|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1093 |
8.87e-117 |
|
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).
:
Pssm-ID: 464966 [Multi-domain] Cd Length: 299 Bit Score: 367.95 E-value: 8.87e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 790 AENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 870 DHFSRRGKTLPQQESL-EIELTEEKPVKRSIITVEeltEIERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 949 -EFDLDKALEEVPIHIED----PPFPSLRQEK------RSSGFISELPSeEGKKLEHFTKLRPKRNKKQQPTQAALFVlq 1017
Cdd:pfam16000 152 sELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV-- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622935413 1018 vcaanIVSQDGEQNGHMGRVDEGVDEFFTKKVTKMDSKkwSTRGSESHELNEGGDEKKKRDSRKsSGFLNLIKSRS 1093
Cdd:pfam16000 229 -----GPAQDGEQNGLSGRVDEGLEDFFSKKVIKLSTP--TSPTSEPSSSSLFPDSPKKRKKRK-SGFFNFIKPRS 296
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
1.04e-35 |
|
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.
:
Pssm-ID: 436119 Cd Length: 94 Bit Score: 130.87 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVICSKSAQMVVETEKCNISMKMASPEDVSEVLAHIGTCLRKI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 1622935413 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
260-662 |
5.37e-17 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
The actual alignment was detected with superfamily member COG5238:
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 85.23 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 260 IDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSlsqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNA--------------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 340 VHLDLSGNVLRGDDLSHMYNFLaQPNAIAHLDLSNTECSLD---MVCGALLRGclQYLAVLNLSRTVFshrkGKEVPPSF 416
Cdd:COG5238 156 VHLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDEgieELAEALTQN--TTVTTLWLKRNPI----GDEGAEIL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 417 KQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELGHclrsGGAQVLEGCIAEIHNITSLDISDN 496
Cdd:COG5238 229 AEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGA----EGAIALAKALQGNTTLTSLDLSVN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 497 GLesdlstlivwlsKNRSIqhLALGKNFNNMKsknltpvldnlvqmiqdeesPLQSLSLADSKLKTEVTI-IINALGSNT 575
Cdd:COG5238 303 RI------------GDEGA--IALAEGLQGNK--------------------TLHTLNLAYNGIGAQGAIaLAKALQENT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 576 SLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDASQAlktnpeK 653
Cdd:COG5238 349 TLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------R 422
|
....*....
gi 1622935413 654 TEEALQKIE 662
Cdd:COG5238 423 LEQLLERIK 431
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1093 |
8.87e-117 |
|
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).
Pssm-ID: 464966 [Multi-domain] Cd Length: 299 Bit Score: 367.95 E-value: 8.87e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 790 AENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 870 DHFSRRGKTLPQQESL-EIELTEEKPVKRSIITVEeltEIERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 949 -EFDLDKALEEVPIHIED----PPFPSLRQEK------RSSGFISELPSeEGKKLEHFTKLRPKRNKKQQPTQAALFVlq 1017
Cdd:pfam16000 152 sELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV-- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622935413 1018 vcaanIVSQDGEQNGHMGRVDEGVDEFFTKKVTKMDSKkwSTRGSESHELNEGGDEKKKRDSRKsSGFLNLIKSRS 1093
Cdd:pfam16000 229 -----GPAQDGEQNGLSGRVDEGLEDFFSKKVIKLSTP--TSPTSEPSSSSLFPDSPKKRKKRK-SGFFNFIKPRS 296
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
1.04e-35 |
|
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.
Pssm-ID: 436119 Cd Length: 94 Bit Score: 130.87 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVICSKSAQMVVETEKCNISMKMASPEDVSEVLAHIGTCLRKI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 1622935413 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
260-662 |
5.37e-17 |
|
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: 85.23 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 260 IDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSlsqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNA--------------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 340 VHLDLSGNVLRGDDLSHMYNFLaQPNAIAHLDLSNTECSLD---MVCGALLRGclQYLAVLNLSRTVFshrkGKEVPPSF 416
Cdd:COG5238 156 VHLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDEgieELAEALTQN--TTVTTLWLKRNPI----GDEGAEIL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 417 KQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELGHclrsGGAQVLEGCIAEIHNITSLDISDN 496
Cdd:COG5238 229 AEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGA----EGAIALAKALQGNTTLTSLDLSVN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 497 GLesdlstlivwlsKNRSIqhLALGKNFNNMKsknltpvldnlvqmiqdeesPLQSLSLADSKLKTEVTI-IINALGSNT 575
Cdd:COG5238 303 RI------------GDEGA--IALAEGLQGNK--------------------TLHTLNLAYNGIGAQGAIaLAKALQENT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 576 SLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDASQAlktnpeK 653
Cdd:COG5238 349 TLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------R 422
|
....*....
gi 1622935413 654 TEEALQKIE 662
Cdd:COG5238 423 LEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
229-373 |
4.45e-12 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 68.92 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622935413 309 HLNLSKTSLSPKGVNSLsqsLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIAHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAAL---ASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
231-587 |
4.34e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 48.31 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 231 STDVCEQILRVVSRSNRLEELVLENAGLridfAQKLASALAHNPNsgLHTINLAGNPLEdrgvSSLSIQFAKLPKGLKHL 310
Cdd:PLN00113 54 SADVCLWQGITCNNSSRVVSIDLSGKNI----SGKISSAIFRLPY--IQTINLSNNQLS----GPIPDDIFTTSSSLRYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 311 NLSKTSLS---PKGVNSLSQSL--SANPLTA---------STLVHLDLSGNVLRGddlsHMYNFLAQPNAIAHLDLSNTE 376
Cdd:PLN00113 124 NLSNNNFTgsiPRGSIPNLETLdlSNNMLSGeipndigsfSSLKVLDLGGNVLVG----KIPNSLTNLTSLEFLTLASNQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 377 C--SLDMVCGALLRGCLQYLAVLNLSrtvfshrkgKEVPPSFKQFFS-SSLALMHINLSGtklsPEPlkalllglacnhn 453
Cdd:PLN00113 200 LvgQIPRELGQMKSLKWIYLGYNNLS---------GEIPYEIGGLTSlNHLDLVYNNLTG----PIP------------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 454 lkgVSL-DLSNCELGHCLRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLsKNRSIQHLalgknFNNMKSKNL 532
Cdd:PLN00113 254 ---SSLgNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQL-QNLEILHL-----FSNNFTGKI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622935413 533 TPVLDNLVQmiqdeespLQSLSLADSKLKTEvtiIINALGSNTSLTKVDISGNGM 587
Cdd:PLN00113 325 PVALTSLPR--------LQVLQLWSNKFSGE---IPKNLGKHNNLTVLDLSTNNL 368
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1093 |
8.87e-117 |
|
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).
Pssm-ID: 464966 [Multi-domain] Cd Length: 299 Bit Score: 367.95 E-value: 8.87e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 790 AENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 870 DHFSRRGKTLPQQESL-EIELTEEKPVKRSIITVEeltEIERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 949 -EFDLDKALEEVPIHIED----PPFPSLRQEK------RSSGFISELPSeEGKKLEHFTKLRPKRNKKQQPTQAALFVlq 1017
Cdd:pfam16000 152 sELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV-- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622935413 1018 vcaanIVSQDGEQNGHMGRVDEGVDEFFTKKVTKMDSKkwSTRGSESHELNEGGDEKKKRDSRKsSGFLNLIKSRS 1093
Cdd:pfam16000 229 -----GPAQDGEQNGLSGRVDEGLEDFFSKKVIKLSTP--TSPTSEPSSSSLFPDSPKKRKKRK-SGFFNFIKPRS 296
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
1.04e-35 |
|
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.
Pssm-ID: 436119 Cd Length: 94 Bit Score: 130.87 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVICSKSAQMVVETEKCNISMKMASPEDVSEVLAHIGTCLRKI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 1622935413 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
260-662 |
5.37e-17 |
|
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: 85.23 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 260 IDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSlsqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNA--------------- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 340 VHLDLSGNVLRGDDLSHMYNFLaQPNAIAHLDLSNTECSLD---MVCGALLRGclQYLAVLNLSRTVFshrkGKEVPPSF 416
Cdd:COG5238 156 VHLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDEgieELAEALTQN--TTVTTLWLKRNPI----GDEGAEIL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 417 KQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELGHclrsGGAQVLEGCIAEIHNITSLDISDN 496
Cdd:COG5238 229 AEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGA----EGAIALAKALQGNTTLTSLDLSVN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 497 GLesdlstlivwlsKNRSIqhLALGKNFNNMKsknltpvldnlvqmiqdeesPLQSLSLADSKLKTEVTI-IINALGSNT 575
Cdd:COG5238 303 RI------------GDEGA--IALAEGLQGNK--------------------TLHTLNLAYNGIGAQGAIaLAKALQENT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 576 SLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDASQAlktnpeK 653
Cdd:COG5238 349 TLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------R 422
|
....*....
gi 1622935413 654 TEEALQKIE 662
Cdd:COG5238 423 LEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
229-373 |
4.45e-12 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 68.92 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622935413 309 HLNLSKTSLSPKGVNSLsqsLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIAHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAAL---ASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
281-599 |
5.39e-12 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 68.54 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 281 INLAGNPLEDRGVSSLSiQFAKLPKGLKHLNLS--KTSLSPKGVNSLSQSLSANPLtastLVHLDLSGNVLrGDDLSHMY 358
Cdd:cd00116 28 LRLEGNTLGEEAAKALA-SALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGCG----LQELDLSDNAL-GPDGCGVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 359 NFLAQPNAIAHLDLSNTECS---LDMVCGALlRGCLQYLAVLNLSRTVFSHRKGKEVppsfKQFFSSSLALMHINLSGTK 435
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGdrgLRLLAKGL-KDLPPALEKLVLGRNRLEGASCEAL----AKALRANRDLKELNLANNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 436 LSPEPLKALLLGLACNHNLKgvSLDLSNCelghCLRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKNRSI 515
Cdd:cd00116 177 IGDAGIRALAEGLKANCNLE--VLDLNNN----GLTDEGASALAETLASLKSLEVLNLGDNNL------------TDAGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 516 QHLALGknfnnMKSKNLTpvldnlvqmiqdeespLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKM 594
Cdd:cd00116 239 AALASA-----LLSPNIS----------------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEGAQL 297
|
....*
gi 1622935413 595 LAKAL 599
Cdd:cd00116 298 LAESL 302
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
221-466 |
1.18e-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: 67.77 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 221 TKLSSKDLKLSTDVCeQILRVVSRSNRLEELVLENAGLRIDFAQKLASALAHNPnSGLHTINLAGNPLEDRGVSSLSIQF 300
Cdd:cd00116 84 QELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLP-PALEKLVLGRNRLEGASCEALAKAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 301 AKLPKgLKHLNLSKTSLSPKGVNSLSQSLSANPLtastLVHLDLSGNVLRGDDLSHMYNFLAQPNAIAHLDLSNteCSLD 380
Cdd:cd00116 162 RANRD-LKELNLANNGIGDAGIRALAEGLKANCN----LEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD--NNLT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 381 MVCGALL----RGCLQYLAVLNLSRTVFSHRKGKevppSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNlKG 456
Cdd:cd00116 235 DAGAAALasalLSPNISLLTLSLSCNDITDDGAK----DLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN-EL 309
|
250
....*....|
gi 1622935413 457 VSLDLSNCEL 466
Cdd:cd00116 310 ESLWVKDDSF 319
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
246-638 |
9.28e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 65.73 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 246 NRLEELVLENAGLRIDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSL 325
Cdd:COG4886 1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 326 SQSLSANPLTA----STLVHLDLSGNvlrgddlshmyNFLAQPNAIAHLDLSNTECSlDMvcGALLRGcLQYLAVLNLSR 401
Cdd:COG4886 81 LLSLLLLGLTDlgdlTNLTELDLSGN-----------EELSNLTNLESLDLSGNQLT-DL--PEELAN-LTNLKELDLSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 402 TVFShrkgkEVPPSFKQFfsSSLAlmHINLSGTKLS--PEPLKALllglacnHNLKgvSLDLSNCELghclrsggaQVLE 479
Cdd:COG4886 146 NQLT-----DLPEPLGNL--TNLK--SLDLSNNQLTdlPEELGNL-------TNLK--ELDLSNNQI---------TDLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 480 GCIAEIHNITSLDISDNglesDLSTLIVWLSKNRSIQHLALGKNfnnmkskNLT--PVLDNLVQmiqdeespLQSLSLAD 557
Cdd:COG4886 199 EPLGNLTNLEELDLSGN----QLTDLPEPLANLTNLETLDLSNN-------QLTdlPELGNLTN--------LEELDLSN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 558 SKLKTevtiiINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMP 637
Cdd:COG4886 260 NQLTD-----LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLL 334
|
.
gi 1622935413 638 I 638
Cdd:COG4886 335 V 335
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
244-352 |
1.23e-09 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 62.11 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 244 RSNRLEELVLENAGLRIDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVN 323
Cdd:COG5238 318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIAL-AKYLEGNTTLRELNLGKNNIGKQGAE 394
|
90 100
....*....|....*....|....*....
gi 1622935413 324 SLSQSLSANPLTAstlvhLDLSGNVLRGD 352
Cdd:COG5238 395 ALIDALQTNRLHT-----LILDGNLIGAE 418
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
217-479 |
2.21e-09 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 61.34 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 217 NQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSL 296
Cdd:COG5238 179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKS--LTTLDLSNNQIGDEGVIAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 297 sIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPltasTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIAHLDLSNte 376
Cdd:COG5238 257 -AEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT----TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 377 CSLDMVCGALLRGCLQY---LAVLNLSrtvfSHRKGKEVPPSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNhN 453
Cdd:COG5238 330 NGIGAQGAIALAKALQEnttLHSLDLS----DNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-R 404
|
250 260
....*....|....*....|....*.
gi 1622935413 454 LKgvSLDLSNCELGHCLRSGGAQVLE 479
Cdd:COG5238 405 LH--TLILDGNLIGAEAQQRLEQLLE 428
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
418-636 |
9.89e-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: 58.52 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 418 QFFSSSLALMHINLSGTKLSPE---PLKALLLGLACNHnlkgvsLDLSNCELGhclRSGGAQVLEGCIAEIHNITSLDIS 494
Cdd:cd00116 75 QGLTKGCGLQELDLSDNALGPDgcgVLESLLRSSSLQE------LKLNNNGLG---DRGLRLLAKGLKDLPPALEKLVLG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 495 DNGLESDLST-LIVWLSKNRSIQHLALGKNfnnmksknltPVLDNLVQMIQD---EESPLQSLSLADSKL-KTEVTIIIN 569
Cdd:cd00116 146 RNRLEGASCEaLAKALRANRDLKELNLANN----------GIGDAGIRALAEglkANCNLEVLDLNNNGLtDEGASALAE 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622935413 570 ALGSNTSLTKVDISGNGMGDMGAKMLAKAL-QINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFM 636
Cdd:cd00116 216 TLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLEL 283
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
417-634 |
1.69e-08 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 57.75 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 417 KQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELGHCLRsgGAQVLEGCIAEIHNITSLDISDN 496
Cdd:cd00116 16 TELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLK--ELCLSLNETGRIPR--GLQSLLQGLTKGCGLQELDLSDN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 497 GLESDLSTLIVWLSKNRSIQHL-----ALGKNFNNMKSKNLTPVldnlvqmiqdeESPLQSLSLADSKLKTEVTI-IINA 570
Cdd:cd00116 92 ALGPDGCGVLESLLRSSSLQELklnnnGLGDRGLRLLAKGLKDL-----------PPALEKLVLGRNRLEGASCEaLAKA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622935413 571 LGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLR 634
Cdd:cd00116 161 LRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLE 224
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
482-651 |
1.23e-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: 55.44 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 482 IAEIHNITSLDISDNGL-ESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNL--------------------V 540
Cdd:cd00116 19 LPKLLCLQVLRLEGNTLgEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQGLtkgcglqeldlsdnalgpdgC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 541 QMIQD--EESPLQSLSLADSKL-KTEVTIIINALGSNT-SLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNIT 616
Cdd:cd00116 99 GVLESllRSSSLQELKLNNNGLgDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622935413 617 AQGFQDIAVAMEKNYTLR--------FMPIPMYDASQALKTNP 651
Cdd:cd00116 179 DAGIRALAEGLKANCNLEvldlnnngLTDEGASALAETLASLK 221
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
187-347 |
1.33e-07 |
|
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: 55.95 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 187 LTQDT--RELNLQDfSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLEnaGLRIDF-- 262
Cdd:COG5238 204 LTQNTtvTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLS--GNQIGAeg 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 263 AQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPltasTLVHL 342
Cdd:COG5238 281 AIALAKALQGNTT--LTSLDLSVNRIGDEGAIAL-AEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENT----TLHSL 353
|
....*
gi 1622935413 343 DLSGN 347
Cdd:COG5238 354 DLSDN 358
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
231-587 |
4.34e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 48.31 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 231 STDVCEQILRVVSRSNRLEELVLENAGLridfAQKLASALAHNPNsgLHTINLAGNPLEdrgvSSLSIQFAKLPKGLKHL 310
Cdd:PLN00113 54 SADVCLWQGITCNNSSRVVSIDLSGKNI----SGKISSAIFRLPY--IQTINLSNNQLS----GPIPDDIFTTSSSLRYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 311 NLSKTSLS---PKGVNSLSQSL--SANPLTA---------STLVHLDLSGNVLRGddlsHMYNFLAQPNAIAHLDLSNTE 376
Cdd:PLN00113 124 NLSNNNFTgsiPRGSIPNLETLdlSNNMLSGeipndigsfSSLKVLDLGGNVLVG----KIPNSLTNLTSLEFLTLASNQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 377 C--SLDMVCGALLRGCLQYLAVLNLSrtvfshrkgKEVPPSFKQFFS-SSLALMHINLSGtklsPEPlkalllglacnhn 453
Cdd:PLN00113 200 LvgQIPRELGQMKSLKWIYLGYNNLS---------GEIPYEIGGLTSlNHLDLVYNNLTG----PIP------------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622935413 454 lkgVSL-DLSNCELGHCLRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLsKNRSIQHLalgknFNNMKSKNL 532
Cdd:PLN00113 254 ---SSLgNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQL-QNLEILHL-----FSNNFTGKI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622935413 533 TPVLDNLVQmiqdeespLQSLSLADSKLKTEvtiIINALGSNTSLTKVDISGNGM 587
Cdd:PLN00113 325 PVALTSLPR--------LQVLQLWSNKFSGE---IPKNLGKHNNLTVLDLSTNNL 368
|
|
| |
