDAMI--FNNIEVLHcernqLVTLNV 825
Cdd:PLN00113 246 NNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLsGEIPELViqLQNLEILH-----LFSNNF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 826 CGYFLKALyASSNELAQLDVYpvpnylsymdvSRNCLESVPEWVCESRKLEVLDIGHNQIC-ELPARLfCNS-SLRKLLA 903
Cdd:PLN00113 321 TGKIPVAL-TSLPRLQVLQLW-----------SNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEIPEGL-CSSgNLFKLIL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 904 GHNRL-ARLPERLER-TSVEVLDVQHNQITELPPNLLMKADSLRFLNASANKLETLPPATLSEETSsiLQELYLTNNCLT 981
Cdd:PLN00113 388 FSNSLeGEIPKSLGAcRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPS--LQMLSLARNKFF 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 982 DKcVPLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKLKA-IPTTIMNCRRMHTV-IAHSNCIEVFPEVM- 1058
Cdd:PLN00113 466 GG-LPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLdLSHNQLSGQIPASFs 544
|
490 500
....*....|....*....|....*
gi 257467468 1059 QLPEVKCVDLSCNELS-EItlPENL 1082
Cdd:PLN00113 545 EMPVLSQLDLSQNQLSgEI--PKNL 567
|
|
| RA_PHLPP2 |
cd17241 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
426-484 |
1.67e-19 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase 2 (PHLPP2); PHLPP2, also termed PH domain leucine-rich repeat-containing protein phosphatase-like (PHLPP-like), 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. PHLPP2 also plays critical roles in many cancers, such as glioma, hypopharyngeal squamous cell carcinomas, and non-small cell lung cancer. PHLPP2 contains a Ras-associating (RA) domain followed by a PH domain, leucine-rich repeats and protein phosphatase 2C (PP2C) domain.
Pssm-ID: 340761 Cd Length: 108 Bit Score: 85.32 E-value: 1.67e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 257467468 426 SLYVQLHGETTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 484
Cdd:cd17241 50 SLYLQLHGDLVRRLDPTERPLQIVYDYLSGLGFEDPVRIQEEAANSDLSCMIRFYSEKP 108
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
848-1094 |
2.90e-19 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 94.38 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 848 VPNYLSYMDVSRNCLESVPEWVceSRKLEVLDIGHNQICELPARLfcNSSLRKLLAGHNRLARLPERLErTSVEVLDVQH 927
Cdd:PRK15370 197 IPEQITTLILDNNELKSLPENL--QGNIKTLYANSNQLTSIPATL--PDTIQEMELSINRITELPERLP-SALQSLDLFH 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 928 NQITELPPNLlmkADSLRFLNASANKLETLPpatlsEETSSILQELYLTNNCLTdkCVPLlTGHPRLKILHMAYNRLQSF 1007
Cdd:PRK15370 272 NKISCLPENL---PEELRYLSVYDNSIRTLP-----AHLPSGITHLNVQSNSLT--ALPE-TLPPGLKTLEAGENALTSL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1008 PASKMAkleELEEIDISGNKLKAIPTTImncrrmhtviahsncievfPevmqlPEVKCVDLSCNELseITLPENLPPKLQ 1087
Cdd:PRK15370 341 PASLPP---ELQVLDVSKNQITVLPETL-------------------P-----PTITTLDVSRNAL--TNLPENLPAALQ 391
|
....*..
gi 257467468 1088 ELDLTGN 1094
Cdd:PRK15370 392 IMQASRN 398
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
862-1094 |
2.85e-18 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 91.30 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 862 LESVPEWVCESRKLEVLDigHNQICELPARLFCNssLRKLLAGHNRLARLPERLERTsVEVLDVQHNQITELPPNLlmkA 941
Cdd:PRK15370 190 LTTIPACIPEQITTLILD--NNELKSLPENLQGN--IKTLYANSNQLTSIPATLPDT-IQEMELSINRITELPERL---P 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 942 DSLRFLNASANKLETLPPaTLSEEtssilqelyltnncltdkcvplltghprLKILHMAYNRLQSFPASKMAKLEELeei 1021
Cdd:PRK15370 262 SALQSLDLFHNKISCLPE-NLPEE----------------------------LRYLSVYDNSIRTLPAHLPSGITHL--- 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257467468 1022 DISGNKLKAIPTTI-MNcrrMHTVIAHSNCIEVFPEVMQlPEVKCVDLSCNELSeiTLPENLPPKLQELDLTGN 1094
Cdd:PRK15370 310 NVQSNSLTALPETLpPG---LKTLEAGENALTSLPASLP-PELQVLDVSKNQIT--VLPETLPPTITTLDVSRN 377
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
177-219 |
1.88e-14 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase 1 (PHLPP1); PHLPP1, also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP), 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. PHLPP1 also plays critical roles in many cancers, such as gastric cancer, sacral chordoma, gallbladder cancer, hypopharyngeal squamous cell carcinomas, and non-small cell lung cancer. It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role in learning and memory. PHLPP1 contains a Ras-associating (RA) domain followed by a pleckstrin homology (PH) domain, a series of leucine-rich repeats and a protein phosphatase 2C (PP2C) domain.
Pssm-ID: 340760 Cd Length: 90 Bit Score: 70.24 E-value: 1.88e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 257467468 177 GCVHVFDRHMaSSYLRPVLCTLDTTAAEVAARLLQLGHKGGGV 219
Cdd:cd17240 1 GCIHVYDRHM-SSYLRPVLCTLDTTASEVAARLLQLQLHGETV 42
|
|
| PLN03145 |
PLN03145 |
Protein phosphatase 2c; Provisional |
1151-1376 |
6.24e-14 |
|
Protein phosphatase 2c; Provisional
Pssm-ID: 215603 [Multi-domain] Cd Length: 365 Bit Score: 75.34 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1151 VNNFRDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNEEEYMVNTFIVMQRKLGTA----GQKLGGAAVLCHI 1226
Cdd:PLN03145 95 LKNSEDGPSAFYGVFDGHGGKHAADFACYHLPRFIVEDEDFPREIEKVVSSAFLQTDTAFAEAcsldASLASGTTALAAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1227 KpdpvdLGGSftLTSANVGKCQTVLCRNGKPLSLSRSYIMSCEEERKRIKQHKAIItEDGKVNGVTESTRILGYTFLH-- 1304
Cdd:PLN03145 175 V-----VGRS--LVVANAGDCRAVLCRRGKAIEMSRDHKPMCSKERKRIEASGGYV-YDGYLNGQLNVARALGDWHMEgm 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1305 -----PSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSIDEAVEAVRNV----PDALAAAKKLCTLAQSYGCHDSISAVV 1375
Cdd:PLN03145 247 kgsdgGPLSAEPELMTTQLTEEDEFLIIGCDGIWDVFRSQNAVDFARRRlqehNDPVMCSKELVDEALKRKSGDNLAVVV 326
|
.
gi 257467468 1376 V 1376
Cdd:PLN03145 327 V 327
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
733-964 |
7.37e-14 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 77.04 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 733 EVLEKLTAVDKL--CMAGNCVEtLRLQALR--RMPHIKHVDLRLNILRK--LMADEVDFVQHVTQLDLRDNKLGDLDAMI 806
Cdd:PRK15370 161 EAANREEAVQRMrdCLKNNKTE-LRLKILGltTIPACIPEQITTLILDNneLKSLPENLQGNIKTLYANSNQLTSIPATL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 807 FNNIEVLHCERNQLVTL-NVCGYFLKALYASSNELAQLdvyP--VPNYLSYMDVSRNCLESVPEWVCES----------- 872
Cdd:PRK15370 240 PDTIQEMELSINRITELpERLPSALQSLDLFHNKISCL---PenLPEELRYLSVYDNSIRTLPAHLPSGithlnvqsnsl 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 873 --------RKLEVLDIGHNQICELPARLfcNSSLRKLLAGHNRLARLPERLERTsVEVLDVQHNQITELPPNLlmkADSL 944
Cdd:PRK15370 317 talpetlpPGLKTLEAGENALTSLPASL--PPELQVLDVSKNQITVLPETLPPT-ITTLDVSRNALTNLPENL---PAAL 390
|
250 260
....*....|....*....|...
gi 257467468 945 RFLNASANKLETLP---PATLSE 964
Cdd:PRK15370 391 QIMQASRNNLVRLPeslPHFRGE 413
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
674-932 |
3.27e-13 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 74.73 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 674 ELNVSCNALREVPAAVGdmQNLQTFLLDGNFLQSLPAELESmhQLSYLGLSFNEFTDIPEVLEKltAVDKLCMAGNCVET 753
Cdd:PRK15370 182 ELRLKILGLTTIPACIP--EQITTLILDNNELKSLPENLQG--NIKTLYANSNQLTSIPATLPD--TIQEMELSINRITE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 754 LRlqalRRMPH-IKHVDLRLNILRKLMADEVDFVQHvtqLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTL-NVCGYFLK 831
Cdd:PRK15370 256 LP----ERLPSaLQSLDLFHNKISCLPENLPEELRY---LSVYDNSIRTLPAHLPSGITHLNVQSNSLTALpETLPPGLK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 832 ALYASSNELAQLDVyPVPNYLSYMDVSRNCLESVPEWVCESrkLEVLDIGHNQICELPARLfcNSSLRKLLAGHNRLARL 911
Cdd:PRK15370 329 TLEAGENALTSLPA-SLPPELQVLDVSKNQITVLPETLPPT--ITTLDVSRNALTNLPENL--PAALQIMQASRNNLVRL 403
|
250 260
....*....|....*....|....*.
gi 257467468 912 PERL-----ERTSVEVLDVQHNQITE 932
Cdd:PRK15370 404 PESLphfrgEGPQPTRIIVEYNPFSE 429
|
|
| PTZ00224 |
PTZ00224 |
protein phosphatase 2C; Provisional |
1146-1379 |
2.05e-12 |
|
protein phosphatase 2C; Provisional
Pssm-ID: 240318 [Multi-domain] Cd Length: 381 Bit Score: 70.96 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1146 VAALSVNNFRDNRE-----------ALYGVFDGDRNVevpyllQCtmSDILAEEL-QKTKNEEEYMvnTFIVMQR----- 1208
Cdd:PTZ00224 24 CASACVNGYRESMEdahllyltddwGFFGVFDGHVND------EC--SQYLARAWpQALEKEPEPM--TDERMEElclei 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1209 -----KLGTAGqklGGAAVLCHIKPDpvdlggsFTLTSANVGKCQTVLCRNGKPLSLSRSYIMSCEEERKRIKQHKAIIt 1283
Cdd:PTZ00224 94 deewmDSGREG---GSTGTFCVIMKD-------VHLQVGNVGDSRVLVCRDGKLVFATEDHKPNNPGERQRIEACGGRV- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 1284 EDGKVNGVTESTRILG---------YTFLHPSVVPRPHVQSVLLTPQDeFFILGSKGLWD-SLSIDEAV----EAVRNVP 1349
Cdd:PTZ00224 163 VSNRVDGDLAVSRAFGdrsfkvkgtGDYLEQKVIAVPDVTHLTCQSND-FIILACDGVFEgNFSNEEVVafvkEQLETCD 241
|
250 260 270
....*....|....*....|....*....|
gi 257467468 1350 DALAAAKKLCTLAQSYGCHDSISAVVVQLS 1379
Cdd:PTZ00224 242 DLAVVAGRVCDEAIRRGSKDNISCLIVQLK 271
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
581-885 |
6.55e-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: 68.54 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 581 LRWLRQVSKVasQRISSVDLSCCSL--EHLPA---NLFYSQDLTHLNLKQNFLRQTPTLPAARGLGeLQRFTKLKSLNLS 655
Cdd:cd00116 13 ERATELLPKL--LCLQVLRLEGNTLgeEAAKAlasALRPQPSLKELCLSLNETGRIPRGLQSLLQG-LTKGCGLQELDLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 656 NNHLG----AFPSAVCSIPTLAELNVSCNALREVPAAvgdmqnlqtFLLDGnfLQSLPAELESMhQLSYLGLSFNEFTDI 731
Cdd:cd00116 90 DNALGpdgcGVLESLLRSSSLQELKLNNNGLGDRGLR---------LLAKG--LKDLPPALEKL-VLGRNRLEGASCEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 732 PEVLEKLTAVDKLCMAGNCV-----ETLrLQALRRMPHIKHVDLRLNILR----KLMADEVDFVQHVTQLDLRDNKLGDL 802
Cdd:cd00116 158 AKALRANRDLKELNLANNGIgdagiRAL-AEGLKANCNLEVLDLNNNGLTdegaSALAETLASLKSLEVLNLGDNNLTDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 803 DAMIFNnievlhcerNQLVTLNVCgyfLKALYASSNELAQLDVYPVPNYLS------YMDVSRNCL------ESVPEWVC 870
Cdd:cd00116 237 GAAALA---------SALLSPNIS---LLTLSLSCNDITDDGAKDLAEVLAekesllELDLRGNKFgeegaqLLAESLLE 304
|
330
....*....|....*
gi 257467468 871 ESRKLEVLDIGHNQI 885
Cdd:cd00116 305 PGNELESLWVKDDSF 319
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
608-959 |
1.49e-10 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 66.41 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 608 LPANLFYSQDLTHLNLKQNFLR-QTPTLpaargLGELQrftKLKSLNL-SNNHLGAFPSAVCSIPTLaelnvscnalrev 685
Cdd:PLN00113 276 IPPSIFSLQKLISLDLSDNSLSgEIPEL-----VIQLQ---NLEILHLfSNNFTGKIPVALTSLPRL------------- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 686 paavgdmQNLQtfLLDGNFLQSLPAELESMHQLSYLGLSFNEFT-DIPEVLEKLTAVDKLCMAGNCVETLRLQALRRMPH 764
Cdd:PLN00113 335 -------QVLQ--LWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 765 IKHVDLRLNILRKLMADEVDFVQHVTQLDLRDNKL-GDLDAMIFN--NIEVLHCERNQlvtlnvcgyFLKALYASSNEla 841
Cdd:PLN00113 406 LRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLqGRINSRKWDmpSLQMLSLARNK---------FFGGLPDSFGS-- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 842 qldvypvpNYLSYMDVSRNCL-ESVPEWVCESRKLEVLDIGHNQIC-ELPARLfcnSSLRKLLA---GHNRLA-RLPERL 915
Cdd:PLN00113 475 --------KRLENLDLSRNQFsGAVPRKLGSLSELMQLKLSENKLSgEIPDEL---SSCKKLVSldlSHNQLSgQIPASF 543
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 257467468 916 ERTSV-EVLDVQHNQIT-ELPPNlLMKADSLRFLNASANKLE-TLPP 959
Cdd:PLN00113 544 SEMPVlSQLDLSQNQLSgEIPKN-LGNVESLVQVNISHNHLHgSLPS 589
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
788-1078 |
1.83e-10 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 65.95 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 788 HVTQLDLRDNKLGDLDAMIfNNIEVLHCERNQLVTLNVCGYFLKALYASSNELAQLDVypVPNYLSYMDVSRNCLESVPe 867
Cdd:PRK15387 223 HITTLVIPDNNLTSLPALP-PELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPA--LPSGLCKLWIFGNQLTSLP- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 868 wvCESRKLEVLDIGHNQICELPArlfCNSSLRKLLAGHNRLARLPErlertsvevldvqhnqiteLPpnllmkaDSLRFL 947
Cdd:PRK15387 299 --VLPPGLQELSVSDNQLASLPA---LPSELCKLWAYNNQLTSLPT-------------------LP-------SGLQEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 948 NASANKLETLPpaTLSEEtssiLQELYLTNNCLTDkcVPLLTGHprLKILHMAYNRLQSFPASKmaklEELEEIDISGNK 1027
Cdd:PRK15387 348 SVSDNQLASLP--TLPSE----LYKLWAYNNRLTS--LPALPSG--LKELIVSGNRLTSLPVLP----SELKELMVSGNR 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 257467468 1028 LKAIPttiMNCRRMHTVIAHSNCIEVFPE-VMQLPEVKCVDLSCNELSEITL 1078
Cdd:PRK15387 414 LTSLP---MLPSGLLSLSVYRNQLTRLPEsLIHLSSETTVNLEGNPLSERTL 462
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
852-1119 |
1.85e-10 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 66.02 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 852 LSYMDVSRNCLES-VPEWVCESRKLEVLDIGHNQIC-ELPARLFCNSSLRKLLAGHNRLA-RLPERLER-TSVEVLDVQH 927
Cdd:PLN00113 166 LKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGlTSLNHLDLVY 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 928 NQITELPPNLLMKADSLRFLNASANKLE-TLPPA---------------TLSEETSSI------LQELYLTNNCLTDKCV 985
Cdd:PLN00113 246 NNLTGPIPSSLGNLKNLQYLFLYQNKLSgPIPPSifslqklisldlsdnSLSGEIPELviqlqnLEILHLFSNNFTGKIP 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 986 PLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKLKA-IPTTIMNCRRMHTVIAHSNCIEvfpevMQLPEvk 1064
Cdd:PLN00113 326 VALTSLPRLQVLQLWSNKFSGEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSSGNLFKLILFSNSLE-----GEIPK-- 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 1065 cvDLS-CNELSEITLPEN-----LPPKLQELDLTgnprLALDHKSLELLNNIRCFKIDQPS 1119
Cdd:PLN00113 399 --SLGaCRSLRRVRLQDNsfsgeLPSEFTKLPLV----YFLDISNNNLQGRINSRKWDMPS 453
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
245-427 |
1.45e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.42 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 245 GRDVEPPPSSGTVgavrgpARAPPADLPLPGGAWTRCAPRISPAPSDSSPGELFAGGPgsPPRAPRPASDtesfSLSPSA 324
Cdd:PHA03247 2728 ARQASPALPAAPA------PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP--PRRLTRPAVA----SLSESR 2795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 325 ESVSDRLDPYSSGGG-GSSSSSEELEADPAMPHRPGRPAQPRPPsPKTSALLQPKAPTGvdstGVIAGEGPGDDKAMAAA 403
Cdd:PHA03247 2796 ESLPSPWDPADPPAAvLAPAAALPPAASPAGPLPPPTSAQPTAP-PPPPGPPPPSLPLG----GSVAPGGDVRRRPPSRS 2870
|
170 180
....*....|....*....|....
gi 257467468 404 APDVPlSTSGRIRetVQKTSPPSL 427
Cdd:PHA03247 2871 PAAKP-AAPARPP--VRRLARPAV 2891
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
768-1030 |
1.71e-09 |
|
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: 61.22 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 768 VDLRLNILRKLMADEV-DFVQHVTQLDLRDNKLGDLDA-MIFNNIEVlhceRNQLVTLNVCGYFLKALyaSSNELAQLDV 845
Cdd:cd00116 3 LSLKGELLKTERATELlPKLLCLQVLRLEGNTLGEEAAkALASALRP----QPSLKELCLSLNETGRI--PRGLQSLLQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 846 YPVPNYLSYMDVSRNCL--ESVPEW--VCESRKLEVLDIGHNQICELPARLFCNS------SLRKLLAGHNRL-ARLPER 914
Cdd:cd00116 77 LTKGCGLQELDLSDNALgpDGCGVLesLLRSSSLQELKLNNNGLGDRGLRLLAKGlkdlppALEKLVLGRNRLeGASCEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 915 L-----ERTSVEVLDVQHNQITE-----LPPNLLMKAdSLRFLNASANKLETLPPATLSE--ETSSILQELYLTNNCLTD 982
Cdd:cd00116 157 LakalrANRDLKELNLANNGIGDagiraLAEGLKANC-NLEVLDLNNNGLTDEGASALAEtlASLKSLEVLNLGDNNLTD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 257467468 983 KCV-----PLLTGHPRLKILHMAYNRLQSFPASK----MAKLEELEEIDISGNKLKA 1030
Cdd:cd00116 236 AGAaalasALLSPNISLLTLSLSCNDITDDGAKDlaevLAEKESLLELDLRGNKFGE 292
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
591-824 |
6.14e-09 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 60.19 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 591 ASQRISSVDLSC-----CSLEHLPANLFYSQDLTHLNLKQNFLrqtpTLPAARGLGE-LQRFTKLKSLNLSNNHLG---- 660
Cdd:COG5238 178 QNNSVETVYLGCnqigdEGIEELAEALTQNTTVTTLWLKRNPI----GDEGAEILAEaLKGNKSLTTLDLSNNQIGdegv 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 661 -AFPSAVCSIPTLAELNVSCNALrEVPAAVGDMQNLQTFLldgnflqslpaelesmhQLSYLGLSFNEFTD-----IPEV 734
Cdd:COG5238 254 iALAEALKNNTTVETLYLSGNQI-GAEGAIALAKALQGNT-----------------TLTSLDLSVNRIGDegaiaLAEG 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 735 LEKLTAVDKLCMAGN-----CVETLrLQALRRMPHIKHVDLRLNILR----KLMADEVDFVQHVTQLDLRDNKLGDLDAM 805
Cdd:COG5238 316 LQGNKTLHTLNLAYNgigaqGAIAL-AKALQENTTLHSLDLSDNQIGdegaIALAKYLEGNTTLRELNLGKNNIGKQGAE 394
|
250
....*....|....*....
gi 257467468 806 IFNNievlHCERNQLVTLN 824
Cdd:COG5238 395 ALID----ALQTNRLHTLI 409
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
906-1109 |
9.61e-09 |
|
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: 57.49 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 906 NRLARLpERLER-TSVEVLDVQHNQITELPPnllmkadslrflnasankLETLPPatlseetssiLQELYLTNNCLTdkC 984
Cdd:cd21340 34 NKITKI-ENLEFlTNLTHLYLQNNQIEKIEN------------------LENLVN----------LKKLYLGGNRIS--V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 985 VPLLTGHPRLKILHMAYNRLQS-----F-PASKMAKLEELEEIDISGNKLKAIpTTIMNCRRMHTVIAHSNCIEVFPEVm 1058
Cdd:cd21340 83 VEGLENLTNLEELHIENQRLPPgekltFdPRSLAALSNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEEL- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 1059 qlpevkCVDLSCNelseitlpenlpPKLQELDLTGNPrLALDHK----------SLELLNN 1109
Cdd:cd21340 161 ------LDLLSSW------------PSLRELDLTGNP-VCKKPKyrdkiilaskSLEVLDG 202
|
|
| RA_PHLPP |
cd17213 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
177-226 |
2.23e-08 |
|
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein phosphatase PHLPP1, PHLPP2, 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 targets oncogenic kinases and may act as a tumor suppressor in several types of cancers. Two PHLPP isoforms are included in this family, PHLPP1 and PHLPP2. They regulate Akt activation together when both phosphatases are expressed. PHLPP1 is also termed pleckstrin homology domain-containing family E member 1, or PH domain-containing family E member 1, or suprachiasmatic nucleus circadian oscillatory protein (SCOP). It plays a suppression role in inflammatory response of glioma. Its loss contributes to gliomas development and progression. Loss of PHLPP1 also protects against colitis by inhibiting intestinal epithelial cell apoptosis. The overexpression of PHLPP1 impairs hippocampus-dependent learning, suggesting a role for PHLPP1 in learning and memory. PHLPP2 is also termed PH domain leucine-rich repeat-containing protein phosphatase-like (PHLPP-like). Both PHLPP1 and PHLPP2 contain 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.
Pssm-ID: 340733 Cd Length: 97 Bit Score: 53.45 E-value: 2.23e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 177 GCVHVFDRHMASSYLRPVLCTLDTTAAEVAARLLQLGHK-----GGGVVKVLGYG 226
Cdd:cd17213 1 GFIRVYDPDSPSDRSKLVPCTLETTAEDICKKLGISSLYlyvqlGGDHIRRLEPD 55
|
|
| RA_PHLPP_like |
cd01775 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
430-484 |
3.20e-08 |
|
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: 52.87 E-value: 3.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 430 QLHGETTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMdSEIGCLIRFYAGKP 484
Cdd:cd01775 46 LKHGGLVRRLRPDEKPLRIQRDLLLLLGYTDPDRQEEATN-PDLSYVIKFVFEKP 99
|
|
| PH |
cd00821 |
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
495-585 |
5.52e-08 |
|
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 275388 [Multi-domain] Cd Length: 92 Bit Score: 52.16 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 495 LSGMYNVRKGKmqlPVNRWTRRQVILCGTCLIVS-SVKDSVSGKMHVLPLIGG-KVEEVKKHQHCLAFSSSGPQSQTYYI 572
Cdd:cd00821 1 KEGYLLKRGGG---GLKSWKKRWFVLFEGVLLYYkSKKDSSYKPKGSIPLSGIlEVEEVSPKERPHCFELVTPDGRTYYL 77
|
90
....*....|...
gi 257467468 573 CFDTFTEYLRWLR 585
Cdd:cd00821 78 QADSEEERQEWLK 90
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
789-981 |
7.08e-08 |
|
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: 54.79 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 789 VTQLDLRDNKLGDLDAMI-FNNIEVLHCERNQLVTLnvcgyflKALYASSNeLAQLdvypvpnYLSymdvsRNCLESVpE 867
Cdd:cd21340 4 ITHLYLNDKNITKIDNLSlCKNLKVLYLYDNKITKI-------ENLEFLTN-LTHL-------YLQ-----NNQIEKI-E 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 868 WVCESRKLEVLDIGHNQICELpARLFCNSSLRKLLAGHNRLARlPERLE---------RTSVEVLDVQHNQITELPPnlL 938
Cdd:cd21340 63 NLENLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQRLPP-GEKLTfdprslaalSNSLRVLNISGNNIDSLEP--L 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 257467468 939 MKADSLRFLNASANKLETLPPATLSEETSSILQELYLTNNCLT 981
Cdd:cd21340 139 APLRNLEQLDASNNQISDLEELLDLLSSWPSLRELDLTGNPVC 181
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
645-791 |
2.40e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 55.59 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 645 RFTKLKSLNLSNNHL-GAFPSAVCSIPTLAELNVSCNALR-EVPAAVGDMQNLQTFLLDGNFLQS-LPAELES--MHqls 719
Cdd:PLN03150 440 KLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSGrVPAALGGrlLH--- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 720 ylGLSFNeFTD---------IPEVLEKLTAVDKLCMA-GNCVETL-----------RLQALRRMPHIKHVDLRLNILRKL 778
Cdd:PLN03150 517 --RASFN-FTDnaglcgipgLRACGPHLSVGAKIGIAfGVSVAFLflvicamcwwkRRQNILRAQRIAAREAPYAKARTH 593
|
170
....*....|...
gi 257467468 779 MADEVDFVQHVTQ 791
Cdd:PLN03150 594 FSRDVQMTRHHRQ 606
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
249-426 |
2.11e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 249 EPPPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGElfAGGPGSPPRAPRPASdtesfsLSPSAESVS 328
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR--AAQASSPPQRPRRRA------ARPTVGSLT 2696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 329 DRLDPYSSggggssssseelEADPAMPHRPGRPAQPRPPSPKTSALLQPKAPTGVDSTGVIAGEG-PGDDKAMAA----A 403
Cdd:PHA03247 2697 SLADPPPP------------PPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAtPGGPARPARppttA 2764
|
170 180
....*....|....*....|...
gi 257467468 404 APDVPLSTSGRIRETVQKTSPPS 426
Cdd:PHA03247 2765 GPPAPAPPAAPAAGPPRRLTRPA 2787
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
593-762 |
2.25e-06 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 52.47 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 593 QRISSVDLSCCSLEHLPAnlfysqDLTHLNLKQNFLRQTPTLPAarGLGEL----QRFTKLKSLNLSNNHLGAFPSAVCS 668
Cdd:PRK15387 305 QELSVSDNQLASLPALPS------ELCKLWAYNNQLTSLPTLPS--GLQELsvsdNQLASLPTLPSELYKLWAYNNRLTS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 669 IPTL----AELNVSCNALREVPAAVGDMQNLqtfLLDGNFLQSLPAELESMHQLSylgLSFNEFTDIPEVLEKLTAVDKL 744
Cdd:PRK15387 377 LPALpsglKELIVSGNRLTSLPVLPSELKEL---MVSGNRLTSLPMLPSGLLSLS---VYRNQLTRLPESLIHLSSETTV 450
|
170
....*....|....*...
gi 257467468 745 CMAGNCVETLRLQALRRM 762
Cdd:PRK15387 451 NLEGNPLSERTLQALREI 468
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
594-801 |
4.77e-06 |
|
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: 50.94 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 594 RISSVDLS-----CCSLEHLPANLFYSQDLTHLNLKQNFLrqtpTLPAARGLGE-LQRFTKLKSLNLSNNHLGaFPSAVC 667
Cdd:COG5238 237 SLTTLDLSnnqigDEGVIALAEALKNNTTVETLYLSGNQI----GAEGAIALAKaLQGNTTLTSLDLSVNRIG-DEGAIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 668 SIP------TLAELNVSCNALREVPAavgdmqnlqtflldgnflQSLPAELESMHQLSYLGLSFNEFTDIpevlekltAV 741
Cdd:COG5238 312 LAEglqgnkTLHTLNLAYNGIGAQGA------------------IALAKALQENTTLHSLDLSDNQIGDE--------GA 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257467468 742 DKLCmagncvetlrlQALRRMPHIKHVDLRLNILRKLMADEV-DFVQH--VTQLDLRDNKLGD 801
Cdd:COG5238 366 IALA-----------KYLEGNTTLRELNLGKNNIGKQGAEALiDALQTnrLHTLILDGNLIGA 417
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
746-1066 |
5.20e-06 |
|
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: 50.94 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 746 MAGNCVETLRLQALR-RMPHIKHVDLRLNILRKLMADEVDFVQHVTQLDLR-------DNKLGDLDAMIF--NNIEVLHC 815
Cdd:COG5238 70 DPGLNPVALEKAAEAfPTQLLVVDWEGAEEVSPVALAETATAVATPPPDLRrimaktlEDSLILYLALPRriNLIQVLKD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 816 E---RNQLVTLNVCGyfLKALYASSNELAQLDVYPVPNYLSYMDVSRNCLESVPEWVCESRKLEVLDIGHNQICELPARL 892
Cdd:COG5238 150 PlggNAVHLLGLAAR--LGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEI 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 893 FC-----NSSLRKLLAGHNR-----LARLPERLER-TSVEVLDVQHNQITE----LPPNLLMKADSLRFLNASANKLETL 957
Cdd:COG5238 228 LAealkgNKSLTTLDLSNNQigdegVIALAEALKNnTTVETLYLSGNQIGAegaiALAKALQGNTTLTSLDLSVNRIGDE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 958 PPATLSE--ETSSILQELYLTNNCLTDKCVPLLT----GHPRLKILHMAYNRLQSFPASKMAKLEE----LEEIDISGNK 1027
Cdd:COG5238 308 GAIALAEglQGNKTLHTLNLAYNGIGAQGAIALAkalqENTTLHSLDLSDNQIGDEGAIALAKYLEgnttLRELNLGKNN 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 257467468 1028 L---------KAIPTTimncrRMHTVIAHSNCIEVFPE---VMQLPEVKCV 1066
Cdd:COG5238 388 IgkqgaealiDALQTN-----RLHTLILDGNLIGAEAQqrlEQLLERIKSV 433
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
241-445 |
5.30e-06 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 51.61 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 241 DGEHGRDVEPPPSSGTVGAVRGPARAPPADLP-------LPGGAWTRCAPRISPAPS-DSSPGElfAGGPGS-----PPR 307
Cdd:PTZ00449 584 DPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPelldipkSPKRPESPKSPKRPPPPQrPSSPER--PEGPKIikspkPPK 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 308 APRPASD---TESF--SLSPSAESVSDRLDPYSSGGGGSSSSSEELEADPAMPH---RPGRPAQPRPPSPKTSALLQPKA 379
Cdd:PTZ00449 662 SPKPPFDpkfKEKFydDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFttpRPLPPKLPRDEEFPFEPIGDPDA 741
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257467468 380 PTGVDSTGVIAgegpgddkamaaaapdvPLSTSGRIRETVQKTSPPSLYVQL------HGETTRRLEADEKP 445
Cdd:PTZ00449 742 EQPDDIEFFTP-----------------PEEERTFFHETPADTPLPDILAEEfkeediHAETGEPDEAMKRP 796
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
241-426 |
6.72e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 51.33 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 241 DGEHGRDVEPPPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGELfAGGPGSPPRAPRPASDTESFSL 320
Cdd:PHA03307 106 PTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAV-ASDAASSRQAALPLSSPEETAR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 321 SPSAESVSDRLDPyssggggssssseELEADPAMPHRPGRPAQPRPPSPKTSALLQPKAPTGVDSTGVIAGEGPGDDKAM 400
Cdd:PHA03307 185 APSSPPAEPPPST-------------PPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGP 251
|
170 180
....*....|....*....|....*....
gi 257467468 401 AAAAPD---VPLSTSGRIRETVQKTSPPS 426
Cdd:PHA03307 252 ENECPLprpAPITLPTRIWEASGWNGPSS 280
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
593-659 |
8.41e-06 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 44.82 E-value: 8.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 257467468 593 QRISSVDLSCCSLEHLPANLFYS-QDLTHLNLKQNFLRqtpTLPAarglGELQRFTKLKSLNLSNNHL 659
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKGlSNLKVLDLSNNLLT---TLSP----GAFSGLPSLRYLDLSGNRL 61
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
232-436 |
9.72e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 232 APAASDQTLDGEHGRDVEPPPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSS--------PGELFA--GG 301
Cdd:PHA03247 2788 VASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlplggsvaPGGDVRrrPP 2867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 302 PGSPP------------RAPRPA--SDTESFSLSPSAESVSDRLDPYSSGGGGSSSSSEELEADPamPHRPGRPAQPRPP 367
Cdd:PHA03247 2868 SRSPAakpaaparppvrRLARPAvsRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP--PPPPPRPQPPLAP 2945
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257467468 368 SPKTSALLQPKAPTGVDSTG-VIAGEGPGDDKAMAAAAPDVPL---STSGRIRETVQKTSPPSLYVQLHGETT 436
Cdd:PHA03247 2946 TTDPAGAGEPSGAVPQPWLGaLVPGRVAVPRFRVPQPAPSREApasSTPPLTGHSLSRVSSWASSLALHEETD 3018
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
236-446 |
1.32e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.17 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 236 SDQTLDGEHGRDVEPPPSSGTVGAVRGPARAPPADLPLPGGawTRCAPRISPAPSDSSPGElfaGGPGSPPRAPRPASdt 315
Cdd:PHA03307 242 SESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP--GPASSSSSPRERSPSPSP---SSPGSGPAPSSPRA-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 316 eSFSLSPSAESVSDrldpyssGGGGSSSSSEELEADP-AMPHRPGRPAQPRPPSPKTSallQPKAPTGVDSTGVIAGEGP 394
Cdd:PHA03307 315 -SSSSSSSRESSSS-------STSSSSESSRGAAVSPgPSPSRSPSPSRPPPPADPSS---PRKRPRPSRAPSSPAASAG 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 257467468 395 gdDKAMAAAAPDVPLSTSGRIRETVQKTSPPSLYVQLHGETTRRLEADEKPL 446
Cdd:PHA03307 384 --RPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYARYPLL 433
|
|
| PTC1 |
COG0631 |
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms]; |
1309-1383 |
1.42e-05 |
|
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
Pssm-ID: 440396 [Multi-domain] Cd Length: 247 Bit Score: 48.28 E-value: 1.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 1309 PRPHVQSVLLTPQDeFFILGSKGLWDSLSIDEAVEAVRNVPDALAAAKKLCTLAQSYGCHDSISAVVVQLSVTED 1383
Cdd:COG0631 172 VEPDISPLELEPGD-RLLLCSDGLTDMVSDEEIAEILASAGDPQEAAEALIELALEAGGPDNITVVLVRVEDADA 245
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
829-1094 |
1.61e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 49.85 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 829 FLKALYASSNELA-QL--DVYPVPNYLSYMDVSRNCLE-SVPEWVCESrkLEVLDIGHNQIC-ELPARLFCNSSLRklla 903
Cdd:PLN00113 94 YIQTINLSNNQLSgPIpdDIFTTSSSLRYLNLSNNNFTgSIPRGSIPN--LETLDLSNNMLSgEIPNDIGSFSSLK---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 904 ghnrlarlperlertsveVLDVQHNQITELPPNLLMKADSLRFLNASANKLETLPPATLSEETSsiLQELYLTNNCLTDK 983
Cdd:PLN00113 168 ------------------VLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKS--LKWIYLGYNNLSGE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 984 CVPLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKLKA-IPTTIMNCRRMHTVIAHSNCIE-VFPE-VMQL 1060
Cdd:PLN00113 228 IPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGpIPPSIFSLQKLISLDLSDNSLSgEIPElVIQL 307
|
250 260 270
....*....|....*....|....*....|....*.
gi 257467468 1061 PEVKCVDLSCNELSEiTLPENLP--PKLQELDLTGN 1094
Cdd:PLN00113 308 QNLEILHLFSNNFTG-KIPVALTslPRLQVLQLWSN 342
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
592-709 |
2.67e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 49.08 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 592 SQRISSVDLSCCSL-EHLPANLFYSQDLTHLNLKQNFLrqTPTLPAarglgELQRFTKLKSLNLSNNHL-GAFPSAVCSI 669
Cdd:PLN00113 474 SKRLENLDLSRNQFsGAVPRKLGSLSELMQLKLSENKL--SGEIPD-----ELSSCKKLVSLDLSHNQLsGQIPASFSEM 546
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 257467468 670 PTLAELNVSCNALR-EVPAAVGDMQNLQTFLLDGNFLQ-SLP 709
Cdd:PLN00113 547 PVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHgSLP 588
|
|
| PBP1 |
COG5180 |
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ... |
242-425 |
3.66e-05 |
|
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];
Pssm-ID: 444064 [Multi-domain] Cd Length: 548 Bit Score: 48.52 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 242 GEHGRDVEPPPSSGTVGAVRGPARAPPADLP--LPGGAWTRCAPR-----------------ISPAPSDSSPGELFAGGP 302
Cdd:COG5180 286 GSEPQSDAPEAETARPIDVKGVASAPPATRPvrPPGGARDPGTPRpgqpterpagvpeaasdAGQPPSAYPPAEEAVPGK 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 303 GSPPRAPRPASdtesfSLSPSAesvsdrldPYSSGGGGSSSSSEELEA-DPAMPHRPGRPAQPRPPSPKTSALLQPKA-- 379
Cdd:COG5180 366 PLEQGAPRPGS-----SGGDGA--------PFQPPNGAPQPGLGRRGApGPPMGAGDLVQAALDGGGRETASLGGAAGga 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 257467468 380 -----PTGVD------STGVIAGEGPGDDKAMAAAAPDVPLSTSGRIRETVQKTSPP 425
Cdd:COG5180 433 gqgpkADFVPgdaesvSGPAGLADQAGAAASTAMADFVAPVTDATPVDVADVLGVRP 489
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
896-954 |
7.30e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 42.13 E-value: 7.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 896 SSLRKLLAGHNRLARLPERLER--TSVEVLDVQHNQITELPPNLLMKADSLRFLNASANKL 954
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKglSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
918-978 |
8.54e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.74 E-value: 8.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 918 TSVEVLDVQHNQITELPPNLLMKADSLRFLNASANKLETLPPATLSEETSsiLQELYLTNN 978
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPS--LRYLDLSGN 59
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
733-982 |
1.01e-04 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 46.19 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 733 EVLEKLTAVDKLCMAGNCVETLRLQALRRM----PHIKHVDLRLNILRKL---MADEVDFVQHVTQL---DLRDNKLGDL 802
Cdd:cd00116 17 ELLPKLLCLQVLRLEGNTLGEEAAKALASAlrpqPSLKELCLSLNETGRIprgLQSLLQGLTKGCGLqelDLSDNALGPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 803 DAMIFNNIevLHcernqlvtlnvcGYFLKALYASSNELAQLDV-------YPVPNYLSYMDVSRNCLESVPewvCES--- 872
Cdd:cd00116 97 GCGVLESL--LR------------SSSLQELKLNNNGLGDRGLrllakglKDLPPALEKLVLGRNRLEGAS---CEAlak 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 873 -----RKLEVLDIGHNQICELPARLFC-----NSSLRKLL--------AGHNRLARLPERLErtSVEVLDVQHNQIT--- 931
Cdd:cd00116 160 alranRDLKELNLANNGIGDAGIRALAeglkaNCNLEVLDlnnngltdEGASALAETLASLK--SLEVLNLGDNNLTdag 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 932 --ELPPNLLMKADSLRFLNASANKLETLPPATLSE--ETSSILQELYLTNNCLTD 982
Cdd:cd00116 238 aaALASALLSPNISLLTLSLSCNDITDDGAKDLAEvlAEKESLLELDLRGNKFGE 292
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
970-1028 |
1.02e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.74 E-value: 1.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 257467468 970 LQELYLTNNCLTDKCVPLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKL 1028
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| PLN03210 |
PLN03210 |
Resistant to P. syringae 6; Provisional |
605-881 |
1.61e-04 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 46.79 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 605 LEHLPANlFYSQDLTHLNLKQNFLRQtptlpaargLGE-LQRFTKLKSLNL--SNNhLGAFPSavCSIPT-LAELNVS-C 679
Cdd:PLN03210 601 LRCMPSN-FRPENLVKLQMQGSKLEK---------LWDgVHSLTGLRNIDLrgSKN-LKEIPD--LSMATnLETLKLSdC 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 680 NALREVPAAVGDMQNLQTFLLDG-NFLQSLPA--ELESMHQLSYLGLS-FNEFTDIPevleklTAVDKLCMAGNCVET-- 753
Cdd:PLN03210 668 SSLVELPSSIQYLNKLEDLDMSRcENLEILPTgiNLKSLYRLNLSGCSrLKSFPDIS------TNISWLDLDETAIEEfp 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 754 --LRLQALR--RMPHIKHVDL--RLNILRKLMAdevdFVQH-VTQLDLRDN-KLGDLDAMI--FNNIEVLHCER-NQLVT 822
Cdd:PLN03210 742 snLRLENLDelILCEMKSEKLweRVQPLTPLMT----MLSPsLTRLFLSDIpSLVELPSSIqnLHKLEHLEIENcINLET 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 823 LNVcGYFLKALYASS-NELAQLDVYP-VPNYLSYMDVSRNCLESVPEWVCESRKLEVLDIG 881
Cdd:PLN03210 818 LPT-GINLESLESLDlSGCSRLRTFPdISTNISDLNLSRTGIEEVPWWIEKFSNLSFLDMN 877
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
201-409 |
1.80e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.52 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 201 TAAEVAARLLQLGHKGGGVVKVLGYGPPPAAAPAASDQTLDGEHGRDVEPppssGTVGAVRGPARAPPADLPLPGGAWTR 280
Cdd:PRK07764 539 TVLGVRGDTLVLGFSTGGLARRFASPGNAEVLVTALAEELGGDWQVEAVV----GPAPGAAGGEGPPAPASSGPPEEAAR 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 281 CAPRISPAPSDSSPGELFAGGPGSPPRAPRPASDTESFSLSPSAESVSDRLDPYSSGGGGSSSSSEELEADPAMPHRPGR 360
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 257467468 361 PAQPRPPSPKTSAllQPKAPTGVDSTGVIAGEGPGDDKAMAAAAPDVPL 409
Cdd:PRK07764 695 GAAPAQPAPAPAA--TPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL 741
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
234-424 |
2.87e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 234 AASDQTL---------------DGEHGRDVEPPPSSGTV-GAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGE- 296
Cdd:PHA03247 2562 AAPDRSVppprpaprpsepavtSRARRPDAPPQSARPRApVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPh 2641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 297 --LFAGGPGSPPRAP-----RPASDTESFSLSPSAESVSDRLDPYSSGGGGSSSsseeleADPAMPHRPGRPAQPRPPsP 369
Cdd:PHA03247 2642 ppPTVPPPERPRDDPapgrvSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSL------TSLADPPPPPPTPEPAPH-A 2714
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 370 KTSALLQPKAPTGVDSTGVIAGEGPGDDKAMAAAAPDVPLSTSGRIRETVQKTSP 424
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAP 2769
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
242-369 |
4.06e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 45.36 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 242 GEHGRDVEPPPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGELFAGGPGSPPRAPRPASDTESFSLS 321
Cdd:PRK07764 652 HHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAP 731
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 257467468 322 PSAESVSDRLDPYSSGGGGSSSSSEELEADPAMPHRPGRPAQPRPPSP 369
Cdd:PRK07764 732 SPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
249-424 |
4.85e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 44.84 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 249 EPPPSSGTVGAVRGPA-RAPPADLPLPGGAWTRCAPRISPAPSDSSPGELFAGGPGSPPRAPRPASDTESFSLSPSAESV 327
Cdd:PRK07003 424 EAPPAAPAPPATADRGdDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 328 SDRLDPYSSGGGGSSSSSEELEADPAMPHRPGRPAQPRPPSPKTSAllqPKAPTGVDSTG--VIAGEGPGDDKAMAAAAP 405
Cdd:PRK07003 504 PAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGA---AAALDVLRNAGmrVSSDRGARAAAAAKPAAA 580
|
170
....*....|....*....
gi 257467468 406 DVPLSTSGRIRETVQKTSP 424
Cdd:PRK07003 581 PAAAPKPAAPRVAVQVPTP 599
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
238-427 |
5.65e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 45.08 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 238 QTLDGEHGRDVEPPPSSGTVGAVRGPARAPPADlplPGGAWTRCAPRISPAPSDSSPGELFAGGPGSPPRAPRPASDTES 317
Cdd:PRK10263 390 AVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYA---PAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQSTYQTEQ 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 318 FSLSPSAESVSDRLDPYSSGGGGSSSSSEELEADPAMP---------HRPGR--------------PAQ-PRPPSPKTSA 373
Cdd:PRK10263 467 TYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPplyyfeeveEKRARereqlaawyqpipePVKePEPIKSSLKA 546
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257467468 374 LLQPKAPtGVDSTGVIAGEGPGDDKAMAA-------AAPDVPLSTSGRIRETVQKTSPPSL 427
Cdd:PRK10263 547 PSVAAVP-PVEAAAAVSPLASGVKKATLAtgaaatvAAPVFSLANSGGPRPQVKEGIGPQL 606
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
511-592 |
6.78e-04 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 40.62 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 511 NRWTRRQVILCGTCLIV--SSVKDSVSGKMHVLPLIGGKVEEV-----KKHQHCLAFSSSGPQ-SQTYYICFDTFTEYLR 582
Cdd:pfam00169 16 KSWKKRYFVLFDGSLLYykDDKSGKSKEPKGSISLSGCEVVEVvasdsPKRKFCFELRTGERTgKRTYLLQAESEEERKD 95
|
90
....*....|
gi 257467468 583 WLRQVSKVAS 592
Cdd:pfam00169 96 WIKAIQSAIR 105
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
593-773 |
6.79e-04 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 42.85 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 593 QRISSVDL--SCCSLEHLPA---------NLFYSQDLTHLNLKQNFLRQtptlpaargLGELQRFTKLKSLNLSNNHLga 661
Cdd:cd21340 12 KNITKIDNlsLCKNLKVLYLydnkitkieNLEFLTNLTHLYLQNNQIEK---------IENLENLVNLKKLYLGGNRI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 662 fpSAVC---SIPTLAELNVSCNAL-REVP--------AAVGDmqNLQTFLLDGNFLQSLpAELESMHQLSYLGLSFNEFT 729
Cdd:cd21340 81 --SVVEgleNLTNLEELHIENQRLpPGEKltfdprslAALSN--SLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQIS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 257467468 730 DIPEVlekltavdklcmagncvetlrLQALRRMPHIKHVDLRLN 773
Cdd:cd21340 156 DLEEL---------------------LDLLSSWPSLRELDLTGN 178
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
250-381 |
8.84e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 44.37 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 250 PPPSSGTVGAVRGPARAPPADLPlpgGAWTRCAPRISPAP----SDSSPGELFAGGPG-SPPRAPRPASDTESFSLSPSA 324
Cdd:pfam03154 182 SPPSPPPPGTTQAATAGPTPSAP---SVPPQGSPATSQPPnqtqSTAAPHTLIQQTPTlHPQRLPSPHPPLQPMTQPPPP 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 257467468 325 ESVSDRLDPYSSGGGGSSSSSEELEADPA-MPHrPGrPAQPRPPSPKTSALLQPKAPT 381
Cdd:pfam03154 259 SQVSPQPLPQPSLHGQMPPMPHSLQTGPShMQH-PV-PPQPFPLTPQSSQSQVPPGPS 314
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
920-1108 |
1.02e-03 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 44.07 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 920 VEVLDVQHNQIT-ELPPNLLMKADSLRFLNASANK------------LETLPPAT--LSEETS------SILQELYLTNN 978
Cdd:PLN00113 95 IQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNNftgsiprgsipnLETLDLSNnmLSGEIPndigsfSSLKVLDLGGN 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 979 CLTDKCVPLLTGHPRLKILHMAYNRLQSFPASKMAKLEELEEIDISGNKLKA-IPTTIMNCRRM-HTVIAHSNCI-EVFP 1055
Cdd:PLN00113 175 VLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGeIPYEIGGLTSLnHLDLVYNNLTgPIPS 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 1056 EVMQLPEVKCVDLSCNELSeitlpENLPP------KLQELDLTGN------PRLALDHKSLELLN 1108
Cdd:PLN00113 255 SLGNLKNLQYLFLYQNKLS-----GPIPPsifslqKLISLDLSDNslsgeiPELVIQLQNLEILH 314
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
249-407 |
1.29e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 43.68 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 249 EPPPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGELFAGGPGSPPRAPRPASD--TESFSLSPSAES 326
Cdd:PRK07003 408 AALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADsgSASAPASDAPPD 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 327 VSDRLDPYSSGGGGSSSSSEELEADPAMPHRPGRPAQPRPPSPKTSallqPKAPtgvdstgviAGEGPGDDKAMAAAAPD 406
Cdd:PRK07003 488 AAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEAR----PPTP---------AAAAPAARAGGAAAALD 554
|
.
gi 257467468 407 V 407
Cdd:PRK07003 555 V 555
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
251-414 |
1.39e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 251 PPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPS----DSSPGELFAGGPGSPPRAPRPASDTESFSLSPSAES 326
Cdd:PHA03307 777 PAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTAskrkSRSHTPDGGSESSGPARPPGAAARPPPARSSESSKS 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 327 VSDRLDPyssggggssSSSEELEADPAMPHRPgrPAQPRPPSPKTSALLQPKAPtgvdstgviageGPGDDKAMAAAAPD 406
Cdd:PHA03307 857 KPAAAGG---------RARGKNGRRRPRPPEP--RARPGAAAPPKAAAAAPPAG------------APAPRPRPAPRVKL 913
|
....*...
gi 257467468 407 VPLSTSGR 414
Cdd:PHA03307 914 GPMPPGGP 921
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
249-414 |
1.39e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.62 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 249 EPPPSSGTvgAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGElfaggpgSPPRAPRPASDTEsfslSPSAESVS 328
Cdd:PHA03307 70 GPPPGPGT--EAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-------PPPPTPPPASPPP----SPAPDLSE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 329 DRLDPYSSGGGGSSSSSEELEADPAMPHRPGRPAQPRPPSPKTSALLQ----PKAPTGVDSTGVIAGEGPGDDKAMAAAA 404
Cdd:PHA03307 137 MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARapssPPAEPPPSTPPAAASPRPPRRSSPISAS 216
|
170
....*....|
gi 257467468 405 PDVPLSTSGR 414
Cdd:PHA03307 217 ASSPAPAPGR 226
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
604-823 |
1.43e-03 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 43.61 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 604 SLEHLPAnlfYSQDLTHLNLKQNFLRQTPTLPAarGLGELQRFTKLKSlnlsnnHLGAFPSAVCSI-------------- 669
Cdd:PRK15387 233 NLTSLPA---LPPELRTLEVSGNQLTSLPVLPP--GLLELSIFSNPLT------HLPALPSGLCKLwifgnqltslpvlp 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 670 PTLAELNVSCNALREVPAAVGDMQNLQTFlldGNFLQSLPAELESMHQLSYLGLSFNEFTDIPEVLEKLTAVDKlcmagn 749
Cdd:PRK15387 302 PGLQELSVSDNQLASLPALPSELCKLWAY---NNQLTSLPTLPSGLQELSVSDNQLASLPTLPSELYKLWAYNN------ 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257467468 750 cvetlRLQALRRMPH-IKHVDLRLNILRKLMAdevdFVQHVTQLDLRDNKLGDLdAMIFNNIEVLHCERNQLVTL 823
Cdd:PRK15387 373 -----RLTSLPALPSgLKELIVSGNRLTSLPV----LPSELKELMVSGNRLTSL-PMLPSGLLSLSVYRNQLTRL 437
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
512-592 |
3.54e-03 |
|
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.
Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 38.68 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 512 RWTRRQVILCGTCLIVSSVKDSVSGKM--HVLPLIGGKVEEV-----KKHQHClaFSSSGPQSQTYYICFDTFTEYLRWL 584
Cdd:smart00233 17 SWKKRYFVLFNSTLLYYKSKKDKKSYKpkGSIDLSGCTVREApdpdsSKKPHC--FEIKTSDRKTLLLQAESEEEREKWV 94
|
....*...
gi 257467468 585 RQVSKVAS 592
Cdd:smart00233 95 EALRKAIA 102
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
249-426 |
3.80e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 249 EPPPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDS---SPGELFAGGPGSPPRAPRPASDTESFSLSPSAE 325
Cdd:PRK07764 622 AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGgdgWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQP 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 326 SvsdrldpyssggggssssseeleADPAMPHRPGRPAQPRPPSPKTSAllQPKAPTGVDSTGVIAGEGPGDDKAMAAAAP 405
Cdd:PRK07764 702 A-----------------------PAPAATPPAGQADDPAAQPPQAAQ--GASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
|
170 180
....*....|....*....|.
gi 257467468 406 DVPLSTSGRIRETVQKTSPPS 426
Cdd:PRK07764 757 QPPPPPAPAPAAAPAAAPPPS 777
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
250-411 |
4.12e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 250 PPPSSGTVGAVRGPARAPPAdlplPGGAWTRCAPRISPAPSDSSPGELFAGGPGSPPRAPRPASDTESFSLSPSAESVSD 329
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSS----PGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 330 RLDPYSSGGGgssssseeleADPAMPHRPGRPAQPRPPSPKTSALLQPKAP----TGVDSTGVIAGEGPGDDKAMAAAAP 405
Cdd:PHA03307 359 PADPSSPRKR----------PRPSRAPSSPAASAGRPTRRRARAAVAGRARrrdaTGRFPAGRPRPSPLDAGAASGAFYA 428
|
....*.
gi 257467468 406 DVPLST 411
Cdd:PHA03307 429 RYPLLT 434
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
1061-1109 |
4.15e-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: 36.84 E-value: 4.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 257467468 1061 PEVKCVDLSCNELSEITLPENLPpKLQELDLTGNPRLaldhKSLELLNN 1109
Cdd:pfam12799 1 PNLEVLDLSNNQITDIPPLAKLP-NLETLDLSGNNKI----TDLSDLAN 44
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
250-406 |
4.73e-03 |
|
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.
Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 41.29 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 250 PPPSSGTVGAVRGPARappaDL--PLPGGAWTRCA--PRISPAPSDSSPGELfaGGPGSPPRAPRPASDTESfSLSPSAE 325
Cdd:NF040712 170 PGAHGGTVTALDDEAR----WLidPDFGRPLRPLAtvPRLAREPADARPEEV--EPAPAAEGAPATDSDPAE-AGTPDDL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 326 SVSDRLDPYSSGGGGSSSSSEELEADPAMPHRPGRPAQPRPPSPKTSALLQPKAPTGVDSTGVIAGEGPGDDKAMAAAAP 405
Cdd:NF040712 243 ASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAP 322
|
.
gi 257467468 406 D 406
Cdd:NF040712 323 K 323
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
233-426 |
5.00e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 233 PAasdqTLDGEHGRDVEPPPSSGTVGAV--RGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGELFAGGPGS------ 304
Cdd:PHA03247 2747 GP----ATPGGPARPARPPTTAGPPAPAppAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAalppaa 2822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 305 -------PPRAPRPASDTESFSLSPSAESVSDRLDPysSGGGGSSSSSEELEADPAMPHRP--GRPAQPrPPSPKTSALL 375
Cdd:PHA03247 2823 spagplpPPTSAQPTAPPPPPGPPPPSLPLGGSVAP--GGDVRRRPPSRSPAAKPAAPARPpvRRLARP-AVSRSTESFA 2899
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 257467468 376 QPKAPTGVDSTGVIAGEGPGDDKAMAAAAPDVPLSTSGRIRETVQKTSPPS 426
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPA 2950
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
693-749 |
5.06e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 37.12 E-value: 5.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 257467468 693 QNLQTFLLDGNFLQSLPAE-LESMHQLSYLGLSFNEFTDI-PEVLEKLTAVDKLCMAGN 749
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGN 59
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
252-382 |
5.22e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 252 PSSGTVGAVRGPARApPADLPLPGGAWTRcAPRISPAPSDSSPGELFAGGPGSPPRAPRPASDTESFSLSPSAESVSDRL 331
Cdd:PHA03378 686 PIQWAPGTMQPPPRA-PTPMRPPAAPPGR-AQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGR 763
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 257467468 332 DPYSSGGGGSSSSSEELEADPAMPHRP-GRPA-QPRPPSPKTSALLQPKAPTG 382
Cdd:PHA03378 764 ARPPAAAPGAPTPQPPPQAPPAPQQRPrGAPTpQPPPQAGPTSMQLMPRAAPG 816
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
250-405 |
5.85e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.37 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 250 PPPSSGTVGAVRGPARAPPADLPLPGGAWTRCAPRISPAPSDSSPGElfAGGPGSPPRAPRPASDTESF-------SLSP 322
Cdd:PRK07003 373 PARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAA--ATRAEAPPAAPAPPATADRGddaadgdAPVP 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 323 SAESVSDRLDPYSSGGGGSSSSSEELEADPAMPhrpGRPAQPRPPSPkTSALLQPKAPTGVDSTGVIAGEGPGDDKAMAA 402
Cdd:PRK07003 451 AKANARASADSRCDERDAQPPADSGSASAPASD---APPDAAFEPAP-RAAAPSAATPAAVPDARAPAAASREDAPAAAA 526
|
...
gi 257467468 403 AAP 405
Cdd:PRK07003 527 PPA 529
|
|
| PHA03381 |
PHA03381 |
tegument protein VP22; Provisional |
193-330 |
6.36e-03 |
|
tegument protein VP22; Provisional
Pssm-ID: 177618 [Multi-domain] Cd Length: 290 Bit Score: 40.76 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 193 PVLCTLDTTAAEVAARLLQLGHKGGGVVKVLGYGPPPAAAPAASDQTLDGEHGRDVEPP--PSSGTVGAVRGPARAPpad 270
Cdd:PHA03381 32 PARVSFEEPADRARRGAGQARGRSQAERRFHHYDEARADYPYYTGSSSEDERPADPRPSrrPHAQPEASGPGPARGA--- 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 257467468 271 lplPGGAWTRCAPRISPAPSDSSPGELFAggpGSPPRAPRPASDTESFSLSPSAESVSDR 330
Cdd:PHA03381 109 ---RGPAGSRGRGRRAESPSPRDPPNPKG---ASAPRGRKSACADSAALLDAPAPAAPKR 162
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
970-1004 |
6.41e-03 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 36.07 E-value: 6.41e-03
10 20 30
....*....|....*....|....*....|....*
gi 257467468 970 LQELYLTNNCLTDkcVPLLTGHPRLKILHMAYNRL 1004
Cdd:pfam12799 3 LEVLDLSNNQITD--IPPLAKLPNLETLDLSGNNK 35
|
|
| RA_CYR1_like |
cd17214 |
Ras-associating (RA) domain found in Saccharomyces cerevisiae adenylate cyclase and similar ... |
427-479 |
7.77e-03 |
|
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: 37.58 E-value: 7.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 257467468 427 LYVQLHGeTTRRLEADEKPLQIQNDYLFQLGFGELWRVQEEGMDsEIGCLIRF 479
Cdd:cd17214 44 LYLRERG-LERILRSNEKPLLIQKRLLLQAGYTELDGLEEIGRE-DNSYLCRF 94
|
|
| |
