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Conserved domains on  [gi|66392157|ref|NP_001013860|]
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capping protein, Arp2/3 and myosin-I linker protein 2 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 819-1112 7.41e-57

CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).


:

Pssm-ID: 464966 [Multi-domain]  Cd Length: 299  Bit Score: 199.23  E-value: 7.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    819 ARSLCPQMLQGSSWREQLEGVLAGSRGLPELLPEQ-----LLQDAFTRLRDMRLSITGTLAESIVAQALAGLSAARDQLV 893
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    894 ESLAQQ-ATVTMPPALPAPDGGEPSLLEPG-----------ELEGLFFPEEKE--EEKEKDDSPPQKWPE-----LSHGL 954
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGkrhegeierleELETPMATLKSKrkSIHSRKLRPVSVAFSvseldLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    955 HLVPfIHsaaeeaepepelaapGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPLAGQPLRHPTRARPRPRRQHHHRP 1034
Cdd:pfam16000  161 EEVP-IH---------------VEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTR 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392157   1035 PPGGPQVppALPQEGNGLSARVDEGVEEFFSKRLIQQDRLWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1112
Cdd:pfam16000  224 PPGKVGP--AQDGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 430-686 3.09e-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: 79.83  E-value: 3.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  430 TSLTHLDASRNVFsrtksrAAPAALQLF--LSRARTLRHLGLAGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSA 507
Cdd:COG5238  208 TTVTTLWLKRNPI------GDEGAEILAeaLKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  508 GAQVIQDLVCDAGAVSSLDLADNGFGSDMvtlvlAIGRSRSLRHVAlgrnfnvrcketlddvlhrivqlmqdddcPLQSL 587
Cdd:COG5238  280 GAIALAKALQGNTTLTSLDLSVNRIGDEG-----AIALAEGLQGNK-----------------------------TLHTL 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  588 SVAESRLK-LGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNhS 666
Cdd:COG5238  326 NLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-R 404

                        250       260
                 ....*....|....*....|
gi 66392157  667 LKAMPLPLNDVAQAQRSRPE 686
Cdd:COG5238  405 LHTLILDGNLIGAEAQQRLE 424
Carm_PH super family cl39358
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 37-120 1.61e-14

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: 70.39  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157     37 GAVQNHVLALLRWRAYLLHTTcLPLRVDCTFSYLEVQAMALQeTPPQVTFELEsLRELVLEFPGVAALEQLAQHVAAAIK 116
Cdd:pfam17888   14 DKVEDRILVLTPWRLFLLSAK-VPTKVERTFHFLEIRAINSR-NPNQVIVETD-KSNYSLKLASEEDVDHVVGHILTALK 90


                   ....
gi 66392157    117 KVFP 120
Cdd:pfam17888   91 KIFP 94
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 262-376 6.58e-12

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: 69.43  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  262 VRRLAQALAGHSSsgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALATNaafdSTLTHL 341
Cdd:COG5238  281 AIALAKALQGNTT--LTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQEN----TTLHSL 353

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 66392157  342 DLSGNP-GALGASedsgGLYSFLSRPNVLSFLNLAG 376
Cdd:COG5238  354 DLSDNQiGDEGAI----ALAKYLEGNTTLRELNLGK 385
 
Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 819-1112 7.41e-57

CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).


Pssm-ID: 464966 [Multi-domain]  Cd Length: 299  Bit Score: 199.23  E-value: 7.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    819 ARSLCPQMLQGSSWREQLEGVLAGSRGLPELLPEQ-----LLQDAFTRLRDMRLSITGTLAESIVAQALAGLSAARDQLV 893
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    894 ESLAQQ-ATVTMPPALPAPDGGEPSLLEPG-----------ELEGLFFPEEKE--EEKEKDDSPPQKWPE-----LSHGL 954
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGkrhegeierleELETPMATLKSKrkSIHSRKLRPVSVAFSvseldLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    955 HLVPfIHsaaeeaepepelaapGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPLAGQPLRHPTRARPRPRRQHHHRP 1034
Cdd:pfam16000  161 EEVP-IH---------------VEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTR 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392157   1035 PPGGPQVppALPQEGNGLSARVDEGVEEFFSKRLIQQDRLWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1112
Cdd:pfam16000  224 PPGKVGP--AQDGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 430-686 3.09e-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: 79.83  E-value: 3.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  430 TSLTHLDASRNVFsrtksrAAPAALQLF--LSRARTLRHLGLAGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSA 507
Cdd:COG5238  208 TTVTTLWLKRNPI------GDEGAEILAeaLKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  508 GAQVIQDLVCDAGAVSSLDLADNGFGSDMvtlvlAIGRSRSLRHVAlgrnfnvrcketlddvlhrivqlmqdddcPLQSL 587
Cdd:COG5238  280 GAIALAKALQGNTTLTSLDLSVNRIGDEG-----AIALAEGLQGNK-----------------------------TLHTL 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  588 SVAESRLK-LGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNhS 666
Cdd:COG5238  326 NLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-R 404

                        250       260
                 ....*....|....*....|
gi 66392157  667 LKAMPLPLNDVAQAQRSRPE 686
Cdd:COG5238  405 LHTLILDGNLIGAEAQQRLE 424
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 37-120 1.61e-14

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: 70.39  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157     37 GAVQNHVLALLRWRAYLLHTTcLPLRVDCTFSYLEVQAMALQeTPPQVTFELEsLRELVLEFPGVAALEQLAQHVAAAIK 116
Cdd:pfam17888   14 DKVEDRILVLTPWRLFLLSAK-VPTKVERTFHFLEIRAINSR-NPNQVIVETD-KSNYSLKLASEEDVDHVVGHILTALK 90


                   ....
gi 66392157    117 KVFP 120
Cdd:pfam17888   91 KIFP 94
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 277-644 2.03e-12

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 70.08  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  277 LRELSLAGNLLDDRGMTALSRHLERCPGALR-RLSLAQTGLTPRGMRALGRALATNAAfdstLTHLDLSGNPgalgASED 355
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCG----LQELDLSDNA----LGPD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  356 SGGLYSFLSRPNVLSFLNLAgtdtaldtvrgcsvggwmtgradwragRGGLGPPAGvanslppQLFAAVSRGCCTSLTHL 435
Cdd:cd00116   97 GCGVLESLLRSSSLQELKLN---------------------------NNGLGDRGL-------RLLAKGLKDLPPALEKL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  436 DASRNVFSRTKSRAAPAALQLflsrARTLRHLGLAGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDL 515
Cdd:cd00116  143 VLGRNRLEGASCEALAKALRA----NRDLKELNLANNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAET 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  516 VCDAGAVSSLDLADNGFGS-DMVTLVLA-IGRSRSLRHVALGRNfNVRCKetlddvlhrivqlmqdddcplqslsvaesr 593
Cdd:cd00116  217 LASLKSLEVLNLGDNNLTDaGAAALASAlLSPNISLLTLSLSCN-DITDD------------------------------ 265

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 66392157  594 lklGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVW 644
Cdd:cd00116  266 ---GAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLW 313
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 262-376 6.58e-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: 69.43  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  262 VRRLAQALAGHSSsgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALATNaafdSTLTHL 341
Cdd:COG5238  281 AIALAKALQGNTT--LTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQEN----TTLHSL 353

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 66392157  342 DLSGNP-GALGASedsgGLYSFLSRPNVLSFLNLAG 376
Cdd:COG5238  354 DLSDNQiGDEGAI----ALAKYLEGNTTLRELNLGK 385
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 238-515 1.06e-07

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 55.44  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  238 LHMMSQSSHLEELVLETCSLRGDFVRRLaQALagHSSSGLRELSLAGNLLDDRGMTALSRHLERCPGALRRLSLAQTGLT 317
Cdd:cd00116   74 LQGLTKGCGLQELDLSDNALGPDGCGVL-ESL--LRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  318 PRGMRALGRALATNaafdSTLTHLDLSGNP-GALGASEDSGGLYSFLSrpnvLSFLNLagTDTALdTVRGCSvggwmtgr 396
Cdd:cd00116  151 GASCEALAKALRAN----RDLKELNLANNGiGDAGIRALAEGLKANCN----LEVLDL--NNNGL-TDEGAS-------- 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  397 adwragrgglgppagvanslppQLFAAVSRGCCtsLTHLDASRNVFSrtkSRAAPAALQLFLSRARTLRHLGLAGCKLPP 476
Cdd:cd00116  212 ----------------------ALAETLASLKS--LEVLNLGDNNLT---DAGAAALASALLSPNISLLTLSLSCNDITD 264

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 66392157  477 DALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDL 515
Cdd:cd00116  265 DGAKDLAEVLAEKESLL--ELDLRGNKFGEEGAQLLAES 301
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 199-346 4.64e-07

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 53.51  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  199 SHLGSRDLALsvaALSYNLWFRCLSCVDMKLSLEVSEQILHMMSQSSHLEELVLETCSLRGDFVRRLAQALAghSSSGLR 278
Cdd:cd00116  150 EGASCEALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLA--SLKSLE 224

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392157  279 ELSLAGNLLDDRGMTALSRHLERCPGALRRLSLAQTGLTPRGMRALGRALATNaafdSTLTHLDLSGN 346
Cdd:cd00116  225 VLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEK----ESLLELDLRGN 288
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
608-634 3.64e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.93  E-value: 3.64e-04
                            10        20
                    ....*....|....*....|....*..
gi 66392157     608 NPNLTALDISGNAMGDAGAKLLAKALR 634
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
607-630 9.98e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 37.60  E-value: 9.98e-04
                           10        20
                   ....*....|....*....|....
gi 66392157    607 TNPNLTALDISGNAMGDAGAKLLA 630
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 819-1112 7.41e-57

CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).


Pssm-ID: 464966 [Multi-domain]  Cd Length: 299  Bit Score: 199.23  E-value: 7.41e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    819 ARSLCPQMLQGSSWREQLEGVLAGSRGLPELLPEQ-----LLQDAFTRLRDMRLSITGTLAESIVAQALAGLSAARDQLV 893
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    894 ESLAQQ-ATVTMPPALPAPDGGEPSLLEPG-----------ELEGLFFPEEKE--EEKEKDDSPPQKWPE-----LSHGL 954
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGkrhegeierleELETPMATLKSKrkSIHSRKLRPVSVAFSvseldLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157    955 HLVPfIHsaaeeaepepelaapGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPLAGQPLRHPTRARPRPRRQHHHRP 1034
Cdd:pfam16000  161 EEVP-IH---------------VEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTR 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392157   1035 PPGGPQVppALPQEGNGLSARVDEGVEEFFSKRLIQQDRLWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1112
Cdd:pfam16000  224 PPGKVGP--AQDGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 430-686 3.09e-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: 79.83  E-value: 3.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  430 TSLTHLDASRNVFsrtksrAAPAALQLF--LSRARTLRHLGLAGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSA 507
Cdd:COG5238  208 TTVTTLWLKRNPI------GDEGAEILAeaLKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAE 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  508 GAQVIQDLVCDAGAVSSLDLADNGFGSDMvtlvlAIGRSRSLRHVAlgrnfnvrcketlddvlhrivqlmqdddcPLQSL 587
Cdd:COG5238  280 GAIALAKALQGNTTLTSLDLSVNRIGDEG-----AIALAEGLQGNK-----------------------------TLHTL 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  588 SVAESRLK-LGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNhS 666
Cdd:COG5238  326 NLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-R 404

                        250       260
                 ....*....|....*....|
gi 66392157  667 LKAMPLPLNDVAQAQRSRPE 686
Cdd:COG5238  405 LHTLILDGNLIGAEAQQRLE 424
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 37-120 1.61e-14

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: 70.39  E-value: 1.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157     37 GAVQNHVLALLRWRAYLLHTTcLPLRVDCTFSYLEVQAMALQeTPPQVTFELEsLRELVLEFPGVAALEQLAQHVAAAIK 116
Cdd:pfam17888   14 DKVEDRILVLTPWRLFLLSAK-VPTKVERTFHFLEIRAINSR-NPNQVIVETD-KSNYSLKLASEEDVDHVVGHILTALK 90


                   ....
gi 66392157    117 KVFP 120
Cdd:pfam17888   91 KIFP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 449-688 6.29e-13

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 72.52  E-value: 6.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  449 AAPAALQLFLSRARTLRHLGLAGCKLPPDALRALLDGLALNTHLRD-------------LH-LDLSACELRSAGAQVIQD 514
Cdd:COG5238  123 MAKTLEDSLILYLALPRRINLIQVLKDPLGGNAVHLLGLAARLGLLaaismakalqnnsVEtVYLGCNQIGDEGIEELAE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  515 LVCDAGAVSSLDLADNGFGSD-MVTLVLAIGRSRSLRHVALGRNfnvrckETLDDVLHRIVQLMQDDDcPLQSLSVAESR 593
Cdd:COG5238  203 ALTQNTTVTTLWLKRNPIGDEgAEILAEALKGNKSLTTLDLSNN------QIGDEGVIALAEALKNNT-TVETLYLSGNQ 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  594 LKL-GASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQN---HSLKA 669
Cdd:COG5238  276 IGAeGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENttlHSLDL 355

                        250       260
                 ....*....|....*....|....
gi 66392157  670 MPLPLND-----VAQAQRSRPELT 688
Cdd:COG5238  356 SDNQIGDegaiaLAKYLEGNTTLR 379
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 277-644 2.03e-12

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 70.08  E-value: 2.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  277 LRELSLAGNLLDDRGMTALSRHLERCPGALR-RLSLAQTGLTPRGMRALGRALATNAAfdstLTHLDLSGNPgalgASED 355
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCG----LQELDLSDNA----LGPD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  356 SGGLYSFLSRPNVLSFLNLAgtdtaldtvrgcsvggwmtgradwragRGGLGPPAGvanslppQLFAAVSRGCCTSLTHL 435
Cdd:cd00116   97 GCGVLESLLRSSSLQELKLN---------------------------NNGLGDRGL-------RLLAKGLKDLPPALEKL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  436 DASRNVFSRTKSRAAPAALQLflsrARTLRHLGLAGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDL 515
Cdd:cd00116  143 VLGRNRLEGASCEALAKALRA----NRDLKELNLANNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAET 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  516 VCDAGAVSSLDLADNGFGS-DMVTLVLA-IGRSRSLRHVALGRNfNVRCKetlddvlhrivqlmqdddcplqslsvaesr 593
Cdd:cd00116  217 LASLKSLEVLNLGDNNLTDaGAAALASAlLSPNISLLTLSLSCN-DITDD------------------------------ 265

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 66392157  594 lklGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVW 644
Cdd:cd00116  266 ---GAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLW 313
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 262-376 6.58e-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: 69.43  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  262 VRRLAQALAGHSSsgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALATNaafdSTLTHL 341
Cdd:COG5238  281 AIALAKALQGNTT--LTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQEN----TTLHSL 353

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 66392157  342 DLSGNP-GALGASedsgGLYSFLSRPNVLSFLNLAG 376
Cdd:COG5238  354 DLSDNQiGDEGAI----ALAKYLEGNTTLRELNLGK 385
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 429-680 8.41e-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: 68.15  E-value: 8.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  429 CTSLTHLDASRNVFSRTKSRAAPAALQLFlsrarTLRHLGLAGCKLPPDALRALLDGL-ALNTHLRDLhlDLSACELRSA 507
Cdd:cd00116   80 GCGLQELDLSDNALGPDGCGVLESLLRSS-----SLQELKLNNNGLGDRGLRLLAKGLkDLPPALEKL--VLGRNRLEGA 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  508 GAQVIQDLVCDAGAVSSLDLADNGFGSDMVTlvlaigrsrslrhvALGRNFNVRCKetlddvLHRIVqlmqdddcpLQSL 587
Cdd:cd00116  153 SCEALAKALRANRDLKELNLANNGIGDAGIR--------------ALAEGLKANCN------LEVLD---------LNNN 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  588 SVAEsrlkLGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALR-VNSRLRSVVWDRNHTSALGLLDVAQALEQNHS 666
Cdd:cd00116  204 GLTD----EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKES 279

                        250
                 ....*....|....
gi 66392157  667 LKAMPLPLNDVAQA 680
Cdd:cd00116  280 LLELDLRGNKFGEE 293
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 476-688 1.11e-10

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 64.68  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  476 PDALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDLVcDAGAVSSLDLADNGFGSDMVTLVLAIGRSRSLR---HV 552
Cdd:cd00116   67 PRGLQSLLQGLTKGCGLQ--ELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPAlekLV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  553 ALGRNFNVRCKETLDDVLHRIvqlmqdddCPLQSLSVAESRLKL-GASVLLRALATNPNLTALDISGNAMGDAGAKLLAK 631
Cdd:cd00116  144 LGRNRLEGASCEALAKALRAN--------RDLKELNLANNGIGDaGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAE 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392157  632 ALRVNSRLRSVVWDRNHTSALGLLDVAQAL-EQNHSLKAMPLPLN--------DVAQAQRSRPELT 688
Cdd:cd00116  216 TLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNditddgakDLAEVLAEKESLL 281
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 250-535 1.45e-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: 65.20  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  250 LVLETCSLRGDFVRRLAQALAGHSssgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALA 329
Cdd:COG5238  158 LLGLAARLGLLAAISMAKALQNNS---VETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALK 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  330 TNAafdsTLTHLDLSGNP-GALGASEdsggLYSFLSRPNVLSFLNLAGTdtaldtvrgcsvggwmtgradwRAGRGGLgp 408
Cdd:COG5238  234 GNK----SLTTLDLSNNQiGDEGVIA----LAEALKNNTTVETLYLSGN----------------------QIGAEGA-- 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  409 pAGVANSLPPQlfaavsrgccTSLTHLDASRNVFSRtksrAAPAALQLFLSRARTLRHLGLAGCKLPPDALRALLDGLAL 488
Cdd:COG5238  282 -IALAKALQGN----------TTLTSLDLSVNRIGD----EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQE 346

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 66392157  489 NTHLRDlhLDLSACELRSAGAQVIQDLVCDAGAVSSLDLADNGFGSD 535
Cdd:COG5238  347 NTTLHS--LDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQ 391
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 597-740 6.74e-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: 6.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  597 GASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNHSLKAMPLPLND 676
Cdd:COG5238  196 GIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQ 275

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66392157  677 V-AQAQRSRPELTARAVHqIQACLLRNNRADPASS-------DHTTRLQPLGLVSDP-SEQEVNELCQSVQEH 740
Cdd:COG5238  276 IgAEGAIALAKALQGNTT-LTSLDLSVNRIGDEGAialaeglQGNKTLHTLNLAYNGiGAQGAIALAKALQEN 347
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 243-346 8.06e-08

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: 56.34  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  243 QSSHLEELVLETCSLRGDFVRRLAQALAGHSSsgLRELSLAGNLLDDRGMTALSRHLERCPGaLRRLSLAQTGLTPRGMR 322
Cdd:COG5238  318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIALAKYLEGNTT-LRELNLGKNNIGKQGAE 394

                         90       100
                 ....*....|....*....|....
gi 66392157  323 ALGRALATNaafdsTLTHLDLSGN 346
Cdd:COG5238  395 ALIDALQTN-----RLHTLILDGN 413
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 238-515 1.06e-07

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 55.44  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  238 LHMMSQSSHLEELVLETCSLRGDFVRRLaQALagHSSSGLRELSLAGNLLDDRGMTALSRHLERCPGALRRLSLAQTGLT 317
Cdd:cd00116   74 LQGLTKGCGLQELDLSDNALGPDGCGVL-ESL--LRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  318 PRGMRALGRALATNaafdSTLTHLDLSGNP-GALGASEDSGGLYSFLSrpnvLSFLNLagTDTALdTVRGCSvggwmtgr 396
Cdd:cd00116  151 GASCEALAKALRAN----RDLKELNLANNGiGDAGIRALAEGLKANCN----LEVLDL--NNNGL-TDEGAS-------- 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  397 adwragrgglgppagvanslppQLFAAVSRGCCtsLTHLDASRNVFSrtkSRAAPAALQLFLSRARTLRHLGLAGCKLPP 476
Cdd:cd00116  212 ----------------------ALAETLASLKS--LEVLNLGDNNLT---DAGAAALASALLSPNISLLTLSLSCNDITD 264

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 66392157  477 DALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDL 515
Cdd:cd00116  265 DGAKDLAEVLAEKESLL--ELDLRGNKFGEEGAQLLAES 301
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 199-346 4.64e-07

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 53.51  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  199 SHLGSRDLALsvaALSYNLWFRCLSCVDMKLSLEVSEQILHMMSQSSHLEELVLETCSLRGDFVRRLAQALAghSSSGLR 278
Cdd:cd00116  150 EGASCEALAK---ALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLA--SLKSLE 224

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392157  279 ELSLAGNLLDDRGMTALSRHLERCPGALRRLSLAQTGLTPRGMRALGRALATNaafdSTLTHLDLSGN 346
Cdd:cd00116  225 VLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEK----ESLLELDLRGN 288
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 201-346 1.70e-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: 51.59  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  201 LGSRDLALSVAALSYNlwfrclscvdmKLSLEVSEQILHMMSQSSHLEELVLETCSLRGDFVRRLAQALAghSSSGLREL 280
Cdd:cd00116  132 LKDLPPALEKLVLGRN-----------RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK--ANCNLEVL 198

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392157  281 SLAGNLLDDRGMTALSrHLERCPGALRRLSLAQTGLTPRGMRALGRALATNAafdSTLTHLDLSGN 346
Cdd:cd00116  199 DLNNNGLTDEGASALA-ETLASLKSLEVLNLGDNNLTDAGAAALASALLSPN---ISLLTLSLSCN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
415-671 1.01e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.47  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  415 SLPPQLFAavsrgcCTSLTHLDASRNVFSrtksraapaALQLFLSRARTLRHLGLAGCKLP--PDALRAL--LDGLAL-N 489
Cdd:COG4886  127 DLPEELAN------LTNLKELDLSNNQLT---------DLPEPLGNLTNLKSLDLSNNQLTdlPEELGNLtnLKELDLsN 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  490 THLRDLHLDLSACElrsagaqviqdlvcdagAVSSLDLADNGFGSdmvtLVLAIGRSRSLRHVALGRNfnvrckeTLDDv 569
Cdd:COG4886  192 NQITDLPEPLGNLT-----------------NLEELDLSGNQLTD----LPEPLANLTNLETLDLSNN-------QLTD- 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  570 LHRIVQLMQdddcpLQSLSVAESRLKLgasvlLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHT 649
Cdd:COG4886  243 LPELGNLTN-----LEELDLSNNQLTD-----LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLE 312

                        250       260
                 ....*....|....*....|..
gi 66392157  650 SALGLLDVAQALEQNHSLKAMP 671
Cdd:COG4886  313 LLILLLLLTTLLLLLLLLKGLL 334
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
608-634 3.64e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.93  E-value: 3.64e-04
                            10        20
                    ....*....|....*....|....*..
gi 66392157     608 NPNLTALDISGNAMGDAGAKLLAKALR 634
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
607-630 9.98e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 37.60  E-value: 9.98e-04
                           10        20
                   ....*....|....*....|....
gi 66392157    607 TNPNLTALDISGNAMGDAGAKLLA 630
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
197-346 3.67e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  197 DFSHLGSRDLALSVAALSyNLwfRCLSCVDMKLSlEVSEQIlhmmSQSSHLEELVLETCSLRGdfvrrLAQALAGHSSsg 276
Cdd:COG4886  119 DLSGNQLTDLPEELANLT-NL--KELDLSNNQLT-DLPEPL----GNLTNLKSLDLSNNQLTD-----LPEELGNLTN-- 183

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392157  277 LRELSLAGNLLDDrgmtaLSRHLERCPgALRRLSLAQTGLTprgmrALGRALATNaafdSTLTHLDLSGN 346
Cdd:COG4886  184 LKELDLSNNQITD-----LPEPLGNLT-NLEELDLSGNQLT-----DLPEPLANL----TNLETLDLSNN 238
 
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.
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