|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
786-1084 |
2.00e-119 |
|
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: 375.26 E-value: 2.00e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 786 AENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLA 865
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 866 DHFSRRGKTLPQQESL-EIELAEEKPVKRSIITVEeltEIERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM 944
Cdd:pfam16000 81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 945 -EFDLDKALEEVPIHIED----PPFPSLRQEK------RSSGFISELPSeEGKKLEHFTKLRPKRNKKQQPTQAAVCAAn 1013
Cdd:pfam16000 152 sELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKVG- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650747 1014 iVSQDGEQNGLMGRVDEGVDEFFTKKVTKMDSKkwSTRGSESHELNEGGDEKKKRDSRKsSGFLNLIKSRS 1084
Cdd:pfam16000 230 -PAQDGEQNGLSGRVDEGLEDFFSKKVIKLSTP--TSPTSEPSSSSLFPDSPKKRKKRK-SGFFNFIKPRS 296
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
1.01e-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: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGTCLRKI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 1034650747 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
429-658 |
2.26e-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: 86.38 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 429 INLSGTKLSPEPLKALLLGLACNHNLKGvsLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSK 507
Cdd:COG5238 185 VYLGCNQIGDEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 508 NRSIQHLALGKN---------FNNM--KSKNLTPVLDNLVQmIQDE-----------ESPLQSLSLADSKLKTEVTI-II 564
Cdd:COG5238 263 NTTVETLYLSGNqigaegaiaLAKAlqGNTTLTSLDLSVNR-IGDEgaialaeglqgNKTLHTLNLAYNGIGAQGAIaLA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 565 NALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDASQA 642
Cdd:COG5238 342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ 421
|
250
....*....|....*.
gi 1034650747 643 lktnpeKTEDALQKIE 658
Cdd:COG5238 422 ------RLEQLLERIK 431
|
|
| PPP1R42 super family |
cl42388 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
229-373 |
1.43e-12 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
The actual alignment was detected with superfamily member cd00116:
Pssm-ID: 455733 [Multi-domain] Cd Length: 319 Bit Score: 70.46 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034650747 309 HLNLSKTSLSPKGVNSLsqsLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAAL---ASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| PTZ00449 super family |
cl33186 |
104 kDa microneme/rhoptry antigen; Provisional |
1188-1362 |
3.92e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
The actual alignment was detected with superfamily member PTZ00449:
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1188 AQKKLgndAVSQDSSSPALSGVERSDGGGAVPKLHPGLPENRFGLGTPEKNTKA-----EPKAEAGSRSRSSSSTPTSPK 1262
Cdd:PTZ00449 492 SKKKL---APIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEpkeggKPGETKEGEVGKKPGPAKEHK 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1263 PllqSPKPSLAARPVIPQKPRTASRPDDiPDSPSSPKVALLP--------PVLKKVP-SDKERDGQSSPQ--PSP-RTFS 1330
Cdd:PTZ00449 569 P---SKIPTLSKKPEFPKDPKHPKDPEE-PKKPKRPRSAQRPtrpkspklPELLDIPkSPKRPESPKSPKrpPPPqRPSS 644
|
170 180 190
....*....|....*....|....*....|..
gi 1034650747 1331 QEVVQRGDYYKRHSDHDSGKPSSRGKRSSKLY 1362
Cdd:PTZ00449 645 PERPEGPKIIKSPKPPKSPKPPFDPKFKEKFY 676
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
786-1084 |
2.00e-119 |
|
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: 375.26 E-value: 2.00e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 786 AENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLA 865
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 866 DHFSRRGKTLPQQESL-EIELAEEKPVKRSIITVEeltEIERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM 944
Cdd:pfam16000 81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 945 -EFDLDKALEEVPIHIED----PPFPSLRQEK------RSSGFISELPSeEGKKLEHFTKLRPKRNKKQQPTQAAVCAAn 1013
Cdd:pfam16000 152 sELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKVG- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650747 1014 iVSQDGEQNGLMGRVDEGVDEFFTKKVTKMDSKkwSTRGSESHELNEGGDEKKKRDSRKsSGFLNLIKSRS 1084
Cdd:pfam16000 230 -PAQDGEQNGLSGRVDEGLEDFFSKKVIKLSTP--TSPTSEPSSSSLFPDSPKKRKKRK-SGFFNFIKPRS 296
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
1.01e-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: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGTCLRKI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 1034650747 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
429-658 |
2.26e-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: 86.38 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 429 INLSGTKLSPEPLKALLLGLACNHNLKGvsLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSK 507
Cdd:COG5238 185 VYLGCNQIGDEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 508 NRSIQHLALGKN---------FNNM--KSKNLTPVLDNLVQmIQDE-----------ESPLQSLSLADSKLKTEVTI-II 564
Cdd:COG5238 263 NTTVETLYLSGNqigaegaiaLAKAlqGNTTLTSLDLSVNR-IGDEgaialaeglqgNKTLHTLNLAYNGIGAQGAIaLA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 565 NALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDASQA 642
Cdd:COG5238 342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ 421
|
250
....*....|....*.
gi 1034650747 643 lktnpeKTEDALQKIE 658
Cdd:COG5238 422 ------RLEQLLERIK 431
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
229-373 |
1.43e-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: 70.46 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034650747 309 HLNLSKTSLSPKGVNSLsqsLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAAL---ASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
281-595 |
1.75e-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: 70.08 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 281 INLAGNPLEDRGVSSLSiQFAKLPKGLKHLNLS--KTSLSPKGVNSLSQSLSANPLtastLVHLDLSGNVLrGDDLSHMY 358
Cdd:cd00116 28 LRLEGNTLGEEAAKALA-SALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGCG----LQELDLSDNAL-GPDGCGVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 359 NFLAQPNAIVHLDLSNTECS---LDMVCGALlRGCLQYLAVLNLSRTVFSHRKGKEVppsfKQFFSSSLALMHINLSGTK 435
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGdrgLRLLAKGL-KDLPPALEKLVLGRNRLEGASCEAL----AKALRANRDLKELNLANNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 436 LSPEPLKALLLGLACNHNLKgvSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKNRSIQHLA 515
Cdd:cd00116 177 IGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL------------TDAGAAALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 516 LGknfnnMKSKNLTpvldnlvqmiqdeespLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKA 594
Cdd:cd00116 243 SA-----LLSPNIS----------------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAES 301
|
.
gi 1034650747 595 L 595
Cdd:cd00116 302 L 302
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
244-352 |
3.42e-10 |
|
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: 64.04 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 244 RSNRLEELVLENAGLRTDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVN 323
Cdd:COG5238 318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIAL-AKYLEGNTTLRELNLGKNNIGKQGAE 394
|
90 100
....*....|....*....|....*....
gi 1034650747 324 SLSQSLSANPLTAstlvhLDLSGNVLRGD 352
Cdd:COG5238 395 ALIDALQTNRLHT-----LILDGNLIGAE 418
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1188-1362 |
3.92e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1188 AQKKLgndAVSQDSSSPALSGVERSDGGGAVPKLHPGLPENRFGLGTPEKNTKA-----EPKAEAGSRSRSSSSTPTSPK 1262
Cdd:PTZ00449 492 SKKKL---APIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEpkeggKPGETKEGEVGKKPGPAKEHK 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1263 PllqSPKPSLAARPVIPQKPRTASRPDDiPDSPSSPKVALLP--------PVLKKVP-SDKERDGQSSPQ--PSP-RTFS 1330
Cdd:PTZ00449 569 P---SKIPTLSKKPEFPKDPKHPKDPEE-PKKPKRPRSAQRPtrpkspklPELLDIPkSPKRPESPKSPKrpPPPqRPSS 644
|
170 180 190
....*....|....*....|....*....|..
gi 1034650747 1331 QEVVQRGDYYKRHSDHDSGKPSSRGKRSSKLY 1362
Cdd:PTZ00449 645 PERPEGPKIIKSPKPPKSPKPPFDPKFKEKFY 676
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
231-583 |
9.97e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 47.15 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 231 STDVCEQILRVVSRSNRLEELVLENaglrTDFAQKLASALAHNPNsgLHTINLAGNPLEdrgvSSLSIQFAKLPKGLKHL 310
Cdd:PLN00113 54 SADVCLWQGITCNNSSRVVSIDLSG----KNISGKISSAIFRLPY--IQTINLSNNQLS----GPIPDDIFTTSSSLRYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 311 NLSKTSLS---PKGVNSLSQSL--SANPLTA---------STLVHLDLSGNVLRGddlsHMYNFLAQPNAIVHLDLSNTE 376
Cdd:PLN00113 124 NLSNNNFTgsiPRGSIPNLETLdlSNNMLSGeipndigsfSSLKVLDLGGNVLVG----KIPNSLTNLTSLEFLTLASNQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 377 C--SLDMVCGALLRGCLQYLAVLNLSrtvfshrkgKEVPPSFKQFFS-SSLALMHINLSGtklsPEPlkalllglacnhn 453
Cdd:PLN00113 200 LvgQIPRELGQMKSLKWIYLGYNNLS---------GEIPYEIGGLTSlNHLDLVYNNLTG----PIP------------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 454 lkgVSL-DLSNCELRSGGAQVLEGCIA----EIHNITSLDISDNGLESDLSTLIVWLsKNRSIQHLalgknFNNMKSKNL 528
Cdd:PLN00113 254 ---SSLgNLKNLQYLFLYQNKLSGPIPpsifSLQKLISLDLSDNSLSGEIPELVIQL-QNLEILHL-----FSNNFTGKI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034650747 529 TPVLDNLVQmiqdeespLQSLSLADSKLKTEvtiIINALGSNTSLTKVDISGNGM 583
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 ... |
786-1084 |
2.00e-119 |
|
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: 375.26 E-value: 2.00e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 786 AENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLA 865
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 866 DHFSRRGKTLPQQESL-EIELAEEKPVKRSIITVEeltEIERLEDLDTCMtlcctsMTPKSKRKSIHSRMLRPVSRAFEM 944
Cdd:pfam16000 81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPM------ATLKSKRKSIHSRKLRPVSVAFSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 945 -EFDLDKALEEVPIHIED----PPFPSLRQEK------RSSGFISELPSeEGKKLEHFTKLRPKRNKKQQPTQAAVCAAn 1013
Cdd:pfam16000 152 sELDLDKAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGKVG- 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034650747 1014 iVSQDGEQNGLMGRVDEGVDEFFTKKVTKMDSKkwSTRGSESHELNEGGDEKKKRDSRKsSGFLNLIKSRS 1084
Cdd:pfam16000 230 -PAQDGEQNGLSGRVDEGLEDFFSKKVIKLSTP--TSPTSEPSSSSLFPDSPKKRKKRK-SGFFNFIKPRS 296
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
38-119 |
1.01e-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: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGTCLRKI 117
Cdd:pfam17888 13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92
|
..
gi 1034650747 118 FP 119
Cdd:pfam17888 93 FP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
429-658 |
2.26e-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: 86.38 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 429 INLSGTKLSPEPLKALLLGLACNHNLKGvsLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSK 507
Cdd:COG5238 185 VYLGCNQIGDEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKN 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 508 NRSIQHLALGKN---------FNNM--KSKNLTPVLDNLVQmIQDE-----------ESPLQSLSLADSKLKTEVTI-II 564
Cdd:COG5238 263 NTTVETLYLSGNqigaegaiaLAKAlqGNTTLTSLDLSVNR-IGDEgaialaeglqgNKTLHTLNLAYNGIGAQGAIaLA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 565 NALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKN--YTLRFMPIPMYDASQA 642
Cdd:COG5238 342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ 421
|
250
....*....|....*.
gi 1034650747 643 lktnpeKTEDALQKIE 658
Cdd:COG5238 422 ------RLEQLLERIK 431
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
250-624 |
9.15e-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: 78.29 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 250 ELVLENAGLRTDFAQKLASALAH----NPNSGLHTINLAGNPLEDRGVSSLSIQFAKlPKGLKHLNLSKTSLSPKGVNSL 325
Cdd:COG5238 150 PLGGNAVHLLGLAARLGLLAAISmakaLQNNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEIL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 326 SQSLSANPltasTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDlsntecsldmvcgallrgclqylavlnlsrtvfs 405
Cdd:COG5238 229 AEALKGNK----SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLY---------------------------------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 406 hrkgkevppsfkqffssslalmhinLSGTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELRSGGAQVLEGCIAEIHNIT 485
Cdd:COG5238 271 -------------------------LSGNQIGAEGAIALAKALQGNTTLT--SLDLSVNRIGDEGAIALAEGLQGNKTLH 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 486 SLDISDNGLESDLSTLIvwlsknrsIQHLALGKNfnnmksknltpvldnlvqmiqdeespLQSLSLADSKLKTE-VTIII 564
Cdd:COG5238 324 TLNLAYNGIGAQGAIAL--------AKALQENTT--------------------------LHSLDLSDNQIGDEgAIALA 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 565 NALGSNTSLTKVDISGNGMGDMGAKMLAKALQINtKLRTVIWDKNNITAQGFQDIAVAME 624
Cdd:COG5238 370 KYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLEQLLE 428
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
441-651 |
4.58e-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: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 441 LKALLLGLACNHNLKGV------SLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSKNRSIQH 513
Cdd:COG5238 161 LAARLGLLAAISMAKALqnnsveTVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIgDEGAEILAEALKGNKSLTT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 514 LALGKNfnNMKSKNLTPVLDNLvqmiqDEESPLQSLSLADSKLKTEVTI-IINALGSNTSLTKVDISGNGMGDMGAKMLA 592
Cdd:COG5238 241 LDLSNN--QIGDEGVIALAEAL-----KNNTTVETLYLSGNQIGAEGAIaLAKALQGNTTLTSLDLSVNRIGDEGAIALA 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034650747 593 KALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRF---MPIPMYDAS-----QALKTNPEKTE 651
Cdd:COG5238 314 EGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSldlSDNQIGDEGaialaKYLEGNTTLRE 380
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
451-630 |
6.47e-13 |
|
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: 72.52 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 451 NHNLKGV-SLDLSNCELRSGGAQVLEGCIAEI-HNITSLDISDNGLESD-LSTLIVWLSKNRSIQHLALGKNfnNMKSKN 527
Cdd:COG5238 147 LKDPLGGnAVHLLGLAARLGLLAAISMAKALQnNSVETVYLGCNQIGDEgIEELAEALTQNTTVTTLWLKRN--PIGDEG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 528 LtpvlDNLVQMIQDEESpLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIW 606
Cdd:COG5238 225 A----EILAEALKGNKS-LTTLDLSNNQIGDEgVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDL 299
|
170 180
....*....|....*....|....
gi 1034650747 607 DKNNITAQGFQDIAVAMEKNYTLR 630
Cdd:COG5238 300 SVNRIGDEGAIALAEGLQGNKTLH 323
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
229-373 |
1.43e-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: 70.46 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 229 KLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLSIQFAKLPKgLK 308
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTDEGASALAETLASLKS-LE 224
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034650747 309 HLNLSKTSLSPKGVNSLsqsLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLS 373
Cdd:cd00116 225 VLNLGDNNLTDAGAAAL---ASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
281-595 |
1.75e-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: 70.08 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 281 INLAGNPLEDRGVSSLSiQFAKLPKGLKHLNLS--KTSLSPKGVNSLSQSLSANPLtastLVHLDLSGNVLrGDDLSHMY 358
Cdd:cd00116 28 LRLEGNTLGEEAAKALA-SALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGCG----LQELDLSDNAL-GPDGCGVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 359 NFLAQPNAIVHLDLSNTECS---LDMVCGALlRGCLQYLAVLNLSRTVFSHRKGKEVppsfKQFFSSSLALMHINLSGTK 435
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGdrgLRLLAKGL-KDLPPALEKLVLGRNRLEGASCEAL----AKALRANRDLKELNLANNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 436 LSPEPLKALLLGLACNHNLKgvSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKNRSIQHLA 515
Cdd:cd00116 177 IGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL------------TDAGAAALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 516 LGknfnnMKSKNLTpvldnlvqmiqdeespLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKA 594
Cdd:cd00116 243 SA-----LLSPNIS----------------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAES 301
|
.
gi 1034650747 595 L 595
Cdd:cd00116 302 L 302
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
310-634 |
1.16e-11 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 68.42 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 310 LNLSKTSLSPKGVNSLSQSLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLSNTECSLDmvcgallrg 389
Cdd:COG4886 41 SLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 390 cLQYLAVLNLSRTvfshrKGKEVPPSFKQFFSsslaLMHINLSGTKLS--PEPLKALllglacnHNLKgvSLDLSNCELR 467
Cdd:COG4886 112 -LTNLESLDLSGN-----QLTDLPEELANLTN----LKELDLSNNQLTdlPEPLGNL-------TNLK--SLDLSNNQLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 468 SggaqvLEGCIAEIHNITSLDISDNGLeSDLSTlivWLSKNRSIQHLALGKN--------FNNMKskNLT---------- 529
Cdd:COG4886 173 D-----LPEELGNLTNLKELDLSNNQI-TDLPE---PLGNLTNLEELDLSGNqltdlpepLANLT--NLEtldlsnnqlt 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 530 --PVLDNLVQmiqdeespLQSLSLADSKLKTevtiiINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWD 607
Cdd:COG4886 242 dlPELGNLTN--------LEELDLSNNQLTD-----LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
|
330 340
....*....|....*....|....*..
gi 1034650747 608 KNNITAQGFQDIAVAMEKNYTLRFMPI 634
Cdd:COG4886 309 NLLELLILLLLLTTLLLLLLLLKGLLV 335
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
221-466 |
4.09e-11 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 65.84 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 221 TKLSSKDLKLSTDVCeQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPnSGLHTINLAGNPLEDRGVSSLSIQF 300
Cdd:cd00116 84 QELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLP-PALEKLVLGRNRLEGASCEALAKAL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 301 AKLPKgLKHLNLSKTSLSPKGVNSLSQSLSANPLtastLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLSNteCSLD 380
Cdd:cd00116 162 RANRD-LKELNLANNGIGDAGIRALAEGLKANCN----LEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD--NNLT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 381 MVCGALL----RGCLQYLAVLNLSRTVFSHRKGKevppSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNlKG 456
Cdd:cd00116 235 DAGAAALasalLSPNISLLTLSLSCNDITDDGAK----DLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN-EL 309
|
250
....*....|
gi 1034650747 457 VSLDLSNCEL 466
Cdd:cd00116 310 ESLWVKDDSF 319
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
244-352 |
3.42e-10 |
|
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: 64.04 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 244 RSNRLEELVLENAGLRTDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVN 323
Cdd:COG5238 318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIAL-AKYLEGNTTLRELNLGKNNIGKQGAE 394
|
90 100
....*....|....*....|....*....
gi 1034650747 324 SLSQSLSANPLTAstlvhLDLSGNVLRGD 352
Cdd:COG5238 395 ALIDALQTNRLHT-----LILDGNLIGAE 418
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
217-481 |
3.64e-10 |
|
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: 64.04 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 217 NQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNsgLHTINLAGNPLEDRGVSSL 296
Cdd:COG5238 179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKS--LTTLDLSNNQIGDEGVIAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 297 sIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPltasTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLSNte 376
Cdd:COG5238 257 -AEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT----TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 377 CSLDMVCGALLRGCLQY---LAVLNLSrtvfSHRKGKEVPPSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNhN 453
Cdd:COG5238 330 NGIGAQGAIALAKALQEnttLHSLDLS----DNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-R 404
|
250 260
....*....|....*....|....*...
gi 1034650747 454 LKgvSLDLSNCELRSGGAQVLEGCIAEI 481
Cdd:COG5238 405 LH--TLILDGNLIGAEAQQRLEQLLERI 430
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
280-632 |
7.52e-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: 61.99 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 280 TINLAGNPLEDRGVSSLsiqFAKLPKgLKHLNLSKTSLSPKGVNSLSQSLSANPltasTLVHLDLSGNVLRGDD--LSHM 357
Cdd:cd00116 2 QLSLKGELLKTERATEL---LPKLLC-LQVLRLEGNTLGEEAAKALASALRPQP----SLKELCLSLNETGRIPrgLQSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 358 YNFLAQPNAIVHLDLSNTECSLDMVcgALLRGCLQylavlnlsrtvfshrkgkevppsfkqffSSSLALMHINLSGTKLS 437
Cdd:cd00116 74 LQGLTKGCGLQELDLSDNALGPDGC--GVLESLLR----------------------------SSSLQELKLNNNGLGDR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 438 PEPLKALLLgLACNHNLKgvSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLstlivwlsknrsIQHLALG 517
Cdd:cd00116 124 GLRLLAKGL-KDLPPALE--KLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG------------IRALAEG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 518 knfnnMKsknltpvldnlvqmiqdEESPLQSLSLADSKL-KTEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKAL- 595
Cdd:cd00116 189 -----LK-----------------ANCNLEVLDLNNNGLtDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALl 246
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034650747 596 QINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFM 632
Cdd:cd00116 247 SPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLEL 283
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
457-647 |
4.23e-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: 56.59 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 457 VSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLS---KNRSIQHLALgknFNNMKSKNLTPVLD 533
Cdd:cd00116 26 QVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQgltKGCGLQELDL---SDNALGPDGCGVLE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 534 NLVQmiqdeESPLQSLSLADSKL-KTEVTIIINALGSNT-SLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNI 611
Cdd:cd00116 103 SLLR-----SSSLQELKLNNNGLgDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034650747 612 TAQGFQDIAVAMEKNYTLR--------FMPIPMYDASQALKTNP 647
Cdd:cd00116 178 GDAGIRALAEGLKANCNLEvldlnnngLTDEGASALAETLASLK 221
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
187-347 |
1.43e-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: 55.57 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 187 LTQDT--RELNLQDfSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQ 264
Cdd:COG5238 204 LTQNTtvTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAI 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 265 KLASALAHNPNsgLHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPltasTLVHLDL 344
Cdd:COG5238 283 ALAKALQGNTT--LTSLDLSVNRIGDEGAIAL-AEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENT----TLHSLDL 355
|
...
gi 1034650747 345 SGN 347
Cdd:COG5238 356 SDN 358
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
1188-1362 |
3.92e-05 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 48.53 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1188 AQKKLgndAVSQDSSSPALSGVERSDGGGAVPKLHPGLPENRFGLGTPEKNTKA-----EPKAEAGSRSRSSSSTPTSPK 1262
Cdd:PTZ00449 492 SKKKL---APIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEpkeggKPGETKEGEVGKKPGPAKEHK 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1263 PllqSPKPSLAARPVIPQKPRTASRPDDiPDSPSSPKVALLP--------PVLKKVP-SDKERDGQSSPQ--PSP-RTFS 1330
Cdd:PTZ00449 569 P---SKIPTLSKKPEFPKDPKHPKDPEE-PKKPKRPRSAQRPtrpkspklPELLDIPkSPKRPESPKSPKrpPPPqRPSS 644
|
170 180 190
....*....|....*....|....*....|..
gi 1034650747 1331 QEVVQRGDYYKRHSDHDSGKPSSRGKRSSKLY 1362
Cdd:PTZ00449 645 PERPEGPKIIKSPKPPKSPKPPFDPKFKEKFY 676
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
231-583 |
9.97e-05 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 47.15 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 231 STDVCEQILRVVSRSNRLEELVLENaglrTDFAQKLASALAHNPNsgLHTINLAGNPLEdrgvSSLSIQFAKLPKGLKHL 310
Cdd:PLN00113 54 SADVCLWQGITCNNSSRVVSIDLSG----KNISGKISSAIFRLPY--IQTINLSNNQLS----GPIPDDIFTTSSSLRYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 311 NLSKTSLS---PKGVNSLSQSL--SANPLTA---------STLVHLDLSGNVLRGddlsHMYNFLAQPNAIVHLDLSNTE 376
Cdd:PLN00113 124 NLSNNNFTgsiPRGSIPNLETLdlSNNMLSGeipndigsfSSLKVLDLGGNVLVG----KIPNSLTNLTSLEFLTLASNQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 377 C--SLDMVCGALLRGCLQYLAVLNLSrtvfshrkgKEVPPSFKQFFS-SSLALMHINLSGtklsPEPlkalllglacnhn 453
Cdd:PLN00113 200 LvgQIPRELGQMKSLKWIYLGYNNLS---------GEIPYEIGGLTSlNHLDLVYNNLTG----PIP------------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 454 lkgVSL-DLSNCELRSGGAQVLEGCIA----EIHNITSLDISDNGLESDLSTLIVWLsKNRSIQHLalgknFNNMKSKNL 528
Cdd:PLN00113 254 ---SSLgNLKNLQYLFLYQNKLSGPIPpsifSLQKLISLDLSDNSLSGEIPELVIQL-QNLEILHL-----FSNNFTGKI 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034650747 529 TPVLDNLVQmiqdeespLQSLSLADSKLKTEvtiIINALGSNTSLTKVDISGNGM 583
Cdd:PLN00113 325 PVALTSLPR--------LQVLQLWSNKFSGE---IPKNLGKHNNLTVLDLSTNNL 368
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1082-1360 |
3.81e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.08 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1082 SRSKSERPPTILMTEEPSSPKGAVRSPPVDCPRKDTKAAEHngnseriEEIKTPDSFEESQgeeigkverSDSKSSPQAG 1161
Cdd:PHA03307 110 GPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAA-------SPPAAGASPAAVA---------SDAASSRQAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1162 RrygVQVMG-------SGLLAEMKAKQEKRAACAQKKLGNDAVSQDSSSPALSGvERSDGGGAVPKLHPGLPENRFGLGT 1234
Cdd:PHA03307 174 L---PLSSPeetarapSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAP-GRSAADDAGASSSDSSSSESSGCGW 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1235 PEKNTKAEPKAEAGSRSRSSSSTPTspkPLLQSPKPSLAArpviPQKPRTASRPDDIPDSPSSPKVALLPPVLKKVPSDK 1314
Cdd:PHA03307 250 GPENECPLPRPAPITLPTRIWEASG---WNGPSSRPGPAS----SSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSR 322
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034650747 1315 ErDGQSSPQPSPRTFSQEVVQRGDYYKRHSDHDSGKPSSRGKRSSK 1360
Cdd:PHA03307 323 E-SSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRK 367
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1095-1333 |
4.79e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1095 TEEPSSPKGAvrSPPVDCPRKDTKAAEHNGNSERIEEIKTPDSFEESQGEEIGKVERSDSKSSPQAGRRYGVQVMGSGLL 1174
Cdd:PHA03307 182 TARAPSSPPA--EPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPR 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1175 AEMKAKQEKRAACAqkklGNDAVSQDSSSPALSGVERSDGGGAVPK--LHPGLPENRFGLGTPEKNTKAEPKAEAGSRSR 1252
Cdd:PHA03307 260 PAPITLPTRIWEAS----GWNGPSSRPGPASSSSSPRERSPSPSPSspGSGPAPSSPRASSSSSSSRESSSSSTSSSSES 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650747 1253 SSSSTPTSPKPLLQSPKPSLAARPVIPQKPRTASRPDDIPDSPSSPKVALLPPVLKKVPSDKERdGQSSPQPSPRTFSQE 1332
Cdd:PHA03307 336 SRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRAR-RRDATGRFPAGRPRP 414
|
.
gi 1034650747 1333 V 1333
Cdd:PHA03307 415 S 415
|
|
| |
