|
Name |
Accession |
Description |
Interval |
E-value |
| PH_PHLPP-like |
cd13322 |
PH domain leucine-rich repeat protein phosphatase family Pleckstrin homology-like domain; The ... |
535-631 |
5.54e-61 |
|
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: 203.21 E-value: 5.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 535 ERIQLSGMYNVRKGKMQLpvNRWTRRQVILCGTCLIVSSVKDSLTGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTY 614
Cdd:cd13322 1 ERILLSGIYNVRKGKTQL--HKWAERQVILCGTCLIVSSVKDSQTGKMHILPLVGGKVEEVKRRQHCLAFSSAGPQAQTY 78
|
90
....*....|....*..
gi 291219891 615 YICFDTFTEYLRWLRQV 631
Cdd:cd13322 79 YVSFDTLAEYQRWHRQA 95
|
|
| PP2Cc |
smart00332 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1168-1420 |
4.22e-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: 204.15 E-value: 4.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1168 SGAPAVWSHGYTEASGVKNKLCVAALSVNNFCDNrEALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE----EEYM 1243
Cdd:smart00332 3 SGKNLGLRYGLSSMQGVRKPMEDAHVITPDLSDS-GGFFGVFDGHGGSEAAKFLSKNLPEILAEELIKEKDEledvEEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1244 VNTFIVMQRKLGTAGQKLGGA-AVLCHIKHDpvdpggsfTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQH 1322
Cdd:smart00332 82 RKAFLSTDEEILEELEALSGStAVVALISGN--------KLYVANVGDSRAVLCRNGKAVQLTEDHKPSNEDERARIEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1323 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNVP--DALAAAK 1400
Cdd:smart00332 154 GGFV-INGRVNGVLALSRAIGDFFLKPYVSAEPDVTVVELTEKDDFLILASDGLWDVLSNQEVVDIVRKHLskDPKEAAK 232
|
250 260
....*....|....*....|
gi 291219891 1401 KLCTLAQSYGCHDSISAVVV 1420
Cdd:smart00332 233 RLIDLALARGSKDNITVVVV 252
|
|
| PP2Cc |
cd00143 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1174-1422 |
4.99e-57 |
|
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 238083 [Multi-domain] Cd Length: 254 Bit Score: 198.32 E-value: 4.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1174 WSHGYTEASGVKNKLCVAALSVNNFCDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE-----EEYMVNTFI 1248
Cdd:cd00143 1 FSAGVSDKGGDRKTNEDAVVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLseediEEALRKAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1249 VMQRKLGTAGQKL------GGAAVLCHIKHDpvdpggsfTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQH 1322
Cdd:cd00143 81 RADEEILEEAQDEpddarsGTTAVVALIRGN--------KLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEEERERIEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1323 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNVP---DALAAA 1399
Cdd:cd00143 153 GGRV-SNGRVPGVLAVTRALGDFDLKPGVSAEPDVTVVKLTEDDDFLILASDGLWDVLSNQEAVDIVRSELakeDLQEAA 231
|
250 260
....*....|....*....|...
gi 291219891 1400 KKLCTLAQSYGCHDSISAVVVQL 1422
Cdd:cd00143 232 QELVDLALRRGSHDNITVVVVRL 254
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
637-898 |
7.53e-35 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 139.30 E-value: 7.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 637 QRISSVDLSCCSlehlpaNLFYSQDLTHLNLKQNFLRqnpSLPAarglnELQRFTKLKSLNLSNNHLGDFPLAVCSIPTL 716
Cdd:COG4886 96 TNLTELDLSGNE------ELSNLTNLESLDLSGNQLT---DLPE-----ELANLTNLKELDLSNNQLTDLPEPLGNLTNL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 717 AELNVSCNALRSVPAAVGVMHNLQTFLLDGNFLQSLPAELENMKQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMSGNCVE 796
Cdd:COG4886 162 KSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 797 TLRlqALRKMPHIKHVDLRLNVIRKLiaDEVDFLQHVTQLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTLDICGYFLKA 876
Cdd:COG4886 242 DLP--ELGNLTNLEELDLSNNQLTDL--PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
|
250 260
....*....|....*....|..
gi 291219891 877 LYASSNELVQLDVYPVPNYLSY 898
Cdd:COG4886 318 LLLTTLLLLLLLLKGLLVTLTT 339
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
471-528 |
4.00e-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: 123.40 E-value: 4.00e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 471 LYVQLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 528
Cdd:cd17240 33 LQLQLHGETVRRLEPHEKPLQIQNDYLFQLGFGDLWRVQEEGMDPEIGCLIRFYAGKP 90
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
952-1154 |
1.19e-32 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 132.75 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 952 LARLPERLERTSVEVLDVQHNQLLELPPNLLmKADSLRFLNASANKLESLPPAtLSEETNsiLQELYLTNNSLTDkcVPL 1031
Cdd:COG4886 103 LSGNEELSNLTNLESLDLSGNQLTDLPEELA-NLTNLKELDLSNNQLTDLPEP-LGNLTN--LKSLDLSNNQLTD--LPE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1032 -LTGHPHLKILHMAYNRLQSFPASkMAKLEELEEIDLSGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVMQLPEIKCV 1110
Cdd:COG4886 177 eLGNLTNLKELDLSNNQITDLPEP-LGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEEL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 291219891 1111 DLSCNELSEVTLPENLpPKLQELDLTGNPRLVLDHKTLELLNNI 1154
Cdd:COG4886 256 DLSNNQLTDLPPLANL-TNLKTLDLSNNQLTDLKLKELELLLGL 298
|
|
| PP2C |
pfam00481 |
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ... |
1174-1415 |
1.83e-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: 121.67 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1174 WSHGYTEASGVKNKLCVAALSVNNFC----DNREALYGVFDGDRNVEVPYLLQCTMSDILAE--ELQKTKNEEEYMVNTF 1247
Cdd:pfam00481 1 IDLGGPRMQGWRKSMEDAHIDLPNLNsssgKDSWSFFAVFDGHGGSEAAKYCGKHLHTILALrrSFLEGEKLEDALRKSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1248 I----VMQRKLGTAGQKLGGAAVLCHIKHDpvdpggsfTLTSANVGKCQTVLCRNGKP-LPLSRSYIMSCEEELKRIKQH 1322
Cdd:pfam00481 81 LedtdEVLRSAEKEDLDSGCTAVVALISGN--------KLYVANVGDSRAVLCRNGNAiKRLTKDHKPSDEDERRRIRAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1323 KAIITEDGKVNGVTESTRILGYTFLHPS---VVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNV----PDA 1395
Cdd:pfam00481 153 GGFVSRNGRVNGVLAVSRAFGDFELKPGeqaVSAEPDITSHTITEDDEFLILACDGLWDVLSDQEVVDLVRSElsdgGSP 232
|
250 260
....*....|....*....|
gi 291219891 1396 LAAAKKLCTLAQSYGCHDSI 1415
Cdd:pfam00481 233 MEAAEELRDEAIAYGSEDNI 252
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
639-1126 |
1.32e-25 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 115.72 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 639 ISSVDLSCCSLE-HLPANLFY-SQDLTHLNLKQNflrqNPSLPAARGLnelqrFTKLKSLNLSNNHL-GDFPLAVCSIPT 715
Cdd:PLN00113 95 IQTINLSNNQLSgPIPDDIFTtSSSLRYLNLSNN----NFTGSIPRGS-----IPNLETLDLSNNMLsGEIPNDIGSFSS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 716 LAELNVSCNALRS-VPAAVGVMHNLQTFLLDGN-FLQSLPAELENMKQLSYLGLSFNEFT-DIPEVLEKLTAVDKLCMSG 792
Cdd:PLN00113 166 LKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNqLVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 793 NCVETLRLQALRKMPHIKHVDLRLNVIRKLIADEVDFLQHVTQLDLRDNKL-GDLDAMI--FNNIEVLHcernqLVTLDI 869
Cdd:PLN00113 246 NNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLsGEIPELViqLQNLEILH-----LFSNNF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 870 CGYFLKALyassNELVQLDVypvpnylsyMDVSRNRLE-NVPEWVCESRKLEVLDIGHNQIC-ELPARLfCNS-SLRKLL 946
Cdd:PLN00113 321 TGKIPVAL----TSLPRLQV---------LQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTgEIPEGL-CSSgNLFKLI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 947 AGHNQL-ARLPERLER-TSVEVLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNsiLQELYLTNNSL 1024
Cdd:PLN00113 387 LFSNSLeGEIPKSLGAcRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPS--LQMLSLARNKF 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1025 TDKcVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKLKA-IPTTIMNCRRMHTV-IAHSNCIEVFPEVM 1102
Cdd:PLN00113 465 FGG-LPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLdLSHNQLSGQIPASF 543
|
490 500
....*....|....*....|....*
gi 291219891 1103 -QLPEIKCVDLSCNELSEvTLPENL 1126
Cdd:PLN00113 544 sEMPVLSQLDLSQNQLSG-EIPKNL 567
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
901-1138 |
1.65e-18 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 92.07 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 901 VSRNRLENVPEWVCESRKLEVLDigHNQICELPARLFCNssLRKLLAGHNQLARLPERLERTsVEVLDVQHNQLLELPPN 980
Cdd:PRK15370 185 LKILGLTTIPACIPEQITTLILD--NNELKSLPENLQGN--IKTLYANSNQLTSIPATLPDT-IQEMELSINRITELPER 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 981 LlmkADSLRFLNASANKLESLPPaTLSEEtnsiLQELYLTNNSLTDKCVPLLTGHPHLKILHmayNRLQSFPASKMAKLE 1060
Cdd:PRK15370 260 L---PSALQSLDLFHNKISCLPE-NLPEE----LRYLSVYDNSIRTLPAHLPSGITHLNVQS---NSLTALPETLPPGLK 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 1061 ELEEIDlsgNKLKAIPTTIMNCRRMHTViaHSNCIEVFPEVMQlPEIKCVDLSCNELseVTLPENLPPKLQELDLTGN 1138
Cdd:PRK15370 329 TLEAGE---NALTSLPASLPPELQVLDV--SKNQITVLPETLP-PTITTLDVSRNAL--TNLPENLPAALQIMQASRN 398
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
202-244 |
1.48e-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: 70.63 E-value: 1.48e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 291219891 202 GCVHVFDRHMaSTYLRPVLCTLDTTAGEVAARLLQLGHKGGGV 244
Cdd:cd17240 1 GCIHVYDRHM-SSYLRPVLCTLDTTASEVAARLLQLQLHGETV 42
|
|
| PLN03145 |
PLN03145 |
Protein phosphatase 2c; Provisional |
1282-1420 |
7.30e-13 |
|
Protein phosphatase 2c; Provisional
Pssm-ID: 215603 [Multi-domain] Cd Length: 365 Bit Score: 72.25 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1282 TLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQHKAIItEDGKVNGVTESTRILGYTFLH-------PSVVPR 1354
Cdd:PLN03145 179 SLVVANAGDCRAVLCRRGKAIEMSRDHKPMCSKERKRIEASGGYV-YDGYLNGQLNVARALGDWHMEgmkgsdgGPLSAE 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1355 PHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNV----PDALAAAKKLCTLAQSYGCHDSISAVVV 1420
Cdd:PLN03145 258 PELMTTQLTEEDEFLIIGCDGIWDVFRSQNAVDFARRRlqehNDPVMCSKELVDEALKRKSGDNLAVVVV 327
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
625-929 |
8.03e-11 |
|
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: 65.45 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 625 LRWLRQVSKVasQRISSVDLSCCSL--EHLPA---NLFYSQDLTHLNLKQNFLRQNPSLPAARGLNeLQRFTKLKSLNLS 699
Cdd:cd00116 13 ERATELLPKL--LCLQVLRLEGNTLgeEAAKAlasALRPQPSLKELCLSLNETGRIPRGLQSLLQG-LTKGCGLQELDLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 700 NNHLGD----FPLAVCSIPTLAELNVSCNALRSVPAAvgvmhnlqtFLLDGnfLQSLPAELENMkQLSYLGLSFNEFTDI 775
Cdd:cd00116 90 DNALGPdgcgVLESLLRSSSLQELKLNNNGLGDRGLR---------LLAKG--LKDLPPALEKL-VLGRNRLEGASCEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 776 PEVLEKLTAVDKLCMSGNCV-----ETLrLQALRKMPHIKHVDLRLNVIR----KLIADEVDFLQHVTQLDLRDNKLGDL 846
Cdd:cd00116 158 AKALRANRDLKELNLANNGIgdagiRAL-AEGLKANCNLEVLDLNNNGLTdegaSALAETLASLKSLEVLNLGDNNLTDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 847 DAMIFNnievlhcerNQLVTLDICgyfLKALYASSNELVQLDVYPVPNYLS------YMDVSRNRL------ENVPEWVC 914
Cdd:cd00116 237 GAAALA---------SALLSPNIS---LLTLSLSCNDITDDGAKDLAEVLAekesllELDLRGNKFgeegaqLLAESLLE 304
|
330
....*....|....*
gi 291219891 915 ESRKLEVLDIGHNQI 929
Cdd:cd00116 305 PGNELESLWVKDDSF 319
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-444 |
1.63e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.42 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 273 PPEPR------DSEVPPARSAPGAFGGPPRAPPADLPLPVGG--PGGWSRRASPA-----PSDSSPGEPFVGGPvssPRA 339
Cdd:PHA03247 2707 TPEPAphalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPatPGGPARPARPPttagpPAPAPPAAPAAGPP---RRL 2783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 340 PRPVVSdtesfSLSPSAESVSDRLDPYSSGGGSsssseeLEADAASAPTGVPGQPRRPGHPAQPLPlPQTASSPQPQQKA 419
Cdd:PHA03247 2784 TRPAVA-----SLSESRESLPSPWDPADPPAAV------LAPAAALPPAASPAGPLPPPTSAQPTA-PPPPPGPPPPSLP 2851
|
170 180
....*....|....*....|....*
gi 291219891 420 PRAIDSPGGAVREGSCEEKAAAAVA 444
Cdd:PHA03247 2852 LGGSVAPGGDVRRRPPSRSPAAKPA 2876
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
996-1153 |
5.21e-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: 55.18 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 996 NKLESLPPatLSEETNsiLQELYLTNNSLTdkCVPLLTGHPHLKILHMAYNRLqsfpaSKMA---KLEELEEIDLSGNKL 1072
Cdd:cd21340 34 NKITKIEN--LEFLTN--LTHLYLQNNQIE--KIENLENLVNLKKLYLGGNRI-----SVVEgleNLTNLEELHIENQRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1073 KAIPTTIMNCRRMHTV--------IAHSN-----CIEVFPEVMQLpeikcvDLSCNELS---EVTLPENLPPKLQELDLT 1136
Cdd:cd21340 103 PPGEKLTFDPRSLAALsnslrvlnISGNNidslePLAPLRNLEQL------DASNNQISdleELLDLLSSWPSLRELDLT 176
|
170 180
....*....|....*....|....*.
gi 291219891 1137 GNP---------RLVLDHKTLELLNN 1153
Cdd:cd21340 177 GNPvckkpkyrdKIILASKSLEVLDG 202
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1014-1072 |
3.37e-07 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 48.67 E-value: 3.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 291219891 1014 LQELYLTNNSLTDKCVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKL 1072
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-444 |
4.33e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 51.53 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 2 EPAAAATVQRLPELGREDRASAPAAAAAAAAAaaaaaaalaaaAGGGRSPEPALTPAAPSGGNGSGSGAREEAPGEAPPG 81
Cdd:PRK07764 368 SDDERGLLARLERLERRLGVAGGAGAPAAAAP-----------SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 82 PLPGRAGGAGRRRRRGAPQPIAGGAAPVPGAGGGANSlllrrgrlkrnlsaaaAAASSSSSSSAAAASHSPGAAGLPASC 161
Cdd:PRK07764 437 PAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA----------------PEPTAAPAPAPPAAPAPAAAPAAPAAP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 162 SASASlctrSLDRKTLLLKHRQTLQLQPSD-RDWVRHQLQRGCVHVFDrhmastylRPVLcTLDTTAGEVAARLLQLGHK 240
Cdd:PRK07764 501 AAPAG----ADDAATLRERWPEILAAVPKRsRKTWAILLPEATVLGVR--------GDTL-VLGFSTGGLARRFASPGNA 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 241 G----------GGVVKVL----GQGPGAAAAREPAEPPPEAGPRLAPPEPRDSEVPPARSAPGAFGGPPRAPP------- 299
Cdd:PRK07764 568 EvlvtalaeelGGDWQVEavvgPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASaapapgv 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 300 ---------ADLPLPVGGPGGWSRRA----------SPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVS 360
Cdd:PRK07764 648 aapehhpkhVAVPDASDGGDGWPAKAggaapaapppAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 361 DRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGScEEKAA 440
Cdd:PRK07764 728 ASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDA-EEVAM 806
|
....
gi 291219891 441 AAVA 444
Cdd:PRK07764 807 ELLE 810
|
|
| PTC1 |
COG0631 |
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms]; |
1353-1427 |
8.71e-06 |
|
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
Pssm-ID: 440396 [Multi-domain] Cd Length: 247 Bit Score: 49.05 E-value: 8.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291219891 1353 PRPHVQSVLLTPQDeFFILGSKGLWDSLSVEEAVEAVRNVPDALAAAKKLCTLAQSYGCHDSISAVVVQLSVTED 1427
Cdd:COG0631 172 VEPDISPLELEPGD-RLLLCSDGLTDMVSDEEIAEILASAGDPQEAAEALIELALEAGGPDNITVVLVRVEDADA 245
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
637-703 |
1.07e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 44.44 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 637 QRISSVDLSCCSLEHLPANLFYS-QDLTHLNLKQNFLRqnpSLPAarglNELQRFTKLKSLNLSNNHL 703
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKGlSNLKVLDLSNNLLT---TLSP----GAFSGLPSLRYLDLSGNRL 61
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
555-636 |
7.99e-04 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 40.62 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 555 NRWTRRQVILCGTCLIVSSVKDSLTGK--MHVLPLIGGKVEEV-----KKHQHCLAFSSSGPQ-SQTYYICFDTFTEYLR 626
Cdd:pfam00169 16 KSWKKRYFVLFDGSLLYYKDDKSGKSKepKGSISLSGCEVVEVvasdsPKRKFCFELRTGERTgKRTYLLQAESEEERKD 95
|
90
....*....|
gi 291219891 627 WLRQVSKVAS 636
Cdd:pfam00169 96 WIKAIQSAIR 105
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
272-422 |
1.50e-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: 42.83 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPRDSEVPPARSAPGAfggPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFS 351
Cdd:NF040712 193 GRPLRPLATVPRLAREPAD---ARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAE 269
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291219891 352 LSPSAEsvsdrlDPYSSGGGSSSSSEELEADAASAPTgVPGQPRRPGHPAQPLPLPQTAssPQPQQKAPRA 422
Cdd:NF040712 270 PDEATR------DAGEPPAPGAAETPEAAEPPAPAPA-APAAPAAPEAEEPARPEPPPA--PKPKRRRRRA 331
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
556-636 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 556 RWTRRQVILCGTCLIVSSVKDSLTGKM--HVLPLIGGKVEEV-----KKHQHClaFSSSGPQSQTYYICFDTFTEYLRWL 628
Cdd:smart00233 17 SWKKRYFVLFNSTLLYYKSKKDKKSYKpkGSIDLSGCTVREApdpdsSKKPHC--FEIKTSDRKTLLLQAESEEEREKWV 94
|
....*...
gi 291219891 629 RQVSKVAS 636
Cdd:smart00233 95 EALRKAIA 102
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
271-425 |
4.49e-03 |
|
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: 42.06 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 271 LAPPEPRDSEVPPARSAPGAfGGPPRA---PPADLPLPVGGPggwsRRASPAPSDSSPGE----PFVGGP----VSSPRA 339
Cdd:pfam03154 317 APGQSQQRIHTPPSQSQLQS-QQPPREqplPPAPLSMPHIKP----PPTTPIPQLPNPQShkhpPHLSGPspfqMNSNLP 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 340 PRPVVSDTESFSL--SPSAE-------SVSDRLDPYSSGGGSSSSSEELEADAASAPTG-----VPGQPRRPGHPAQPLP 405
Cdd:pfam03154 392 PPPALKPLSSLSThhPPSAHppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTsglhqVPSQSPFPQHPFVPGG 471
|
170 180
....*....|....*....|
gi 291219891 406 LPQTASSPQPQQKAPRAIDS 425
Cdd:pfam03154 472 PPPITPPSGPPTSTSSAMPG 491
|
|
| SAV_2336_NTERM |
NF041121 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
272-340 |
6.30e-03 |
|
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.
Pssm-ID: 469044 [Multi-domain] Cd Length: 473 Bit Score: 41.14 E-value: 6.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291219891 272 APPEPRDSEVP-----PARSAPGAFGGPPRAPPADLPLPVGGPGGwSRRASPAPSDSSPGEPFVGGPVSSPRAP 340
Cdd:NF041121 25 EGPAPTAASQPatpppPAAPPSPPGDPPEPPAPEPAPLPAPYPGS-LAPPPPPPPGPAGAAPGAALPVRVPAPP 97
|
|
| KLF17_N |
cd21574 |
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like ... |
282-421 |
7.04e-03 |
|
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like factor 17, is a protein that, in humans, is encoded by the KLF17 gene and acts as a tumor suppressor. It negatively regulates epithelial-mesenchymal transition and metastasis in breast cancer. KLF17 is thought to be the human ortholog of the mouse gene, zinc finger protein 393 (Zfp393), although it has diverged significantly. KLF17 can regulate gene transcription from CACCC-box elements. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF17.
Pssm-ID: 410567 Cd Length: 286 Bit Score: 40.45 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 282 PPARSAPGAFGGPPRAPPAdlPLPVGGPGGwsrrASPAPSDSSPGEPFVGGP-VSSPRA---PR----PVVSDTESFSLS 353
Cdd:cd21574 131 PNIPGVAMTFSGNLRMPPS--GLPVSASSG----IPMMSHIRAPTMPYSGPPtVPSNRDsltPKmllaPTMPSTEAQAVL 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291219891 354 PSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTA-SSPQPQQKAPR 421
Cdd:cd21574 205 PSLAQMLPPRDPHNLGMPPAGSPSLLALESQDSLVSQPASQEDPFLPEQPIPAPQRAeQNSRAQERAPR 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PH_PHLPP-like |
cd13322 |
PH domain leucine-rich repeat protein phosphatase family Pleckstrin homology-like domain; The ... |
535-631 |
5.54e-61 |
|
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: 203.21 E-value: 5.54e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 535 ERIQLSGMYNVRKGKMQLpvNRWTRRQVILCGTCLIVSSVKDSLTGKMHVLPLIGGKVEEVKKHQHCLAFSSSGPQSQTY 614
Cdd:cd13322 1 ERILLSGIYNVRKGKTQL--HKWAERQVILCGTCLIVSSVKDSQTGKMHILPLVGGKVEEVKRRQHCLAFSSAGPQAQTY 78
|
90
....*....|....*..
gi 291219891 615 YICFDTFTEYLRWLRQV 631
Cdd:cd13322 79 YVSFDTLAEYQRWHRQA 95
|
|
| PP2Cc |
smart00332 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1168-1420 |
4.22e-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: 204.15 E-value: 4.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1168 SGAPAVWSHGYTEASGVKNKLCVAALSVNNFCDNrEALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE----EEYM 1243
Cdd:smart00332 3 SGKNLGLRYGLSSMQGVRKPMEDAHVITPDLSDS-GGFFGVFDGHGGSEAAKFLSKNLPEILAEELIKEKDEledvEEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1244 VNTFIVMQRKLGTAGQKLGGA-AVLCHIKHDpvdpggsfTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQH 1322
Cdd:smart00332 82 RKAFLSTDEEILEELEALSGStAVVALISGN--------KLYVANVGDSRAVLCRNGKAVQLTEDHKPSNEDERARIEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1323 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNVP--DALAAAK 1400
Cdd:smart00332 154 GGFV-INGRVNGVLALSRAIGDFFLKPYVSAEPDVTVVELTEKDDFLILASDGLWDVLSNQEVVDIVRKHLskDPKEAAK 232
|
250 260
....*....|....*....|
gi 291219891 1401 KLCTLAQSYGCHDSISAVVV 1420
Cdd:smart00332 233 RLIDLALARGSKDNITVVVV 252
|
|
| PP2Cc |
cd00143 |
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ... |
1174-1422 |
4.99e-57 |
|
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 238083 [Multi-domain] Cd Length: 254 Bit Score: 198.32 E-value: 4.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1174 WSHGYTEASGVKNKLCVAALSVNNFCDNREALYGVFDGDRNVEVPYLLQCTMSDILAEELQKTKNE-----EEYMVNTFI 1248
Cdd:cd00143 1 FSAGVSDKGGDRKTNEDAVVIKPNLNNEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLseediEEALRKAFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1249 VMQRKLGTAGQKL------GGAAVLCHIKHDpvdpggsfTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQH 1322
Cdd:cd00143 81 RADEEILEEAQDEpddarsGTTAVVALIRGN--------KLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEEERERIEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1323 KAIItEDGKVNGVTESTRILGYTFLHPSVVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNVP---DALAAA 1399
Cdd:cd00143 153 GGRV-SNGRVPGVLAVTRALGDFDLKPGVSAEPDVTVVKLTEDDDFLILASDGLWDVLSNQEAVDIVRSELakeDLQEAA 231
|
250 260
....*....|....*....|...
gi 291219891 1400 KKLCTLAQSYGCHDSISAVVVQL 1422
Cdd:cd00143 232 QELVDLALRRGSHDNITVVVVRL 254
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
637-898 |
7.53e-35 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 139.30 E-value: 7.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 637 QRISSVDLSCCSlehlpaNLFYSQDLTHLNLKQNFLRqnpSLPAarglnELQRFTKLKSLNLSNNHLGDFPLAVCSIPTL 716
Cdd:COG4886 96 TNLTELDLSGNE------ELSNLTNLESLDLSGNQLT---DLPE-----ELANLTNLKELDLSNNQLTDLPEPLGNLTNL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 717 AELNVSCNALRSVPAAVGVMHNLQTFLLDGNFLQSLPAELENMKQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMSGNCVE 796
Cdd:COG4886 162 KSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 797 TLRlqALRKMPHIKHVDLRLNVIRKLiaDEVDFLQHVTQLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTLDICGYFLKA 876
Cdd:COG4886 242 DLP--ELGNLTNLEELDLSNNQLTDL--PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILL 317
|
250 260
....*....|....*....|..
gi 291219891 877 LYASSNELVQLDVYPVPNYLSY 898
Cdd:COG4886 318 LLLTTLLLLLLLLKGLLVTLTT 339
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
471-528 |
4.00e-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: 123.40 E-value: 4.00e-33
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 471 LYVQLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 528
Cdd:cd17240 33 LQLQLHGETVRRLEPHEKPLQIQNDYLFQLGFGDLWRVQEEGMDPEIGCLIRFYAGKP 90
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
952-1154 |
1.19e-32 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 132.75 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 952 LARLPERLERTSVEVLDVQHNQLLELPPNLLmKADSLRFLNASANKLESLPPAtLSEETNsiLQELYLTNNSLTDkcVPL 1031
Cdd:COG4886 103 LSGNEELSNLTNLESLDLSGNQLTDLPEELA-NLTNLKELDLSNNQLTDLPEP-LGNLTN--LKSLDLSNNQLTD--LPE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1032 -LTGHPHLKILHMAYNRLQSFPASkMAKLEELEEIDLSGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVMQLPEIKCV 1110
Cdd:COG4886 177 eLGNLTNLKELDLSNNQITDLPEP-LGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEEL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 291219891 1111 DLSCNELSEVTLPENLpPKLQELDLTGNPRLVLDHKTLELLNNI 1154
Cdd:COG4886 256 DLSNNQLTDLPPLANL-TNLKTLDLSNNQLTDLKLKELELLLGL 298
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
654-1009 |
1.84e-31 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 129.28 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 654 ANLFYSQDLTHLNLKQNFLRQNPSLPAARGLNELQRFTKLKSLNLSNNhlgdfpLAVCSIPTLAELNVSCNALRSVPAAV 733
Cdd:COG4886 59 DLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEEL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 734 GVMHNLQTFLLDGNFLQSLPAELENMKQLSYLGLSFNEFTDIPEVLEKLTAVDKLCMSGNCVETLRlQALRKMPHIKHVD 813
Cdd:COG4886 133 ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLP-EPLGNLTNLEELD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 814 LRLNVIRKLiADEVDFLQHVTQLDLRDNKLGDLDAMI-FNNIEVLHCERNQLVTLDICGYF--LKALYASSN-----ELV 885
Cdd:COG4886 212 LSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLPELGnLTNLEELDLSNNQLTDLPPLANLtnLKTLDLSNNqltdlKLK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 886 QLDVYPVPNYLSYMDVSRNRLENVPEWVCESRKLEVLDIGHNQICELPARLFCNSSLRKLLAGHNQLARLPERLERTSVE 965
Cdd:COG4886 291 ELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLG 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 291219891 966 VLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEE 1009
Cdd:COG4886 371 LLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
902-1154 |
6.01e-31 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 127.74 E-value: 6.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 902 SRNRLENVPEWVCESRKLEVLDIGHNQIcelparLFCNSSLRKLLAGHNQLARLPERLER-TSVEVLDVQHNQLLELPPN 980
Cdd:COG4886 81 LLSLLLLGLTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANlTNLKELDLSNNQLTDLPEP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 981 LlMKADSLRFLNASANKLESLPPAtLSEETNsiLQELYLTNNSLTDkcVPL-LTGHPHLKILHMAYNRLQSFPASkMAKL 1059
Cdd:COG4886 155 L-GNLTNLKSLDLSNNQLTDLPEE-LGNLTN--LKELDLSNNQITD--LPEpLGNLTNLEELDLSGNQLTDLPEP-LANL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1060 EELEEIDLSGNKLKAIPTtIMNCRRMHTVIAHSNCIEVFPEVMQLPEIKCVDLSCNELSEVTLpENLPPKLQELDLTGNP 1139
Cdd:COG4886 228 TNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKL-KELELLLGLNSLLLLL 305
|
250
....*....|....*
gi 291219891 1140 RLVLDHKTLELLNNI 1154
Cdd:COG4886 306 LLLNLLELLILLLLL 320
|
|
| PP2C |
pfam00481 |
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ... |
1174-1415 |
1.83e-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: 121.67 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1174 WSHGYTEASGVKNKLCVAALSVNNFC----DNREALYGVFDGDRNVEVPYLLQCTMSDILAE--ELQKTKNEEEYMVNTF 1247
Cdd:pfam00481 1 IDLGGPRMQGWRKSMEDAHIDLPNLNsssgKDSWSFFAVFDGHGGSEAAKYCGKHLHTILALrrSFLEGEKLEDALRKSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1248 I----VMQRKLGTAGQKLGGAAVLCHIKHDpvdpggsfTLTSANVGKCQTVLCRNGKP-LPLSRSYIMSCEEELKRIKQH 1322
Cdd:pfam00481 81 LedtdEVLRSAEKEDLDSGCTAVVALISGN--------KLYVANVGDSRAVLCRNGNAiKRLTKDHKPSDEDERRRIRAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1323 KAIITEDGKVNGVTESTRILGYTFLHPS---VVPRPHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNV----PDA 1395
Cdd:pfam00481 153 GGFVSRNGRVNGVLAVSRAFGDFELKPGeqaVSAEPDITSHTITEDDEFLILACDGLWDVLSDQEVVDLVRSElsdgGSP 232
|
250 260
....*....|....*....|
gi 291219891 1396 LAAAKKLCTLAQSYGCHDSI 1415
Cdd:pfam00481 233 MEAAEELRDEAIAYGSEDNI 252
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
690-1042 |
1.50e-29 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 123.51 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 690 FTKLKSLNLSNNHLGDFPLAVCSIPTLAELNVSCNALRSVPAAVGVMHNLQTFLLDGNFLQSLPAELENMKQLSYLGLSF 769
Cdd:COG4886 3 LLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 770 NEFTDIPEVLEKLTAVDKLCMSGNcvetlrlQALRKMPHIKHVDLRLNVIRKLiADEVDFLQHVTQLDLRDNKLGDLDAM 849
Cdd:COG4886 83 SLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQLTDLPEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 850 IFN--NIEVLHCERNQLVTLdicgyflkalyasSNELVQLdvypvPNyLSYMDVSRNRLENVPEWVCESRKLEVLDIGHN 927
Cdd:COG4886 155 LGNltNLKSLDLSNNQLTDL-------------PEELGNL-----TN-LKELDLSNNQITDLPEPLGNLTNLEELDLSGN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 928 QICELPARLFCNSSLRKLLAGHNQLARLPERLERTSVEVLDVQHNQLLELPPnlLMKADSLRFLNASANKLESLPPATLS 1007
Cdd:COG4886 216 QLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPP--LANLTNLKTLDLSNNQLTDLKLKELE 293
|
330 340 350
....*....|....*....|....*....|....*
gi 291219891 1008 EETNSILQELYLTNNSLTDKCVPLLTGHPHLKILH 1042
Cdd:COG4886 294 LLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLL 328
|
|
| RA_PHLPP |
cd17213 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
471-528 |
2.66e-27 |
|
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: 107.38 E-value: 2.66e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 471 LYVQLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 528
Cdd:cd17213 40 LYVQLGGDHIRRLEPDERPLQIQNEFLASLGYSDPSRIQREGTDPDLGHLIRFYAGRP 97
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
639-1126 |
1.32e-25 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 115.72 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 639 ISSVDLSCCSLE-HLPANLFY-SQDLTHLNLKQNflrqNPSLPAARGLnelqrFTKLKSLNLSNNHL-GDFPLAVCSIPT 715
Cdd:PLN00113 95 IQTINLSNNQLSgPIPDDIFTtSSSLRYLNLSNN----NFTGSIPRGS-----IPNLETLDLSNNMLsGEIPNDIGSFSS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 716 LAELNVSCNALRS-VPAAVGVMHNLQTFLLDGN-FLQSLPAELENMKQLSYLGLSFNEFT-DIPEVLEKLTAVDKLCMSG 792
Cdd:PLN00113 166 LKVLDLGGNVLVGkIPNSLTNLTSLEFLTLASNqLVGQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 793 NCVETLRLQALRKMPHIKHVDLRLNVIRKLIADEVDFLQHVTQLDLRDNKL-GDLDAMI--FNNIEVLHcernqLVTLDI 869
Cdd:PLN00113 246 NNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLsGEIPELViqLQNLEILH-----LFSNNF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 870 CGYFLKALyassNELVQLDVypvpnylsyMDVSRNRLE-NVPEWVCESRKLEVLDIGHNQIC-ELPARLfCNS-SLRKLL 946
Cdd:PLN00113 321 TGKIPVAL----TSLPRLQV---------LQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTgEIPEGL-CSSgNLFKLI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 947 AGHNQL-ARLPERLER-TSVEVLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNsiLQELYLTNNSL 1024
Cdd:PLN00113 387 LFSNSLeGEIPKSLGAcRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPS--LQMLSLARNKF 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1025 TDKcVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKLKA-IPTTIMNCRRMHTV-IAHSNCIEVFPEVM 1102
Cdd:PLN00113 465 FGG-LPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLdLSHNQLSGQIPASF 543
|
490 500
....*....|....*....|....*
gi 291219891 1103 -QLPEIKCVDLSCNELSEvTLPENL 1126
Cdd:PLN00113 544 sEMPVLSQLDLSQNQLSG-EIPKNL 567
|
|
| RA_PHLPP2 |
cd17241 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
471-528 |
8.46e-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: 83.40 E-value: 8.46e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 471 LYVQLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMDSEIGCLIRFYAGKP 528
Cdd:cd17241 51 LYLQLHGDLVRRLDPTERPLQIVYDYLSGLGFEDPVRIQEEAANSDLSCMIRFYSEKP 108
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
901-1138 |
1.65e-18 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 92.07 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 901 VSRNRLENVPEWVCESRKLEVLDigHNQICELPARLFCNssLRKLLAGHNQLARLPERLERTsVEVLDVQHNQLLELPPN 980
Cdd:PRK15370 185 LKILGLTTIPACIPEQITTLILD--NNELKSLPENLQGN--IKTLYANSNQLTSIPATLPDT-IQEMELSINRITELPER 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 981 LlmkADSLRFLNASANKLESLPPaTLSEEtnsiLQELYLTNNSLTDKCVPLLTGHPHLKILHmayNRLQSFPASKMAKLE 1060
Cdd:PRK15370 260 L---PSALQSLDLFHNKISCLPE-NLPEE----LRYLSVYDNSIRTLPAHLPSGITHLNVQS---NSLTALPETLPPGLK 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 1061 ELEEIDlsgNKLKAIPTTIMNCRRMHTViaHSNCIEVFPEVMQlPEIKCVDLSCNELseVTLPENLPPKLQELDLTGN 1138
Cdd:PRK15370 329 TLEAGE---NALTSLPASLPPELQVLDV--SKNQITVLPETLP-PTITTLDVSRNAL--TNLPENLPAALQIMQASRN 398
|
|
| PRK15370 |
PRK15370 |
type III secretion system effector E3 ubiquitin transferase SlrP; |
718-959 |
1.54e-15 |
|
type III secretion system effector E3 ubiquitin transferase SlrP;
Pssm-ID: 185268 [Multi-domain] Cd Length: 754 Bit Score: 82.44 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 718 ELNVSCNALRSVPAAVGvmHNLQTFLLDGNFLQSLPAELE-NMKQLSylgLSFNEFTDIPEVLEKltAVDKLCMSGNCVE 796
Cdd:PRK15370 182 ELRLKILGLTTIPACIP--EQITTLILDNNELKSLPENLQgNIKTLY---ANSNQLTSIPATLPD--TIQEMELSINRIT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 797 TLRlqalRKMPH-IKHVDLRLNVIRKLIADEVDFLQHvtqLDLRDNKLGDLDAMIFNNIEVLHCERNQLVTL-DICGYFL 874
Cdd:PRK15370 255 ELP----ERLPSaLQSLDLFHNKISCLPENLPEELRY---LSVYDNSIRTLPAHLPSGITHLNVQSNSLTALpETLPPGL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 875 KALYASSNELVQLDVyPVPNYLSYMDVSRNRLENVPEWVCESrkLEVLDIGHNQICELPARLfcNSSLRKLLAGHNQLAR 954
Cdd:PRK15370 328 KTLEAGENALTSLPA-SLPPELQVLDVSKNQITVLPETLPPT--ITTLDVSRNALTNLPENL--PAALQIMQASRNNLVR 402
|
....*
gi 291219891 955 LPERL 959
Cdd:PRK15370 403 LPESL 407
|
|
| RA_PHLPP1 |
cd17240 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
202-244 |
1.48e-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: 70.63 E-value: 1.48e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 291219891 202 GCVHVFDRHMaSTYLRPVLCTLDTTAGEVAARLLQLGHKGGGV 244
Cdd:cd17240 1 GCIHVYDRHM-SSYLRPVLCTLDTTASEVAARLLQLQLHGETV 42
|
|
| PLN03145 |
PLN03145 |
Protein phosphatase 2c; Provisional |
1282-1420 |
7.30e-13 |
|
Protein phosphatase 2c; Provisional
Pssm-ID: 215603 [Multi-domain] Cd Length: 365 Bit Score: 72.25 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1282 TLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQHKAIItEDGKVNGVTESTRILGYTFLH-------PSVVPR 1354
Cdd:PLN03145 179 SLVVANAGDCRAVLCRRGKAIEMSRDHKPMCSKERKRIEASGGYV-YDGYLNGQLNVARALGDWHMEgmkgsdgGPLSAE 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1355 PHVQSVLLTPQDEFFILGSKGLWDSLSVEEAVEAVRNV----PDALAAAKKLCTLAQSYGCHDSISAVVV 1420
Cdd:PLN03145 258 PELMTTQLTEEDEFLIIGCDGIWDVFRSQNAVDFARRRlqehNDPVMCSKELVDEALKRKSGDNLAVVVV 327
|
|
| PTZ00224 |
PTZ00224 |
protein phosphatase 2C; Provisional |
1190-1423 |
1.53e-11 |
|
protein phosphatase 2C; Provisional
Pssm-ID: 240318 [Multi-domain] Cd Length: 381 Bit Score: 68.26 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1190 VAALSVNNFCDNRE-----------ALYGVFDGDRNVevpyllQCtmSDILAEEL-QKTKNEEEYMvnTFIVMQR----- 1252
Cdd:PTZ00224 24 CASACVNGYRESMEdahllyltddwGFFGVFDGHVND------EC--SQYLARAWpQALEKEPEPM--TDERMEElclei 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1253 -----KLGTAGqklGGAAVLCHIKHDpvdpggsFTLTSANVGKCQTVLCRNGKPLPLSRSYIMSCEEELKRIKQHKAIIt 1327
Cdd:PTZ00224 94 deewmDSGREG---GSTGTFCVIMKD-------VHLQVGNVGDSRVLVCRDGKLVFATEDHKPNNPGERQRIEACGGRV- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1328 EDGKVNGVTESTRILG---------YTFLHPSVVPRPHVQSVLLTPQDeFFILGSKGLWD-SLSVEEAV----EAVRNVP 1393
Cdd:PTZ00224 163 VSNRVDGDLAVSRAFGdrsfkvkgtGDYLEQKVIAVPDVTHLTCQSND-FIILACDGVFEgNFSNEEVVafvkEQLETCD 241
|
250 260 270
....*....|....*....|....*....|
gi 291219891 1394 DALAAAKKLCTLAQSYGCHDSISAVVVQLS 1423
Cdd:PTZ00224 242 DLAVVAGRVCDEAIRRGSKDNISCLIVQLK 271
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
635-869 |
4.27e-11 |
|
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: 67.12 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 635 ASQRISSVDLSCCSLEHLPANLFYSQDLTHLNLKQNFLRQNP-SLPAARGLNE-LQRFTKLKSLNLSNNHLGDFPLAVcs 712
Cdd:COG5238 178 QNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPiGDEGAEILAEaLKGNKSLTTLDLSNNQIGDEGVIA-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 713 iptLAElnvscnALRSvpaavgvMHNLQTFLLDGNFL-----QSLPAELENMKQLSYLGLSFNEFTD-----IPEVLEKL 782
Cdd:COG5238 256 ---LAE------ALKN-------NTTVETLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVNRIGDegaiaLAEGLQGN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 783 TAVDKLCMSGN-----CVETLrLQALRKMPHIKHVDLRLNVIR----KLIADEVDFLQHVTQLDLRDNKLGDLDAMIFNN 853
Cdd:COG5238 320 KTLHTLNLAYNgigaqGAIAL-AKALQENTTLHSLDLSDNQIGdegaIALAKYLEGNTTLRELNLGKNNIGKQGAEALID 398
|
250
....*....|....*.
gi 291219891 854 ievlHCERNQLVTLDI 869
Cdd:COG5238 399 ----ALQTNRLHTLIL 410
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
832-1122 |
4.45e-11 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 67.88 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 832 HVTQLDLRDNKLGDLDAMIfNNIEVLHCERNQLVTLDICGYFLKALYASSNELVQLDVypVPNYLSYMDVSRNRLENVPe 911
Cdd:PRK15387 223 HITTLVIPDNNLTSLPALP-PELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPA--LPSGLCKLWIFGNQLTSLP- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 912 wvCESRKLEVLDIGHNQICELPArlfCNSSLRKLLAGHNQLARLPErlertsvevldvqhnqlleLPpnllmkaDSLRFL 991
Cdd:PRK15387 299 --VLPPGLQELSVSDNQLASLPA---LPSELCKLWAYNNQLTSLPT-------------------LP-------SGLQEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 992 NASANKLESLPpaTLSEEtnsiLQELYLTNNSLTDkcVPLLTGHphLKILHMAYNRLQSFPASKmaklEELEEIDLSGNK 1071
Cdd:PRK15387 348 SVSDNQLASLP--TLPSE----LYKLWAYNNRLTS--LPALPSG--LKELIVSGNRLTSLPVLP----SELKELMVSGNR 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 291219891 1072 LKAIPttiMNCRRMHTVIAHSNCIEVFPE-VMQLPEIKCVDLSCNELSEVTL 1122
Cdd:PRK15387 414 LTSLP---MLPSGLLSLSVYRNQLTRLPEsLIHLSSETTVNLEGNPLSERTL 462
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
625-929 |
8.03e-11 |
|
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: 65.45 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 625 LRWLRQVSKVasQRISSVDLSCCSL--EHLPA---NLFYSQDLTHLNLKQNFLRQNPSLPAARGLNeLQRFTKLKSLNLS 699
Cdd:cd00116 13 ERATELLPKL--LCLQVLRLEGNTLgeEAAKAlasALRPQPSLKELCLSLNETGRIPRGLQSLLQG-LTKGCGLQELDLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 700 NNHLGD----FPLAVCSIPTLAELNVSCNALRSVPAAvgvmhnlqtFLLDGnfLQSLPAELENMkQLSYLGLSFNEFTDI 775
Cdd:cd00116 90 DNALGPdgcgVLESLLRSSSLQELKLNNNGLGDRGLR---------LLAKG--LKDLPPALEKL-VLGRNRLEGASCEAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 776 PEVLEKLTAVDKLCMSGNCV-----ETLrLQALRKMPHIKHVDLRLNVIR----KLIADEVDFLQHVTQLDLRDNKLGDL 846
Cdd:cd00116 158 AKALRANRDLKELNLANNGIgdagiRAL-AEGLKANCNLEVLDLNNNGLTdegaSALAETLASLKSLEVLNLGDNNLTDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 847 DAMIFNnievlhcerNQLVTLDICgyfLKALYASSNELVQLDVYPVPNYLS------YMDVSRNRL------ENVPEWVC 914
Cdd:cd00116 237 GAAALA---------SALLSPNIS---LLTLSLSCNDITDDGAKDLAEVLAekesllELDLRGNKFgeegaqLLAESLLE 304
|
330
....*....|....*
gi 291219891 915 ESRKLEVLDIGHNQI 929
Cdd:cd00116 305 PGNELESLWVKDDSF 319
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
814-1074 |
1.02e-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: 61.99 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 814 LRLNVIRKLIADEVDFLQHVTQLDLRDNKLGDLDA-MIFNNIEVlhceRNQLVTLDICGYFLKALyaSSNELVQLDVYPV 892
Cdd:cd00116 6 KGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAkALASALRP----QPSLKELCLSLNETGRI--PRGLQSLLQGLTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 893 PNYLSYMDVSRNRL--ENVPEW--VCESRKLEVLDIGHNQICELPARLFCNS------SLRKLLAGHNQL-ARLPERL-- 959
Cdd:cd00116 80 GCGLQELDLSDNALgpDGCGVLesLLRSSSLQELKLNNNGLGDRGLRLLAKGlkdlppALEKLVLGRNRLeGASCEALak 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 960 ---ERTSVEVLDVQHNQLLE-----LPPNLLMKAdSLRFLNASANKLESLPPATLSE--ETNSILQELYLTNNSLTDKCV 1029
Cdd:cd00116 160 alrANRDLKELNLANNGIGDagiraLAEGLKANC-NLEVLDLNNNGLTDEGASALAEtlASLKSLEVLNLGDNNLTDAGA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 291219891 1030 -----PLLTGHPHLKILHMAYNRLQSFPASK----MAKLEELEEIDLSGNKLKA 1074
Cdd:cd00116 239 aalasALLSPNISLLTLSLSCNDITDDGAKDlaevLAEKESLLELDLRGNKFGE 292
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-444 |
1.63e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 63.42 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 273 PPEPR------DSEVPPARSAPGAFGGPPRAPPADLPLPVGG--PGGWSRRASPA-----PSDSSPGEPFVGGPvssPRA 339
Cdd:PHA03247 2707 TPEPAphalvsATPLPPGPAAARQASPALPAAPAPPAVPAGPatPGGPARPARPPttagpPAPAPPAAPAAGPP---RRL 2783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 340 PRPVVSdtesfSLSPSAESVSDRLDPYSSGGGSsssseeLEADAASAPTGVPGQPRRPGHPAQPLPlPQTASSPQPQQKA 419
Cdd:PHA03247 2784 TRPAVA-----SLSESRESLPSPWDPADPPAAV------LAPAAALPPAASPAGPLPPPTSAQPTA-PPPPPGPPPPSLP 2851
|
170 180
....*....|....*....|....*
gi 291219891 420 PRAIDSPGGAVREGSCEEKAAAAVA 444
Cdd:PHA03247 2852 LGGSVAPGGDVRRRPPSRSPAAKPA 2876
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
803-1066 |
3.77e-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: 58.64 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 803 LRKMPHIKHVDLRLNVIrkliaDEVDFLQHVTQLDLRDNKLgdldamifNNIEVLHCERNqlvtldicgyfLKALYASSN 882
Cdd:cd21340 1 LKRITHLYLNDKNITKI-----DNLSLCKNLKVLYLYDNKI--------TKIENLEFLTN-----------LTHLYLQNN 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 883 ELvqldvypvpnylsymdvsrNRLENVpewvcES-RKLEVLDIGHNQICELparlfcnsslrkllaghnqlarlpERLER 961
Cdd:cd21340 57 QI-------------------EKIENL-----ENlVNLKKLYLGGNRISVV------------------------EGLEN 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 962 -TSVEVLDVQHNQL-----LELPPNLLMK-ADSLRFLNASANKLESLPP-ATLSEetnsiLQELYLTNNSLTD--KCVPL 1031
Cdd:cd21340 89 lTNLEELHIENQRLppgekLTFDPRSLAAlSNSLRVLNISGNNIDSLEPlAPLRN-----LEQLDASNNQISDleELLDL 163
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 291219891 1032 LTGHPHLKILHMAYNrlqsfPASKMAKLEE--------LEEID 1066
Cdd:cd21340 164 LSSWPSLRELDLTGN-----PVCKKPKYRDkiilasksLEVLD 201
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
272-462 |
1.33e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 60.34 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPrdsevPPARSAPGAFGGPPraPPADLPLPVGG---PGG-WSRRA---SPAPSDSSPGEPfvggPVSspRAPRPVV 344
Cdd:PHA03247 2825 AGPLP-----PPTSAQPTAPPPPP--GPPPPSLPLGGsvaPGGdVRRRPpsrSPAAKPAAPARP----PVR--RLARPAV 2891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 345 S-DTESFSLSPsaesvsDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAi 423
Cdd:PHA03247 2892 SrSTESFALPP------DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWL- 2964
|
170 180 190
....*....|....*....|....*....|....*....
gi 291219891 424 dspgGAVregsceekaaaavapgglqsTPGRSGVTAEKA 462
Cdd:PHA03247 2965 ----GAL--------------------VPGRVAVPRFRV 2979
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
272-455 |
4.17e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPRDSEVPPARSAPGAfggPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSS-PRAPRPVVSDTESF 350
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAA---PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAlPPAASPAGPLPPPT 2832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 351 SLSPSAESV-SDRLDPYSSGGGSSSSSEELEADAAS-APTGVPGQPRRP--GHPAQPLPLPQTASSPQP--QQKAPRAID 424
Cdd:PHA03247 2833 SAQPTAPPPpPGPPPPSLPLGGSVAPGGDVRRRPPSrSPAAKPAAPARPpvRRLARPAVSRSTESFALPpdQPERPPQPQ 2912
|
170 180 190
....*....|....*....|....*....|.
gi 291219891 425 SPGGAVREGSCEEKAAAAVAPgglqSTPGRS 455
Cdd:PHA03247 2913 APPPPQPQPQPPPPPQPQPPP----PPPPRP 2939
|
|
| RA_PHLPP |
cd17213 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
202-249 |
4.32e-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: 52.30 E-value: 4.32e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 291219891 202 GCVHVFDRHMASTYLRPVLCTLDTTAGEVAARLLQLGHK-----GGGVVKVLG 249
Cdd:cd17213 1 GFIRVYDPDSPSDRSKLVPCTLETTAEDICKKLGISSLYlyvqlGGDHIRRLE 53
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
996-1153 |
5.21e-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: 55.18 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 996 NKLESLPPatLSEETNsiLQELYLTNNSLTdkCVPLLTGHPHLKILHMAYNRLqsfpaSKMA---KLEELEEIDLSGNKL 1072
Cdd:cd21340 34 NKITKIEN--LEFLTN--LTHLYLQNNQIE--KIENLENLVNLKKLYLGGNRI-----SVVEgleNLTNLEELHIENQRL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1073 KAIPTTIMNCRRMHTV--------IAHSN-----CIEVFPEVMQLpeikcvDLSCNELS---EVTLPENLPPKLQELDLT 1136
Cdd:cd21340 103 PPGEKLTFDPRSLAALsnslrvlnISGNNidslePLAPLRNLEQL------DASNNQISdleELLDLLSSWPSLRELDLT 176
|
170 180
....*....|....*....|....*.
gi 291219891 1137 GNP---------RLVLDHKTLELLNN 1153
Cdd:cd21340 177 GNPvckkpkyrdKIILASKSLEVLDG 202
|
|
| PH |
cd00821 |
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ... |
539-629 |
1.10e-07 |
|
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: 51.00 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 539 LSGMYNVRKGKmqlPVNRWTRRQVILCGTCLIVS-SVKDSLTGKMHVLPLIGG-KVEEVKKHQHCLAFSSSGPQSQTYYI 616
Cdd:cd00821 1 KEGYLLKRGGG---GLKSWKKRWFVLFEGVLLYYkSKKDSSYKPKGSIPLSGIlEVEEVSPKERPHCFELVTPDGRTYYL 77
|
90
....*....|...
gi 291219891 617 CFDTFTEYLRWLR 629
Cdd:cd00821 78 QADSEEERQEWLK 90
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
685-776 |
1.22e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 56.75 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 685 NELQRFTKLKSLNLSNNHL-GDFPLAVCSIPTLAELNVSCNALR-SVPAAVGVMHNLQTFLLDGNFLQS-LPAELENmkq 761
Cdd:PLN03150 436 NDISKLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSGrVPAALGG--- 512
|
90
....*....|....*
gi 291219891 762 LSYLGLSFNeFTDIP 776
Cdd:PLN03150 513 RLLHRASFN-FTDNA 526
|
|
| RA_PHLPP_like |
cd01775 |
Ras-associating (RA) domain found in PH domain leucine-rich repeat-containing protein ... |
474-528 |
1.71e-07 |
|
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: 50.94 E-value: 1.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 291219891 474 QLHGETTRRLEAEEKPLQIQNDYLFQLGFGELWRVQEEGMdSEIGCLIRFYAGKP 528
Cdd:cd01775 46 LKHGGLVRRLRPDEKPLRIQRDLLLLLGYTDPDRQEEATN-PDLSYVIKFVFEKP 99
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
777-1026 |
1.82e-07 |
|
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: 55.05 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 777 EVLEKLTAVDKLCMSGNCVETLRLQALRKM----PHIKHVDLRLN---VIRKLIADEVDFLQHVTQL---DLRDNKLGDL 846
Cdd:cd00116 17 ELLPKLLCLQVLRLEGNTLGEEAAKALASAlrpqPSLKELCLSLNetgRIPRGLQSLLQGLTKGCGLqelDLSDNALGPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 847 DAMIFNNIevLHcernqlvtldicGYFLKALYASSNEL-------VQLDVYPVPNYLSYMDVSRNRLENVPewvCES--- 916
Cdd:cd00116 97 GCGVLESL--LR------------SSSLQELKLNNNGLgdrglrlLAKGLKDLPPALEKLVLGRNRLEGAS---CEAlak 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 917 -----RKLEVLDIGHNQICELPARLFC-----NSSLRKLL--------AGHNQLARLPERLErtSVEVLDVQHNQL---- 974
Cdd:cd00116 160 alranRDLKELNLANNGIGDAGIRALAeglkaNCNLEVLDlnnngltdEGASALAETLASLK--SLEVLNLGDNNLtdag 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 291219891 975 -LELPPNLLMKADSLRFLNASANKLESLPPATLSE--ETNSILQELYLTNNSLTD 1026
Cdd:cd00116 238 aAALASALLSPNISLLTLSLSCNDITDDGAKDLAEvlAEKESLLELDLRGNKFGE 292
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1014-1072 |
3.37e-07 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 48.67 E-value: 3.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 291219891 1014 LQELYLTNNSLTDKCVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKL 1072
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
662-976 |
5.67e-07 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 54.40 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 662 LTHLNLKQNFLRQNPSLPAarglnelqrftKLKSLNLSNNHLGDFPLAVcsiPTLAELNVSCNALRSVPAAVGVMHNLQT 741
Cdd:PRK15387 224 ITTLVIPDNNLTSLPALPP-----------ELRTLEVSGNQLTSLPVLP---PGLLELSIFSNPLTHLPALPSGLCKLWI 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 742 FlldGNFLQSLPAELENMKQLSylgLSFNEFTDIPEVLEKLTavdKLCMSGNcvetlRLQALRKMPhikhvdlrlnvirk 821
Cdd:PRK15387 290 F---GNQLTSLPVLPPGLQELS---VSDNQLASLPALPSELC---KLWAYNN-----QLTSLPTLP-------------- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 822 liadevdflQHVTQLDLRDNKLGDLDAMIfNNIEVLHCERNQLVTLDICGYFLKALYASSNELVQLDVypVPNYLSYMDV 901
Cdd:PRK15387 342 ---------SGLQELSVSDNQLASLPTLP-SELYKLWAYNNRLTSLPALPSGLKELIVSGNRLTSLPV--LPSELKELMV 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291219891 902 SRNRLENVPEwvcesrklevldighnqiceLPARLFCNSSLRkllaghNQLARLPERLERTSVE-VLDVQHNQLLE 976
Cdd:PRK15387 410 SGNRLTSLPM--------------------LPSGLLSLSVYR------NQLTRLPESLIHLSSEtTVNLEGNPLSE 459
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
808-1110 |
1.09e-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: 53.26 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 808 HIKHVDLRLNVIR----KLIADEVDFLQHVTQLDLRDNKLGDLDAMIFnnIEVLhCERNQLVTLDicgyflkalyassne 883
Cdd:COG5238 181 SVETVYLGCNQIGdegiEELAEALTQNTTVTTLWLKRNPIGDEGAEIL--AEAL-KGNKSLTTLD--------------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 884 lvqldvypvpnyLSYMDVSRNRLENVPEWVCESRKLEVLDIGHNQICELPARlfcnsSLRKLLAGHnqlarlperlerTS 963
Cdd:COG5238 243 ------------LSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAI-----ALAKALQGN------------TT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 964 VEVLDVQHNQLLElpPNLLMKADSLrflnasankleslppatlseETNSILQELYLTNNSLTDKCVPLLT----GHPHLK 1039
Cdd:COG5238 294 LTSLDLSVNRIGD--EGAIALAEGL--------------------QGNKTLHTLNLAYNGIGAQGAIALAkalqENTTLH 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1040 ILHMAYNRLQSFPASKMAKLEE----LEEIDLSGNKL---------KAIPTTimncrRMHTVIAHSNCIEVFPE---VMQ 1103
Cdd:COG5238 352 SLDLSDNQIGDEGAIALAKYLEgnttLRELNLGKNNIgkqgaealiDALQTN-----RLHTLILDGNLIGAEAQqrlEQL 426
|
....*..
gi 291219891 1104 LPEIKCV 1110
Cdd:COG5238 427 LERIKSV 433
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
972-1139 |
1.10e-06 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 53.01 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 972 NQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNSILQELYLTNNSLTDKCVPLLTGHPHLKILHMAYNRLQSF 1051
Cdd:COG4886 9 TLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1052 PaSKMAKLEELEEID-----------------LSGNKLKAIPTTIMNCRRMHTVIAHSNCIEVFPEVM-QLPEIKCVDLS 1113
Cdd:COG4886 89 L-TDLGDLTNLTELDlsgneelsnltnlesldLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLgNLTNLKSLDLS 167
|
170 180
....*....|....*....|....*..
gi 291219891 1114 CNELSEVTLP-ENLpPKLQELDLTGNP 1139
Cdd:COG4886 168 NNQLTDLPEElGNL-TNLKELDLSNNQ 193
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
873-1138 |
1.38e-06 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 53.31 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 873 FLKALYASSNEL---VQLDVYPVPNYLSYMDVSRNRLE-NVPEWVCESrkLEVLDIGHNQIC-ELPARLFCNSSLRklla 947
Cdd:PLN00113 94 YIQTINLSNNQLsgpIPDDIFTTSSSLRYLNLSNNNFTgSIPRGSIPN--LETLDLSNNMLSgEIPNDIGSFSSLK---- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 948 ghnqlarlperlertsveVLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNsiLQELYLTNNSLTDK 1027
Cdd:PLN00113 168 ------------------VLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKS--LKWIYLGYNNLSGE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1028 CVPLLTGHPHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKLKA-IPTTIMNCRRMHTVIAHSNCIE-VFPE-VMQL 1104
Cdd:PLN00113 228 IPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGpIPPSIFSLQKLISLDLSDNSLSgEIPElVIQL 307
|
250 260 270
....*....|....*....|....*....|....*.
gi 291219891 1105 PEIKCVDLSCNELSEvTLPENLP--PKLQELDLTGN 1138
Cdd:PLN00113 308 QNLEILHLFSNNFTG-KIPVALTslPRLQVLQLWSN 342
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
272-456 |
1.92e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.87 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPRDSEVPPARSAPGafggpPRAPPADLPLPVGGPGGWSRRAS-PAPSDSSPGEPfvggpvssPRAPRPVVSDTESF 350
Cdd:PHA03307 240 SSSESSGCGWGPENECPL-----PRPAPITLPTRIWEASGWNGPSSrPGPASSSSSPR--------ERSPSPSPSSPGSG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 351 SLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAV 430
Cdd:PHA03307 307 PAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPT 386
|
170 180
....*....|....*....|....*..
gi 291219891 431 RegsceEKAAAAVAPGGLQS-TPGRSG 456
Cdd:PHA03307 387 R-----RRARAAVAGRARRRdATGRFP 408
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
270-459 |
2.09e-06 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 52.87 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 270 RLAPPEPRDSEVPPARSAPGafgGPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTES 349
Cdd:PHA03307 96 APASPAREGSPTPPGPSSPD---PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 350 FSLSPSAESVSDRLDPyssgggssssseeleaDAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPqQKAPRAIDSPGGA 429
Cdd:PHA03307 173 ALPLSSPEETARAPSS----------------PPAEPPPSTPPAAASPRPPRRSSPISASASSPAP-APGRSAADDAGAS 235
|
170 180 190
....*....|....*....|....*....|
gi 291219891 430 VREGSCEEKAAAAVAPGGLQSTPGRSGVTA 459
Cdd:PHA03307 236 SSDSSSSESSGCGWGPENECPLPRPAPITL 265
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
638-845 |
3.59e-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: 51.33 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 638 RISSVDLS-----CCSLEHLPANLFYSQDLTHLNLKQNFLrqnpSLPAARGLNE-LQRFTKLKSLNLSNNHLGDfPLAVC 711
Cdd:COG5238 237 SLTTLDLSnnqigDEGVIALAEALKNNTTVETLYLSGNQI----GAEGAIALAKaLQGNTTLTSLDLSVNRIGD-EGAIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 712 SIP------TLAELNVSCNALRSVPAavgvmhnlqtflldgnflQSLPAELENMKQLSYLGLSFNEFTDIpevlekltAV 785
Cdd:COG5238 312 LAEglqgnkTLHTLNLAYNGIGAQGA------------------IALAKALQENTTLHSLDLSDNQIGDE--------GA 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291219891 786 DKLCmsgncvetlrlQALRKMPHIKHVDLRLNVIRKLIADEV-DFLQH--VTQLDLRDNKLGD 845
Cdd:COG5238 366 IALA-----------KYLEGNTTLRELNLGKNNIGKQGAEALiDALQTnrLHTLILDGNLIGA 417
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
273-489 |
3.85e-06 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 52.00 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 273 PPEPRDSEVPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPAPSD--SSPGEPfvGGPvSSPRAPRPVVSDTESF 350
Cdd:PTZ00449 591 PEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPQrpSSPERP--EGP-KIIKSPKPPKSPKPPF 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 351 SLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLP--LPQTASSPQPQQKAPRAiDSPGG 428
Cdd:PTZ00449 668 DPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTTPRPLPpkLPRDEEFPFEPIGDPDA-EQPDD 746
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291219891 429 AVREGSCEEKAAAavapggLQSTPGRS---GVTAEKAPPPpppptlyvQLHGETTRRLEAEEKP 489
Cdd:PTZ00449 747 IEFFTPPEEERTF------FHETPADTplpDILAEEFKEE--------DIHAETGEPDEAMKRP 796
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
2-444 |
4.33e-06 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 51.53 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 2 EPAAAATVQRLPELGREDRASAPAAAAAAAAAaaaaaaalaaaAGGGRSPEPALTPAAPSGGNGSGSGAREEAPGEAPPG 81
Cdd:PRK07764 368 SDDERGLLARLERLERRLGVAGGAGAPAAAAP-----------SAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 82 PLPGRAGGAGRRRRRGAPQPIAGGAAPVPGAGGGANSlllrrgrlkrnlsaaaAAASSSSSSSAAAASHSPGAAGLPASC 161
Cdd:PRK07764 437 PAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAA----------------PEPTAAPAPAPPAAPAPAAAPAAPAAP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 162 SASASlctrSLDRKTLLLKHRQTLQLQPSD-RDWVRHQLQRGCVHVFDrhmastylRPVLcTLDTTAGEVAARLLQLGHK 240
Cdd:PRK07764 501 AAPAG----ADDAATLRERWPEILAAVPKRsRKTWAILLPEATVLGVR--------GDTL-VLGFSTGGLARRFASPGNA 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 241 G----------GGVVKVL----GQGPGAAAAREPAEPPPEAGPRLAPPEPRDSEVPPARSAPGAFGGPPRAPP------- 299
Cdd:PRK07764 568 EvlvtalaeelGGDWQVEavvgPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASaapapgv 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 300 ---------ADLPLPVGGPGGWSRRA----------SPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVS 360
Cdd:PRK07764 648 aapehhpkhVAVPDASDGGDGWPAKAggaapaapppAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQG 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 361 DRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGScEEKAA 440
Cdd:PRK07764 728 ASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDA-EEVAM 806
|
....
gi 291219891 441 AAVA 444
Cdd:PRK07764 807 ELLE 810
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
270-459 |
5.15e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 270 RLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLP--VGGPGGWSRRASPAPSDSSPGEPfvggpvsSPRAPRPVVSDT 347
Cdd:PHA03247 2623 APDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrVSRPRRARRLGRAAQASSPPQRP-------RRRAARPTVGSL 2695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 348 ESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQP-----LPLPQTASSPqPQQKAPRA 422
Cdd:PHA03247 2696 TSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPggparPARPPTTAGP-PAPAPPAA 2774
|
170 180 190
....*....|....*....|....*....|....*..
gi 291219891 423 idSPGGAVREGSCEEKAAAAVAPGGLQSTPGRSGVTA 459
Cdd:PHA03247 2775 --PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPA 2809
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
273-459 |
5.19e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 51.86 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 273 PPEP------RDSEVPPARSAPGAFGGPPRAPPADLPlPVGGPGGWSRRASPAPSDSS-PGEPFVGGPVSSPRAPRPVVS 345
Cdd:PHA03247 2577 PSEPavtsraRRPDAPPQSARPRAPVDDRGDPRGPAP-PSPLPPDTHAPDPPPPSPSPaANEPDPHPPPTVPPPERPRDD 2655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 346 DtesfslSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTG-VPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAID 424
Cdd:PHA03247 2656 P------APGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGsLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAAR 2729
|
170 180 190
....*....|....*....|....*....|....*
gi 291219891 425 SPGGAVREGSCEEKAAAAVAPGGLQSTPGRSGVTA 459
Cdd:PHA03247 2730 QASPALPAAPAPPAVPAGPATPGGPARPARPPTTA 2764
|
|
| PTC1 |
COG0631 |
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms]; |
1353-1427 |
8.71e-06 |
|
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
Pssm-ID: 440396 [Multi-domain] Cd Length: 247 Bit Score: 49.05 E-value: 8.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291219891 1353 PRPHVQSVLLTPQDeFFILGSKGLWDSLSVEEAVEAVRNVPDALAAAKKLCTLAQSYGCHDSISAVVVQLSVTED 1427
Cdd:COG0631 172 VEPDISPLELEPGD-RLLLCSDGLTDMVSDEEIAEILASAGDPQEAAEALIELALEAGGPDNITVVLVRVEDADA 245
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
637-703 |
1.07e-05 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 44.44 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 637 QRISSVDLSCCSLEHLPANLFYS-QDLTHLNLKQNFLRqnpSLPAarglNELQRFTKLKSLNLSNNHL 703
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKGlSNLKVLDLSNNLLT---TLSP----GAFSGLPSLRYLDLSGNRL 61
|
|
| PRK15387 |
PRK15387 |
type III secretion system effector E3 ubiquitin transferase SspH2; |
637-806 |
1.79e-05 |
|
type III secretion system effector E3 ubiquitin transferase SspH2;
Pssm-ID: 185285 [Multi-domain] Cd Length: 788 Bit Score: 49.78 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 637 QRISSVDLSCCSLEHLPANL----FYSQDLT----------HLNLKQNFLRQNPSLPaarglnelqrfTKLKSLNLSNNH 702
Cdd:PRK15387 305 QELSVSDNQLASLPALPSELcklwAYNNQLTslptlpsglqELSVSDNQLASLPTLP-----------SELYKLWAYNNR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 703 LGDFPlavcSIPT-LAELNVSCNALRSVPAavgVMHNLQTFLLDGNFLQSLPAELENMKQLSylgLSFNEFTDIPEVLEK 781
Cdd:PRK15387 374 LTSLP----ALPSgLKELIVSGNRLTSLPV---LPSELKELMVSGNRLTSLPMLPSGLLSLS---VYRNQLTRLPESLIH 443
|
170 180
....*....|....*....|....*
gi 291219891 782 LTAVDKLCMSGNCVETLRLQALRKM 806
Cdd:PRK15387 444 LSSETTVNLEGNPLSERTLQALREI 468
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
266-456 |
2.69e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 266 EAGPRLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLP---VGGPGGWSRRAS--------PAPSDSSPGEPFVGGPV 334
Cdd:PHA03307 119 PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASpaaVASDAASSRQAAlplsspeeTARAPSSPPAEPPPSTP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 335 SSPRAPRPVVSDTESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTG-----------VPGQPRRPGHPAQP 403
Cdd:PHA03307 199 PAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENecplprpapitLPTRIWEASGWNGP 278
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291219891 404 LPLPQTASS--------PQPQQKAPRA--------IDSPGGAVREGSCEEKAAAAVAPGGLQSTPGRSG 456
Cdd:PHA03307 279 SSRPGPASSsssprersPSPSPSSPGSgpapssprASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSP 347
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
271-446 |
2.76e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.55 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 271 LAPPEPrDSEVPPARSAPGAFggpPRAPPADLPLP----------------VGGPggwsrrASPAPSDSSPGEPFVGGPV 334
Cdd:PHA03247 2501 GGPPDP-DAPPAPSRLAPAIL---PDEPVGEPVHPrmltwirgleelasddAGDP------PPPLPPAAPPAAPDRSVPP 2570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 335 SSPrAPRPVVSDTESFSLSPSAESVSDRldpyssgggssssseeleadaASAPTGVPGQPRRPGHPAqPLPLPQTASSPQ 414
Cdd:PHA03247 2571 PRP-APRPSEPAVTSRARRPDAPPQSAR---------------------PRAPVDDRGDPRGPAPPS-PLPPDTHAPDPP 2627
|
170 180 190
....*....|....*....|....*....|..
gi 291219891 415 PQQKAPRAIDSPGGAVREGSCEEKAAAAVAPG 446
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPG 2659
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
270-428 |
3.18e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.01 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 270 RLAPPEPRDSEVPPArsapgafGGPPRAPPADLPLPVGGPGGWSRRASPAPsDSSPGEPFVGGPVSSPRAPRPVvsdtes 349
Cdd:PHA03307 59 AAACDRFEPPTGPPP-------GPGTEAPANESRSTPTWSLSTLAPASPAR-EGSPTPPGPSSPDPPPPTPPPA------ 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291219891 350 fslSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGG 428
Cdd:PHA03307 125 ---SPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPA 200
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
637-817 |
6.16e-05 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 46.32 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 637 QRISSVDL--SCCSLEHLPA---------NLFYSQDLTHLNLKQNFLRQnpslpaargLNELQRFTKLKSLNLSNNHL-- 703
Cdd:cd21340 12 KNITKIDNlsLCKNLKVLYLydnkitkieNLEFLTNLTHLYLQNNQIEK---------IENLENLVNLKKLYLGGNRIsv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 704 --GdfpLAVCsiPTLAELNVSCNAL----------RSVpAAVGvmHNLQTFLLDGNFLQSLpAELENMKQLSYLGLSFNE 771
Cdd:cd21340 83 veG---LENL--TNLEELHIENQRLppgekltfdpRSL-AALS--NSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 291219891 772 FTDIPEVlekltavdklcmsgncvetlrLQALRKMPHIKHVDLRLN 817
Cdd:cd21340 154 ISDLEEL---------------------LDLLSSWPSLRELDLTGN 178
|
|
| PLN03150 |
PLN03150 |
hypothetical protein; Provisional |
719-793 |
8.63e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 178695 [Multi-domain] Cd Length: 623 Bit Score: 47.50 E-value: 8.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 719 LNVSCNALRS-VPAAVGVMHNLQTFLLDGNFLQ-SLPAELENMKQLSYLGLSFNEFT-DIPEVLEKLTAVDKLCMSGN 793
Cdd:PLN03150 423 LGLDNQGLRGfIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGN 500
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
261-440 |
8.66e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.56 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 261 AEPPPEAGPRLAPPEPRDSE--VPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPfvggPVSSPR 338
Cdd:PRK12323 394 AAAPAPAAPPAAPAAAPAAAaaARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAAR----PAAAGP 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 339 APRPVVSDTESFSLSPSAESVSDRLD---------------PYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQP 403
Cdd:PRK12323 470 RPVAAAAAAAPARAAPAAAPAPADDDpppweelppefaspaPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAP 549
|
170 180 190
....*....|....*....|....*....|....*..
gi 291219891 404 LPLPQTASSPQPQQKAPRAIDSPGGAVREGSCEEKAA 440
Cdd:PRK12323 550 APRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAA 586
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
270-453 |
9.76e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 47.37 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 270 RLAPPEPRDSEVPPARSAPGAfGGPPRAPPADLPLPVGGPGGwSRRASPAPSDSSPgepfvggPVSSPRAPRPvvsdtes 349
Cdd:PHA03378 693 TMQPPPRAPTPMRPPAAPPGR-AQRPAAATGRARPPAAAPGR-ARPPAAAPGRARP-------PAAAPGRARP------- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 350 fslspsAESVSDRLDPyssgggssssseelEADAASAPTGVPgQPRRPGHPAQ-----PLPLPQTASSPQPQQKAPRAID 424
Cdd:PHA03378 757 ------PAAAPGRARP--------------PAAAPGAPTPQP-PPQAPPAPQQrprgaPTPQPPPQAGPTSMQLMPRAAP 815
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 291219891 425 SPGGAV---------------REGSCEEKAAAAVAPGGLQSTPG 453
Cdd:PHA03378 816 GQQGPTkqilrqlltggvkrgRPSLKKPAALERQAAAGPTPSPG 859
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
962-1024 |
1.45e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 41.36 E-value: 1.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291219891 962 TSVEVLDVQHNQLLELPPNLLMKADSLRFLNASANKLESLPPATLSEETNsiLQELYLTNNSL 1024
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPS--LRYLDLSGNRL 61
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
53-421 |
1.55e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 53 PALTPAAPSGGNGSGSGAREEAPGEAPPG-----PLPGRAGGAGRRRRRGAPQPIAGGAAPVPGAGGGANSlllrrgrlk 127
Cdd:PHA03247 2686 RAARPTVGSLTSLADPPPPPPTPEPAPHAlvsatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPAR--------- 2756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 128 rnlSAAAAAASSSSSSSAAAASHSPGAAGLPASCSASASLCTRSLdrktlllkhrqtlqlqPSDRDWVRHqlqrgcvhvf 207
Cdd:PHA03247 2757 ---PARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESL----------------PSPWDPADP---------- 2807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 208 drhmastylrPVLCTLDTTAGEVAArllqlghkgggvvkvlgqgpgaaaarepaepppeagpRLAPPEPrdsevPPARSA 287
Cdd:PHA03247 2808 ----------PAAVLAPAAALPPAA-------------------------------------SPAGPLP-----PPTSAQ 2835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 288 PGAFGGPPraPPADLPLPVGG---PGG-WSRRA---SPAPSDSSPGEPfvggPVSspRAPRPVVS-DTESFSLSPsaesv 359
Cdd:PHA03247 2836 PTAPPPPP--GPPPPSLPLGGsvaPGGdVRRRPpsrSPAAKPAAPARP----PVR--RLARPAVSrSTESFALPP----- 2902
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291219891 360 sDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPR 421
Cdd:PHA03247 2903 -DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
|
|
| PHA03381 |
PHA03381 |
tegument protein VP22; Provisional |
272-420 |
2.11e-04 |
|
tegument protein VP22; Provisional
Pssm-ID: 177618 [Multi-domain] Cd Length: 290 Bit Score: 45.39 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPRDSEVPPARSAPGAfgGPPRAPP-------------ADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPvSSPR 338
Cdd:PHA03381 30 ASPARVSFEEPADRARRGA--GQARGRSqaerrfhhydearADYPYYTGSSSEDERPADPRPSRRPHAQPEASGP-GPAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 339 APRPVVSdteSFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVpgQPRRPGHPAQPLPLPQTA--SSPQPQ 416
Cdd:PHA03381 107 GARGPAG---SRGRGRRAESPSPRDPPNPKGASAPRGRKSACADSAALLDAP--APAAPKRQKTPAGLARKLhfSTAPTS 181
|
....
gi 291219891 417 QKAP 420
Cdd:PHA03381 182 PTAP 185
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
292-464 |
2.19e-04 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 46.13 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 292 GGPPRAPPADLPLPVGGPGGWSRRASPAPSDSsPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVSDRLDPYSSGGG 371
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAA-PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 372 SSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGSCEEKAAAAVAPGGLQST 451
Cdd:PRK07764 668 GWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
|
170
....*....|...
gi 291219891 452 PGRSGVTAEKAPP 464
Cdd:PRK07764 748 PPDPAGAPAQPPP 760
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
272-429 |
2.38e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 46.00 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPRDSEVPPARSAPGAFGGPPRaPPADLPLPVGGPGGWSRRASPAPS-----DSSPGEPFVGGPVSSPRAPRPVVSD 346
Cdd:PRK07003 387 AAAAVGASAVPAVTAVTGAAGAALA-PKAAAAAAATRAEAPPAAPAPPATadrgdDAADGDAPVPAKANARASADSRCDE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 347 ---TESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAi 423
Cdd:PRK07003 466 rdaQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAA- 544
|
....*.
gi 291219891 424 dSPGGA 429
Cdd:PRK07003 545 -RAGGA 549
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
738-793 |
3.03e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 40.59 E-value: 3.03e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 291219891 738 NLQTFLLDGNFLQSLPAE-LENMKQLSYLGLSFNEFTDI-PEVLEKLTAVDKLCMSGN 793
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGN 59
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
270-442 |
3.61e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 45.55 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 270 RLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPAPSDS----SPGEPFVGGPVSSPRAPRPVVS 345
Cdd:PHA03307 774 LLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDggseSSGPARPPGAAARPPPARSSES 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 346 DTESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQ---QKAPRA 422
Cdd:PHA03307 854 SKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMPPGGPDPRggfRRVPPG 933
|
170 180
....*....|....*....|...
gi 291219891 423 I---DSPGGAVREGSCEEKAAAA 442
Cdd:PHA03307 934 DlhtPAPSAAALAAYCPPEVVAE 956
|
|
| PH |
pfam00169 |
PH domain; PH stands for pleckstrin homology. |
555-636 |
7.99e-04 |
|
PH domain; PH stands for pleckstrin homology.
Pssm-ID: 459697 [Multi-domain] Cd Length: 105 Bit Score: 40.62 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 555 NRWTRRQVILCGTCLIVSSVKDSLTGK--MHVLPLIGGKVEEV-----KKHQHCLAFSSSGPQ-SQTYYICFDTFTEYLR 626
Cdd:pfam00169 16 KSWKKRYFVLFDGSLLYYKDDKSGKSKepKGSISLSGCEVVEVvasdsPKRKFCFELRTGERTgKRTYLLQAESEEERKD 95
|
90
....*....|
gi 291219891 627 WLRQVSKVAS 636
Cdd:pfam00169 96 WIKAIQSAIR 105
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
287-465 |
1.40e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 43.68 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 287 APGAFGGPPRAPPADLPLPVGGPGgwSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVsdrldPY 366
Cdd:PRK07003 361 AVTGGGAPGGGVPARVAGAVPAPG--ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPA-----PP 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 367 SSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAP-RAIDSPGGAVREGSCEEKAAAAVAP 445
Cdd:PRK07003 434 ATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDaAFEPAPRAAAPSAATPAAVPDARAP 513
|
170 180
....*....|....*....|
gi 291219891 446 GGLQstpgrsgvTAEKAPPP 465
Cdd:PRK07003 514 AAAS--------REDAPAAA 525
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
955-1139 |
1.41e-03 |
|
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: 42.73 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 955 LPERLE-RTSVEVLDVQHNQLLELPPNL------LMKADSLRFLNASANKLESLPPATL-SEETNSILQELYLTNNSLTD 1026
Cdd:cd00116 43 LASALRpQPSLKELCLSLNETGRIPRGLqsllqgLTKGCGLQELDLSDNALGPDGCGVLeSLLRSSSLQELKLNNNGLGD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 1027 KCVPLLTG-----HPHLKILHMAYNRLQSFPASKMAKL----EELEEIDLSGNKL--KAIPTTI----MNCrRMHTVIAH 1091
Cdd:cd00116 123 RGLRLLAKglkdlPPALEKLVLGRNRLEGASCEALAKAlranRDLKELNLANNGIgdAGIRALAeglkANC-NLEVLDLN 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 291219891 1092 SNCIEvfpevmqlpeikcvDLSCNELSEvTLPENlpPKLQELDLTGNP 1139
Cdd:cd00116 202 NNGLT--------------DEGASALAE-TLASL--KSLEVLNLGDNN 232
|
|
| SepH |
NF040712 |
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
272-422 |
1.50e-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: 42.83 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPRDSEVPPARSAPGAfggPPRAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFS 351
Cdd:NF040712 193 GRPLRPLATVPRLAREPAD---ARPEEVEPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAE 269
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291219891 352 LSPSAEsvsdrlDPYSSGGGSSSSSEELEADAASAPTgVPGQPRRPGHPAQPLPLPQTAssPQPQQKAPRA 422
Cdd:NF040712 270 PDEATR------DAGEPPAPGAAETPEAAEPPAPAPA-APAAPAAPEAEEPARPEPPPA--PKPKRRRRRA 331
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
917-998 |
1.64e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 38.27 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 917 RKLEVLDIGHNQICELPARLFcnSSLRKLlaghnqlarlperlertsvEVLDVQHNQLLELPPNLLMKADSLRFLNASAN 996
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAF--KGLSNL-------------------KVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGN 59
|
..
gi 291219891 997 KL 998
Cdd:pfam13855 60 RL 61
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
1036-1075 |
1.81e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 38.27 E-value: 1.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 291219891 1036 PHLKILHMAYNRLQSFPASKMAKLEELEEIDLSGNKLKAI 1075
Cdd:pfam13855 1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTL 40
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
288-462 |
1.89e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.94 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 288 PGAFGGPPrAPPADLPLPVGGPGGWSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFSLSPSAESVSDRLDPYS 367
Cdd:PRK12323 365 PGQSGGGA-GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARG 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 368 SGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGSCEEkAAAAVAPGG 447
Cdd:PRK12323 444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQ-PDAAPAGWV 522
|
170
....*....|....*
gi 291219891 448 LQSTPGRSGVTAEKA 462
Cdd:PRK12323 523 AESIPDPATADPDDA 537
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
272-465 |
2.64e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 272 APPEPRDSEVPPARSAPGAfGGPPRAPPADLPLPVGGPggwSRRASPAPSDSSPGEPFVGGPVSSPRAPRPVVSDTESFS 351
Cdd:PHA03307 145 GPPPAASPPAAGASPAAVA-SDAASSRQAALPLSSPEE---TARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 352 LSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQ--------PLPLPQT-ASSPQPQQKAPRA 422
Cdd:PHA03307 221 APAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEasgwngpsSRPGPASsSSSPRERSPSPSP 300
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 291219891 423 IDSPGGAVREGSCEEKAAAAVAPGGLQSTPGRSGVTAEKAPPP 465
Cdd:PHA03307 301 SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSP 343
|
|
| PLN03210 |
PLN03210 |
Resistant to P. syringae 6; Provisional |
636-813 |
2.80e-03 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 42.55 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 636 SQRISSVDLSCCSLEHLPANLfYSQDLTHLNL-----KQNFLRQNPSLPAARGLNElqrftKLKSLNLSNN-HLGDFPLA 709
Cdd:PLN03210 724 STNISWLDLDETAIEEFPSNL-RLENLDELILcemksEKLWERVQPLTPLMTMLSP-----SLTRLFLSDIpSLVELPSS 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 710 VCSIPTLAELNV-SCNALRSVPAAVGVMHNLQTFLLDGNFLQSLPAELENMKQLSylgLSFNEFTDIPEVLEKLTAVDKL 788
Cdd:PLN03210 798 IQNLHKLEHLEIeNCINLETLPTGINLESLESLDLSGCSRLRTFPDISTNISDLN---LSRTGIEEVPWWIEKFSNLSFL 874
|
170 180
....*....|....*....|....*.
gi 291219891 789 CMSGnCVETLRLQA-LRKMPHIKHVD 813
Cdd:PLN03210 875 DMNG-CNNLQRVSLnISKLKHLETVD 899
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
381-459 |
3.16e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 3.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291219891 381 ADAASAPTGVPGQPRRPGHPAQPLPLPQTASSPQPQQKAPRAIDSPGGAVREGSCEEKAAAAVAPGGLQSTPGRSGVTA 459
Cdd:PRK07764 409 APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAA 487
|
|
| PRK14951 |
PRK14951 |
DNA polymerase III subunits gamma and tau; Provisional |
270-397 |
3.32e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 42.01 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 270 RLAPPEPRDSEVPPARSAPGAFGGPPRAPPADLPLPVGGPGGWSRRASPA--PSDSSPGEPFVGGPVSSPRAPRPVVSDT 347
Cdd:PRK14951 360 RLLAFKPAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAaaSAPAAPPAAAPPAPVAAPAAAAPAAAPA 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 291219891 348 ESFSLSPSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRP 397
Cdd:PRK14951 440 AAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLT 489
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
987-1048 |
3.51e-03 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 37.50 E-value: 3.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291219891 987 SLRFLNASANKLESLPPATLSeeTNSILQELYLTNNSLTDKCVPLLTGHPHLKILHMAYNRL 1048
Cdd:pfam13855 2 NLRSLDLSNNRLTSLDDGAFK--GLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
|
|
| PH |
smart00233 |
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ... |
556-636 |
3.64e-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: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 556 RWTRRQVILCGTCLIVSSVKDSLTGKM--HVLPLIGGKVEEV-----KKHQHClaFSSSGPQSQTYYICFDTFTEYLRWL 628
Cdd:smart00233 17 SWKKRYFVLFNSTLLYYKSKKDKKSYKpkGSIDLSGCTVREApdpdsSKKPHC--FEIKTSDRKTLLLQAESEEEREKWV 94
|
....*...
gi 291219891 629 RQVSKVAS 636
Cdd:smart00233 95 EALRKAIA 102
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
1014-1048 |
4.48e-03 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 36.45 E-value: 4.48e-03
10 20 30
....*....|....*....|....*....|....*
gi 291219891 1014 LQELYLTNNSLTDkcVPLLTGHPHLKILHMAYNRL 1048
Cdd:pfam12799 3 LEVLDLSNNQITD--IPPLAKLPNLETLDLSGNNK 35
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
271-425 |
4.49e-03 |
|
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: 42.06 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 271 LAPPEPRDSEVPPARSAPGAfGGPPRA---PPADLPLPVGGPggwsRRASPAPSDSSPGE----PFVGGP----VSSPRA 339
Cdd:pfam03154 317 APGQSQQRIHTPPSQSQLQS-QQPPREqplPPAPLSMPHIKP----PPTTPIPQLPNPQShkhpPHLSGPspfqMNSNLP 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 340 PRPVVSDTESFSL--SPSAE-------SVSDRLDPYSSGGGSSSSSEELEADAASAPTG-----VPGQPRRPGHPAQPLP 405
Cdd:pfam03154 392 PPPALKPLSSLSThhPPSAHppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTsglhqVPSQSPFPQHPFVPGG 471
|
170 180
....*....|....*....|
gi 291219891 406 LPQTASSPQPQQKAPRAIDS 425
Cdd:pfam03154 472 PPPITPPSGPPTSTSSAMPG 491
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
269-426 |
5.99e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 41.59 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 269 PRLAPPEPRDSEVPPARSAPGAF---GGP-PRAPPADLPLPVGG-------------PGG--WSRRASPAPSDSSPgEPF 329
Cdd:PHA03378 621 PRQWPMPLRPIPMRPLRMQPITFnvlVFPtPHQPPQVEITPYKPtwtqighipyqpsPTGanTMLPIQWAPGTMQP-PPR 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 330 VGGPVSSPRAP-----RPVVSDTEsfslSPSAESVSDRLDPySSGGGSSSSSEELEADAASAPTGVPGQPRRP-GHPAQP 403
Cdd:PHA03378 700 APTPMRPPAAPpgraqRPAAATGR----ARPPAAAPGRARP-PAAAPGRARPPAAAPGRARPPAAAPGRARPPaAAPGAP 774
|
170 180
....*....|....*....|...
gi 291219891 404 LPLPQTASSPQPQQKaPRAIDSP 426
Cdd:PHA03378 775 TPQPPPQAPPAPQQR-PRGAPTP 796
|
|
| SAV_2336_NTERM |
NF041121 |
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ... |
272-340 |
6.30e-03 |
|
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.
Pssm-ID: 469044 [Multi-domain] Cd Length: 473 Bit Score: 41.14 E-value: 6.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291219891 272 APPEPRDSEVP-----PARSAPGAFGGPPRAPPADLPLPVGGPGGwSRRASPAPSDSSPGEPFVGGPVSSPRAP 340
Cdd:NF041121 25 EGPAPTAASQPatpppPAAPPSPPGDPPEPPAPEPAPLPAPYPGS-LAPPPPPPPGPAGAAPGAALPVRVPAPP 97
|
|
| KLF17_N |
cd21574 |
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like ... |
282-421 |
7.04e-03 |
|
N-terminal domain of Kruppel-like factor 17; Kruppel-like factor 17 (KLF17), or Krueppel-like factor 17, is a protein that, in humans, is encoded by the KLF17 gene and acts as a tumor suppressor. It negatively regulates epithelial-mesenchymal transition and metastasis in breast cancer. KLF17 is thought to be the human ortholog of the mouse gene, zinc finger protein 393 (Zfp393), although it has diverged significantly. KLF17 can regulate gene transcription from CACCC-box elements. It belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF17.
Pssm-ID: 410567 Cd Length: 286 Bit Score: 40.45 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291219891 282 PPARSAPGAFGGPPRAPPAdlPLPVGGPGGwsrrASPAPSDSSPGEPFVGGP-VSSPRA---PR----PVVSDTESFSLS 353
Cdd:cd21574 131 PNIPGVAMTFSGNLRMPPS--GLPVSASSG----IPMMSHIRAPTMPYSGPPtVPSNRDsltPKmllaPTMPSTEAQAVL 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291219891 354 PSAESVSDRLDPYSSGGGSSSSSEELEADAASAPTGVPGQPRRPGHPAQPLPLPQTA-SSPQPQQKAPR 421
Cdd:cd21574 205 PSLAQMLPPRDPHNLGMPPAGSPSLLALESQDSLVSQPASQEDPFLPEQPIPAPQRAeQNSRAQERAPR 273
|
|
| LRR_4 |
pfam12799 |
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
1105-1153 |
9.03e-03 |
|
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.
Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 35.68 E-value: 9.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 291219891 1105 PEIKCVDLSCNELSEVTLPENLPpKLQELDLTGNPRLvldhKTLELLNN 1153
Cdd:pfam12799 1 PNLEVLDLSNNQITDIPPLAKLP-NLETLDLSGNNKI----TDLSDLAN 44
|
|
| |
