|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1081 |
2.75e-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: 368.72 E-value: 2.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 790 AETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 870 NHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDltEVERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEM-EFDLDK 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLPDGDRPESSPLGPGKRHEG--EIERLEELETPMATLKSKRKSIHSRKLRPVSVAFSVsELDLDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 949 ALEEVPIHIED----PPFPSVRQEK------RSSGLISELPSeEGRRLEHFTKLRPKRNKKQQPTQAAVCTisILPQDGE 1018
Cdd:pfam16000 159 APEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV--GPAQDGE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40850674 1019 QNGLMGRVDEGVDEFFTKKVTKMDcKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSR 1081
Cdd:pfam16000 236 QNGLSGRVDEGLEDFFSKKVIKLS-TPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSS 297
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
2.92e-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: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 38 GDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 40850674 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 |
6.25e-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: 88.31 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 260 IDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSLcqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNAV-------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 340 tHLDLSGNALRGDDLSHMYNFLaQPNTIVHLDLSNTECSLEmvcsallrGCLQCLAVLNLSRSVFShrkgkevppsfkqf 419
Cdd:COG5238 157 -HLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDE--------GIEELAEALTQNTTVTT-------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 420 fssslaliqINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEIHNITSLDISDNGL- 498
Cdd:COG5238 213 ---------LWLKRNPIGDEGAEILAEALKGNKSLT--TLDLSNNQIG----DEGVIALAEALKNNTTVETLYLSGNQIg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 499 ESDLSTLIVWLSKNRSIQHLALgkNFNNMKSKNLTpvldNLVQMIQdEDSPLQSLSLADSKLKAEVTI-IINALGSNTSL 577
Cdd:COG5238 278 AEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAI----ALAEGLQ-GNKTLHTLNLAYNGIGAQGAIaLAKALQENTTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 578 TKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDAAQAlktnpeKTE 655
Cdd:COG5238 351 HSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------RLE 424
|
....*..
gi 40850674 656 EALQKIE 662
Cdd:COG5238 425 QLLERIK 431
|
|
| PHA02682 super family |
cl31817 |
ORF080 virion core protein; Provisional |
1113-1318 |
1.40e-05 |
|
ORF080 virion core protein; Provisional
The actual alignment was detected with superfamily member PHA02682:
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 48.70 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 1113 IKAAEHNGAPDrtEEIktpEPLEEGPAEEAGRaersdsrgspqggrrYVQvmgsgllAEMKAKqerrAACAQKKLGNDVI 1192
Cdd:PHA02682 34 IPAPAAPCPPD--ADV---DPLDKYSVKEAGR---------------YYQ-------SRLKAN----SACMQRPSGQSPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 1193 SQDPSSPV------SCNTERLEGGATVPKLQPGLPEARFGSGTPEKNAKAEPRVDGGCRSRSSSSMPTSPKPllqSPKPS 1266
Cdd:PHA02682 83 APSPACAApapacpACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLP---TPKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 40850674 1267 PSARPSIPQKPRTasrPEDTPDSPSGPSSPKVALLPPILKKVPsDKERDGQN 1318
Cdd:PHA02682 160 PAAKPIFLHNQLP---PPDYPAASCPTIETAPAASPVLEPRIP-DKIIDADN 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1081 |
2.75e-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: 368.72 E-value: 2.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 790 AETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 870 NHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDltEVERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEM-EFDLDK 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLPDGDRPESSPLGPGKRHEG--EIERLEELETPMATLKSKRKSIHSRKLRPVSVAFSVsELDLDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 949 ALEEVPIHIED----PPFPSVRQEK------RSSGLISELPSeEGRRLEHFTKLRPKRNKKQQPTQAAVCTisILPQDGE 1018
Cdd:pfam16000 159 APEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV--GPAQDGE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40850674 1019 QNGLMGRVDEGVDEFFTKKVTKMDcKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSR 1081
Cdd:pfam16000 236 QNGLSGRVDEGLEDFFSKKVIKLS-TPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSS 297
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
2.92e-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: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 38 GDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 40850674 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
260-662 |
6.25e-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: 88.31 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 260 IDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSLcqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNAV-------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 340 tHLDLSGNALRGDDLSHMYNFLaQPNTIVHLDLSNTECSLEmvcsallrGCLQCLAVLNLSRSVFShrkgkevppsfkqf 419
Cdd:COG5238 157 -HLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDE--------GIEELAEALTQNTTVTT-------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 420 fssslaliqINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEIHNITSLDISDNGL- 498
Cdd:COG5238 213 ---------LWLKRNPIGDEGAEILAEALKGNKSLT--TLDLSNNQIG----DEGVIALAEALKNNTTVETLYLSGNQIg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 499 ESDLSTLIVWLSKNRSIQHLALgkNFNNMKSKNLTpvldNLVQMIQdEDSPLQSLSLADSKLKAEVTI-IINALGSNTSL 577
Cdd:COG5238 278 AEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAI----ALAEGLQ-GNKTLHTLNLAYNGIGAQGAIaLAKALQENTTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 578 TKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDAAQAlktnpeKTE 655
Cdd:COG5238 351 HSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------RLE 424
|
....*..
gi 40850674 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 |
3.20e-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: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40850674 309 HLNLSKTSLSPKGVNSLCqslSANPLTASTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAALA---SALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
1113-1318 |
1.40e-05 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 48.70 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 1113 IKAAEHNGAPDrtEEIktpEPLEEGPAEEAGRaersdsrgspqggrrYVQvmgsgllAEMKAKqerrAACAQKKLGNDVI 1192
Cdd:PHA02682 34 IPAPAAPCPPD--ADV---DPLDKYSVKEAGR---------------YYQ-------SRLKAN----SACMQRPSGQSPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 1193 SQDPSSPV------SCNTERLEGGATVPKLQPGLPEARFGSGTPEKNAKAEPRVDGGCRSRSSSSMPTSPKPllqSPKPS 1266
Cdd:PHA02682 83 APSPACAApapacpACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLP---TPKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 40850674 1267 PSARPSIPQKPRTasrPEDTPDSPSGPSSPKVALLPPILKKVPsDKERDGQN 1318
Cdd:PHA02682 160 PAAKPIFLHNQLP---PPDYPAASCPTIETAPAASPVLEPRIP-DKIIDADN 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
790-1081 |
2.75e-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: 368.72 E-value: 2.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 790 AETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLA 869
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 870 NHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDltEVERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEM-EFDLDK 948
Cdd:pfam16000 81 RHLSQRGRTLLEPESLPDGDRPESSPLGPGKRHEG--EIERLEELETPMATLKSKRKSIHSRKLRPVSVAFSVsELDLDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 949 ALEEVPIHIED----PPFPSVRQEK------RSSGLISELPSeEGRRLEHFTKLRPKRNKKQQPTQAAVCTisILPQDGE 1018
Cdd:pfam16000 159 APEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKV--GPAQDGE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40850674 1019 QNGLMGRVDEGVDEFFTKKVTKMDcKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSR 1081
Cdd:pfam16000 236 QNGLSGRVDEGLEDFFSKKVIKLS-TPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSS 297
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
2.92e-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: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 38 GDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 40850674 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
260-662 |
6.25e-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: 88.31 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 260 IDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKglkHLNLSKTSLSPKGVNSLcqslsanpltastl 339
Cdd:COG5238 94 WEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPR---RINLIQVLKDPLGGNAV-------------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 340 tHLDLSGNALRGDDLSHMYNFLaQPNTIVHLDLSNTECSLEmvcsallrGCLQCLAVLNLSRSVFShrkgkevppsfkqf 419
Cdd:COG5238 157 -HLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDE--------GIEELAEALTQNTTVTT-------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 420 fssslaliqINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEIHNITSLDISDNGL- 498
Cdd:COG5238 213 ---------LWLKRNPIGDEGAEILAEALKGNKSLT--TLDLSNNQIG----DEGVIALAEALKNNTTVETLYLSGNQIg 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 499 ESDLSTLIVWLSKNRSIQHLALgkNFNNMKSKNLTpvldNLVQMIQdEDSPLQSLSLADSKLKAEVTI-IINALGSNTSL 577
Cdd:COG5238 278 AEGAIALAKALQGNTTLTSLDL--SVNRIGDEGAI----ALAEGLQ-GNKTLHTLNLAYNGIGAQGAIaLAKALQENTTL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 578 TKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDAAQAlktnpeKTE 655
Cdd:COG5238 351 HSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ------RLE 424
|
....*..
gi 40850674 656 EALQKIE 662
Cdd:COG5238 425 QLLERIK 431
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
250-628 |
2.80e-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: 79.83 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 250 ELVLENAGLRIDFAQKLAGALAH----NPNSGLHTINLAGNSLEDRGVSSLSIQFAKlPKGLKHLNLSKTSLSPKGVNSL 325
Cdd:COG5238 150 PLGGNAVHLLGLAARLGLLAAISmakaLQNNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEIL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 326 CQSLSANPltasTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDlsntecslemvcsallrgclqclavlnlsrsvfs 405
Cdd:COG5238 229 AEALKGNK----SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLY---------------------------------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 406 hrkgkevppsfkqffssslaliqinLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGhclrSGGAQVLEGCIAEI 485
Cdd:COG5238 271 -------------------------LSGNQIGAEGAIALAKALQGNTTLT--SLDLSVNRIG----DEGAIALAEGLQGN 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 486 HNITSLDISDNGLESDLSTLIvwlsknrsIQHLALGKNfnnmksknltpvldnlvqmiqdedspLQSLSLADSKLKAE-V 564
Cdd:COG5238 320 KTLHTLNLAYNGIGAQGAIAL--------AKALQENTT--------------------------LHSLDLSDNQIGDEgA 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40850674 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 |
5.75e-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: 75.98 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 403 VFSHRKGKEVPpSFKQFFSSSLALIQINLSGTKLSPEPLKALLLGlacNHSLKGVS---LDLSNCELGHCLRSGGAQVLE 479
Cdd:COG5238 103 VALAETATAVA-TPPPDLRRIMAKTLEDSLILYLALPRRINLIQV---LKDPLGGNavhLLGLAARLGLLAAISMAKALQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 480 GCIAEIHNITSLDISDNGLESdlstLIVWLSKNRSIQHLALGKNfnNMKSKNLtpvlDNLVQMIQdEDSPLQSLSLADSK 559
Cdd:COG5238 179 NNSVETVYLGCNQIGDEGIEE----LAEALTQNTTVTTLWLKRN--PIGDEGA----EILAEALK-GNKSLTTLDLSNNQ 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 560 LKAE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPI 638
Cdd:COG5238 248 IGDEgVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNL 327
|
250 260 270
....*....|....*....|....*....|....*.
gi 40850674 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 |
3.20e-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: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40850674 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 |
4.83e-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: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 281 INLAGNSLEDRGVSSLSiQFAKLPKGLKHLNLS--KTSLSPKGVNSLCQSLSANPLtastLTHLDLSGNALrGDDLSHMY 358
Cdd:cd00116 28 LRLEGNTLGEEAAKALA-SALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGCG----LQELDLSDNAL-GPDGCGVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 359 NFLAQPNTIVHLDLSNteCSLE-----MVCSALLRgcLQC-LAVLNLSRSVFSHRKGKEVppsfKQFFSSSLALIQINLS 432
Cdd:cd00116 102 ESLLRSSSLQELKLNN--NGLGdrglrLLAKGLKD--LPPaLEKLVLGRNRLEGASCEAL----AKALRANRDLKELNLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 433 GTKLSPEPLKALLLGLACNHSLKgvSLDLSNCelghCLRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKN 512
Cdd:cd00116 174 NNGIGDAGIRALAEGLKANCNLE--VLDLNNN----GLTDEGASALAETLASLKSLEVLNLGDNNL------------TD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 513 RSIQHLALGknfnnMKSKNLTpvldnlvqmiqdedspLQSLSLADSKLKAE-VTIIINALGSNTSLTKVDISGNGMGDMG 591
Cdd:cd00116 236 AGAAALASA-----LLSPNIS----------------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEG 294
|
....*...
gi 40850674 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 |
7.22e-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: 71.23 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 221 TKLSSKDLKLSTDVCeQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPnSGLHTINLAGNSLEDRGVSSLSIQF 300
Cdd:cd00116 84 QELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLP-PALEKLVLGRNRLEGASCEALAKAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 301 AKLPKgLKHLNLSKTSLSPKGVNSLCQSLSANPLtastLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLSNTECSLE 380
Cdd:cd00116 162 RANRD-LKELNLANNGIGDAGIRALAEGLKANCN----LEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDA 236
|
170 180
....*....|....*....|...
gi 40850674 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 |
9.17e-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: 67.77 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 248 LEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQ 327
Cdd:cd00116 195 LEVLDLNNNGLTDEGASALAETLASLKS--LEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAE 272
|
90 100 110
....*....|....*....|....*....|
gi 40850674 328 SLSANPltasTLTHLDLSGNAL--RGDDLS 355
Cdd:cd00116 273 VLAEKE----SLLELDLRGNKFgeEGAQLL 298
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
280-624 |
1.31e-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: 64.30 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 280 TINLAGNSLEDRGVSSLsiqFAKLPKgLKHLNLSKTSLSPKGVNSLCQSLSANPltasTLTHLDLSGNALRGDD---LSH 356
Cdd:cd00116 2 QLSLKGELLKTERATEL---LPKLLC-LQVLRLEGNTLGEEAAKALASALRPQP----SLKELCLSLNETGRIPrglQSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 357 MYNFLAQPNtIVHLDLSNteCSLEMVCSALLRGCLQ--CLAVLNLSRSVFSHRKGKEVPPSFKqffSSSLALIQINLSGT 434
Cdd:cd00116 74 LQGLTKGCG-LQELDLSD--NALGPDGCGVLESLLRssSLQELKLNNNGLGDRGLRLLAKGLK---DLPPALEKLVLGRN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 435 KLSPEPLKALLLGLACNHSLKgvSLDLSNCELGHclrsGGAQVLEGCIAEIHNITSLDISDNGLE----SDLSTLivwLS 510
Cdd:cd00116 148 RLEGASCEALAKALRANRDLK--ELNLANNGIGD----AGIRALAEGLKANCNLEVLDLNNNGLTdegaSALAET---LA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 511 KNRSIQHLALGKNfnnmkskNLTpvldnlvqmiqdeDSPLQSLSLADSKLkaevtiiinalgsNTSLTKVDISGNGMGDM 590
Cdd:cd00116 219 SLKSLEVLNLGDN-------NLT-------------DAGAAALASALLSP-------------NISLLTLSLSCNDITDD 265
|
330 340 350
....*....|....*....|....*....|....
gi 40850674 591 GAKMLAKALQINTKLRTVIWDKNNITAQGFQDIA 624
Cdd:cd00116 266 GAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLA 299
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
294-663 |
1.43e-10 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 64.95 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 294 SSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQSLSANPLTASTLTHLDLSGNalrgddlshmyNFLAQPNTIVHLDLS 373
Cdd:COG4886 53 LSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----------EELSNLTNLESLDLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 374 NTEcsLEMVCSALLRgcLQCLAVLNLSRSVFShrkgkEVPPSFKQFfsssLALIQINLSGTKLS--PEPLKALllglacn 451
Cdd:COG4886 122 GNQ--LTDLPEELAN--LTNLKELDLSNNQLT-----DLPEPLGNL----TNLKSLDLSNNQLTdlPEELGNL------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 452 HSLKgvSLDLSNCELghclrsggaQVLEGCIAEIHNITSLDISDNglesDLSTLIVWLSKNRSIQHLALGKNfnnmkskN 531
Cdd:COG4886 182 TNLK--ELDLSNNQI---------TDLPEPLGNLTNLEELDLSGN----QLTDLPEPLANLTNLETLDLSNN-------Q 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 532 LT--PVLDNLVQmiqdedspLQSLSLADSKLKAevtiiINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVI 609
Cdd:COG4886 240 LTdlPELGNLTN--------LEELDLSNNQLTD-----LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLL 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 40850674 610 WDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDAAQALKTNPEKTEEALQKIEN 663
Cdd:COG4886 307 LLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLS 360
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
417-634 |
4.15e-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: 62.76 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 417 KQFFSSSLALIQINLSGTKLSPEPLKALLLGLACNHSLKgvSLDLSNCELGHCLRsgGAQVLEGCIAEIHNITSLDISDN 496
Cdd:cd00116 16 TELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLK--ELCLSLNETGRIPR--GLQSLLQGLTKGCGLQELDLSDN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 497 GLESDLSTLIVWLSKNRSIQHL-----ALGKNFNNMKSKNLTPVldnlvqmiqdeDSPLQSLSLADSKLKAEVTI-IINA 570
Cdd:cd00116 92 ALGPDGCGVLESLLRSSSLQELklnnnGLGDRGLRLLAKGLKDL-----------PPALEKLVLGRNRLEGASCEaLAKA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40850674 571 LGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLR 634
Cdd:cd00116 161 LRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLE 224
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
244-352 |
2.19e-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: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 244 RSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVN 323
Cdd:COG5238 318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIAL-AKYLEGNTTLRELNLGKNNIGKQGAE 394
|
90 100
....*....|....*....|....*....
gi 40850674 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 |
2.77e-09 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 60.96 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 217 NQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNsgLHTINLAGNSLEDRGVSSL 296
Cdd:COG5238 179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKS--LTTLDLSNNQIGDEGVIAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 297 sIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQSLSANPltasTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLSNte 376
Cdd:COG5238 257 -AEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT----TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 377 CSLEMVCSALLRGCLQC---LAVLNLSrsvfSHRKGKEVPPSFKQFFSSSLALIQINLSGTKLSPEPLKALLLGLACNhs 453
Cdd:COG5238 330 NGIGAQGAIALAKALQEnttLHSLDLS----DNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-- 403
|
250 260
....*....|....*....|....*.
gi 40850674 454 lKGVSLDLSNCELGHCLRSGGAQVLE 479
Cdd:COG5238 404 -RLHTLILDGNLIGAEAQQRLEQLLE 428
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
1113-1318 |
1.40e-05 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 48.70 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 1113 IKAAEHNGAPDrtEEIktpEPLEEGPAEEAGRaersdsrgspqggrrYVQvmgsgllAEMKAKqerrAACAQKKLGNDVI 1192
Cdd:PHA02682 34 IPAPAAPCPPD--ADV---DPLDKYSVKEAGR---------------YYQ-------SRLKAN----SACMQRPSGQSPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40850674 1193 SQDPSSPV------SCNTERLEGGATVPKLQPGLPEARFGSGTPEKNAKAEPRVDGGCRSRSSSSMPTSPKPllqSPKPS 1266
Cdd:PHA02682 83 APSPACAApapacpACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLP---TPKPA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 40850674 1267 PSARPSIPQKPRTasrPEDTPDSPSGPSSPKVALLPPILKKVPsDKERDGQN 1318
Cdd:PHA02682 160 PAAKPIFLHNQLP---PPDYPAASCPTIETAPAASPVLEPRIP-DKIIDADN 207
|
|
| |
