|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
778-1066 |
3.99e-84 |
|
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: 277.04 E-value: 3.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 778 TQELCPVAMRVAEGHNKMLSNVAERVTVPRNFIRGALLEQAGQDIQNKLDEVKLSVVTYLTSSIVDEILQELYHSHKSLA 857
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 858 RHLTQL-RTLSDPPGCP-GQGQDLSSRGRGRNHDHEETTDDELGTNIDTMAIKKQKR-CRKIRPVSAFISGSPQDMESQL 934
Cdd:pfam16000 81 RHLSQRgRTLLEPESLPdGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIhSRKLRPVSVAFSVSELDLDKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 935 GNLGI--------PPGWFSGLGGSQPTASGSWEGLSELPTHGYKLRHQTQGRPRPPRTTPPGPGRPSMPAPGTRQENGMA 1006
Cdd:pfam16000 161 EEVPIhvedassgPPLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGPAQDGEQNGLS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462498135 1007 TRLDEGLEDFFSRRVLEEssSYPRTLRTVRPGLSEAP-LPPLQKKRRRGLFHFRRPRSFKG 1066
Cdd:pfam16000 241 GRVDEGLEDFFSKKVIKL--STPTSPTSEPSSSSLFPdSPKKRKKRKSGFFNFIKPRSSKG 299
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
31-118 |
5.18e-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: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 31 VKLETKPKKFEDRVLALTSWRLHLFLLKVPAKVESSFNVLEIRAFNTLSQNQILVETERGMVSMRLPSAESVDQVTRHVS 110
Cdd:pfam17888 7 VKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHIL 86
|
....*...
gi 2462498135 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 |
2.12e-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: 83.30 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 274 VLHALTLSHNPIEDKGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPA---FASSLRYLDLSKNPGLLAT 350
Cdd:COG5238 88 QLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQvlkDPLGGNAVHLLGLAARLGL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 351 DEANALYSFLaQPNALVHLDLSGT---DCVIDLLLGALLHGccSHLTYLNLARNSCshrkGREAPPAFKQFFSSAYTLSH 427
Cdd:COG5238 168 LAAISMAKAL-QNNSVETVYLGCNqigDEGIEELAEALTQN--TTVTTLWLKRNPI----GDEGAEILAEALKGNKSLTT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 428 VNLSATKLPLEALRALLQGLSLNSHLSdlHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGF-DSDLLTLVPALGK 506
Cdd:COG5238 241 LDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIgDEGAIALAEGLQG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 507 NKSLKHLFLGKNfNVKAKTLEeilhklvqliqeedcslqslsvadsrlklrtsILINALGSNTCLAKVDLSGNGMEDIGA 586
Cdd:COG5238 319 NKTLHTLNLAYN-GIGAQGAI--------------------------------ALAKALQENTTLHSLDLSDNQIGDEGA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462498135 587 KMLSKALQINSSLRTILWDRNNTSALGFLDIARALESNhTLRFMSFPVSDISQAYRSapeRTEDVWQKIQW 657
Cdd:COG5238 366 IALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQ---RLEQLLERIKS 432
|
|
| PRK12323 super family |
cl46901 |
DNA polymerase III subunit gamma/tau; |
1144-1325 |
5.14e-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: 47.56 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1144 AWQKRRSSDDAGPGSWKPPPPPQSTkPSFSAMRRAEATwHIAEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLPARNA 1223
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPA-PAAAAPAAAAPA-PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1224 KD---PALAPWPPKPVAVPRGRQPPQEPGVREEAEAGDAAPGVNKPRLRLSSQQDQEEPEVQGPPDPGRRTAPLKPKRTR 1300
Cdd:PRK12323 440 SArgpGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519
|
170 180
....*....|....*....|....*
gi 2462498135 1301 RAQSCDKLEPDRRRPPDPTAGTSEP 1325
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 ... |
778-1066 |
3.99e-84 |
|
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: 277.04 E-value: 3.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 778 TQELCPVAMRVAEGHNKMLSNVAERVTVPRNFIRGALLEQAGQDIQNKLDEVKLSVVTYLTSSIVDEILQELYHSHKSLA 857
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 858 RHLTQL-RTLSDPPGCP-GQGQDLSSRGRGRNHDHEETTDDELGTNIDTMAIKKQKR-CRKIRPVSAFISGSPQDMESQL 934
Cdd:pfam16000 81 RHLSQRgRTLLEPESLPdGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIhSRKLRPVSVAFSVSELDLDKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 935 GNLGI--------PPGWFSGLGGSQPTASGSWEGLSELPTHGYKLRHQTQGRPRPPRTTPPGPGRPSMPAPGTRQENGMA 1006
Cdd:pfam16000 161 EEVPIhvedassgPPLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGPAQDGEQNGLS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462498135 1007 TRLDEGLEDFFSRRVLEEssSYPRTLRTVRPGLSEAP-LPPLQKKRRRGLFHFRRPRSFKG 1066
Cdd:pfam16000 241 GRVDEGLEDFFSKKVIKL--STPTSPTSEPSSSSLFPdSPKKRKKRKSGFFNFIKPRSSKG 299
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
31-118 |
5.18e-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: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 31 VKLETKPKKFEDRVLALTSWRLHLFLLKVPAKVESSFNVLEIRAFNTLSQNQILVETERGMVSMRLPSAESVDQVTRHVS 110
Cdd:pfam17888 7 VKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHIL 86
|
....*...
gi 2462498135 111 SALSKVCP 118
Cdd:pfam17888 87 TALKKIFP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
274-657 |
2.12e-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: 83.30 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 274 VLHALTLSHNPIEDKGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPA---FASSLRYLDLSKNPGLLAT 350
Cdd:COG5238 88 QLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQvlkDPLGGNAVHLLGLAARLGL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 351 DEANALYSFLaQPNALVHLDLSGT---DCVIDLLLGALLHGccSHLTYLNLARNSCshrkGREAPPAFKQFFSSAYTLSH 427
Cdd:COG5238 168 LAAISMAKAL-QNNSVETVYLGCNqigDEGIEELAEALTQN--TTVTTLWLKRNPI----GDEGAEILAEALKGNKSLTT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 428 VNLSATKLPLEALRALLQGLSLNSHLSdlHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGF-DSDLLTLVPALGK 506
Cdd:COG5238 241 LDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIgDEGAIALAEGLQG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 507 NKSLKHLFLGKNfNVKAKTLEeilhklvqliqeedcslqslsvadsrlklrtsILINALGSNTCLAKVDLSGNGMEDIGA 586
Cdd:COG5238 319 NKTLHTLNLAYN-GIGAQGAI--------------------------------ALAKALQENTTLHSLDLSDNQIGDEGA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462498135 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 |
1.03e-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: 70.85 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 339 LDLSKNpgLLATDEANALYSFLAQPNALVHLDLS-----GTDCVIDLLLGALLHGCCshLTYLNLARNSCShrkgrEAPP 413
Cdd:cd00116 28 LRLEGN--TLGEEAAKALASALRPQPSLKELCLSlnetgRIPRGLQSLLQGLTKGCG--LQELDLSDNALG-----PDGC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 414 AFKQFFSSAYTLSHVNLSATKLPLEALRALLQGL-SLNSHLSDLhlDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNG 492
Cdd:cd00116 99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLkDLPPALEKL--VLGRNRLEGASCEALAKALRANRDLKELNLANNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 493 F-DSDLLTLVPALGKNKSLKHLFLGKNF--NVKAKTLEEILHKLVQL--IQEEDCSLQSLSVADsrlklrtsiLINALGS 567
Cdd:cd00116 177 IgDAGIRALAEGLKANCNLEVLDLNNNGltDEGASALAETLASLKSLevLNLGDNNLTDAGAAA---------LASALLS 247
|
250 260 270
....*....|....*....|....*....|....
gi 2462498135 568 -NTCLAKVDLSGNGMEDIGAKMLSKALQINSSLR 600
Cdd:cd00116 248 pNISLLTLSLSCNDITDDGAKDLAEVLAEKESLL 281
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1144-1325 |
5.14e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.56 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1144 AWQKRRSSDDAGPGSWKPPPPPQSTkPSFSAMRRAEATwHIAEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLPARNA 1223
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPA-PAAAAPAAAAPA-PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1224 KD---PALAPWPPKPVAVPRGRQPPQEPGVREEAEAGDAAPGVNKPRLRLSSQQDQEEPEVQGPPDPGRRTAPLKPKRTR 1300
Cdd:PRK12323 440 SArgpGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519
|
170 180
....*....|....*....|....*
gi 2462498135 1301 RAQSCDKLEPDRRRPPDPTAGTSEP 1325
Cdd:PRK12323 520 GWVAESIPDPATADPDDAFETLAPA 544
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1132-1315 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1132 MGPGPDQEGSTQAWQKRRSSDDAGPGSWKPPPPP----QSTKPSFSAMRRAEATWHIAEESAPNHSCQsPSPASQDGEEE 1207
Cdd:NF033839 299 MQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVkpqpEKPKPEVKPQLETPKPEVKPQPEKPKPEVK-PQPEKPKPEVK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1208 KE-GTLFPERTlPARNAKDPALAPWP--PKPVAVPRGRQPpqEPGVREEAEAG--DAAPGVNKPRLRLSSQQDQEEPEVQ 1282
Cdd:NF033839 378 PQpETPKPEVK-PQPEKPKPEVKPQPekPKPEVKPQPEKP--KPEVKPQPEKPkpEVKPQPEKPKPEVKPQPEKPKPEVK 454
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462498135 1283 ---GPPDPGRRTAPLKPKRTRRAQScDKLEPDRRRP 1315
Cdd:NF033839 455 pqpETPKPEVKPQPEKPKPEVKPQP-EKPKPDNSKP 489
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CARMIL_C |
pfam16000 |
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ... |
778-1066 |
3.99e-84 |
|
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: 277.04 E-value: 3.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 778 TQELCPVAMRVAEGHNKMLSNVAERVTVPRNFIRGALLEQAGQDIQNKLDEVKLSVVTYLTSSIVDEILQELYHSHKSLA 857
Cdd:pfam16000 1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 858 RHLTQL-RTLSDPPGCP-GQGQDLSSRGRGRNHDHEETTDDELGTNIDTMAIKKQKR-CRKIRPVSAFISGSPQDMESQL 934
Cdd:pfam16000 81 RHLSQRgRTLLEPESLPdGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIhSRKLRPVSVAFSVSELDLDKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 935 GNLGI--------PPGWFSGLGGSQPTASGSWEGLSELPTHGYKLRHQTQGRPRPPRTTPPGPGRPSMPAPGTRQENGMA 1006
Cdd:pfam16000 161 EEVPIhvedassgPPLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGPAQDGEQNGLS 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462498135 1007 TRLDEGLEDFFSRRVLEEssSYPRTLRTVRPGLSEAP-LPPLQKKRRRGLFHFRRPRSFKG 1066
Cdd:pfam16000 241 GRVDEGLEDFFSKKVIKL--STPTSPTSEPSSSSLFPdSPKKRKKRKSGFFNFIKPRSSKG 299
|
|
| Carm_PH |
pfam17888 |
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ... |
31-118 |
5.18e-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: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 31 VKLETKPKKFEDRVLALTSWRLHLFLLKVPAKVESSFNVLEIRAFNTLSQNQILVETERGMVSMRLPSAESVDQVTRHVS 110
Cdd:pfam17888 7 VKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHIL 86
|
....*...
gi 2462498135 111 SALSKVCP 118
Cdd:pfam17888 87 TALKKIFP 94
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
274-657 |
2.12e-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: 83.30 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 274 VLHALTLSHNPIEDKGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPA---FASSLRYLDLSKNPGLLAT 350
Cdd:COG5238 88 QLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQvlkDPLGGNAVHLLGLAARLGL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 351 DEANALYSFLaQPNALVHLDLSGT---DCVIDLLLGALLHGccSHLTYLNLARNSCshrkGREAPPAFKQFFSSAYTLSH 427
Cdd:COG5238 168 LAAISMAKAL-QNNSVETVYLGCNqigDEGIEELAEALTQN--TTVTTLWLKRNPI----GDEGAEILAEALKGNKSLTT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 428 VNLSATKLPLEALRALLQGLSLNSHLSdlHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGF-DSDLLTLVPALGK 506
Cdd:COG5238 241 LDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIgDEGAIALAEGLQG 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 507 NKSLKHLFLGKNfNVKAKTLEeilhklvqliqeedcslqslsvadsrlklrtsILINALGSNTCLAKVDLSGNGMEDIGA 586
Cdd:COG5238 319 NKTLHTLNLAYN-GIGAQGAI--------------------------------ALAKALQENTTLHSLDLSDNQIGDEGA 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462498135 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 |
9.13e-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: 75.21 E-value: 9.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 189 REFNLLDFSHLESRDLALMVAALAYNQWFTKLYCKDLRLGSEVLEQVLHTLSKSGSLEELVLDNAGLKTDFVQKLAGVFG 268
Cdd:COG5238 154 NAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 269 ENGScvLHALTLSHNPIEDKGFLSLSqQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPafasSLRYLDLSKNPgll 348
Cdd:COG5238 234 GNKS--LTTLDLSNNQIGDEGVIALA-EALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT----TLTSLDLSVNR--- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 349 ATDE-ANALYSFLAQPNALVHLDLS----GTDCVIdLLLGALLHGccSHLTYLNLARNscshRKGREAPPAFKQFFSSAY 423
Cdd:COG5238 304 IGDEgAIALAEGLQGNKTLHTLNLAyngiGAQGAI-ALAKALQEN--TTLHSLDLSDN----QIGDEGAIALAKYLEGNT 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462498135 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 |
1.03e-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: 70.85 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 339 LDLSKNpgLLATDEANALYSFLAQPNALVHLDLS-----GTDCVIDLLLGALLHGCCshLTYLNLARNSCShrkgrEAPP 413
Cdd:cd00116 28 LRLEGN--TLGEEAAKALASALRPQPSLKELCLSlnetgRIPRGLQSLLQGLTKGCG--LQELDLSDNALG-----PDGC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 414 AFKQFFSSAYTLSHVNLSATKLPLEALRALLQGL-SLNSHLSDLhlDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNG 492
Cdd:cd00116 99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLkDLPPALEKL--VLGRNRLEGASCEALAKALRANRDLKELNLANNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 493 F-DSDLLTLVPALGKNKSLKHLFLGKNF--NVKAKTLEEILHKLVQL--IQEEDCSLQSLSVADsrlklrtsiLINALGS 567
Cdd:cd00116 177 IgDAGIRALAEGLKANCNLEVLDLNNNGltDEGASALAETLASLKSLevLNLGDNNLTDAGAAA---------LASALLS 247
|
250 260 270
....*....|....*....|....*....|....
gi 2462498135 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 |
1.09e-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: 64.68 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 428 VNLSATKLPLEALRALlqGLSLNSHLSDLHLDLSSCELRS--AGAQALQEQLGAVTCVGSLDLSDNGFDSDLLTLVPALG 505
Cdd:cd00116 28 LRLEGNTLGEEAAKAL--ASALRPQPSLKELCLSLNETGRipRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 506 KNKSLKHLFLGKN------FNVKAKTLEEILHKLVQLIQE-----------------EDCSLQSLSVADSRLKLR-TSIL 561
Cdd:cd00116 106 RSSSLQELKLNNNglgdrgLRLLAKGLKDLPPALEKLVLGrnrlegascealakalrANRDLKELNLANNGIGDAgIRAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462498135 562 INALGSNTCLAKVDLSGNGMEDIGAKMLSKALQINSSLRTILWDRNNTSALGFLDIARALES-NHTLR 628
Cdd:cd00116 186 AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSpNISLL 253
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
334-663 |
4.20e-09 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 60.33 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 334 SSLRYLDLSKNPGLlatdeanalysflAQPNALVHLDLSGTDCV-IDLLLGALlhgccSHLTYLNLARNSCShrkgrEAP 412
Cdd:COG4886 96 TNLTELDLSGNEEL-------------SNLTNLESLDLSGNQLTdLPEELANL-----TNLKELDLSNNQLT-----DLP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 413 PAFKQFFSsaytLSHVNLSATKL-----PLEALRALlQGLSL-NSHLSDLHLDLSSCElrsagaqALQEqlgavtcvgsL 486
Cdd:COG4886 153 EPLGNLTN----LKSLDLSNNQLtdlpeELGNLTNL-KELDLsNNQITDLPEPLGNLT-------NLEE----------L 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 487 DLSDNGFDSdlltLVPALGKNKSLKHLFLGKNfnvKAKTLEEILhklvQLIqeedcSLQSLSVADSRLKLrtsilINALG 566
Cdd:COG4886 211 DLSGNQLTD----LPEPLANLTNLETLDLSNN---QLTDLPELG----NLT-----NLEELDLSNNQLTD-----LPPLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 567 SNTCLAKVDLSGNGMEDIGAKMLSKALQINSSLRTILWDRNNTSALGFLDIARALESNHTLRFMSFPVSDISQAYRSAPE 646
Cdd:COG4886 270 NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLAL 349
|
330
....*....|....*..
gi 2462498135 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 |
2.16e-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: 54.28 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 210 ALAYNQWFTKLYCKDLRLGS--EVLEQVLHTLSKSGSLEELVLDNAGLKTDFVQKLAGVFGengSCVLHALTLSHNPIED 287
Cdd:cd00116 46 ALRPQPSLKELCLSLNETGRipRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLLR---SSSLQELKLNNNGLGD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 288 KGFLSLSQQLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANPafasSLRYLDLSKNPglLATDEANALYSFLAQPNALV 367
Cdd:cd00116 123 RGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANR----DLKELNLANNG--IGDAGIRALAEGLKANCNLE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 368 HLDLSgtDCVID-----LLLGALLHGCCshLTYLNLARNSCSHRKGREAPPAFKqffSSAYTLSHVNLSATKLPLEALRA 442
Cdd:cd00116 197 VLDLN--NNGLTdegasALAETLASLKS--LEVLNLGDNNLTDAGAAALASALL---SPNISLLTLSLSCNDITDDGAKD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462498135 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 |
4.90e-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: 53.13 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 185 AEDNREFNLLDFS--HLESRDLALMVAALAYnQWFTKLYCKDLR------LGSEVLEQVLHtlskSGSLEELVLDNAGLK 256
Cdd:cd00116 47 LRPQPSLKELCLSlnETGRIPRGLQSLLQGL-TKGCGLQELDLSdnalgpDGCGVLESLLR----SSSLQELKLNNNGLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 257 TDFVQKLAGVFGENgSCVLHALTLSHNPIEDKGFLSLSQqLLCFPSGLTKLCLAKTAISPRGLQALGQTFGANpafaSSL 336
Cdd:cd00116 122 DRGLRLLAKGLKDL-PPALEKLVLGRNRLEGASCEALAK-ALRANRDLKELNLANNGIGDAGIRALAEGLKAN----CNL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 337 RYLDLSKNpgLLATDEANALYSFLAQPNALVHLDLSgtDCVIDLLlgallhgCCSHLtylnlarnscshrkgreappafk 416
Cdd:cd00116 196 EVLDLNNN--GLTDEGASALAETLASLKSLEVLNLG--DNNLTDA-------GAAAL----------------------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 417 qffssaytlshvnlsatklpLEALRALLQGLslnshlsdLHLDLSSCELRSAGAQALQEQLGAVTCVGSLDLSDNGFDSD 496
Cdd:cd00116 242 --------------------ASALLSPNISL--------LTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
|
....*
gi 2462498135 497 LLTLV 501
Cdd:cd00116 294 GAQLL 298
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
475-640 |
5.57e-06 |
|
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: 50.05 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 475 EQLGAVTCVGSLDLSDNGFDSD-LLTLVPALGKNKSLKHLFLGKNFnvkaktLEEILHKLVQLIQ--EEDCSLQSLSVAD 551
Cdd:cd00116 17 ELLPKLLCLQVLRLEGNTLGEEaAKALASALRPQPSLKELCLSLNE------TGRIPRGLQSLLQglTKGCGLQELDLSD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 552 SRLKLRTSILINALGSNTCLAKVDLSGNGMEDIGAKMLSKALQINS-SLRTILWDRNNTSALGFLDIARALESNHTLRFM 630
Cdd:cd00116 91 NALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKEL 170
|
170
....*....|
gi 2462498135 631 SFPVSDISQA 640
Cdd:cd00116 171 NLANNGIGDA 180
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
1144-1325 |
5.14e-05 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.56 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1144 AWQKRRSSDDAGPGSWKPPPPPQSTkPSFSAMRRAEATwHIAEESAPNHSCQSPSPASQDGEEEKEGTLFPERTLPARNA 1223
Cdd:PRK12323 362 AFRPGQSGGGAGPATAAAAPVAQPA-PAAAAPAAAAPA-PAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1224 KD---PALAPWPPKPVAVPRGRQPPQEPGVREEAEAGDAAPGVNKPRLRLSSQQDQEEPEVQGPPDPGRRTAPLKPKRTR 1300
Cdd:PRK12323 440 SArgpGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPA 519
|
170 180
....*....|....*....|....*
gi 2462498135 1301 RAQSCDKLEPDRRRPPDPTAGTSEP 1325
Cdd:PRK12323 520 GWVAESIPDPATADPDDAFETLAPA 544
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
1132-1315 |
1.44e-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: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1132 MGPGPDQEGSTQAWQKRRSSDDAGPGSWKPPPPP----QSTKPSFSAMRRAEATWHIAEESAPNHSCQsPSPASQDGEEE 1207
Cdd:NF033839 299 MQPSPQPEKKEVKPEPETPKPEVKPQLEKPKPEVkpqpEKPKPEVKPQLETPKPEVKPQPEKPKPEVK-PQPEKPKPEVK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1208 KE-GTLFPERTlPARNAKDPALAPWP--PKPVAVPRGRQPpqEPGVREEAEAG--DAAPGVNKPRLRLSSQQDQEEPEVQ 1282
Cdd:NF033839 378 PQpETPKPEVK-PQPEKPKPEVKPQPekPKPEVKPQPEKP--KPEVKPQPEKPkpEVKPQPEKPKPEVKPQPEKPKPEVK 454
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462498135 1283 ---GPPDPGRRTAPLKPKRTRRAQScDKLEPDRRRP 1315
Cdd:NF033839 455 pqpETPKPEVKPQPEKPKPEVKPQP-EKPKPDNSKP 489
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
239-576 |
2.15e-04 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 45.31 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 239 LSKSGSLEELVLDNAGLKT--DFVQKLAGvfgengscvLHALTLSHNPIEDkgflsLSQQLLCFPSgLTKLCLAKTAIS- 315
Cdd:COG4886 109 LSNLTNLESLDLSGNQLTDlpEELANLTN---------LKELDLSNNQLTD-----LPEPLGNLTN-LKSLDLSNNQLTd 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 316 -PRGLQALgqtfganpafaSSLRYLDLSKNPgllATDEANAlysfLAQPNALVHLDLSGTD-CVIDLLLGALlhgccSHL 393
Cdd:COG4886 174 lPEELGNL-----------TNLKELDLSNNQ---ITDLPEP----LGNLTNLEELDLSGNQlTDLPEPLANL-----TNL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 394 TYLNLARNscshrKGREAPpafkqFFSSAYTLSHVNLSATKlplealralLQGLSLNSHLSDL-HLDLSSCELRSAGAQA 472
Cdd:COG4886 231 ETLDLSNN-----QLTDLP-----ELGNLTNLEELDLSNNQ---------LTDLPPLANLTNLkTLDLSNNQLTDLKLKE 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 473 LQE-------QLGAVTCVGSLDLSDNGFDSDLLTLVPALGKNKSLKHLFLGKNFNVKAKTLEEILHKLVQLIQEEDCSLQ 545
Cdd:COG4886 292 LELllglnslLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGL 371
|
330 340 350
....*....|....*....|....*....|.
gi 2462498135 546 SLSVADSRLKLRTSILINALGSNTCLAKVDL 576
Cdd:COG4886 372 LGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
1177-1325 |
4.03e-04 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 45.06 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1177 RAEATWHIAEESAPNHSCQSPSPASQDgeeekegTLFPERTLPARnAKDPALAPWP-PKPVAVPRGRQPPQEPGVREEAE 1255
Cdd:PHA03378 656 QVEITPYKPTWTQIGHIPYQPSPTGAN-------TMLPIQWAPGT-MQPPPRAPTPmRPPAAPPGRAQRPAAATGRARPP 727
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1256 AGdaAPGVNKPRlrlssqqdqeepevQGPPDPGRRTAPlKPKRTRRAQSCdklePDRRRPPDPTAGTSEP 1325
Cdd:PHA03378 728 AA--APGRARPP--------------AAAPGRARPPAA-APGRARPPAAA----PGRARPPAAAPGAPTP 776
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
1235-1318 |
1.48e-03 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 41.53 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1235 PVAVPRGRQPPqePGVREEAEAGDAAPGVNKP-RLRLSSQQDQEEPEVQGPPDPGRRTAPlKPKRTRRAQSCDKLEPdrr 1313
Cdd:PRK11633 58 AATQALPTQPP--EGAAEAVRAGDAAAPSLDPaTVAPPNTPVEPEPAPVEPPKPKPVEKP-KPKPKPQQKVEAPPAP--- 131
|
....*
gi 2462498135 1314 rPPDP 1318
Cdd:PRK11633 132 -KPEP 135
|
|
| PRK07003 |
PRK07003 |
DNA polymerase III subunit gamma/tau; |
1151-1325 |
2.09e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 42.53 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1151 SDDAGPGSWKPPPPPQSTKPSFSAMRRAEATWHIAEESAPNHSCQSPSPASQDGEEEKE---GTLFPERTLPARNAKDPA 1227
Cdd:PRK07003 435 TADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPApraAAPSAATPAAVPDARAPA 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1228 LAPWP--PKPVAVPRGRQPPQEPGV-REEAEAGDAAPGVNKPR---LRLSSQQDQE---------EPEVQGPPDPGRRTA 1292
Cdd:PRK07003 515 AASREdaPAAAAPPAPEARPPTPAAaAPAARAGGAAAALDVLRnagMRVSSDRGARaaaaakpaaAPAAAPKPAAPRVAV 594
|
170 180 190
....*....|....*....|....*....|...
gi 2462498135 1293 PLKPKRTRRAQSCDKLEPDRRRPPDPTAGTSEP 1325
Cdd:PRK07003 595 QVPTPRARAATGDAPPNGAARAEQAAESRGAPP 627
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
1110-1292 |
2.39e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 42.28 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1110 PEEESSLLPGFGGGRGPSFRRKMGPGPDQEGSTQAWQKRRSSDDAGPGSWKPPPPPQSTKPSFSAMRRAEATWHIAE--- 1186
Cdd:PRK07764 618 PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAgaa 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1187 --ESAPNHSCQSPSPASQDGEEEKEGTLFPERTLPARNAKDPALAPWPPKPVAVPR-GRQPPQEPGVREEAEAGDAAPgv 1263
Cdd:PRK07764 698 paQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGaPAQPPPPPAPAPAAAPAAAPP-- 775
|
170 180 190
....*....|....*....|....*....|...
gi 2462498135 1264 nkprlrlSSQQDQEEPEV----QGPPDPGRRTA 1292
Cdd:PRK07764 776 -------PSPPSEEEEMAeddaPSMDDEDRRDA 801
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
1101-1291 |
3.79e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1101 GNNSSPCWSPEEESSLLPGfGGGRGPSFRRKMGPGPDQE--GSTQAWQKRRSSDDAGPGSWKPPPPPQSTKPSFSAMRRA 1178
Cdd:PHA03169 75 TAEESRHGEKEERGQGGPS-GSGSESVGSPTPSPSGSAEelASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462498135 1179 EAtwHIAEESAPNHSCQspsPASQDGEEEKEgtlfPERTLPARNAKDPalaPWPPKPVAVPRGRQPPQEPGvREEAEAGD 1258
Cdd:PHA03169 154 SH--NPSPNQQPSSFLQ---PSHEDSPEEPE----PPTSEPEPDSPGP---PQSETPTSSPPPQSPPDEPG-EPQSPTPQ 220
|
170 180 190
....*....|....*....|....*....|...
gi 2462498135 1259 AAPGVNKPRlRLSSQQDQEEPEVQGPPDPGRRT 1291
Cdd:PHA03169 221 QAPSPNTQQ-AVEHEDEPTEPEREGPPFPGHRS 252
|
|
| |
