NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1017349095|ref|NP_001309450|]
View 

CARMIL pleckstrin homology domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Carm_PH super family cl39358
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 31-128 5.18e-19

Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.


The actual alignment was detected with superfamily member pfam17888:

Pssm-ID: 436119  Cd Length: 94  Bit Score: 82.72  E-value: 5.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095   31 RIVVQVDVAHKADKYEPRIFIISKFRIFFLMGKTTSslKIEKSFHVLAIKAIHVISEEELVIHLDDGVHKKKINikcSIH 110
Cdd:pfam17888    2 KLVKSVKLETKGDKVEDRILVLTPWRLFLLSAKVPT--KVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLA---SEE 76

                           90
                   ....*....|....*...
gi 1017349095  111 PAVHLARQLLSAVKHYFP 128
Cdd:pfam17888   77 DVDHVVGHILTALKKIFP 94
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 415-637 4.08e-15

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: 79.06  E-value: 4.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  415 EGVQTAKEYFSMAVNLSHISFNNTSmpSEYLKAVLLGLASNQQLQPFRLDLDATCEKGSASVLDACIGGIRCETLSLRDN 494
Cdd:COG5238    169 AAISMAKALQNNSVETVYLGCNQIG--DEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNN 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  495 NL-DGELQGVLQSLMMVTCLRRLDIGGSN--------MNQLKKNNKQVHVINkvlLDVVKLySEEG------------CL 553
Cdd:COG5238    247 QIgDEGVIALAEALKNNTTVETLYLSGNQigaegaiaLAKALQGNTTLTSLD---LSVNRI-GDEGaialaeglqgnkTL 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  554 EELNLSDCRLGAYLSV-LINTLAATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLATSIKM 632
Cdd:COG5238    323 HTLNLAYNGIGAQGAIaLAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQT 402


                   ....*..
gi 1017349095  633 N--HTLT 637
Cdd:COG5238    403 NrlHTLI 409
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
246-466 3.35e-08

Leucine-rich repeat (LRR) protein [Transcription];


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  246 IRKSQNLKKLQLRSCSlpkdfITLLASAFHNNQNacLEYLDLSRNPIDDkkgftiLSSVLPRLNQLKYVNFSECQLSDks 325
Cdd:COG4886    109 LSNLTNLESLDLSGNQ-----LTDLPEELANLTN--LKELDLSNNQLTD------LPEPLGNLTNLKSLDLSNNQLTD-- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  326 inllctgLYNGMTSCKsggmQLTELILSANPMKD---DISGIINLVSIS----------------TSLRVLDFSDTGI-H 385
Cdd:COG4886    174 -------LPEELGNLT----NLKELDLSNNQITDlpePLGNLTNLEELDlsgnqltdlpeplanlTNLETLDLSNNQLtD 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  386 LDKLWNsLKfgglQIEKLILNGCSLSKKSEGVQTAkeyfsmavNLSHISFNNTSMPSEYLKAVLLGLASNQQLQPFRLDL 465
Cdd:COG4886    243 LPELGN-LT----NLEELDLSNNQLTDLPPLANLT--------NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309


                   .
gi 1017349095  466 D 466
Cdd:COG4886    310 L 310
 
Name Accession Description Interval E-value
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 31-128 5.18e-19

Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.


Pssm-ID: 436119  Cd Length: 94  Bit Score: 82.72  E-value: 5.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095   31 RIVVQVDVAHKADKYEPRIFIISKFRIFFLMGKTTSslKIEKSFHVLAIKAIHVISEEELVIHLDDGVHKKKINikcSIH 110
Cdd:pfam17888    2 KLVKSVKLETKGDKVEDRILVLTPWRLFLLSAKVPT--KVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLA---SEE 76

                           90
                   ....*....|....*...
gi 1017349095  111 PAVHLARQLLSAVKHYFP 128
Cdd:pfam17888   77 DVDHVVGHILTALKKIFP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 415-637 4.08e-15

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 79.06  E-value: 4.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  415 EGVQTAKEYFSMAVNLSHISFNNTSmpSEYLKAVLLGLASNQQLQPFRLDLDATCEKGSASVLDACIGGIRCETLSLRDN 494
Cdd:COG5238    169 AAISMAKALQNNSVETVYLGCNQIG--DEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNN 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  495 NL-DGELQGVLQSLMMVTCLRRLDIGGSN--------MNQLKKNNKQVHVINkvlLDVVKLySEEG------------CL 553
Cdd:COG5238    247 QIgDEGVIALAEALKNNTTVETLYLSGNQigaegaiaLAKALQGNTTLTSLD---LSVNRI-GDEGaialaeglqgnkTL 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  554 EELNLSDCRLGAYLSV-LINTLAATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLATSIKM 632
Cdd:COG5238    323 HTLNLAYNGIGAQGAIaLAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQT 402


                   ....*..
gi 1017349095  633 N--HTLT 637
Cdd:COG5238    403 NrlHTLI 409
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 281-606 1.24e-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: 63.91  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  281 CLEYLDLSRNPIDDKKGfTILSSVLPRLNQLKYVNFS--ECQLSDKSINLLCTGLYNGMtscksggmQLTELILSANPMK 358
Cdd:cd00116     24 CLQVLRLEGNTLGEEAA-KALASALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGC--------GLQELDLSDNALG 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  359 DDISGIINLVSISTSLRVLDFSDTGI---HLDKLWNSLKFGGLQIEKLILNGCSLSkkSEGVQTAKEYFSMAVNLSHISF 435
Cdd:cd00116     95 PDGCGVLESLLRSSSLQELKLNNNGLgdrGLRLLAKGLKDLPPALEKLVLGRNRLE--GASCEALAKALRANRDLKELNL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  436 NNTSMPSEYLKAVLLGLASNQQLQPFRLDLDATCEKGsASVLDACIGGIRC-ETLSLRDNNLDGElqgvlqslmmvtCLR 514
Cdd:cd00116    173 ANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEG-ASALAETLASLKSlEVLNLGDNNLTDA------------GAA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  515 RLDiggsnmNQLKKNNKqvhvinkvlldvvklyseegCLEELNLSDCRLGAYLSV-LINTLAATTTLKSLDISGNEMGNF 593
Cdd:cd00116    240 ALA------SALLSPNI--------------------SLLTLSLSCNDITDDGAKdLAEVLAEKESLLELDLRGNKFGEE 293

                          330
                   ....*....|...
gi 1017349095  594 GARILSKALQVNV 606
Cdd:cd00116    294 GAQLLAESLLEPG 306
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
246-466 3.35e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  246 IRKSQNLKKLQLRSCSlpkdfITLLASAFHNNQNacLEYLDLSRNPIDDkkgftiLSSVLPRLNQLKYVNFSECQLSDks 325
Cdd:COG4886    109 LSNLTNLESLDLSGNQ-----LTDLPEELANLTN--LKELDLSNNQLTD------LPEPLGNLTNLKSLDLSNNQLTD-- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  326 inllctgLYNGMTSCKsggmQLTELILSANPMKD---DISGIINLVSIS----------------TSLRVLDFSDTGI-H 385
Cdd:COG4886    174 -------LPEELGNLT----NLKELDLSNNQITDlpePLGNLTNLEELDlsgnqltdlpeplanlTNLETLDLSNNQLtD 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  386 LDKLWNsLKfgglQIEKLILNGCSLSKKSEGVQTAkeyfsmavNLSHISFNNTSMPSEYLKAVLLGLASNQQLQPFRLDL 465
Cdd:COG4886    243 LPELGN-LT----NLEELDLSNNQLTDLPPLANLT--------NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309


                   .
gi 1017349095  466 D 466
Cdd:COG4886    310 L 310
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 227-360 3.87e-06

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 50.05  E-value: 3.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  227 LICDAVRVSSEVIDVVLSVIRKSQNLKKLQLRSCSLPKDFITLLASAFHNNQNacLEYLDLSRNPIDDkKGFTILSSVLP 306
Cdd:cd00116    142 LVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTD-EGASALAETLA 218

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1017349095  307 RLNQLKYVNFSECQLSDKSINLLCTGLyngmtscKSGGMQLTELILSANPMKDD 360
Cdd:cd00116    219 SLKSLEVLNLGDNNLTDAGAAALASAL-------LSPNISLLTLSLSCNDITDD 265
 
Name Accession Description Interval E-value
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 31-128 5.18e-19

Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.


Pssm-ID: 436119  Cd Length: 94  Bit Score: 82.72  E-value: 5.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095   31 RIVVQVDVAHKADKYEPRIFIISKFRIFFLMGKTTSslKIEKSFHVLAIKAIHVISEEELVIHLDDGVHKKKINikcSIH 110
Cdd:pfam17888    2 KLVKSVKLETKGDKVEDRILVLTPWRLFLLSAKVPT--KVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLA---SEE 76

                           90
                   ....*....|....*...
gi 1017349095  111 PAVHLARQLLSAVKHYFP 128
Cdd:pfam17888   77 DVDHVVGHILTALKKIFP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 415-637 4.08e-15

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 79.06  E-value: 4.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  415 EGVQTAKEYFSMAVNLSHISFNNTSmpSEYLKAVLLGLASNQQLQPFRLDLDATCEKGSASVLDACIGGIRCETLSLRDN 494
Cdd:COG5238    169 AAISMAKALQNNSVETVYLGCNQIG--DEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNN 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  495 NL-DGELQGVLQSLMMVTCLRRLDIGGSN--------MNQLKKNNKQVHVINkvlLDVVKLySEEG------------CL 553
Cdd:COG5238    247 QIgDEGVIALAEALKNNTTVETLYLSGNQigaegaiaLAKALQGNTTLTSLD---LSVNRI-GDEGaialaeglqgnkTL 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  554 EELNLSDCRLGAYLSV-LINTLAATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLATSIKM 632
Cdd:COG5238    323 HTLNLAYNGIGAQGAIaLAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQT 402


                   ....*..
gi 1017349095  633 N--HTLT 637
Cdd:COG5238    403 NrlHTLI 409
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 553-638 6.27e-14

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 75.21  E-value: 6.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  553 LEELNLSDCRLGAY-LSVLINTLAATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLATSIK 631
Cdd:COG5238    182 VETVYLGCNQIGDEgIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALK 261


                   ....*..
gi 1017349095  632 MNHTLTH 638
Cdd:COG5238    262 NNTTVET 268
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 281-606 1.24e-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: 63.91  E-value: 1.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  281 CLEYLDLSRNPIDDKKGfTILSSVLPRLNQLKYVNFS--ECQLSDKSINLLCTGLYNGMtscksggmQLTELILSANPMK 358
Cdd:cd00116     24 CLQVLRLEGNTLGEEAA-KALASALRPQPSLKELCLSlnETGRIPRGLQSLLQGLTKGC--------GLQELDLSDNALG 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  359 DDISGIINLVSISTSLRVLDFSDTGI---HLDKLWNSLKFGGLQIEKLILNGCSLSkkSEGVQTAKEYFSMAVNLSHISF 435
Cdd:cd00116     95 PDGCGVLESLLRSSSLQELKLNNNGLgdrGLRLLAKGLKDLPPALEKLVLGRNRLE--GASCEALAKALRANRDLKELNL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  436 NNTSMPSEYLKAVLLGLASNQQLQPFRLDLDATCEKGsASVLDACIGGIRC-ETLSLRDNNLDGElqgvlqslmmvtCLR 514
Cdd:cd00116    173 ANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEG-ASALAETLASLKSlEVLNLGDNNLTDA------------GAA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  515 RLDiggsnmNQLKKNNKqvhvinkvlldvvklyseegCLEELNLSDCRLGAYLSV-LINTLAATTTLKSLDISGNEMGNF 593
Cdd:cd00116    240 ALA------SALLSPNI--------------------SLLTLSLSCNDITDDGAKdLAEVLAEKESLLELDLRGNKFGEE 293

                          330
                   ....*....|...
gi 1017349095  594 GARILSKALQVNV 606
Cdd:cd00116    294 GAQLLAESLLEPG 306
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 398-637 1.83e-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: 63.53  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  398 LQIEKLILNGCSLSKKS-EGVQTAKEYFSMAVNLsHISFNNTSMPSEYLKAVLLGLASNQQLQPFRLDLDATCEKGSAsV 476
Cdd:cd00116     23 LCLQVLRLEGNTLGEEAaKALASALRPQPSLKEL-CLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCG-V 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  477 LDACIGGIRCETLSLRDNNLDGE----LQGVLQSLMMVtcLRRLDIGGSNMNQ---------LKKNN--KQVHVIN---- 537
Cdd:cd00116    101 LESLLRSSSLQELKLNNNGLGDRglrlLAKGLKDLPPA--LEKLVLGRNRLEGascealakaLRANRdlKELNLANngig 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  538 ----KVLLDVVKLYSEegcLEELNLSDC---RLGAylSVLINTLAATTTLKSLDISGNEMGNFGARILSKAL-QVNVSLR 609
Cdd:cd00116    179 dagiRALAEGLKANCN---LEVLDLNNNgltDEGA--SALAETLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLL 253

                          250       260
                   ....*....|....*....|....*...
gi 1017349095  610 SVSIDNNHIGADGFVDLATSIKMNHTLT 637
Cdd:cd00116    254 TLSLSCNDITDDGAKDLAEVLAEKESLL 281
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 470-638 2.36e-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: 60.06  E-value: 2.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  470 EKGSASVLDACIGGIRCETLSLRDNNLDGELQGVLQSLMMVTCLRRLDiggsnmnqlKKNNKQVHVINKVLLDVVKLYSE 549
Cdd:cd00116     67 PRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELK---------LNNNGLGDRGLRLLAKGLKDLPP 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  550 EgcLEELNLSDCRLGAYLSV-LINTLAATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLAT 628
Cdd:cd00116    138 A--LEKLVLGRNRLEGASCEaLAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAE 215

                          170
                   ....*....|
gi 1017349095  629 SIKMNHTLTH 638
Cdd:cd00116    216 TLASLKSLEV 225
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
246-466 3.35e-08

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 57.25  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  246 IRKSQNLKKLQLRSCSlpkdfITLLASAFHNNQNacLEYLDLSRNPIDDkkgftiLSSVLPRLNQLKYVNFSECQLSDks 325
Cdd:COG4886    109 LSNLTNLESLDLSGNQ-----LTDLPEELANLTN--LKELDLSNNQLTD------LPEPLGNLTNLKSLDLSNNQLTD-- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  326 inllctgLYNGMTSCKsggmQLTELILSANPMKD---DISGIINLVSIS----------------TSLRVLDFSDTGI-H 385
Cdd:COG4886    174 -------LPEELGNLT----NLKELDLSNNQITDlpePLGNLTNLEELDlsgnqltdlpeplanlTNLETLDLSNNQLtD 242

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  386 LDKLWNsLKfgglQIEKLILNGCSLSKKSEGVQTAkeyfsmavNLSHISFNNTSMPSEYLKAVLLGLASNQQLQPFRLDL 465
Cdd:COG4886    243 LPELGN-LT----NLEELDLSNNQLTDLPPLANLT--------NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309


                   .
gi 1017349095  466 D 466
Cdd:COG4886    310 L 310
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 576-638 2.60e-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: 51.33  E-value: 2.60e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1017349095  576 ATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLATSIKMNHTLTH 638
Cdd:COG5238    178 QNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTT 240
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 227-360 3.87e-06

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 50.05  E-value: 3.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  227 LICDAVRVSSEVIDVVLSVIRKSQNLKKLQLRSCSLPKDFITLLASAFHNNQNacLEYLDLSRNPIDDkKGFTILSSVLP 306
Cdd:cd00116    142 LVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCN--LEVLDLNNNGLTD-EGASALAETLA 218

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1017349095  307 RLNQLKYVNFSECQLSDKSINLLCTGLyngmtscKSGGMQLTELILSANPMKDD 360
Cdd:cd00116    219 SLKSLEVLNLGDNNLTDAGAAALASAL-------LSPNISLLTLSLSCNDITDD 265
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 249-360 9.89e-06

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 48.89  E-value: 9.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  249 SQNLKKLQLRSCSLPKDFITLLASAFhnNQNACLEYLDLSRNPIDDKKGFTILSSVLPRLNQLKYVNFSECQLSDKSINL 328
Cdd:cd00116    192 NCNLEVLDLNNNGLTDEGASALAETL--ASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKD 269

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1017349095  329 LCTGLYNGMTscksggmqLTELILSANPMKDD 360
Cdd:cd00116    270 LAEVLAEKES--------LLELDLRGNKFGEE 293
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 242-507 1.27e-05

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: 48.51  E-value: 1.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  242 VLSVIRKSQNLKKLQLRSCSLPKDFITLLASAFHNNQ----------------------------NACLEYLDLSRNPID 293
Cdd:cd00116     15 ATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPslkelclslnetgriprglqsllqgltkGCGLQELDLSDNALG 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  294 DkKGFTILSSVLpRLNQLKYVNFSECQLSDKSINLLCTGLynGMTSCKSGGMQLTELILSANPMKDdisgIINLVSISTS 373
Cdd:cd00116     95 P-DGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGL--KDLPPALEKLVLGRNRLEGASCEA----LAKALRANRD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  374 LRVLDFSDTGIH---LDKLWNSLK-FGGLQIEKLILNGCSlskkSEGVQTAKEYFSMAVNLSHISFNNTSMPSEYLKAVL 449
Cdd:cd00116    167 LKELNLANNGIGdagIRALAEGLKaNCNLEVLDLNNNGLT----DEGASALAETLASLKSLEVLNLGDNNLTDAGAAALA 242

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1017349095  450 LGLAS-NQQLQpfRLDLDAT--CEKGSASVLDACIGGIRCETLSLRDNNLDGELQGVLQSL 507
Cdd:cd00116    243 SALLSpNISLL--TLSLSCNdiTDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAES 301
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 218-423 4.89e-05

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: 46.58  E-value: 4.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  218 LQYSAYFTGLICDAVRVssevidvVLSVIRKSQNLKKLQLRSCSLPKDFITLLASAFhnnQNACLEYLDLSRNPIDDKKG 297
Cdd:cd00116     56 LCLSLNETGRIPRGLQS-------LLQGLTKGCGLQELDLSDNALGPDGCGVLESLL---RSSSLQELKLNNNGLGDRGL 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  298 FTI----------------------------LSSVLPRLNQLKYVNFSECQLSDKSINLLCTGLyngMTSCksggmQLTE 349
Cdd:cd00116    126 RLLakglkdlppaleklvlgrnrlegasceaLAKALRANRDLKELNLANNGIGDAGIRALAEGL---KANC-----NLEV 197

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1017349095  350 LILSANPMKDD-ISGIINLVSISTSLRVLDFSDTGIH---LDKLWNSLKFGGLQIEKLILNGCSLskKSEGVQTAKEY 423
Cdd:cd00116    198 LDLNNNGLTDEgASALAETLASLKSLEVLNLGDNNLTdagAAALASALLSPNISLLTLSLSCNDI--TDDGAKDLAEV 273
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
487-618 1.02e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.08  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  487 ETLSLRDNNLDgELQGVLQSLmmvTCLRRLDIGGsnmNQLKKnnkqvhvINKVLLDVVKLyseegclEELNLSDCRLgay 566
Cdd:COG4886    139 KELDLSNNQLT-DLPEPLGNL---TNLKSLDLSN---NQLTD-------LPEELGNLTNL-------KELDLSNNQI--- 194

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1017349095  567 lSVLINTLAATTTLKSLDISGNEMGNfgariLSKALQVNVSLRSVSIDNNHI 618
Cdd:COG4886    195 -TDLPEPLGNLTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQL 240
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
251-629 3.37e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  251 NLKKLQLRSCSLPKDFITLLASAFHNNQNACLEYLDLSRNPIDDKKGFTILSSVLPRLNQLKYVNFSECQLSDKSINLLC 330
Cdd:COG4886      2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  331 TGLYNGMTSCKSGGMQLTELILSANPmkddisGIINLvsisTSLRVLDFSDTGI-HLDKLWNSLKfgglQIEKLILNGCS 409
Cdd:COG4886     82 LSLLLLGLTDLGDLTNLTELDLSGNE------ELSNL----TNLESLDLSGNQLtDLPEELANLT----NLKELDLSNNQ 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  410 LSkksegvqTAKEYFSMAVNLSHISFNN---TSMPSEylkavllgLASNQQLQpfRLDLDATcekgSASVLDACIGGI-R 485
Cdd:COG4886    148 LT-------DLPEPLGNLTNLKSLDLSNnqlTDLPEE--------LGNLTNLK--ELDLSNN----QITDLPEPLGNLtN 206

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017349095  486 CETLSLRDNNLdGELQGVLQSLmmvTCLRRLDIGGsnmNQLKKnnkqvhvinkvLLDVVKLYSeegcLEELNLSDCRLGA 565
Cdd:COG4886    207 LEELDLSGNQL-TDLPEPLANL---TNLETLDLSN---NQLTD-----------LPELGNLTN----LEELDLSNNQLTD 264

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1017349095  566 ylsvlINTLAATTTLKSLDISGNEMGNFGARILSKALQVNVSLRSVSIDNNHIGADGFVDLATS 629
Cdd:COG4886    265 -----LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTL 323
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH