|
Name |
Accession |
Description |
Interval |
E-value |
| Atypical_Card |
pfam18461 |
Atypical caspase recruitment domain; The N-terminal effector domain found in NLRC5. It adopts ... |
1-79 |
3.93e-44 |
|
Atypical caspase recruitment domain; The N-terminal effector domain found in NLRC5. It adopts a six alpha-helix bundle with a general death fold. Structure and sequence analysis of the NLRC5-N indicate that it possesses a fold similar to the one of the death-fold domains; however, it displays significant differences in the number of core alpha-helices and their relative orientation. Hence, it is suggested that NLRC5 belongs to the caspase recruitment domain (CARD) subfamily as an atypical CARD.
:
Pssm-ID: 436519 Cd Length: 95 Bit Score: 155.19 E-value: 3.93e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 1 MDPIDLQLGNKNLWSCLVRLLSKDPEWLNAKMKFFLPNTDLDSRNETLDPEQRVILQLNKLHVQGSATWQSFIHCVCMQ 79
Cdd:pfam18461 1 MDPESLQLGTENLWPWLVRLLSKNPEWLSAKVKFFLPNMDLGSSNEAPDPTQKVILQLDRLEAQGLATWQSFIHCVCME 79
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
222-383 |
6.44e-44 |
|
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.
:
Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 157.47 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 222 RVTVLLGKAGMGKTTLAHRLCQKWAEGHLD-CFQALFLFEFRQLNLITRFLTLSQLLFDLYLSPESDPDAVFQYLEKNAD 300
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPqGFDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEVWAVILELPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 301 QVLLIFDGLDEALQPMGP-DGPGSVLTLFSRLCRGTLLPGCRVMATSRPG---KLPACLpAEAATVYMLGFDGPRVEEYV 376
Cdd:pfam05729 81 RLLLILDGLDELVSDLGQlDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDalrDLRRGL-EEPRYLEVRGFSESDRKQYV 159
|
....*..
gi 1622911992 377 NHFFSAQ 383
Cdd:pfam05729 160 RKYFSDE 166
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1560-1851 |
1.72e-33 |
|
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: 135.69 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1560 LLLNSSALTLLTHGLSHM-----------TRLQSLRLKRNSIGDVGCCHLSEALRAATSLEELDLSHNQIGDAGVQHLAT 1628
Cdd:COG5238 151 LGGNAVHLLGLAARLGLLaaismakalqnNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1629 ILPGLPELRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGCNALGDPTALGLAREL--PQHLRVLHLPFSHLGPGGAL 1706
Cdd:COG5238 231 ALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgNTTLTSLDLSVNRIGDEGAI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1707 SLTQALDGSPHLEEISLAennlaggvlhfckelpllrqidlvSCKIDNQTIKLLTSSFTRCPALEVILLSWNLLGDEAAA 1786
Cdd:COG5238 311 ALAEGLQGNKTLHTLNLA------------------------YNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAI 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622911992 1787 ELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLaQGSSIQVIRLWNNPIPCDMAQRLKSQEPRL 1851
Cdd:COG5238 367 ALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL-QTNRLHTLILDGNLIGAEAQQRLEQLLERI 430
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
171-547 |
9.94e-25 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
:
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 112.98 E-value: 9.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 171 ALHQVYVPPILRRATASLDTQEGAIMGDLKVEDGTDVSISDLFNTRV-NKGPRVTVLLGKAGMGKTTLAHRLCQKWAEGH 249
Cdd:COG5635 129 LLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRLELlEAKKKRLLILGEPGSGKTTLLRYLALELAERY 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 250 LDCFQAL-FLFEFRQLNlitRFLTLSQLLFDLYLSPESDPDAVFQYLeKNADQVLLIFDGLDEALQPMGPDgpgSVLTLF 328
Cdd:COG5635 209 LDAEDPIpILIELRDLA---EEASLEDLLAEALEKRGGEPEDALERL-LRNGRLLLLLDGLDEVPDEADRD---EVLNQL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 329 SRLCRGtlLPGCRVMATSRPGKLPACLPAEAATVYMLGFDGPRVEEYVNHFFSAQPLQ-EGALAELQTNGRLRSLCAVPA 407
Cdd:COG5635 282 RRFLER--YPKARVIITSRPEGYDSSELEGFEVLELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 408 LCQVacLCLHHLLPDHAPGQSVALLptmtQLYMQMVLA-LSPRGHLPTTSLLD-------LGEVALRGLETGKVIFYAKD 479
Cdd:COG5635 360 LLTL--LALLLRERGELPDTRAELY----EQFVELLLErWDEQRGLTIYRELSreelrelLSELALAMQENGRTEFAREE 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622911992 480 ----IAPPLIAFGATHSLLTSFCVRTGP--GHQQTGYAFTHVSLQEFLAALHLMASPKVDKDTLTQHVTLHSRW 547
Cdd:COG5635 434 leeiLREYLGRRKDAEALLDELLLRTGLlvERGEGRYSFAHRSFQEYLAARALVEELDEELLELLAEHLEDPRW 507
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1299-1676 |
6.64e-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: 85.61 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1299 PRVREASVNLGSEQSFRIHFSKEDQAGKTLRLSECSFRPEHVSRLATGLSQSLQLTELTLTQCCLDQEQLAILlslvgrp 1378
Cdd:COG5238 156 VHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEIL------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1379 aglfslrvqepwadragilsllevcaqasgsvteisisktqqqlcvqlefprqeenpeavalrlahcdlgthhsllvGQL 1458
Cdd:COG5238 229 -----------------------------------------------------------------------------AEA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1459 METCARLQQLSLSqvnlceDNddsslllqnlllslselktfrltssCVSTEGLAHLASGLGHCHHLEELDLSNNQFDEEG 1538
Cdd:COG5238 232 LKGNKSLTTLDLS------NN-------------------------QIGDEGVIALAEALKNNTTVETLYLSGNQIGAEG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1539 TKALMRALEGKWMLKRLDLGHLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCCHLSEALRAATSLEELDLSHNQI 1618
Cdd:COG5238 281 AIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQI 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622911992 1619 GDAGVQHLATILPGLPELRKIDLSVNSISPAGGMQLAESLILCRhLEELMLGCNALGD 1676
Cdd:COG5238 361 GDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGA 417
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
687-915 |
2.83e-14 |
|
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: 77.52 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 687 QIENLSFKSRKCGDAFAEALSRSLPTMGRLQMLGLAGSKITARGISHLVKALPLCPQLEEVSFRDNQLSDQVVLNIVEVL 766
Cdd:COG5238 181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 767 PHLPRLRKLDLSGNSVCVSTLLCLARVAVTCPTIRTLQARKADLIFllspptETTAELqrAPDLQESDGQRkgaqsrslT 846
Cdd:COG5238 261 KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGD------EGAIAL--AEGLQGNKTLH--------T 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 847 LRLQKCQLQVHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDNGLSLAGV 915
Cdd:COG5238 325 LNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGA 393
|
|
| RNA1 super family |
cl34950 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
839-1069 |
7.61e-14 |
|
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: 75.98 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 839 GAQSRSLTLRLQKCQLQvHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDNGLSLAGVHCV 918
Cdd:COG5238 150 PLGGNAVHLLGLAARLG-LLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEIL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 919 LRAVSACWTLAELHISLRHKTvvfmfaqepeeqegPQERAAFLDSLmlqmpsELPLSSRRMRLTHCGLQAKHLEQLCKAL 998
Cdd:COG5238 229 AEALKGNKSLTTLDLSNNQIG--------------DEGVIALAEAL------KNNTTVETLYLSGNQIGAEGAIALAKAL 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622911992 999 GGSCHLGHLHLdfSGNALGDEGATRLAQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLDISF 1069
Cdd:COG5238 289 QGNTTLTSLDL--SVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSD 357
|
|
| PPP1R42 super family |
cl42388 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1009-1307 |
1.68e-11 |
|
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: 67.38 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1009 LDFSGNALGDEGATrlaQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLDISFEsqhillrgdKTGRDIWAT 1088
Cdd:cd00116 3 LSLKGELLKTERAT---ELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLN---------ETGRIPRGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1089 GSSPDF------------------PAGAEFL-GFRRRCIPRSLRLSECPLEPPSLTHLCATLKECPGPLE-LQLSCEFLS 1148
Cdd:cd00116 71 QSLLQGltkgcglqeldlsdnalgPDGCGVLeSLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEkLVLGRNRLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1149 DQSLETLLDCLPRLPQLSLLQLNQTGLSPKSPFLLANTLSLCPRVKKVDLRSlhhatlhfrsneeqegvccgrftgCSLS 1228
Cdd:cd00116 151 GASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNN------------------------NGLT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1229 QEHVESLCRLLSKCKDLSQVDLSANLLGDSGLRCLLECLPQVPIS-GSLDLSHNSVSQESALYLVETLPSCPRVREASVN 1307
Cdd:cd00116 207 DEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISlLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| NLRC4_HD2 super family |
cl39284 |
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
514-628 |
5.14e-10 |
|
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.
The actual alignment was detected with superfamily member pfam17776:
Pssm-ID: 465499 [Multi-domain] Cd Length: 122 Bit Score: 58.84 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 514 HVSLQEFLAALHLMASPKVDKDTLTqHVTLHSRWVQRTKARLDLS--------DHLPTFLAGLASCTCRPFLSHLaQGNE 585
Cdd:pfam17776 1 HLSFQEFFAALFYVLSFKEEKSNPL-KEFFGLRKRESLKSLLDKAlksknghlDLFLRFLFGLLNEENQRLLEGL-LGCK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622911992 586 DCVGTKQAaVVQVLKKLATRKLTGPKVVELCHCVNETQEPELA 628
Cdd:pfam17776 79 LSSEIKQE-LLQWIKSLIQKELSSERFLNLFHCLYELQDESFV 120
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Atypical_Card |
pfam18461 |
Atypical caspase recruitment domain; The N-terminal effector domain found in NLRC5. It adopts ... |
1-79 |
3.93e-44 |
|
Atypical caspase recruitment domain; The N-terminal effector domain found in NLRC5. It adopts a six alpha-helix bundle with a general death fold. Structure and sequence analysis of the NLRC5-N indicate that it possesses a fold similar to the one of the death-fold domains; however, it displays significant differences in the number of core alpha-helices and their relative orientation. Hence, it is suggested that NLRC5 belongs to the caspase recruitment domain (CARD) subfamily as an atypical CARD.
Pssm-ID: 436519 Cd Length: 95 Bit Score: 155.19 E-value: 3.93e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 1 MDPIDLQLGNKNLWSCLVRLLSKDPEWLNAKMKFFLPNTDLDSRNETLDPEQRVILQLNKLHVQGSATWQSFIHCVCMQ 79
Cdd:pfam18461 1 MDPESLQLGTENLWPWLVRLLSKNPEWLSAKVKFFLPNMDLGSSNEAPDPTQKVILQLDRLEAQGLATWQSFIHCVCME 79
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
222-383 |
6.44e-44 |
|
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.
Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 157.47 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 222 RVTVLLGKAGMGKTTLAHRLCQKWAEGHLD-CFQALFLFEFRQLNLITRFLTLSQLLFDLYLSPESDPDAVFQYLEKNAD 300
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPqGFDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEVWAVILELPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 301 QVLLIFDGLDEALQPMGP-DGPGSVLTLFSRLCRGTLLPGCRVMATSRPG---KLPACLpAEAATVYMLGFDGPRVEEYV 376
Cdd:pfam05729 81 RLLLILDGLDELVSDLGQlDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDalrDLRRGL-EEPRYLEVRGFSESDRKQYV 159
|
....*..
gi 1622911992 377 NHFFSAQ 383
Cdd:pfam05729 160 RKYFSDE 166
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1560-1851 |
1.72e-33 |
|
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: 135.69 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1560 LLLNSSALTLLTHGLSHM-----------TRLQSLRLKRNSIGDVGCCHLSEALRAATSLEELDLSHNQIGDAGVQHLAT 1628
Cdd:COG5238 151 LGGNAVHLLGLAARLGLLaaismakalqnNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1629 ILPGLPELRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGCNALGDPTALGLAREL--PQHLRVLHLPFSHLGPGGAL 1706
Cdd:COG5238 231 ALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgNTTLTSLDLSVNRIGDEGAI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1707 SLTQALDGSPHLEEISLAennlaggvlhfckelpllrqidlvSCKIDNQTIKLLTSSFTRCPALEVILLSWNLLGDEAAA 1786
Cdd:COG5238 311 ALAEGLQGNKTLHTLNLA------------------------YNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAI 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622911992 1787 ELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLaQGSSIQVIRLWNNPIPCDMAQRLKSQEPRL 1851
Cdd:COG5238 367 ALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL-QTNRLHTLILDGNLIGAEAQQRLEQLLERI 430
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1522-1822 |
2.25e-30 |
|
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: 123.62 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1522 HHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLG--HLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCcHLS 1599
Cdd:cd00116 23 LCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGC-GVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1600 EALRAATSLEELDLSHNQIGDAGVQHLATILPGLPE-LRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGCNALGDPT 1678
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1679 ALGLARELP--QHLRVLHLPFSHLGPGGALSLTQALDGSPHLEEISLAENNLAggvlhfckelpllrqiDLVSCKIDNQT 1756
Cdd:cd00116 182 IRALAEGLKanCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLT----------------DAGAAALASAL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622911992 1757 IKLLTSsftrcpaLEVILLSWNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLAQ 1822
Cdd:cd00116 246 LSPNIS-------LLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLE 304
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
171-547 |
9.94e-25 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 112.98 E-value: 9.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 171 ALHQVYVPPILRRATASLDTQEGAIMGDLKVEDGTDVSISDLFNTRV-NKGPRVTVLLGKAGMGKTTLAHRLCQKWAEGH 249
Cdd:COG5635 129 LLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRLELlEAKKKRLLILGEPGSGKTTLLRYLALELAERY 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 250 LDCFQAL-FLFEFRQLNlitRFLTLSQLLFDLYLSPESDPDAVFQYLeKNADQVLLIFDGLDEALQPMGPDgpgSVLTLF 328
Cdd:COG5635 209 LDAEDPIpILIELRDLA---EEASLEDLLAEALEKRGGEPEDALERL-LRNGRLLLLLDGLDEVPDEADRD---EVLNQL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 329 SRLCRGtlLPGCRVMATSRPGKLPACLPAEAATVYMLGFDGPRVEEYVNHFFSAQPLQ-EGALAELQTNGRLRSLCAVPA 407
Cdd:COG5635 282 RRFLER--YPKARVIITSRPEGYDSSELEGFEVLELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 408 LCQVacLCLHHLLPDHAPGQSVALLptmtQLYMQMVLA-LSPRGHLPTTSLLD-------LGEVALRGLETGKVIFYAKD 479
Cdd:COG5635 360 LLTL--LALLLRERGELPDTRAELY----EQFVELLLErWDEQRGLTIYRELSreelrelLSELALAMQENGRTEFAREE 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622911992 480 ----IAPPLIAFGATHSLLTSFCVRTGP--GHQQTGYAFTHVSLQEFLAALHLMASPKVDKDTLTQHVTLHSRW 547
Cdd:COG5635 434 leeiLREYLGRRKDAEALLDELLLRTGLlvERGEGRYSFAHRSFQEYLAARALVEELDEELLELLAEHLEDPRW 507
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1299-1676 |
6.64e-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: 85.61 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1299 PRVREASVNLGSEQSFRIHFSKEDQAGKTLRLSECSFRPEHVSRLATGLSQSLQLTELTLTQCCLDQEQLAILlslvgrp 1378
Cdd:COG5238 156 VHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEIL------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1379 aglfslrvqepwadragilsllevcaqasgsvteisisktqqqlcvqlefprqeenpeavalrlahcdlgthhsllvGQL 1458
Cdd:COG5238 229 -----------------------------------------------------------------------------AEA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1459 METCARLQQLSLSqvnlceDNddsslllqnlllslselktfrltssCVSTEGLAHLASGLGHCHHLEELDLSNNQFDEEG 1538
Cdd:COG5238 232 LKGNKSLTTLDLS------NN-------------------------QIGDEGVIALAEALKNNTTVETLYLSGNQIGAEG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1539 TKALMRALEGKWMLKRLDLGHLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCCHLSEALRAATSLEELDLSHNQI 1618
Cdd:COG5238 281 AIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQI 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622911992 1619 GDAGVQHLATILPGLPELRKIDLSVNSISPAGGMQLAESLILCRhLEELMLGCNALGD 1676
Cdd:COG5238 361 GDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGA 417
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1440-1630 |
1.58e-15 |
|
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: 79.71 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1440 LRLAHCDLG-THHSLLVGQLMETCARLQQLSLSQVNLcedNDDSSLLLQNLLLSLSELKTFRLTSSCVSTEGLAHLASGL 1518
Cdd:cd00116 113 LKLNNNGLGdRGLRLLAKGLKDLPPALEKLVLGRNRL---EGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1519 GHCHHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLGH-LLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCCH 1597
Cdd:cd00116 190 KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDnNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKD 269
|
170 180 190
....*....|....*....|....*....|...
gi 1622911992 1598 LSEALRAATSLEELDLSHNQIGDAGVQHLATIL 1630
Cdd:cd00116 270 LAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
687-915 |
2.83e-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: 77.52 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 687 QIENLSFKSRKCGDAFAEALSRSLPTMGRLQMLGLAGSKITARGISHLVKALPLCPQLEEVSFRDNQLSDQVVLNIVEVL 766
Cdd:COG5238 181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 767 PHLPRLRKLDLSGNSVCVSTLLCLARVAVTCPTIRTLQARKADLIFllspptETTAELqrAPDLQESDGQRkgaqsrslT 846
Cdd:COG5238 261 KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGD------EGAIAL--AEGLQGNKTLH--------T 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 847 LRLQKCQLQVHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDNGLSLAGV 915
Cdd:COG5238 325 LNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGA 393
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
839-1069 |
7.61e-14 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 75.98 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 839 GAQSRSLTLRLQKCQLQvHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDNGLSLAGVHCV 918
Cdd:COG5238 150 PLGGNAVHLLGLAARLG-LLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEIL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 919 LRAVSACWTLAELHISLRHKTvvfmfaqepeeqegPQERAAFLDSLmlqmpsELPLSSRRMRLTHCGLQAKHLEQLCKAL 998
Cdd:COG5238 229 AEALKGNKSLTTLDLSNNQIG--------------DEGVIALAEAL------KNNTTVETLYLSGNQIGAEGAIALAKAL 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622911992 999 GGSCHLGHLHLdfSGNALGDEGATRLAQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLDISF 1069
Cdd:COG5238 289 QGNTTLTSLDL--SVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSD 357
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
845-1202 |
1.20e-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: 71.23 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 845 LTLRLQKCQLQVHDAETLIALLQegpHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDN--GLSLAGVHCVLRAV 922
Cdd:cd00116 1 LQLSLKGELLKTERATELLPKLL---CLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNetGRIPRGLQSLLQGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 923 SACWTLAELHISlrhktvvfmfaqepeeqegpqeRAAFLDSLMLQMPSELPLSS-RRMRLTHCGLQAKHLEQLCKALGG- 1000
Cdd:cd00116 78 TKGCGLQELDLS----------------------DNALGPDGCGVLESLLRSSSlQELKLNNNGLGDRGLRLLAKGLKDl 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1001 SCHLGHLHLdfSGNALGDEGATRLAQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLdisfesqhillrgdk 1080
Cdd:cd00116 136 PPALEKLVL--GRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVL--------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1081 tgrDIWATGSSPDfpaGAEFL--GFRRRCIPRSLRLSECPLEPPSLTHLC-ATLKECPGPLELQLSCEFLSDQSLETLLD 1157
Cdd:cd00116 199 ---DLNNNGLTDE---GASALaeTLASLKSLEVLNLGDNNLTDAGAAALAsALLSPNISLLTLSLSCNDITDDGAKDLAE 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622911992 1158 CLPRLPQLSLLQLNQTGLSPKSPFLLANTLsLCPRVKKVDLRSLH 1202
Cdd:cd00116 273 VLAEKESLLELDLRGNKFGEEGAQLLAESL-LEPGNELESLWVKD 316
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1009-1307 |
1.68e-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: 67.38 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1009 LDFSGNALGDEGATrlaQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLDISFEsqhillrgdKTGRDIWAT 1088
Cdd:cd00116 3 LSLKGELLKTERAT---ELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLN---------ETGRIPRGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1089 GSSPDF------------------PAGAEFL-GFRRRCIPRSLRLSECPLEPPSLTHLCATLKECPGPLE-LQLSCEFLS 1148
Cdd:cd00116 71 QSLLQGltkgcglqeldlsdnalgPDGCGVLeSLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEkLVLGRNRLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1149 DQSLETLLDCLPRLPQLSLLQLNQTGLSPKSPFLLANTLSLCPRVKKVDLRSlhhatlhfrsneeqegvccgrftgCSLS 1228
Cdd:cd00116 151 GASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNN------------------------NGLT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1229 QEHVESLCRLLSKCKDLSQVDLSANLLGDSGLRCLLECLPQVPIS-GSLDLSHNSVSQESALYLVETLPSCPRVREASVN 1307
Cdd:cd00116 207 DEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISlLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
764-1062 |
2.01e-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: 67.38 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 764 EVLPHLPRLRKLDLSGNSVCVSTLLCLARVavtcptirtLQARKADLIFLLSpptetTAELQRAPDLQESDGQRKGAQSR 843
Cdd:cd00116 17 ELLPKLLCLQVLRLEGNTLGEEAAKALASA---------LRPQPSLKELCLS-----LNETGRIPRGLQSLLQGLTKGCG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 844 SLTLRLQKCQLQVHDAETLIALLQeGPHLEEVDLSGNQLEDEGCRLMAEAASQL-HIARKLDLSDNGLSLAGVHCVLRAV 922
Cdd:cd00116 83 LQELDLSDNALGPDGCGVLESLLR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEGASCEALAKAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 923 SACWTLAELHISLRHktvvfmfaqepeeqegpqERAAFLDSLMLQMPSELPLssRRMRLTHCGLQAKHLEQLCKALGGSC 1002
Cdd:cd00116 162 RANRDLKELNLANNG------------------IGDAGIRALAEGLKANCNL--EVLDLNNNGLTDEGASALAETLASLK 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622911992 1003 HLghLHLDFSGNALGDEGATRLA-QLLPGLGALQSLNLSENGLSLDAVLGLARC---FSTLQWL 1062
Cdd:cd00116 222 SL--EVLNLGDNNLTDAGAAALAsALLSPNISLLTLSLSCNDITDDGAKDLAEVlaeKESLLEL 283
|
|
| NLRC4_HD2 |
pfam17776 |
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
514-628 |
5.14e-10 |
|
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.
Pssm-ID: 465499 [Multi-domain] Cd Length: 122 Bit Score: 58.84 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 514 HVSLQEFLAALHLMASPKVDKDTLTqHVTLHSRWVQRTKARLDLS--------DHLPTFLAGLASCTCRPFLSHLaQGNE 585
Cdd:pfam17776 1 HLSFQEFFAALFYVLSFKEEKSNPL-KEFFGLRKRESLKSLLDKAlksknghlDLFLRFLFGLLNEENQRLLEGL-LGCK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622911992 586 DCVGTKQAaVVQVLKKLATRKLTGPKVVELCHCVNETQEPELA 628
Cdd:pfam17776 79 LSSEIKQE-LLQWIKSLIQKELSSERFLNLFHCLYELQDESFV 120
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
986-1296 |
2.10e-06 |
|
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: 52.48 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 986 LQAKHLEQLCKALGGSCHLGHLHLdfSGNALGDEGATRLAQLLPGLGALQSLNLSENGLSLDAVLGLARcfstlqwlfhl 1065
Cdd:COG5238 192 IGDEGIEELAEALTQNTTVTTLWL--KRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAE----------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1066 diSFESQHILLRGDKTGRDIWATgsspdfpaGAEFLGfrrrciprslrlsecpleppslthlcATLKECPGPLELQLSCE 1145
Cdd:COG5238 259 --ALKNNTTVETLYLSGNQIGAE--------GAIALA--------------------------KALQGNTTLTSLDLSVN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1146 FLSDQSLETLLDCLPRLPQLSLLQLNQTGLSPKSPFLLANTLSLCPRVKKVDLrslhhatlhfrsneeqegvccgrfTGC 1225
Cdd:COG5238 303 RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDL------------------------SDN 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622911992 1226 SLSQEHVESLCRLLSKCKDLSQVDLSANLLGDSGLRCLLECLpQVPISGSLDLSHNSVSQESALYLVETLP 1296
Cdd:COG5238 359 QIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL-QTNRLHTLILDGNLIGAEAQQRLEQLLE 428
|
|
| LRR_6 |
pfam13516 |
Leucine Rich repeat; |
1606-1627 |
7.19e-04 |
|
Leucine Rich repeat;
Pssm-ID: 463907 [Multi-domain] Cd Length: 24 Bit Score: 38.37 E-value: 7.19e-04
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1518-1674 |
1.98e-03 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 43.30 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1518 LGHCHHLEELDLSNNQFDEEGTKALMRalegkwmlkrLDLGHLL-LNSSALT-LLTHGLSHMTRLQSLRLKRNSIGDvgc 1595
Cdd:PLN00113 400 LGACRSLRRVRLQDNSFSGELPSEFTK----------LPLVYFLdISNNNLQgRINSRKWDMPSLQMLSLARNKFFG--- 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 1596 cHLSEALRAaTSLEELDLSHNQIGDAGVQHLATilpgLPELRKIDLSVNSISPaggmQLAESLILCRHLEELMLGCNAL 1674
Cdd:PLN00113 467 -GLPDSFGS-KRLENLDLSRNQFSGAVPRKLGS----LSELMQLKLSENKLSG----EIPDELSSCKKLVSLDLSHNQL 535
|
|
| LRR_RI |
smart00368 |
Leucine rich repeat, ribonuclease inhibitor type; |
1606-1627 |
6.51e-03 |
|
Leucine rich repeat, ribonuclease inhibitor type;
Pssm-ID: 197686 [Multi-domain] Cd Length: 28 Bit Score: 35.85 E-value: 6.51e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Atypical_Card |
pfam18461 |
Atypical caspase recruitment domain; The N-terminal effector domain found in NLRC5. It adopts ... |
1-79 |
3.93e-44 |
|
Atypical caspase recruitment domain; The N-terminal effector domain found in NLRC5. It adopts a six alpha-helix bundle with a general death fold. Structure and sequence analysis of the NLRC5-N indicate that it possesses a fold similar to the one of the death-fold domains; however, it displays significant differences in the number of core alpha-helices and their relative orientation. Hence, it is suggested that NLRC5 belongs to the caspase recruitment domain (CARD) subfamily as an atypical CARD.
Pssm-ID: 436519 Cd Length: 95 Bit Score: 155.19 E-value: 3.93e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 1 MDPIDLQLGNKNLWSCLVRLLSKDPEWLNAKMKFFLPNTDLDSRNETLDPEQRVILQLNKLHVQGSATWQSFIHCVCMQ 79
Cdd:pfam18461 1 MDPESLQLGTENLWPWLVRLLSKNPEWLSAKVKFFLPNMDLGSSNEAPDPTQKVILQLDRLEAQGLATWQSFIHCVCME 79
|
|
| NACHT |
pfam05729 |
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
222-383 |
6.44e-44 |
|
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.
Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 157.47 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 222 RVTVLLGKAGMGKTTLAHRLCQKWAEGHLD-CFQALFLFEFRQLNLITRFLTLSQLLFDLYLSPESDPDAVFQYLEKNAD 300
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPqGFDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEVWAVILELPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 301 QVLLIFDGLDEALQPMGP-DGPGSVLTLFSRLCRGTLLPGCRVMATSRPG---KLPACLpAEAATVYMLGFDGPRVEEYV 376
Cdd:pfam05729 81 RLLLILDGLDELVSDLGQlDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDalrDLRRGL-EEPRYLEVRGFSESDRKQYV 159
|
....*..
gi 1622911992 377 NHFFSAQ 383
Cdd:pfam05729 160 RKYFSDE 166
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1560-1851 |
1.72e-33 |
|
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: 135.69 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1560 LLLNSSALTLLTHGLSHM-----------TRLQSLRLKRNSIGDVGCCHLSEALRAATSLEELDLSHNQIGDAGVQHLAT 1628
Cdd:COG5238 151 LGGNAVHLLGLAARLGLLaaismakalqnNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1629 ILPGLPELRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGCNALGDPTALGLAREL--PQHLRVLHLPFSHLGPGGAL 1706
Cdd:COG5238 231 ALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALqgNTTLTSLDLSVNRIGDEGAI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1707 SLTQALDGSPHLEEISLAennlaggvlhfckelpllrqidlvSCKIDNQTIKLLTSSFTRCPALEVILLSWNLLGDEAAA 1786
Cdd:COG5238 311 ALAEGLQGNKTLHTLNLA------------------------YNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAI 366
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622911992 1787 ELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLaQGSSIQVIRLWNNPIPCDMAQRLKSQEPRL 1851
Cdd:COG5238 367 ALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL-QTNRLHTLILDGNLIGAEAQQRLEQLLERI 430
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1512-1801 |
6.55e-32 |
|
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: 131.07 E-value: 6.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1512 AHLASGLGHCHHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLGHLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIG 1591
Cdd:COG5238 170 AISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1592 DVGCCHLSEALRAATSLEELDLSHNQIGDAGVQHLATILPGLPELRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGC 1671
Cdd:COG5238 250 DEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1672 NALGDPTALGLARELPQHLRV--LHLPFSHLGPGGALSLTQALDGSPHLEEISLAENNL-AGGVLHFCKELpllrQIdlv 1748
Cdd:COG5238 330 NGIGAQGAIALAKALQENTTLhsLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIgKQGAEALIDAL----QT--- 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622911992 1749 sckidNQTIKLLtssftrcpalevilLSWNLLGDEAAAELAQVLPqmgRLKRV 1801
Cdd:COG5238 403 -----NRLHTLI--------------LDGNLIGAEAQQRLEQLLE---RIKSV 433
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1522-1822 |
2.25e-30 |
|
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: 123.62 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1522 HHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLG--HLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCcHLS 1599
Cdd:cd00116 23 LCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGC-GVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1600 EALRAATSLEELDLSHNQIGDAGVQHLATILPGLPE-LRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGCNALGDPT 1678
Cdd:cd00116 102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1679 ALGLARELP--QHLRVLHLPFSHLGPGGALSLTQALDGSPHLEEISLAENNLAggvlhfckelpllrqiDLVSCKIDNQT 1756
Cdd:cd00116 182 IRALAEGLKanCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLT----------------DAGAAALASAL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622911992 1757 IKLLTSsftrcpaLEVILLSWNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLAQ 1822
Cdd:cd00116 246 LSPNIS-------LLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLE 304
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1507-1728 |
8.49e-28 |
|
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: 116.30 E-value: 8.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1507 STEGLAHLASGLGHCHHLEELDLSNNQFDEEGTKALMRALEGkWMLKRLDLGHLLLNSSALTLLTHGL-SHMTRLQSLRL 1585
Cdd:cd00116 66 IPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLkDLPPALEKLVL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1586 KRNSIGDVGCCHLSEALRAATSLEELDLSHNQIGDAGVQHLATILPGLPELRKIDLSVNSISPAGGMQLAESLILCRHLE 1665
Cdd:cd00116 145 GRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLE 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622911992 1666 ELMLGCNALGDPTALGLA---RELPQHLRVLHLPFSHLGPGGALSLTQALDGSPHLEEISLAENNL 1728
Cdd:cd00116 225 VLNLGDNNLTDAGAAALAsalLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKF 290
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1451-1713 |
2.30e-25 |
|
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: 111.42 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1451 HSLLVGQLMETCARLQQLSLSQVNLCEDN--DDSSLLLQNLLLSLSELKTFRLTSSCVSTEGLAHLASGLGHCHHLEELD 1528
Cdd:COG5238 163 ARLGLLAAISMAKALQNNSVETVYLGCNQigDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1529 LSNNQFDEEGTKALMRALEGKWMLKRLDLGHLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCCHLSEALRAATSL 1608
Cdd:COG5238 243 LSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1609 EELDLSHNQIGDAGVQHLATILPGLPELRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGCNALGDPTALGLARELpQ 1688
Cdd:COG5238 323 HTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL-Q 401
|
250 260
....*....|....*....|....*..
gi 1622911992 1689 HLRVLHLPFS--HLGPGGALSLTQALD 1713
Cdd:COG5238 402 TNRLHTLILDgnLIGAEAQQRLEQLLE 428
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
171-547 |
9.94e-25 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 112.98 E-value: 9.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 171 ALHQVYVPPILRRATASLDTQEGAIMGDLKVEDGTDVSISDLFNTRV-NKGPRVTVLLGKAGMGKTTLAHRLCQKWAEGH 249
Cdd:COG5635 129 LLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRLELlEAKKKRLLILGEPGSGKTTLLRYLALELAERY 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 250 LDCFQAL-FLFEFRQLNlitRFLTLSQLLFDLYLSPESDPDAVFQYLeKNADQVLLIFDGLDEALQPMGPDgpgSVLTLF 328
Cdd:COG5635 209 LDAEDPIpILIELRDLA---EEASLEDLLAEALEKRGGEPEDALERL-LRNGRLLLLLDGLDEVPDEADRD---EVLNQL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 329 SRLCRGtlLPGCRVMATSRPGKLPACLPAEAATVYMLGFDGPRVEEYVNHFFSAQPLQ-EGALAELQTNGRLRSLCAVPA 407
Cdd:COG5635 282 RRFLER--YPKARVIITSRPEGYDSSELEGFEVLELAPLSDEQIEEFLKKWFEATERKaERLLEALEENPELRELARNPL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 408 LCQVacLCLHHLLPDHAPGQSVALLptmtQLYMQMVLA-LSPRGHLPTTSLLD-------LGEVALRGLETGKVIFYAKD 479
Cdd:COG5635 360 LLTL--LALLLRERGELPDTRAELY----EQFVELLLErWDEQRGLTIYRELSreelrelLSELALAMQENGRTEFAREE 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622911992 480 ----IAPPLIAFGATHSLLTSFCVRTGP--GHQQTGYAFTHVSLQEFLAALHLMASPKVDKDTLTQHVTLHSRW 547
Cdd:COG5635 434 leeiLREYLGRRKDAEALLDELLLRTGLlvERGEGRYSFAHRSFQEYLAARALVEELDEELLELLAEHLEDPRW 507
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1442-1697 |
2.10e-23 |
|
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: 103.20 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1442 LAHCDLGTHHS-------LLVGQLMETCARLQQLSLSQVNLCEDNddssLLLQNLLLSLSELKTFRLTSSCVSTEGLAHL 1514
Cdd:cd00116 53 LKELCLSLNETgriprglQSLLQGLTKGCGLQELDLSDNALGPDG----CGVLESLLRSSSLQELKLNNNGLGDRGLRLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1515 ASGLGHC-HHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLGHLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDV 1593
Cdd:cd00116 129 AKGLKDLpPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1594 GCCHLSEALRAATSLEELDLSHNQIGDAGVQHLATILP-GLPELRKIDLSVNSISPAGGMQLAESLILCRHLEELMLGCN 1672
Cdd:cd00116 209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288
|
250 260 270
....*....|....*....|....*....|.
gi 1622911992 1673 ALGDPTA--LGLARELPQH----LRVLHLPF 1697
Cdd:cd00116 289 KFGEEGAqlLAESLLEPGNelesLWVKDDSF 319
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1440-1834 |
3.32e-17 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 86.14 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1440 LRLAHCDLGTHHSLLVGQLMETCARLQQLSLSQVNLCEDNDDSSLLLQNLLLSLSELKTFRLTSSCVSTEGLAHLASGLG 1519
Cdd:COG4886 14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1520 HCHHLEELDLSNNQfdeegtkalmrALEGKWMLKRLDlghllLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDvgcchLS 1599
Cdd:COG4886 94 DLTNLTELDLSGNE-----------ELSNLTNLESLD-----LSGNQLTDLPEELANLTNLKELDLSNNQLTD-----LP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1600 EALRAATSLEELDLSHNQIGDagvqhLATILPGLPELRKIDLSVNSISpaggmQLAESLILCRHLEELMLGCNALGDpta 1679
Cdd:COG4886 153 EPLGNLTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTD--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1680 lgLARELPQ--HLRVLHLPFSHlgpggaLSLTQALDGSPHLEEISLAENNLAGgvLHFCKELPLLRQIDLVSCKIDNQTI 1757
Cdd:COG4886 220 --LPEPLANltNLETLDLSNNQ------LTDLPELGNLTNLEELDLSNNQLTD--LPPLANLTNLKTLDLSNNQLTDLKL 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622911992 1758 KLLTSSFTRCPALEVILLSWNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLAQGSSIQVIRLWNN 1834
Cdd:COG4886 290 KELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLL 366
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1299-1676 |
6.64e-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: 85.61 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1299 PRVREASVNLGSEQSFRIHFSKEDQAGKTLRLSECSFRPEHVSRLATGLSQSLQLTELTLTQCCLDQEQLAILlslvgrp 1378
Cdd:COG5238 156 VHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEIL------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1379 aglfslrvqepwadragilsllevcaqasgsvteisisktqqqlcvqlefprqeenpeavalrlahcdlgthhsllvGQL 1458
Cdd:COG5238 229 -----------------------------------------------------------------------------AEA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1459 METCARLQQLSLSqvnlceDNddsslllqnlllslselktfrltssCVSTEGLAHLASGLGHCHHLEELDLSNNQFDEEG 1538
Cdd:COG5238 232 LKGNKSLTTLDLS------NN-------------------------QIGDEGVIALAEALKNNTTVETLYLSGNQIGAEG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1539 TKALMRALEGKWMLKRLDLGHLLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCCHLSEALRAATSLEELDLSHNQI 1618
Cdd:COG5238 281 AIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQI 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622911992 1619 GDAGVQHLATILPGLPELRKIDLSVNSISPAGGMQLAESLILCRhLEELMLGCNALGD 1676
Cdd:COG5238 361 GDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGA 417
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1581-1831 |
1.22e-16 |
|
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: 83.17 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1581 QSLRLKRNSIGDvgcCHLSEALRAATSLEELDLSHNQIGDAGVQHLATILPGLPE------------------------- 1635
Cdd:cd00116 1 LQLSLKGELLKT---ERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSlkelclslnetgriprglqsllqgl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1636 -----LRKIDLSVNSISPAgGMQLAESLILCRHLEELMLGCNALGDPTALGLAR---ELPQHLRVLHLPFSHLGPGGALS 1707
Cdd:cd00116 78 tkgcgLQELDLSDNALGPD-GCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKglkDLPPALEKLVLGRNRLEGASCEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1708 LTQALDGSPHLEEISLAENNLAG-GVLHFCKELP---LLRQIDLVSCKIDNQTIKLLTSSFTRCPALEVILLSWNLLGDE 1783
Cdd:cd00116 157 LAKALRANRDLKELNLANNGIGDaGIRALAEGLKancNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDA 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622911992 1784 AAAELAQVLPQMG-RLKRVDLEKNQITAFGAWLLAEGLAQGSSIQVIRL 1831
Cdd:cd00116 237 GAAALASALLSPNiSLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDL 285
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1516-1834 |
7.14e-16 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 82.29 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1516 SGLGHCHHLEELDLSNNQFDEegtkaLMRALEGKWMLKRLDlghllLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDvgc 1595
Cdd:COG4886 107 EELSNLTNLESLDLSGNQLTD-----LPEELANLTNLKELD-----LSNNQLTDLPEPLGNLTNLKSLDLSNNQLTD--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1596 chLSEALRAATSLEELDLSHNQIGDagvqhLATILPGLPELRKIDLSVNSISpaggmQLAESLILCRHLEELMLGCNALG 1675
Cdd:COG4886 174 --LPEELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1676 DPTALGlarELPQhLRVLHL---PFSHLGPGGALsltqaldgsPHLEEISLAENNLAGGVLHFCKELPLLR--QIDLVSC 1750
Cdd:COG4886 242 DLPELG---NLTN-LEELDLsnnQLTDLPPLANL---------TNLKTLDLSNNQLTDLKLKELELLLGLNslLLLLLLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1751 KIDNQTIKLLTSSFTRCPALEVILLSWNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLAQGSSIQVIR 1830
Cdd:COG4886 309 NLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLT 388
|
....
gi 1622911992 1831 LWNN 1834
Cdd:COG4886 389 LLLL 392
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1440-1630 |
1.58e-15 |
|
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: 79.71 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1440 LRLAHCDLG-THHSLLVGQLMETCARLQQLSLSQVNLcedNDDSSLLLQNLLLSLSELKTFRLTSSCVSTEGLAHLASGL 1518
Cdd:cd00116 113 LKLNNNGLGdRGLRLLAKGLKDLPPALEKLVLGRNRL---EGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1519 GHCHHLEELDLSNNQFDEEGTKALMRALEGKWMLKRLDLGH-LLLNSSALTLLTHGLSHMTRLQSLRLKRNSIGDVGCCH 1597
Cdd:cd00116 190 KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDnNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKD 269
|
170 180 190
....*....|....*....|....*....|...
gi 1622911992 1598 LSEALRAATSLEELDLSHNQIGDAGVQHLATIL 1630
Cdd:cd00116 270 LAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1580-1847 |
1.03e-14 |
|
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: 77.40 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1580 LQSLRLKRNSIGDVGCCHLSEALRAATSLEELDLSHNQIG--DAGVQHLATILPGLPELRKIDLSVNSISPAGgMQLAES 1657
Cdd:cd00116 25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTKGCGLQELDLSDNALGPDG-CGVLES 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1658 LILCRHLEELMLGCNALGDPTALGLARELPQHlrvlhlpfshlgpggalsltqaldgSPHLEEISLAENNLAGGvlhfck 1737
Cdd:cd00116 104 LLRSSSLQELKLNNNGLGDRGLRLLAKGLKDL-------------------------PPALEKLVLGRNRLEGA------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1738 elpllrqidlvSCKIdnqtiklLTSSFTRCPALEVILLSWNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITAFGAWLLA 1817
Cdd:cd00116 153 -----------SCEA-------LAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALA 214
|
250 260 270
....*....|....*....|....*....|
gi 1622911992 1818 EGLAQGSSIQVIRLWNNPIPCDMAQRLKSQ 1847
Cdd:cd00116 215 ETLASLKSLEVLNLGDNNLTDAGAAALASA 244
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
687-915 |
2.83e-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: 77.52 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 687 QIENLSFKSRKCGDAFAEALSRSLPTMGRLQMLGLAGSKITARGISHLVKALPLCPQLEEVSFRDNQLSDQVVLNIVEVL 766
Cdd:COG5238 181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 767 PHLPRLRKLDLSGNSVCVSTLLCLARVAVTCPTIRTLQARKADLIFllspptETTAELqrAPDLQESDGQRkgaqsrslT 846
Cdd:COG5238 261 KNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGD------EGAIAL--AEGLQGNKTLH--------T 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 847 LRLQKCQLQVHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDNGLSLAGV 915
Cdd:COG5238 325 LNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGA 393
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
839-1069 |
7.61e-14 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 75.98 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 839 GAQSRSLTLRLQKCQLQvHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDNGLSLAGVHCV 918
Cdd:COG5238 150 PLGGNAVHLLGLAARLG-LLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEIL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 919 LRAVSACWTLAELHISLRHKTvvfmfaqepeeqegPQERAAFLDSLmlqmpsELPLSSRRMRLTHCGLQAKHLEQLCKAL 998
Cdd:COG5238 229 AEALKGNKSLTTLDLSNNQIG--------------DEGVIALAEAL------KNNTTVETLYLSGNQIGAEGAIALAKAL 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622911992 999 GGSCHLGHLHLdfSGNALGDEGATRLAQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLDISF 1069
Cdd:COG5238 289 QGNTTLTSLDL--SVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSD 357
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
845-1202 |
1.20e-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: 71.23 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 845 LTLRLQKCQLQVHDAETLIALLQegpHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDN--GLSLAGVHCVLRAV 922
Cdd:cd00116 1 LQLSLKGELLKTERATELLPKLL---CLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNetGRIPRGLQSLLQGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 923 SACWTLAELHISlrhktvvfmfaqepeeqegpqeRAAFLDSLMLQMPSELPLSS-RRMRLTHCGLQAKHLEQLCKALGG- 1000
Cdd:cd00116 78 TKGCGLQELDLS----------------------DNALGPDGCGVLESLLRSSSlQELKLNNNGLGDRGLRLLAKGLKDl 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1001 SCHLGHLHLdfSGNALGDEGATRLAQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLdisfesqhillrgdk 1080
Cdd:cd00116 136 PPALEKLVL--GRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVL--------------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1081 tgrDIWATGSSPDfpaGAEFL--GFRRRCIPRSLRLSECPLEPPSLTHLC-ATLKECPGPLELQLSCEFLSDQSLETLLD 1157
Cdd:cd00116 199 ---DLNNNGLTDE---GASALaeTLASLKSLEVLNLGDNNLTDAGAAALAsALLSPNISLLTLSLSCNDITDDGAKDLAE 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622911992 1158 CLPRLPQLSLLQLNQTGLSPKSPFLLANTLsLCPRVKKVDLRSLH 1202
Cdd:cd00116 273 VLAEKESLLELDLRGNKFGEEGAQLLAESL-LEPGNELESLWVKD 316
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
715-1053 |
4.41e-12 |
|
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: 70.59 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 715 RLQMLGLAGSKITARGISHLVKALPLCPQLEEVSFRDNQLSDQVVLNIVEVLPHLPRLRKLDLSGNSVCVSTLLCLARVA 794
Cdd:COG5238 181 SVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEAL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 795 VTCPTIRTLqarkadlifllspptettaelqrapdlqesdgqrkgaqsrSLTLRlqkcQLQVHDAETLIALLQEGPHLEE 874
Cdd:COG5238 261 KNNTTVETL----------------------------------------YLSGN----QIGAEGAIALAKALQGNTTLTS 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 875 VDLSGNQLEDEGCRLMAEAASQLHIARKLDLSDNGLSLAGVHCVLRAVsacWTLAELHIslrhktvvfmfaqepeeqegp 954
Cdd:COG5238 297 LDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKAL---QENTTLHS--------------------- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 955 qeraafldslmlqmpselplssrrmrlthcglqakhleqlckalggschlghlhLDFSGNALGDEGATRLAQLLPGLGAL 1034
Cdd:COG5238 353 ------------------------------------------------------LDLSDNQIGDEGAIALAKYLEGNTTL 378
|
330
....*....|....*....
gi 1622911992 1035 QSLNLSENGLSLDAVLGLA 1053
Cdd:COG5238 379 RELNLGKNNIGKQGAEALI 397
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1009-1307 |
1.68e-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: 67.38 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1009 LDFSGNALGDEGATrlaQLLPGLGALQSLNLSENGLSLDAVLGLARCFSTLQWLFHLDISFEsqhillrgdKTGRDIWAT 1088
Cdd:cd00116 3 LSLKGELLKTERAT---ELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLN---------ETGRIPRGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1089 GSSPDF------------------PAGAEFL-GFRRRCIPRSLRLSECPLEPPSLTHLCATLKECPGPLE-LQLSCEFLS 1148
Cdd:cd00116 71 QSLLQGltkgcglqeldlsdnalgPDGCGVLeSLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEkLVLGRNRLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1149 DQSLETLLDCLPRLPQLSLLQLNQTGLSPKSPFLLANTLSLCPRVKKVDLRSlhhatlhfrsneeqegvccgrftgCSLS 1228
Cdd:cd00116 151 GASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNN------------------------NGLT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1229 QEHVESLCRLLSKCKDLSQVDLSANLLGDSGLRCLLECLPQVPIS-GSLDLSHNSVSQESALYLVETLPSCPRVREASVN 1307
Cdd:cd00116 207 DEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISlLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
764-1062 |
2.01e-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: 67.38 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 764 EVLPHLPRLRKLDLSGNSVCVSTLLCLARVavtcptirtLQARKADLIFLLSpptetTAELQRAPDLQESDGQRKGAQSR 843
Cdd:cd00116 17 ELLPKLLCLQVLRLEGNTLGEEAAKALASA---------LRPQPSLKELCLS-----LNETGRIPRGLQSLLQGLTKGCG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 844 SLTLRLQKCQLQVHDAETLIALLQeGPHLEEVDLSGNQLEDEGCRLMAEAASQL-HIARKLDLSDNGLSLAGVHCVLRAV 922
Cdd:cd00116 83 LQELDLSDNALGPDGCGVLESLLR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNRLEGASCEALAKAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 923 SACWTLAELHISLRHktvvfmfaqepeeqegpqERAAFLDSLMLQMPSELPLssRRMRLTHCGLQAKHLEQLCKALGGSC 1002
Cdd:cd00116 162 RANRDLKELNLANNG------------------IGDAGIRALAEGLKANCNL--EVLDLNNNGLTDEGASALAETLASLK 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622911992 1003 HLghLHLDFSGNALGDEGATRLA-QLLPGLGALQSLNLSENGLSLDAVLGLARC---FSTLQWL 1062
Cdd:cd00116 222 SL--EVLNLGDNNLTDAGAAALAsALLSPNISLLTLSLSCNDITDDGAKDLAEVlaeKESLLEL 283
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
599-893 |
1.07e-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: 65.07 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 599 LKKLATRKLTGPKVVELCHCVNETQEPELAsltaqslpYQLPFHNFP----LTCTDL---------------ATLTNILE 659
Cdd:cd00116 40 AKALASALRPQPSLKELCLSLNETGRIPRG--------LQSLLQGLTkgcgLQELDLsdnalgpdgcgvlesLLRSSSLQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 660 H------REAPIHLDFDGCPLePHCPEALvgcgqiENLSFKSRKCGDAFAEALSRSLPTMGRLQMLGLAGSKITARGISH 733
Cdd:cd00116 112 ElklnnnGLGDRGLRLLAKGL-KDLPPAL------EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 734 LVKALPLCPQLEEVSFRDNQLSDQVVLNIVEVLPHLPRLRKLDLSGNSVcvsTLLCLARVAvtcptirtlqarkadlifl 813
Cdd:cd00116 185 LAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL---TDAGAAALA------------------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 814 lspptettaelqrapdlqesDGQRKGAQSRsLTLRLQKCQLQVHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEA 893
Cdd:cd00116 243 --------------------SALLSPNISL-LTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAES 301
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
680-910 |
2.65e-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: 64.81 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 680 EALVGCGQIENLSFKSRKCGDAFAEALSRSLPTMGRLQMLGLAGSKITARGISHLVKALPLCPQLEEVSFRDNQLSDQVV 759
Cdd:COG5238 230 EALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 760 LNIVEVLPHLPRLRKLDLSGNSVCVSTLLCLArvavtcptirtlQARKADlifllsppteTTAElqrapdlqesdgqrkg 839
Cdd:COG5238 310 IALAEGLQGNKTLHTLNLAYNGIGAQGAIALA------------KALQEN----------TTLH---------------- 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622911992 840 aqsrslTLRLQKCQLQVHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAeAASQLHIARKLDLSDNGL 910
Cdd:COG5238 352 ------SLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALI-DALQTNRLHTLILDGNLI 415
|
|
| NLRC4_HD2 |
pfam17776 |
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
514-628 |
5.14e-10 |
|
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.
Pssm-ID: 465499 [Multi-domain] Cd Length: 122 Bit Score: 58.84 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 514 HVSLQEFLAALHLMASPKVDKDTLTqHVTLHSRWVQRTKARLDLS--------DHLPTFLAGLASCTCRPFLSHLaQGNE 585
Cdd:pfam17776 1 HLSFQEFFAALFYVLSFKEEKSNPL-KEFFGLRKRESLKSLLDKAlksknghlDLFLRFLFGLLNEENQRLLEGL-LGCK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622911992 586 DCVGTKQAaVVQVLKKLATRKLTGPKVVELCHCVNETQEPELA 628
Cdd:pfam17776 79 LSSEIKQE-LLQWIKSLIQKELSSERFLNLFHCLYELQDESFV 120
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1623-1836 |
9.00e-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: 63.27 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1623 VQHLATILPGLPELRKIDLSVNSiSPAGGMQLAESLILCRHLEELMLGCNALGDPTALGLARELPQHLRVLHLPF--SHL 1700
Cdd:COG5238 87 TQLLVVDWEGAEEVSPVALAETA-TAVATPPPDLRRIMAKTLEDSLILYLALPRRINLIQVLKDPLGGNAVHLLGlaARL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1701 GPGGALSLTQALDGSpHLEEISLAENNLA-GGVLHFCKELPL---LRQIDLVSCKIDNQTIKLLTSSFTRCPALEVILLS 1776
Cdd:COG5238 166 GLLAAISMAKALQNN-SVETVYLGCNQIGdEGIEELAEALTQnttVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLS 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1777 WNLLGDEAAAELAQVLPQMGRLKRVDLEKNQITAFGAWLLAEGLAQGSSIQVIRLWNNPI 1836
Cdd:COG5238 245 NNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRI 304
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
690-1042 |
7.04e-09 |
|
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: 59.68 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 690 NLSFKSRKCGDAFAEALSRSLPTMgrlQMLGLAGSKITARGISHLVKALPLCPQLEEVSFRDNQL--SDQVVLNIVEVLP 767
Cdd:cd00116 2 QLSLKGELLKTERATELLPKLLCL---QVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETgrIPRGLQSLLQGLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 768 HLPRLRKLDLSGNSVCvstllclarvAVTCPTI-RTLQARKADLIFLLSPPTETTAE-------LQRAPDLQESDGQRKG 839
Cdd:cd00116 79 KGCGLQELDLSDNALG----------PDGCGVLeSLLRSSSLQELKLNNNGLGDRGLrllakglKDLPPALEKLVLGRNR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 840 AQSRSL--------------TLRLQKCQLQVHDAETLIALLQEGPHLEEVDLSGNQLEDEGCRLMAEAASQLHIARKLDL 905
Cdd:cd00116 149 LEGASCealakalranrdlkELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 906 SDNGLSLAGvhcvlravsacwtLAELHISLRHKtvvfmfaqepeeqegpqeraafLDSLmlqmpselplssRRMRLTHCG 985
Cdd:cd00116 229 GDNNLTDAG-------------AAALASALLSP----------------------NISL------------LTLSLSCND 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622911992 986 LQAKHLEQLCKALGGSCHLghLHLDFSGNALGDEGATRLAQLLPGLGA-LQSLNLSEN 1042
Cdd:cd00116 262 ITDDGAKDLAEVLAEKESL--LELDLRGNKFGEEGAQLLAESLLEPGNeLESLWVKDD 317
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1517-1667 |
2.10e-06 |
|
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.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 50.55 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1517 GLGHCHHLEELDLSNNQFDE-EGtkalmraLEGKWMLK-------RLDLGHLLLnSSALTLLTHGLShmtrLQSLRLKRN 1588
Cdd:cd21340 63 NLENLVNLKKLYLGGNRISVvEG-------LENLTNLEelhienqRLPPGEKLT-FDPRSLAALSNS----LRVLNISGN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1589 SIGDVgcchlsEALRAATSLEELDLSHNQIGDagVQHLATILPGLPELRKIDLSVNSISpaGGMQLAESLIL-CRHLEEL 1667
Cdd:cd21340 131 NIDSL------EPLAPLRNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPVC--KKPKYRDKIILaSKSLEVL 200
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
986-1296 |
2.10e-06 |
|
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: 52.48 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 986 LQAKHLEQLCKALGGSCHLGHLHLdfSGNALGDEGATRLAQLLPGLGALQSLNLSENGLSLDAVLGLARcfstlqwlfhl 1065
Cdd:COG5238 192 IGDEGIEELAEALTQNTTVTTLWL--KRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAE----------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1066 diSFESQHILLRGDKTGRDIWATgsspdfpaGAEFLGfrrrciprslrlsecpleppslthlcATLKECPGPLELQLSCE 1145
Cdd:COG5238 259 --ALKNNTTVETLYLSGNQIGAE--------GAIALA--------------------------KALQGNTTLTSLDLSVN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1146 FLSDQSLETLLDCLPRLPQLSLLQLNQTGLSPKSPFLLANTLSLCPRVKKVDLrslhhatlhfrsneeqegvccgrfTGC 1225
Cdd:COG5238 303 RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDL------------------------SDN 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622911992 1226 SLSQEHVESLCRLLSKCKDLSQVDLSANLLGDSGLRCLLECLpQVPISGSLDLSHNSVSQESALYLVETLP 1296
Cdd:COG5238 359 QIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL-QTNRLHTLILDGNLIGAEAQQRLEQLLE 428
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
1511-1742 |
2.44e-06 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 52.24 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1511 LAHLASGLGHCHHLEELDLSNNQFdeegtKALMRALEGKWMLKRLDLGHlllnsSALTLLThGLSHMTRLQSLRLKRNSI 1590
Cdd:COG4886 194 ITDLPEPLGNLTNLEELDLSGNQL-----TDLPEPLANLTNLETLDLSN-----NQLTDLP-ELGNLTNLEELDLSNNQL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1591 GDVGcchlseALRAATSLEELDLSHNQIGDAGVQHLATILPGLPELRKIDLSVNSISPAGGMQLAESLILCRHLEELMLG 1670
Cdd:COG4886 263 TDLP------PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVT 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622911992 1671 CNALGDPTALGLARELPQHLRVLHLPFSHLGPGGALSLTQALDGSPHLEEISLAENNLAGGVLHFCKELPLL 1742
Cdd:COG4886 337 LTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALL 408
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1140-1295 |
1.79e-05 |
|
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: 49.40 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1140 LQLSCEFLSDQSLETLLDCLPRLPQLSLLQLNQTGLSPKSPFLLANTLSLCPRVKKVDL-------RSLHHATLHFRSNE 1212
Cdd:COG5238 185 VYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLsnnqigdEGVIALAEALKNNT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1213 EQEGVccgRFTGCSLSQEHVESLCRLLSKCKDLSQVDLSANLLGDSGLRCLLECLPQVPISGSLDLSHNSVSQESALYLV 1292
Cdd:COG5238 265 TVETL---YLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALA 341
|
...
gi 1622911992 1293 ETL 1295
Cdd:COG5238 342 KAL 344
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
704-911 |
1.93e-05 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 49.16 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 704 EALSRSLPTMGRLQMLGLAGSKITargisHLVKALPLCPQLEEVSFRDNQLSDqvvlnIVEVLPHLPRLRKLDLSGNSvc 783
Cdd:COG4886 126 TDLPEELANLTNLKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQ-- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 784 VSTL-LCLARvavtCPTIRTLQARKADLifllsppTETTAELQRAPDLQesdgqrkgaqsrslTLRLQKCQLqvhdaeTL 862
Cdd:COG4886 194 ITDLpEPLGN----LTNLEELDLSGNQL-------TDLPEPLANLTNLE--------------TLDLSNNQL------TD 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622911992 863 IALLQEGPHLEEVDLSGNQLEDegcrlmAEAASQLHIARKLDLSDNGLS 911
Cdd:COG4886 243 LPELGNLTNLEELDLSNNQLTD------LPPLANLTNLKTLDLSNNQLT 285
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
716-911 |
7.36e-05 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 47.24 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 716 LQMLGLAGSKITargisHLVKALPLCPQLEEVSFRDNQLSDqvvlnIVEVLPHLPRLRKLDLSGNSvcvstLLCLARVAV 795
Cdd:COG4886 115 LESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQ-----LTDLPEELG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 796 TCPTIRTLQARKADLifllsppTETTAELQRAPDLQEsdgqrkgaqsrsltLRLQKCQLqvhdaETLIALLQEGPHLEEV 875
Cdd:COG4886 180 NLTNLKELDLSNNQI-------TDLPEPLGNLTNLEE--------------LDLSGNQL-----TDLPEPLANLTNLETL 233
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622911992 876 DLSGNQLEDegcrlmAEAASQLHIARKLDLSDNGLS 911
Cdd:COG4886 234 DLSNNQLTD------LPELGNLTNLEELDLSNNQLT 263
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
705-783 |
1.64e-04 |
|
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.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 45.16 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 705 ALSRSLptmgrlQMLGLAGSKITA-RGISHLVkalplcpQLEEVSFRDNQLSDqvVLNIVEVLPHLPRLRKLDLSGNSVC 783
Cdd:cd21340 117 ALSNSL------RVLNISGNNIDSlEPLAPLR-------NLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPVC 181
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
1110-1312 |
2.88e-04 |
|
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: 45.55 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1110 RSLRLSECPLEPPSLTHLCATLKECPGPLELQLSCEFLSDQSLETLLDCLPRLPQLSLLQLNQTGLSPKSPFLLANTLSL 1189
Cdd:COG5238 211 TTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1190 CPRVKKVDLRSLHhatlhfrsneeqegvccgrftgcsLSQEHVESLCRLLSKCKDLSQVDLSANLLGDSGLRCLLECLPQ 1269
Cdd:COG5238 291 NTTLTSLDLSVNR------------------------IGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQE 346
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622911992 1270 VPISGSLDLSHNSVSQESALYLVETLPSCPRVREasVNLGSEQ 1312
Cdd:COG5238 347 NTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRE--LNLGKNN 387
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
649-780 |
3.69e-04 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 44.92 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 649 TDLATLTNiLEHreapihLDFDGCPLEpHCPEALVGCGQIENLSFKSRKCGDafaeaLSRSLPTMGRLQMLGLAGSKITA 728
Cdd:COG4886 153 EPLGNLTN-LKS------LDLSNNQLT-DLPEELGNLTNLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTD 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622911992 729 rgishLVKALPLCPQLEEVSFRDNQLSDqvvlniVEVLPHLPRLRKLDLSGN 780
Cdd:COG4886 220 -----LPEPLANLTNLETLDLSNNQLTD------LPELGNLTNLEELDLSNN 260
|
|
| LRR_6 |
pfam13516 |
Leucine Rich repeat; |
1606-1627 |
7.19e-04 |
|
Leucine Rich repeat;
Pssm-ID: 463907 [Multi-domain] Cd Length: 24 Bit Score: 38.37 E-value: 7.19e-04
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1552-1810 |
1.06e-03 |
|
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.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 42.47 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1552 LKRLDlgHLLLNSSALTLLtHGLSHMTRLQSLRLKRNSIGDVgcchlsEALRAATSLEELDLSHNQIgdagvqhlATI-- 1629
Cdd:cd21340 1 LKRIT--HLYLNDKNITKI-DNLSLCKNLKVLYLYDNKITKI------ENLEFLTNLTHLYLQNNQI--------EKIen 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1630 LPGLPELRKIDLSVNSISpaggmqLAESLILCRHLEELMLGCNALGDPTALglarelpqhlrvlhlpfsHLGPGGALSLt 1709
Cdd:cd21340 64 LENLVNLKKLYLGGNRIS------VVEGLENLTNLEELHIENQRLPPGEKL------------------TFDPRSLAAL- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1710 qaldgSPHLEEISLAENNLAggvlhfckelpllrqiDLvsckidnQTIKLLTSsftrcpaLEVILLSWNLLGDeaAAELA 1789
Cdd:cd21340 119 -----SNSLRVLNISGNNID----------------SL-------EPLAPLRN-------LEQLDASNNQISD--LEELL 161
|
250 260
....*....|....*....|.
gi 1622911992 1790 QVLPQMGRLKRVDLEKNQITA 1810
Cdd:cd21340 162 DLLSSWPSLRELDLTGNPVCK 182
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
1518-1695 |
1.32e-03 |
|
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.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 42.08 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1518 LGHCHHLEELDLSNNQfdeegtkalmralegkwmLKRLDlghlllNSSALTLLTH------------GLSHMTRLQSLRL 1585
Cdd:cd21340 20 LSLCKNLKVLYLYDNK------------------ITKIE------NLEFLTNLTHlylqnnqiekieNLENLVNLKKLYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1586 KRNSIGDVgcchlsEALRAATSLEELDLSHNQIgDAGVQHL---ATILPGLPELRKIDLSVNSISpaggmQLAEsLILCR 1662
Cdd:cd21340 76 GGNRISVV------EGLENLTNLEELHIENQRL-PPGEKLTfdpRSLAALSNSLRVLNISGNNID-----SLEP-LAPLR 142
|
170 180 190
....*....|....*....|....*....|....
gi 1622911992 1663 HLEELMLGCNALGDPTAL-GLARELPQhLRVLHL 1695
Cdd:cd21340 143 NLEQLDASNNQISDLEELlDLLSSWPS-LRELDL 175
|
|
| PLN00113 |
PLN00113 |
leucine-rich repeat receptor-like protein kinase; Provisional |
1518-1674 |
1.98e-03 |
|
leucine-rich repeat receptor-like protein kinase; Provisional
Pssm-ID: 215061 [Multi-domain] Cd Length: 968 Bit Score: 43.30 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1518 LGHCHHLEELDLSNNQFDEEGTKALMRalegkwmlkrLDLGHLL-LNSSALT-LLTHGLSHMTRLQSLRLKRNSIGDvgc 1595
Cdd:PLN00113 400 LGACRSLRRVRLQDNSFSGELPSEFTK----------LPLVYFLdISNNNLQgRINSRKWDMPSLQMLSLARNKFFG--- 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622911992 1596 cHLSEALRAaTSLEELDLSHNQIGDAGVQHLATilpgLPELRKIDLSVNSISPaggmQLAESLILCRHLEELMLGCNAL 1674
Cdd:PLN00113 467 -GLPDSFGS-KRLENLDLSRNQFSGAVPRKLGS----LSELMQLKLSENKLSG----EIPDELSSCKKLVSLDLSHNQL 535
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
1139-1373 |
2.32e-03 |
|
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: 42.34 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1139 ELQLSCEFLSDQSLETLLDCLPRLPQLSLL--QLNQTGLSPKSPFLLANTLSLCPRVKKVDLRSlhhatlhfrsneeqeg 1216
Cdd:cd00116 27 VLRLEGNTLGEEAAKALASALRPQPSLKELclSLNETGRIPRGLQSLLQGLTKGCGLQELDLSD---------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1217 vccgrftgCSLSQEHVESLCRLLSKcKDLSQVDLSANLLGDSGLRCLLECLPQVPIS-GSLDLSHNSVSQESALYLVETL 1295
Cdd:cd00116 91 --------NALGPDGCGVLESLLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDLPPAlEKLVLGRNRLEGASCEALAKAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622911992 1296 PSCPRVreasvnlgseqsfrihfskedqagKTLRLSECSFRPEHVSRLATGLSQSLQLTELTLTQCCLDQE---QLAILL 1372
Cdd:cd00116 162 RANRDL------------------------KELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEgasALAETL 217
|
.
gi 1622911992 1373 S 1373
Cdd:cd00116 218 A 218
|
|
| LRR_RI |
smart00368 |
Leucine rich repeat, ribonuclease inhibitor type; |
1606-1627 |
6.51e-03 |
|
Leucine rich repeat, ribonuclease inhibitor type;
Pssm-ID: 197686 [Multi-domain] Cd Length: 28 Bit Score: 35.85 E-value: 6.51e-03
|
| |
