|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1087 |
1.70e-114 |
|
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: 361.78 E-value: 1.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 790 AETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 870 NHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDltEVERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM- 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLPDGDRPESSPLGPGKRHEG--EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSVs 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 949 EFDLDKALEEVPIHIED----PPFPSVRQEK------RSSGLISELPSeEGRRLEHFTKLRPKRNKKQQPTQAAVCTisI 1018
Cdd:pfam16000 153 ELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV--G 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755544329 1019 LPQDGEQNGLMGRVDEGVDEFFTKKVTKMDcKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSR 1087
Cdd:pfam16000 230 PAQDGEQNGLSGRVDEGLEDFFSKKVIKLS-TPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSS 297
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
3.16e-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: 129.32 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 38 GDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 755544329 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 |
4.84e-18 |
|
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: 88.69 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 260 IDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSLcqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNAV-------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 340 tHLDLSGNALRGDDLSHMYNFLaQPNTIVHLDLSNTECSLEmvcsallrGCLQCLAVLNLSRSVFShrkgkevppsfkqf 419
Cdd:COG5238 157 -HLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDE--------GIEELAEALTQNTTVTT-------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 420 fssslaliqINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEIHNITSLDISDNGL- 498
Cdd:COG5238 213 ---------LWLKRNPIGDEGAEILAEALKGNKSLT--TLDLSNNQIG----DEGVIALAEALKNNTTVETLYLSGNQIg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 499 ESDLSTLIVWLSKNRSIQHLALgkNFNNMKSKNLTpvldNLVQMIQdEDSPLQSLSLADSKLKAEVTI-IINALGSNTSL 577
Cdd:COG5238 278 AEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAI----ALAEGLQ-GNKTLHTLNLAYNGIGAQGAIaLAKALQENTTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 578 TKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDAAQAlktnpeKTE 655
Cdd:COG5238 351 HSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------RLE 424
|
....*..
gi 755544329 656 EALQKIE 662
Cdd:COG5238 425 QLLERIK 431
|
|
| PHA03307 super family |
cl33723 |
transcriptional regulator ICP4; Provisional |
1007-1394 |
2.20e-05 |
|
transcriptional regulator ICP4; Provisional
The actual alignment was detected with superfamily member PHA03307:
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1007 QPTQAAVCTISILPQD---GEQNGLMGRVDEGVDEFFTkkVTKMDCKRSssRSSDAHELGEGDEKKKRDSRrsgflnliK 1083
Cdd:PHA03307 19 EFFPRPPATPGDAADDllsGSQGQLVSDSAELAAVTVV--AGAAACDRF--EPPTGPPPGPGTEAPANESR--------S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1084 SRSRSERPPTVLMTEELSSPKGAMRSPPVDTTRKEIKAA-EHNGAPDRTEEIKTPEPLEEGP------AEEAGRAERSDS 1156
Cdd:PHA03307 87 TPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASpPPSPAPDLSEMLRPVGSPGPPPaasppaAGASPAAVASDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1157 RGSPQG------GRRYVQVMGSGLlAEMKAKQERRAACAQKKLGNDVISQDPSSPVSCNTERLEGGAtVPKLQPGLPEAR 1230
Cdd:PHA03307 167 ASSRQAalplssPEETARAPSSPP-AEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-GASSSDSSSSES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1231 FGSGTPEKNAKAEPR----VDGGCRSRSSSSMPTSPKPLLQSPKPSPSARPSIPQKPRTASRPEDTPdspsgpsspkval 1306
Cdd:PHA03307 245 SGCGWGPENECPLPRpapiTLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSS------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1307 lPPILKKVSSDKERDGQNSSQSSPRSFSQEVQRGDYFKRHSDHDSGKPSSRGKRSSKlyfaiAEEEANAPGYRKSQPTNA 1386
Cdd:PHA03307 312 -PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK-----RPRPSRAPSSPAASAGRP 385
|
....*...
gi 755544329 1387 SRRSWGPA 1394
Cdd:PHA03307 386 TRRRARAA 393
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1087 |
1.70e-114 |
|
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: 361.78 E-value: 1.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 790 AETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 870 NHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDltEVERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM- 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLPDGDRPESSPLGPGKRHEG--EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSVs 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 949 EFDLDKALEEVPIHIED----PPFPSVRQEK------RSSGLISELPSeEGRRLEHFTKLRPKRNKKQQPTQAAVCTisI 1018
Cdd:pfam16000 153 ELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV--G 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755544329 1019 LPQDGEQNGLMGRVDEGVDEFFTKKVTKMDcKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSR 1087
Cdd:pfam16000 230 PAQDGEQNGLSGRVDEGLEDFFSKKVIKLS-TPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSS 297
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
3.16e-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: 129.32 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 38 GDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 755544329 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
260-662 |
4.84e-18 |
|
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: 88.69 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 260 IDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSLcqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNAV-------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 340 tHLDLSGNALRGDDLSHMYNFLaQPNTIVHLDLSNTECSLEmvcsallrGCLQCLAVLNLSRSVFShrkgkevppsfkqf 419
Cdd:COG5238 157 -HLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDE--------GIEELAEALTQNTTVTT-------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 420 fssslaliqINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEIHNITSLDISDNGL- 498
Cdd:COG5238 213 ---------LWLKRNPIGDEGAEILAEALKGNKSLT--TLDLSNNQIG----DEGVIALAEALKNNTTVETLYLSGNQIg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 499 ESDLSTLIVWLSKNRSIQHLALgkNFNNMKSKNLTpvldNLVQMIQdEDSPLQSLSLADSKLKAEVTI-IINALGSNTSL 577
Cdd:COG5238 278 AEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAI----ALAEGLQ-GNKTLHTLNLAYNGIGAQGAIaLAKALQENTTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 578 TKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDAAQAlktnpeKTE 655
Cdd:COG5238 351 HSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------RLE 424
|
....*..
gi 755544329 656 EALQKIE 662
Cdd:COG5238 425 QLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
229-373 |
2.64e-13 |
|
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: 72.77 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755544329 309 HLNLSKTSLSPKGVNSLCqslSANPLTASTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAALA---SALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1007-1394 |
2.20e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1007 QPTQAAVCTISILPQD---GEQNGLMGRVDEGVDEFFTkkVTKMDCKRSssRSSDAHELGEGDEKKKRDSRrsgflnliK 1083
Cdd:PHA03307 19 EFFPRPPATPGDAADDllsGSQGQLVSDSAELAAVTVV--AGAAACDRF--EPPTGPPPGPGTEAPANESR--------S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1084 SRSRSERPPTVLMTEELSSPKGAMRSPPVDTTRKEIKAA-EHNGAPDRTEEIKTPEPLEEGP------AEEAGRAERSDS 1156
Cdd:PHA03307 87 TPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASpPPSPAPDLSEMLRPVGSPGPPPaasppaAGASPAAVASDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1157 RGSPQG------GRRYVQVMGSGLlAEMKAKQERRAACAQKKLGNDVISQDPSSPVSCNTERLEGGAtVPKLQPGLPEAR 1230
Cdd:PHA03307 167 ASSRQAalplssPEETARAPSSPP-AEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-GASSSDSSSSES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1231 FGSGTPEKNAKAEPR----VDGGCRSRSSSSMPTSPKPLLQSPKPSPSARPSIPQKPRTASRPEDTPdspsgpsspkval 1306
Cdd:PHA03307 245 SGCGWGPENECPLPRpapiTLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSS------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1307 lPPILKKVSSDKERDGQNSSQSSPRSFSQEVQRGDYFKRHSDHDSGKPSSRGKRSSKlyfaiAEEEANAPGYRKSQPTNA 1386
Cdd:PHA03307 312 -PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK-----RPRPSRAPSSPAASAGRP 385
|
....*...
gi 755544329 1387 SRRSWGPA 1394
Cdd:PHA03307 386 TRRRARAA 393
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1087 |
1.70e-114 |
|
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: 361.78 E-value: 1.70e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 790 AETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 870 NHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDltEVERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM- 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLPDGDRPESSPLGPGKRHEG--EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSVs 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 949 EFDLDKALEEVPIHIED----PPFPSVRQEK------RSSGLISELPSeEGRRLEHFTKLRPKRNKKQQPTQAAVCTisI 1018
Cdd:pfam16000 153 ELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV--G 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755544329 1019 LPQDGEQNGLMGRVDEGVDEFFTKKVTKMDcKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSR 1087
Cdd:pfam16000 230 PAQDGEQNGLSGRVDEGLEDFFSKKVIKLS-TPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSS 297
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
3.16e-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: 129.32 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 38 GDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 755544329 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
260-662 |
4.84e-18 |
|
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: 88.69 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 260 IDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSLcqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNAV-------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 340 tHLDLSGNALRGDDLSHMYNFLaQPNTIVHLDLSNTECSLEmvcsallrGCLQCLAVLNLSRSVFShrkgkevppsfkqf 419
Cdd:COG5238 157 -HLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDE--------GIEELAEALTQNTTVTT-------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 420 fssslaliqINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEIHNITSLDISDNGL- 498
Cdd:COG5238 213 ---------LWLKRNPIGDEGAEILAEALKGNKSLT--TLDLSNNQIG----DEGVIALAEALKNNTTVETLYLSGNQIg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 499 ESDLSTLIVWLSKNRSIQHLALgkNFNNMKSKNLTpvldNLVQMIQdEDSPLQSLSLADSKLKAEVTI-IINALGSNTSL 577
Cdd:COG5238 278 AEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAI----ALAEGLQ-GNKTLHTLNLAYNGIGAQGAIaLAKALQENTTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 578 TKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDAAQAlktnpeKTE 655
Cdd:COG5238 351 HSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------RLE 424
|
....*..
gi 755544329 656 EALQKIE 662
Cdd:COG5238 425 QLLERIK 431
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
250-628 |
2.14e-15 |
|
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: 80.22 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 250 ELVLENAGLRIDFAQKLAGALAH----NPNSGLHTINLAGNSLEDRGVSSLSIQFAKlPKGLKHLNLSKTSLSPKGVNSL 325
Cdd:COG5238 150 PLGGNAVHLLGLAARLGLLAAISmakaLQNNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEIL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 326 CQSLSANPltasTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDlsntecslemvcsallrgclqclavlnlsrsvfs 405
Cdd:COG5238 229 AEALKGNK----SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLY---------------------------------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 406 hrkgkevppsfkqffssslaliqinLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEI 485
Cdd:COG5238 271 -------------------------LSGNQIGAEGAIALAKALQGNTTLT--SLDLSVNRIG----DEGAIALAEGLQGN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 486 HNITSLDISDNGLESDLSTLIvwlsknrsIQHLALGKNfnnmksknltpvldnlvqmiqdedspLQSLSLADSKLKAE-V 564
Cdd:COG5238 320 KTLHTLNLAYNGIGAQGAIAL--------AKALQENTT--------------------------LHSLDLSDNQIGDEgA 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755544329 565 TIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINtKLRTVIWDKNNITAQGFQDIAVAME 628
Cdd:COG5238 366 IALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLEQLLE 428
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
403-665 |
4.28e-14 |
|
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: 76.37 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 403 VFSHRKGKEVPpSFKQFFSSSLALIQINLSGTKLSPEPLKALLLGlacNHSLKGVS---LDLSNCELGHCLRSGGAQVLE 479
Cdd:COG5238 103 VALAETATAVA-TPPPDLRRIMAKTLEDSLILYLALPRRINLIQV---LKDPLGGNavhLLGLAARLGLLAAISMAKALQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 480 GCIAEIHNITSLDISDNGLESdlstLIVWLSKNRSIQHLALGKNfnNMKSKNLtpvlDNLVQMIQdEDSPLQSLSLADSK 559
Cdd:COG5238 179 NNSVETVYLGCNQIGDEGIEE----LAEALTQNTTVTTLWLKRN--PIGDEGA----EILAEALK-GNKSLTTLDLSNNQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 560 LKAE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPI 638
Cdd:COG5238 248 IGDEgVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNL 327
|
250 260 270
....*....|....*....|....*....|....*.
gi 755544329 639 pMYDA---------AQALKTNPekTEEALQKIENYL 665
Cdd:COG5238 328 -AYNGigaqgaialAKALQENT--TLHSLDLSDNQI 360
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
229-373 |
2.64e-13 |
|
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: 72.77 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755544329 309 HLNLSKTSLSPKGVNSLCqslSANPLTASTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAALA---SALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
281-599 |
3.67e-13 |
|
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: 72.39 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 281 INLAGNSLEDRGVSSLSiQFAKLPKGLKHLNLS--KTSLSPKGVNSLCQSLSANPLtastLTHLDLSGNALrGDDLSHMY 358
Cdd:cd00116 28 LRLEGNTLGEEAAKALA-SALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGCG----LQELDLSDNAL-GPDGCGVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 359 NFLAQPNTIVHLDLSNteCSLE-----MVCSALLRgcLQC-LAVLNLSRSVFSHRKGKEVppsfKQFFSSSLALIQINLS 432
Cdd:cd00116 102 ESLLRSSSLQELKLNN--NGLGdrglrLLAKGLKD--LPPaLEKLVLGRNRLEGASCEAL----AKALRANRDLKELNLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 433 GTKLSPEPLKALLLGLACNHSLKgvSLDLSNCelghCLRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKN 512
Cdd:cd00116 174 NNGIGDAGIRALAEGLKANCNLE--VLDLNNN----GLTDEGASALAETLASLKSLEVLNLGDNNL------------TD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 513 RSIQHLALGknfnnMKSKNLTpvldnlvqmiqdedspLQSLSLADSKLKAE-VTIIINALGSNTSLTKVDISGNGMGDMG 591
Cdd:cd00116 236 AGAAALASA-----LLSPNIS----------------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEG 294
|
....*...
gi 755544329 592 AKMLAKAL 599
Cdd:cd00116 295 AQLLAESL 302
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
221-400 |
6.30e-13 |
|
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: 71.62 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 221 TKLSSKDLKLSTDVCeQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPnSGLHTINLAGNSLEDRGVSSLSIQF 300
Cdd:cd00116 84 QELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLP-PALEKLVLGRNRLEGASCEALAKAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 301 AKLPKgLKHLNLSKTSLSPKGVNSLCQSLSANPLtastLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLSNTECSLE 380
Cdd:cd00116 162 RANRD-LKELNLANNGIGDAGIRALAEGLKANCN----LEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDA 236
|
170 180
....*....|....*....|...
gi 755544329 381 ---MVCSALLRGcLQCLAVLNLS 400
Cdd:cd00116 237 gaaALASALLSP-NISLLTLSLS 258
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
248-355 |
8.00e-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: 68.15 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 248 LEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQ 327
Cdd:cd00116 195 LEVLDLNNNGLTDEGASALAETLASLKS--LEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAE 272
|
90 100 110
....*....|....*....|....*....|
gi 755544329 328 SLSANPltasTLTHLDLSGNAL--RGDDLS 355
Cdd:cd00116 273 VLAEKE----SLLELDLRGNKFgeEGAQLL 298
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
294-663 |
6.97e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 66.11 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 294 SSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQSLSANPLTASTLTHLDLSGNalrgddlshmyNFLAQPNTIVHLDLS 373
Cdd:COG4886 53 LSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----------EELSNLTNLESLDLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 374 NTEcsLEMVCSALLRgcLQCLAVLNLSRSVFShrkgkEVPPSFKQFfsssLALIQINLSGTKLS--PEPLKALllglacn 451
Cdd:COG4886 122 GNQ--LTDLPEELAN--LTNLKELDLSNNQLT-----DLPEPLGNL----TNLKSLDLSNNQLTdlPEELGNL------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 452 HSLKgvSLDLSNCELghclrsggaQVLEGCIAEIHNITSLDISDNglesDLSTLIVWLSKNRSIQHLALGKNfnnmkskN 531
Cdd:COG4886 182 TNLK--ELDLSNNQI---------TDLPEPLGNLTNLEELDLSGN----QLTDLPEPLANLTNLETLDLSNN-------Q 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 532 LT--PVLDNLVQmiqdedspLQSLSLADSKLKAevtiiINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVI 609
Cdd:COG4886 240 LTdlPELGNLTN--------LEELDLSNNQLTD-----LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLL 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 755544329 610 WDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDAAQALKTNPEKTEEALQKIEN 663
Cdd:COG4886 307 LLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLS 360
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
280-624 |
9.52e-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: 64.68 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 280 TINLAGNSLEDRGVSSLsiqFAKLPKgLKHLNLSKTSLSPKGVNSLCQSLSANPltasTLTHLDLSGNALRGDD---LSH 356
Cdd:cd00116 2 QLSLKGELLKTERATEL---LPKLLC-LQVLRLEGNTLGEEAAKALASALRPQP----SLKELCLSLNETGRIPrglQSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 357 MYNFLAQPNtIVHLDLSNteCSLEMVCSALLRGCLQ--CLAVLNLSRSVFSHRKGKEVPPSFKqffSSSLALIQINLSGT 434
Cdd:cd00116 74 LQGLTKGCG-LQELDLSD--NALGPDGCGVLESLLRssSLQELKLNNNGLGDRGLRLLAKGLK---DLPPALEKLVLGRN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 435 KLSPEPLKALLLGLACNHSLKgvSLDLSNCELGHclrsGGAQVLEGCIAEIHNITSLDISDNGLE----SDLSTLivwLS 510
Cdd:cd00116 148 RLEGASCEALAKALRANRDLK--ELNLANNGIGD----AGIRALAEGLKANCNLEVLDLNNNGLTdegaSALAET---LA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 511 KNRSIQHLALGKNfnnmkskNLTpvldnlvqmiqdeDSPLQSLSLADSKLkaevtiiinalgsNTSLTKVDISGNGMGDM 590
Cdd:cd00116 219 SLKSLEVLNLGDN-------NLT-------------DAGAAALASALLSP-------------NISLLTLSLSCNDITDD 265
|
330 340 350
....*....|....*....|....*....|....
gi 755544329 591 GAKMLAKALQINTKLRTVIWDKNNITAQGFQDIA 624
Cdd:cd00116 266 GAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLA 299
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
417-634 |
3.63e-10 |
|
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: 63.14 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 417 KQFFSSSLALIQINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGHCLRsgGAQVLEGCIAEIHNITSLDISDN 496
Cdd:cd00116 16 TELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLK--ELCLSLNETGRIPR--GLQSLLQGLTKGCGLQELDLSDN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 497 GLESDLSTLIVWLSKNRSIQHL-----ALGKNFNNMKSKNLTPVldnlvqmiqdeDSPLQSLSLADSKLKAEVTI-IINA 570
Cdd:cd00116 92 ALGPDGCGVLESLLRSSSLQELklnnnGLGDRGLRLLAKGLKDL-----------PPALEKLVLGRNRLEGASCEaLAKA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755544329 571 LGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLR 634
Cdd:cd00116 161 LRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLE 224
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
244-352 |
2.06e-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: 61.73 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 244 RSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVN 323
Cdd:COG5238 318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIAL-AKYLEGNTTLRELNLGKNNIGKQGAE 394
|
90 100
....*....|....*....|....*....
gi 755544329 324 SLCQSLSANpltasTLTHLDLSGNALRGD 352
Cdd:COG5238 395 ALIDALQTN-----RLHTLILDGNLIGAE 418
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
217-479 |
2.31e-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: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 217 NQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSL 296
Cdd:COG5238 179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKS--LTTLDLSNNQIGDEGVIAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 297 sIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQSLSANPltasTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLSNte 376
Cdd:COG5238 257 -AEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT----TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 377 CSLEMVCSALLRGCLQC---LAVLNLSrsvfSHRKGKEVPPSFKQFFSSSLALIQINLSGTKLSPEPLKALLLGLACNhs 453
Cdd:COG5238 330 NGIGAQGAIALAKALQEnttLHSLDLS----DNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-- 403
|
250 260
....*....|....*....|....*.
gi 755544329 454 lKGVSLDLSNCELGHCLRSGGAQVLE 479
Cdd:COG5238 404 -RLHTLILDGNLIGAEAQQRLEQLLE 428
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1007-1394 |
2.20e-05 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1007 QPTQAAVCTISILPQD---GEQNGLMGRVDEGVDEFFTkkVTKMDCKRSssRSSDAHELGEGDEKKKRDSRrsgflnliK 1083
Cdd:PHA03307 19 EFFPRPPATPGDAADDllsGSQGQLVSDSAELAAVTVV--AGAAACDRF--EPPTGPPPGPGTEAPANESR--------S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1084 SRSRSERPPTVLMTEELSSPKGAMRSPPVDTTRKEIKAA-EHNGAPDRTEEIKTPEPLEEGP------AEEAGRAERSDS 1156
Cdd:PHA03307 87 TPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASpPPSPAPDLSEMLRPVGSPGPPPaasppaAGASPAAVASDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1157 RGSPQG------GRRYVQVMGSGLlAEMKAKQERRAACAQKKLGNDVISQDPSSPVSCNTERLEGGAtVPKLQPGLPEAR 1230
Cdd:PHA03307 167 ASSRQAalplssPEETARAPSSPP-AEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDA-GASSSDSSSSES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1231 FGSGTPEKNAKAEPR----VDGGCRSRSSSSMPTSPKPLLQSPKPSPSARPSIPQKPRTASRPEDTPdspsgpsspkval 1306
Cdd:PHA03307 245 SGCGWGPENECPLPRpapiTLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSS------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1307 lPPILKKVSSDKERDGQNSSQSSPRSFSQEVQRGDYFKRHSDHDSGKPSSRGKRSSKlyfaiAEEEANAPGYRKSQPTNA 1386
Cdd:PHA03307 312 -PRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK-----RPRPSRAPSSPAASAGRP 385
|
....*...
gi 755544329 1387 SRRSWGPA 1394
Cdd:PHA03307 386 TRRRARAA 393
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
1119-1324 |
2.84e-05 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 47.55 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1119 IKAAEHNGAPDrtEEIktpEPLEEGPAEEAGRaersdsrgspqggrrYVQvmgsgllAEMKAKqerrAACAQKKLGNDVI 1198
Cdd:PHA02682 34 IPAPAAPCPPD--ADV---DPLDKYSVKEAGR---------------YYQ-------SRLKAN----SACMQRPSGQSPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755544329 1199 SQDPSSPV------SCNTERLEGGATVPKLQPGLPEARFGSGTPEKNAKAEPRVDGGCRSRSSSSMPTSPKPllqSPKPS 1272
Cdd:PHA02682 83 APSPACAApapacpACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLP---TPKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 755544329 1273 PSARPSIPQKprTASRPEDTPDSPSGPSSPKVAllPPILKKVSSDKERDGQN 1324
Cdd:PHA02682 160 PAAKPIFLHN--QLPPPDYPAASCPTIETAPAA--SPVLEPRIPDKIIDADN 207
|
|
| |
