|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
778-1067 |
4.83e-81 |
|
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: 268.56 E-value: 4.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 778 TQELCPVAMRVAEGHNKMLSNVAERVTVPRNFIRGALLEQAGQDIQNKLDEVKLSVVTYLTSSIVDEILQELYHSHKSLA 857
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 858 RHLTQL-RTLSDPPGCP-GQGQDLSSRGRGRNHDHEETTDDELGTNIDTMAIKKQKR-CRKIRPVSAFISGSPQDMESQL 934
Cdd:pfam16000 81 RHLSQRgRTLLEPESLPdGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIhSRKLRPVSVAFSVSELDLDKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 935 GNLGI--------PPGWFSGLGGSQPTASGSWEGLSELPTHGYKLRHQTQgRPRPPRTTPPGPGRPSQMPAPGTRQENGM 1006
Cdd:pfam16000 161 EEVPIhvedassgPPLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTK-GRPKRNKTRAPTRPPGKVGPAQDGEQNGL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462542019 1007 ATRLDEGLEDFFSRRVLEEssSYPRTLRTVRPGLSEAP-LPPLQKKRRRGLFHFRRPWSFKG 1067
Cdd:pfam16000 240 SGRVDEGLEDFFSKKVIKL--STPTSPTSEPSSSSLFPdSPKKRKKRKSGFFNFIKPRSSKG 299
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
31-118 |
5.36e-33 |
|
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: 123.16 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 31 VKLETKPKKFEDRVLALTSWRLHLFLLKVPAKVESSFNVLEIRAFNTLSQNQILVETERGMVSMRLPSAESVDQVTRHVS 110
Cdd:pfam17888 7 VKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHIL 86
|
....*...
gi 2462542019 111 SALSKVCP 118
Cdd:pfam17888 87 TALKKIFP 94
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
274-657 |
1.90e-16 |
|
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: 83.69 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 274 VLHALTLSHNPIEDKGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPA---FASSLRYLDLSKNPGLLAT 350
Cdd:COG5238 88 QLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQvlkDPLGGNAVHLLGLAARLGL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 351 DEANALYSFLaQPNALVHLDLSGT---DCVIDLLLGALLHGccSHLTYLNLARNSCshrkGREAPPAFKQFFSSAYTLSH 427
Cdd:COG5238 168 LAAISMAKAL-QNNSVETVYLGCNqigDEGIEELAEALTQN--TTVTTLWLKRNPI----GDEGAEILAEALKGNKSLTT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 428 VNLSATKLPLEALRALLQGLSLNSHLSdlHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGF-DSDLLTLVPALGK 506
Cdd:COG5238 241 LDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIgDEGAIALAEGLQG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 507 NKSLKHLFLGKNfNVKAKTLEeilhklvqliqeedcslqslsvadsrlklrtsILINALGSNTCLAKVDLSGNGMEDIGA 586
Cdd:COG5238 319 NKTLHTLNLAYN-GIGAQGAI--------------------------------ALAKALQENTTLHSLDLSDNQIGDEGA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462542019 587 KMLSKALQINSSLRTILWDRNNTSALGFLDIARALESNhTLRFMSFPVSDISQAYRSapeRTEDVWQKIQW 657
Cdd:COG5238 366 IALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQ---RLEQLLERIKS 432
|
|
| PRK12323 super family |
cl46901 |
DNA polymerase III subunit gamma/tau; |
1188-1369 |
2.61e-05 |
|
DNA polymerase III subunit gamma/tau;
The actual alignment was detected with superfamily member PRK12323:
Pssm-ID: 481241 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1188 AWQKRRSSDDAGPGSWKPPPPPQSTkPSFSAMRRAEATwHIAEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLPARNA 1267
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPA-PAAAAPAAAAPA-PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1268 KD---PALAPWPPKPVAVPRGRQPPQEPGVREEAEAGDAAPGVNKPRLRLSSQQDQEEPEVQGPPDPGRRTAPLKPKRTR 1344
Cdd:PRK12323 440 SArgpGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519
|
170 180
....*....|....*....|....*
gi 2462542019 1345 RAQSCDKLEPDRRRPPDPTGTSEPG 1369
Cdd:PRK12323 520 GWVAESIPDPATADPDDAFETLAPA 544
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
778-1067 |
4.83e-81 |
|
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: 268.56 E-value: 4.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 778 TQELCPVAMRVAEGHNKMLSNVAERVTVPRNFIRGALLEQAGQDIQNKLDEVKLSVVTYLTSSIVDEILQELYHSHKSLA 857
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 858 RHLTQL-RTLSDPPGCP-GQGQDLSSRGRGRNHDHEETTDDELGTNIDTMAIKKQKR-CRKIRPVSAFISGSPQDMESQL 934
Cdd:pfam16000 81 RHLSQRgRTLLEPESLPdGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIhSRKLRPVSVAFSVSELDLDKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 935 GNLGI--------PPGWFSGLGGSQPTASGSWEGLSELPTHGYKLRHQTQgRPRPPRTTPPGPGRPSQMPAPGTRQENGM 1006
Cdd:pfam16000 161 EEVPIhvedassgPPLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTK-GRPKRNKTRAPTRPPGKVGPAQDGEQNGL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462542019 1007 ATRLDEGLEDFFSRRVLEEssSYPRTLRTVRPGLSEAP-LPPLQKKRRRGLFHFRRPWSFKG 1067
Cdd:pfam16000 240 SGRVDEGLEDFFSKKVIKL--STPTSPTSEPSSSSLFPdSPKKRKKRKSGFFNFIKPRSSKG 299
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
31-118 |
5.36e-33 |
|
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: 123.16 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 31 VKLETKPKKFEDRVLALTSWRLHLFLLKVPAKVESSFNVLEIRAFNTLSQNQILVETERGMVSMRLPSAESVDQVTRHVS 110
Cdd:pfam17888 7 VKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHIL 86
|
....*...
gi 2462542019 111 SALSKVCP 118
Cdd:pfam17888 87 TALKKIFP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
274-657 |
1.90e-16 |
|
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: 83.69 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 274 VLHALTLSHNPIEDKGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPA---FASSLRYLDLSKNPGLLAT 350
Cdd:COG5238 88 QLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQvlkDPLGGNAVHLLGLAARLGL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 351 DEANALYSFLaQPNALVHLDLSGT---DCVIDLLLGALLHGccSHLTYLNLARNSCshrkGREAPPAFKQFFSSAYTLSH 427
Cdd:COG5238 168 LAAISMAKAL-QNNSVETVYLGCNqigDEGIEELAEALTQN--TTVTTLWLKRNPI----GDEGAEILAEALKGNKSLTT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 428 VNLSATKLPLEALRALLQGLSLNSHLSdlHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGF-DSDLLTLVPALGK 506
Cdd:COG5238 241 LDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIgDEGAIALAEGLQG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 507 NKSLKHLFLGKNfNVKAKTLEeilhklvqliqeedcslqslsvadsrlklrtsILINALGSNTCLAKVDLSGNGMEDIGA 586
Cdd:COG5238 319 NKTLHTLNLAYN-GIGAQGAI--------------------------------ALAKALQENTTLHSLDLSDNQIGDEGA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462542019 587 KMLSKALQINSSLRTILWDRNNTSALGFLDIARALESNhTLRFMSFPVSDISQAYRSapeRTEDVWQKIQW 657
Cdd:COG5238 366 IALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQ---RLEQLLERIKS 432
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
339-600 |
5.68e-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: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 339 LDLSKNpgLLATDEANALYSFLAQPNALVHLDLS-----GTDCVIDLLLGALLHGCCshLTYLNLARNSCShrkgrEAPP 413
Cdd:cd00116 28 LRLEGN--TLGEEAAKALASALRPQPSLKELCLSlnetgRIPRGLQSLLQGLTKGCG--LQELDLSDNALG-----PDGC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 414 AFKQFFSSAYTLSHVNLSATKLPLEALRALLQGL-SLNSHLSDLhlDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNG 492
Cdd:cd00116 99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLkDLPPALEKL--VLGRNRLEGASCEALAKALRANRDLKELNLANNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 493 F-DSDLLTLVPALGKNKSLKHLFLGKNF--NVKAKTLEEILHKLVQL--IQEEDCSLQSLSVADsrlklrtsiLINALGS 567
Cdd:cd00116 177 IgDAGIRALAEGLKANCNLEVLDLNNNGltDEGASALAETLASLKSLevLNLGDNNLTDAGAAA---------LASALLS 247
|
250 260 270
....*....|....*....|....*....|....
gi 2462542019 568 -NTCLAKVDLSGNGMEDIGAKMLSKALQINSSLR 600
Cdd:cd00116 248 pNISLLTLSLSCNDITDDGAKDLAEVLAEKESLL 281
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1188-1369 |
2.61e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1188 AWQKRRSSDDAGPGSWKPPPPPQSTkPSFSAMRRAEATwHIAEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLPARNA 1267
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPA-PAAAAPAAAAPA-PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1268 KD---PALAPWPPKPVAVPRGRQPPQEPGVREEAEAGDAAPGVNKPRLRLSSQQDQEEPEVQGPPDPGRRTAPLKPKRTR 1344
Cdd:PRK12323 440 SArgpGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519
|
170 180
....*....|....*....|....*
gi 2462542019 1345 RAQSCDKLEPDRRRPPDPTGTSEPG 1369
Cdd:PRK12323 520 GWVAESIPDPATADPDDAFETLAPA 544
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1139-1368 |
1.28e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 46.30 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1139 EPGEGGP-APGTAQQPRVHGVALPGLERAKGWSFDGKREGPGPDQEGSTQAwQKRRSSDDAGPGSWKPPPPPQSTKPSfs 1217
Cdd:NF033839 286 EPGNKKPsAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQP-EKPKPEVKPQLETPKPEVKPQPEKPK-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1218 amrraeatwhiaEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLParnakDPALAPWPPKPVAVPRGRQPpqEPGVREE 1297
Cdd:NF033839 363 ------------PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKP-----EVKPQPEKPKPEVKPQPEKP--KPEVKPQ 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462542019 1298 AEAG--DAAPGVNKPRLRLSSQQDQEEPEVQ---GPPDPGRRTAPLKPKRTRRAQScDKLEPDRRRP-PDPTGTSEP 1368
Cdd:NF033839 424 PEKPkpEVKPQPEKPKPEVKPQPEKPKPEVKpqpETPKPEVKPQPEKPKPEVKPQP-EKPKPDNSKPqADDKKPSTP 499
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
778-1067 |
4.83e-81 |
|
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: 268.56 E-value: 4.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 778 TQELCPVAMRVAEGHNKMLSNVAERVTVPRNFIRGALLEQAGQDIQNKLDEVKLSVVTYLTSSIVDEILQELYHSHKSLA 857
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 858 RHLTQL-RTLSDPPGCP-GQGQDLSSRGRGRNHDHEETTDDELGTNIDTMAIKKQKR-CRKIRPVSAFISGSPQDMESQL 934
Cdd:pfam16000 81 RHLSQRgRTLLEPESLPdGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIhSRKLRPVSVAFSVSELDLDKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 935 GNLGI--------PPGWFSGLGGSQPTASGSWEGLSELPTHGYKLRHQTQgRPRPPRTTPPGPGRPSQMPAPGTRQENGM 1006
Cdd:pfam16000 161 EEVPIhvedassgPPLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTK-GRPKRNKTRAPTRPPGKVGPAQDGEQNGL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462542019 1007 ATRLDEGLEDFFSRRVLEEssSYPRTLRTVRPGLSEAP-LPPLQKKRRRGLFHFRRPWSFKG 1067
Cdd:pfam16000 240 SGRVDEGLEDFFSKKVIKL--STPTSPTSEPSSSSLFPdSPKKRKKRKSGFFNFIKPRSSKG 299
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
31-118 |
5.36e-33 |
|
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: 123.16 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 31 VKLETKPKKFEDRVLALTSWRLHLFLLKVPAKVESSFNVLEIRAFNTLSQNQILVETERGMVSMRLPSAESVDQVTRHVS 110
Cdd:pfam17888 7 VKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHIL 86
|
....*...
gi 2462542019 111 SALSKVCP 118
Cdd:pfam17888 87 TALKKIFP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
274-657 |
1.90e-16 |
|
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: 83.69 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 274 VLHALTLSHNPIEDKGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPA---FASSLRYLDLSKNPGLLAT 350
Cdd:COG5238 88 QLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQvlkDPLGGNAVHLLGLAARLGL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 351 DEANALYSFLaQPNALVHLDLSGT---DCVIDLLLGALLHGccSHLTYLNLARNSCshrkGREAPPAFKQFFSSAYTLSH 427
Cdd:COG5238 168 LAAISMAKAL-QNNSVETVYLGCNqigDEGIEELAEALTQN--TTVTTLWLKRNPI----GDEGAEILAEALKGNKSLTT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 428 VNLSATKLPLEALRALLQGLSLNSHLSdlHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGF-DSDLLTLVPALGK 506
Cdd:COG5238 241 LDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIgDEGAIALAEGLQG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 507 NKSLKHLFLGKNfNVKAKTLEeilhklvqliqeedcslqslsvadsrlklrtsILINALGSNTCLAKVDLSGNGMEDIGA 586
Cdd:COG5238 319 NKTLHTLNLAYN-GIGAQGAI--------------------------------ALAKALQENTTLHSLDLSDNQIGDEGA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462542019 587 KMLSKALQINSSLRTILWDRNNTSALGFLDIARALESNhTLRFMSFPVSDISQAYRSapeRTEDVWQKIQW 657
Cdd:COG5238 366 IALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQ---RLEQLLERIKS 432
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
189-477 |
7.68e-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: 75.60 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 189 REFNLLDFSHLESRDLALMVAALAYNQWFTKLYCKDLRLGSEVLEQVLHTLSKSGSLEELVLDNAGLKTDFVQKLAGVFG 268
Cdd:COG5238 154 NAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 269 ENGScvLHALTLSHNPIEDKGFLSLSqQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPafasSLRYLDLSKNPgll 348
Cdd:COG5238 234 GNKS--LTTLDLSNNQIGDEGVIALA-EALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT----TLTSLDLSVNR--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 349 ATDE-ANALYSFLAQPNALVHLDLS----GTDCVIdLLLGALLHGccSHLTYLNLARNscshRKGREAPPAFKQFFSSAY 423
Cdd:COG5238 304 IGDEgAIALAEGLQGNKTLHTLNLAyngiGAQGAI-ALAKALQEN--TTLHSLDLSDN----QIGDEGAIALAKYLEGNT 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462542019 424 TLSHVNLSATKLPLEALRALLQGLSLNShlsdLH-LDLSSCELRSAGAQALQEQL 477
Cdd:COG5238 377 TLRELNLGKNNIGKQGAEALIDALQTNR----LHtLILDGNLIGAEAQQRLEQLL 427
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
339-600 |
5.68e-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: 5.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 339 LDLSKNpgLLATDEANALYSFLAQPNALVHLDLS-----GTDCVIDLLLGALLHGCCshLTYLNLARNSCShrkgrEAPP 413
Cdd:cd00116 28 LRLEGN--TLGEEAAKALASALRPQPSLKELCLSlnetgRIPRGLQSLLQGLTKGCG--LQELDLSDNALG-----PDGC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 414 AFKQFFSSAYTLSHVNLSATKLPLEALRALLQGL-SLNSHLSDLhlDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNG 492
Cdd:cd00116 99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLkDLPPALEKL--VLGRNRLEGASCEALAKALRANRDLKELNLANNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 493 F-DSDLLTLVPALGKNKSLKHLFLGKNF--NVKAKTLEEILHKLVQL--IQEEDCSLQSLSVADsrlklrtsiLINALGS 567
Cdd:cd00116 177 IgDAGIRALAEGLKANCNLEVLDLNNNGltDEGASALAETLASLKSLevLNLGDNNLTDAGAAA---------LASALLS 247
|
250 260 270
....*....|....*....|....*....|....
gi 2462542019 568 -NTCLAKVDLSGNGMEDIGAKMLSKALQINSSLR 600
Cdd:cd00116 248 pNISLLTLSLSCNDITDDGAKDLAEVLAEKESLL 281
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
428-628 |
7.04e-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: 65.07 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 428 VNLSATKLPLEALRALlqGLSLNSHLSDLHLDLSSCELRS--AGAQALQEQLGAVTCVGSLDLSDNGFDSDLLTLVPALG 505
Cdd:cd00116 28 LRLEGNTLGEEAAKAL--ASALRPQPSLKELCLSLNETGRipRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 506 KNKSLKHLFLGKN------FNVKAKTLEEILHKLVQLIQE-----------------EDCSLQSLSVADSRLKLR-TSIL 561
Cdd:cd00116 106 RSSSLQELKLNNNglgdrgLRLLAKGLKDLPPALEKLVLGrnrlegascealakalrANRDLKELNLANNGIGDAgIRAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462542019 562 INALGSNTCLAKVDLSGNGMEDIGAKMLSKALQINSSLRTILWDRNNTSALGFLDIARALES-NHTLR 628
Cdd:cd00116 186 AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLL 253
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
334-663 |
1.09e-09 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 62.26 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 334 SSLRYLDLSKNPGLlatdeanalysflAQPNALVHLDLSGTDCV-IDLLLGALlhgccSHLTYLNLARNSCShrkgrEAP 412
Cdd:COG4886 96 TNLTELDLSGNEEL-------------SNLTNLESLDLSGNQLTdLPEELANL-----TNLKELDLSNNQLT-----DLP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 413 PAFKQFFSsaytLSHVNLSATKL-----PLEALRALlQGLSL-NSHLSDLHLDLSSCelrsagaQALQEqlgavtcvgsL 486
Cdd:COG4886 153 EPLGNLTN----LKSLDLSNNQLtdlpeELGNLTNL-KELDLsNNQITDLPEPLGNL-------TNLEE----------L 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 487 DLSDNGFDSdlltLVPALGKNKSLKHLFLGKNfnvKAKTLEEILhklvQLIqeedcSLQSLSVADSRLKLrtsilINALG 566
Cdd:COG4886 211 DLSGNQLTD----LPEPLANLTNLETLDLSNN---QLTDLPELG----NLT-----NLEELDLSNNQLTD-----LPPLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 567 SNTCLAKVDLSGNGMEDIGAKMLSKALQINSSLRTILWDRNNTSALGFLDIARALESNHTLRFMSFPVSDISQAYRSAPE 646
Cdd:COG4886 270 NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLAL 349
|
330
....*....|....*..
gi 2462542019 647 RTEDVWQKIQWCLVRNN 663
Cdd:COG4886 350 LTLLLLLNLLSLLLTLL 366
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
210-493 |
1.47e-07 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 55.05 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 210 ALAYNQWFTKLYCKDLRLGS--EVLEQVLHTLSKSGSLEELVLDNAGLKTDFVQKLAGVFGengSCVLHALTLSHNPIED 287
Cdd:cd00116 46 ALRPQPSLKELCLSLNETGRipRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLLR---SSSLQELKLNNNGLGD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 288 KGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPafasSLRYLDLSKNPglLATDEANALYSFLAQPNALV 367
Cdd:cd00116 123 RGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANR----DLKELNLANNG--IGDAGIRALAEGLKANCNLE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 368 HLDLSgtDCVID-----LLLGALLHGCCshLTYLNLARNSCSHRKGREAPPAFKqffSSAYTLSHVNLSATKLPLEALRA 442
Cdd:cd00116 197 VLDLN--NNGLTdegasALAETLASLKS--LEVLNLGDNNLTDAGAAALASALL---SPNISLLTLSLSCNDITDDGAKD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462542019 443 LLQGLSLNSHLsdLHLDLSSCELRSAGAQALQEQLGAVTC-VGSLDLSDNGF 493
Cdd:cd00116 270 LAEVLAEKESL--LELDLRGNKFGEEGAQLLAESLLEPGNeLESLWVKDDSF 319
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
185-501 |
2.80e-07 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 53.90 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 185 AEDNREFNLLDFS--HLESRDLALMVAALAYnQWFTKLYCKDLR------LGSEVLEQVLHtlskSGSLEELVLDNAGLK 256
Cdd:cd00116 47 LRPQPSLKELCLSlnETGRIPRGLQSLLQGL-TKGCGLQELDLSdnalgpDGCGVLESLLR----SSSLQELKLNNNGLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 257 TDFVQKLAGVFGENgSCVLHALTLSHNPIEDKGFLSLSQqLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANpafaSSL 336
Cdd:cd00116 122 DRGLRLLAKGLKDL-PPALEKLVLGRNRLEGASCEALAK-ALRANRDLKELNLANNGIGDAGIRALAEGLKAN----CNL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 337 RYLDLSKNpgLLATDEANALYSFLAQPNALVHLDLSgtDCVIDLLlgallhgCCSHLtylnlarnscshrkgreappafk 416
Cdd:cd00116 196 EVLDLNNN--GLTDEGASALAETLASLKSLEVLNLG--DNNLTDA-------GAAAL----------------------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 417 qffssaytlshvnlsatklpLEALRALLQGLslnshlsdLHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGFDSD 496
Cdd:cd00116 242 --------------------ASALLSPNISL--------LTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
|
....*
gi 2462542019 497 LLTLV 501
Cdd:cd00116 294 GAQLL 298
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1188-1369 |
2.61e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 48.72 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1188 AWQKRRSSDDAGPGSWKPPPPPQSTkPSFSAMRRAEATwHIAEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLPARNA 1267
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPA-PAAAAPAAAAPA-PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1268 KD---PALAPWPPKPVAVPRGRQPPQEPGVREEAEAGDAAPGVNKPRLRLSSQQDQEEPEVQGPPDPGRRTAPLKPKRTR 1344
Cdd:PRK12323 440 SArgpGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519
|
170 180
....*....|....*....|....*
gi 2462542019 1345 RAQSCDKLEPDRRRPPDPTGTSEPG 1369
Cdd:PRK12323 520 GWVAESIPDPATADPDDAFETLAPA 544
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
239-576 |
6.25e-05 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 47.24 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 239 LSKSGSLEELVLDNAGLKT--DFVQKLAGvfgengscvLHALTLSHNPIEDkgflsLSQQLLCFPSgLTKLCLAKTAIS- 315
Cdd:COG4886 109 LSNLTNLESLDLSGNQLTDlpEELANLTN---------LKELDLSNNQLTD-----LPEPLGNLTN-LKSLDLSNNQLTd 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 316 -PRGLQALgqtfganpafaSSLRYLDLSKNPgllATDEANAlysfLAQPNALVHLDLSGTD-CVIDLLLGALlhgccSHL 393
Cdd:COG4886 174 lPEELGNL-----------TNLKELDLSNNQ---ITDLPEP----LGNLTNLEELDLSGNQlTDLPEPLANL-----TNL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 394 TYLNLARNscshrKGREAPpafkqFFSSAYTLSHVNLSATKlplealralLQGLSLNSHLSDL-HLDLSSCELRSAGAQA 472
Cdd:COG4886 231 ETLDLSNN-----QLTDLP-----ELGNLTNLEELDLSNNQ---------LTDLPPLANLTNLkTLDLSNNQLTDLKLKE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 473 LQE-------QLGAVTCVGSLDLSDNGFDSDLLTLVPALGKNKSLKHLFLGKNFNVKAKTLEEILHKLVQLIQEEDCSLQ 545
Cdd:COG4886 292 LELllglnslLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGL 371
|
330 340 350
....*....|....*....|....*....|.
gi 2462542019 546 SLSVADSRLKLRTSILINALGSNTCLAKVDL 576
Cdd:COG4886 372 LGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1123-1335 |
8.96e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 46.50 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1123 GGRGPSFRRKMGTEGSEPGEGGPAPGTA--QQPRVHGVALPGLERAKGWSF----DGKREGPGPDQEGSTQAWQKRRSSD 1196
Cdd:PHA03169 34 GRRRGTAARAAKPAPPAPTTSGPQVRAVaeQGHRQTESDTETAEESRHGEKeergQGGPSGSGSESVGSPTPSPSGSAEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1197 DAGPGSWKPPPPPQSTKP-SFSAMRRAEATWHIAEESAPNHSCQSP--SPASQDGEEEKEGTLFPE--RTLPARNAKDPa 1271
Cdd:PHA03169 114 LASGLSPENTSGSSPESPaSHSPPPSPPSHPGPHEPAPPESHNPSPnqQPSSFLQPSHEDSPEEPEppTSEPEPDSPGP- 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462542019 1272 laPWPPKPVAVPRGRQPPQEPGvREEAEAGDAAPGVNKPRlRLSSQQDQEEPEVQGPPDPGRRT 1335
Cdd:PHA03169 193 --PQSETPTSSPPPQSPPDEPG-EPQSPTPQQAPSPNTQQ-AVEHEDEPTEPEREGPPFPGHRS 252
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1139-1368 |
1.28e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 46.30 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1139 EPGEGGP-APGTAQQPRVHGVALPGLERAKGWSFDGKREGPGPDQEGSTQAwQKRRSSDDAGPGSWKPPPPPQSTKPSfs 1217
Cdd:NF033839 286 EPGNKKPsAPKPGMQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVKPQP-EKPKPEVKPQLETPKPEVKPQPEKPK-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1218 amrraeatwhiaEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLParnakDPALAPWPPKPVAVPRGRQPpqEPGVREE 1297
Cdd:NF033839 363 ------------PEVKPQPEKPKPEVKPQPETPKPEVKPQPEKPKP-----EVKPQPEKPKPEVKPQPEKP--KPEVKPQ 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462542019 1298 AEAG--DAAPGVNKPRLRLSSQQDQEEPEVQ---GPPDPGRRTAPLKPKRTRRAQScDKLEPDRRRP-PDPTGTSEP 1368
Cdd:NF033839 424 PEKPkpEVKPQPEKPKPEVKPQPEKPKPEVKpqpETPKPEVKPQPEKPKPEVKPQP-EKPKPDNSKPqADDKKPSTP 499
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1135-1371 |
2.66e-04 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.61 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1135 TEGSEPGEGGPA--PGTAQQPRVHGVALPGLERAKGWSFDGKREGPGPDQEGSTQAWQKRRS----------SDDAGPGS 1202
Cdd:PRK07003 363 TGGGAPGGGVPArvAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEappaapappaTADRGDDA 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1203 WKPPPPPQSTKPSFSAMRRAEATWHIAEESAPNHSCQSPSPASQDGEEEKE---GTLFPERTLPARNAKDPALAPWP--P 1277
Cdd:PRK07003 443 ADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPApraAAPSAATPAAVPDARAPAAASREdaP 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1278 KPVAVPRGRQPPQEPGV-REEAEAGDAAPGVNKPR---LRLSSQQDQE---------EPEVQGPPDPGRRTAPLKPKRTR 1344
Cdd:PRK07003 523 AAAAPPAPEARPPTPAAaAPAARAGGAAAALDVLRnagMRVSSDRGARaaaaakpaaAPAAAPKPAAPRVAVQVPTPRAR 602
|
250 260
....*....|....*....|....*....
gi 2462542019 1345 RAQSCDKLEPDRRRPP--DPTGTSEPGTD 1371
Cdd:PRK07003 603 AATGDAPPNGAARAEQaaESRGAPPPWED 631
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1120-1366 |
6.67e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1120 GFGGGRGPSFRRKMGTEGSEPGEGGPAPGTAQQPRVHGVALPGLERAKgwsfdgkreGPGPDQEGSTQAWQKRRSSDDAG 1199
Cdd:PHA03247 262 GEGADRAPETARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLAL---------PAPPDPPPPAPAGDAEEEDDEDG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1200 PGSWKPPPPPQSTKPSFSAMRRAEATW----HIAEESAPNHSCQSPSPASQDGEEEKE-------GTLFPERTLPARNAK 1268
Cdd:PHA03247 333 AMEVVSPLPRPRQHYPLGFPKRRRPTWtppsSLEDLSAGRHHPKRASLPTRKRRSARHaatpfarGPGGDDQTRPAAPVP 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1269 DPALAPWPPK-PVAVPRgrqPPQEPGVREEAeAGDAAPGVnkprlrlssqqdqeEPEVQGPPDPGRRTAPLKPKRTRRAq 1347
Cdd:PHA03247 413 ASVPTPAPTPvPASAPP---PPATPLPSAEP-GSDDGPAP--------------PPERQPPAPATEPAPDDPDDATRKA- 473
|
250 260
....*....|....*....|
gi 2462542019 1348 scdkLEPDR-RRPPDPTGTS 1366
Cdd:PHA03247 474 ----LDALReRRPPEPPGAD 489
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
1279-1368 |
7.34e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 42.68 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542019 1279 PVAVPRGRQPPqePGVREEAEAGDAAPGVNKP-RLRLSSQQDQEEPEVQGPPDPGRRTAPlKPKRTRRAQSCDKLEPDRR 1357
Cdd:PRK11633 58 AATQALPTQPP--EGAAEAVRAGDAAAPSLDPaTVAPPNTPVEPEPAPVEPPKPKPVEKP-KPKPKPQQKVEAPPAPKPE 134
|
90
....*....|.
gi 2462542019 1358 RPPDPTGTSEP 1368
Cdd:PRK11633 135 PKPVVEEKAAP 145
|
|
| |
