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Conserved domains on  [gi|949474729|ref|NP_001303955|]
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capping protein, Arp2/3 and myosin-I linker protein 2 isoform 2 [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 ...
 783-1076 7.59e-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: 7.59e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   783 ARSLCPQMLQGSSWREQLEGVLAGSRGLPELLPEQ-----LLQDAFTRLRDMRLSITGTLAESIVAQALAGLSAARDQLV 857
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   858 ESLAQQ-ATVTMPPALPAPDGGEPSLLEPG-----------ELEGLFFPEEKE--EEKEKDDSPPQKWPE-----LSHGL 918
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGkrhegeierleELETPMATLKSKrkSIHSRKLRPVSVAFSvseldLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   919 HLVPfIHsaaeeaepepelaapGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPLAGQPLRHPTRARPRPRRQHHHRP 998
Cdd:pfam16000  161 EEVP-IH---------------VEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTR 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949474729   999 PPGGPQVppALPQEGNGLSARVDEGVEEFFSKRLIQQDRLWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1076
Cdd:pfam16000  224 PPGKVGP--AQDGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 250-650 1.17e-16

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


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 84.07  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  250 LVLETCSLRGDFVRRLAQALAGHSssgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALA 329
Cdd:COG5238   158 LLGLAARLGLLAAISMAKALQNNS---VETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  330 TNAafdsTLTHLDLSGNPgaLGaseDSGglysflsrpnvlsFLNLAgtdtaldtlfaavsrgccTSLTHldasrnvfsrt 409
Cdd:COG5238   234 GNK----SLTTLDLSNNQ--IG---DEG-------------VIALA------------------EALKN----------- 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  410 ksraapaalqlflsrARTLRHLGLAGCKLPPDALRALLDGLALNTHLRDLhlDLSACELRSAGAQVIQDLVCDAGAVSSL 489
Cdd:COG5238   263 ---------------NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL--DLSVNRIGDEGAIALAEGLQGNKTLHTL 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  490 DLADNGFGSDmvtlvlaigrsrslrhvalgrnfnvrcketlddvlhrivqlmqdddcplqslsvaesrlklGASVLLRAL 569
Cdd:COG5238   326 NLAYNGIGAQ-------------------------------------------------------------GAIALAKAL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  570 ATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNhSLKAMPLPLNDVAQAQRSRP 649
Cdd:COG5238   345 QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRL 423


                  .
gi 949474729  650 E 650
Cdd:COG5238   424 E 424
Carm_PH super family cl39358
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 37-120 1.54e-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: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729    37 GAVQNHVLALLRWRAYLLHTTcLPLRVDCTFSYLEVQAMALQeTPPQVTFELEsLRELVLEFPGVAALEQLAQHVAAAIK 116
Cdd:pfam17888   14 DKVEDRILVLTPWRLFLLSAK-VPTKVERTFHFLEIRAINSR-NPNQVIVETD-KSNYSLKLASEEDVDHVVGHILTALK 90


                   ....
gi 949474729   117 KVFP 120
Cdd:pfam17888   91 KIFP 94
 
Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 783-1076 7.59e-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: 7.59e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   783 ARSLCPQMLQGSSWREQLEGVLAGSRGLPELLPEQ-----LLQDAFTRLRDMRLSITGTLAESIVAQALAGLSAARDQLV 857
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   858 ESLAQQ-ATVTMPPALPAPDGGEPSLLEPG-----------ELEGLFFPEEKE--EEKEKDDSPPQKWPE-----LSHGL 918
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGkrhegeierleELETPMATLKSKrkSIHSRKLRPVSVAFSvseldLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   919 HLVPfIHsaaeeaepepelaapGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPLAGQPLRHPTRARPRPRRQHHHRP 998
Cdd:pfam16000  161 EEVP-IH---------------VEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTR 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949474729   999 PPGGPQVppALPQEGNGLSARVDEGVEEFFSKRLIQQDRLWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1076
Cdd:pfam16000  224 PPGKVGP--AQDGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 250-650 1.17e-16

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 84.07  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  250 LVLETCSLRGDFVRRLAQALAGHSssgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALA 329
Cdd:COG5238   158 LLGLAARLGLLAAISMAKALQNNS---VETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  330 TNAafdsTLTHLDLSGNPgaLGaseDSGglysflsrpnvlsFLNLAgtdtaldtlfaavsrgccTSLTHldasrnvfsrt 409
Cdd:COG5238   234 GNK----SLTTLDLSNNQ--IG---DEG-------------VIALA------------------EALKN----------- 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  410 ksraapaalqlflsrARTLRHLGLAGCKLPPDALRALLDGLALNTHLRDLhlDLSACELRSAGAQVIQDLVCDAGAVSSL 489
Cdd:COG5238   263 ---------------NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL--DLSVNRIGDEGAIALAEGLQGNKTLHTL 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  490 DLADNGFGSDmvtlvlaigrsrslrhvalgrnfnvrcketlddvlhrivqlmqdddcplqslsvaesrlklGASVLLRAL 569
Cdd:COG5238   326 NLAYNGIGAQ-------------------------------------------------------------GAIALAKAL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  570 ATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNhSLKAMPLPLNDVAQAQRSRP 649
Cdd:COG5238   345 QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRL 423


                  .
gi 949474729  650 E 650
Cdd:COG5238   424 E 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 277-608 1.45e-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: 82.40  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  277 LRELSLAGNLLDDRGMTALSRHLERCPGALR-RLSLAQTGLTPRGMRALGRALATNAAfdstLTHLDLSGNpgALGAsED 355
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCG----LQELDLSDN--ALGP-DG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  356 SGGLYSFLSRPN--VLSFLNLAGTDTALDTLfAAVSRGCCTSLTHLDASRNVFSRTKSRAAPAALQLflsrARTLRHLGL 433
Cdd:cd00116    98 CGVLESLLRSSSlqELKLNNNGLGDRGLRLL-AKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA----NRDLKELNL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  434 AGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDLVCDAGAVSSLDLADNGFGS-DMVTLVLA-IGRSR 511
Cdd:cd00116   173 ANNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGAAALASAlLSPNI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  512 SLRHVALGRNfNVRCKetlddvlhrivqlmqdddcplqslsvaesrlklGASVLLRALATNPNLTALDISGNAMGDAGAK 591
Cdd:cd00116   251 SLLTLSLSCN-DITDD---------------------------------GAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296

                         330
                  ....*....|....*..
gi 949474729  592 LLAKALRVNSRLRSVVW 608
Cdd:cd00116   297 LLAESLLEPGNELESLW 313
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 37-120 1.54e-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: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729    37 GAVQNHVLALLRWRAYLLHTTcLPLRVDCTFSYLEVQAMALQeTPPQVTFELEsLRELVLEFPGVAALEQLAQHVAAAIK 116
Cdd:pfam17888   14 DKVEDRILVLTPWRLFLLSAK-VPTKVERTFHFLEIRAINSR-NPNQVIVETD-KSNYSLKLASEEDVDHVVGHILTALK 90


                   ....
gi 949474729   117 KVFP 120
Cdd:pfam17888   91 KIFP 94
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
572-598 3.84e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.93  E-value: 3.84e-04
                            10        20
                    ....*....|....*....|....*..
gi 949474729    572 NPNLTALDISGNAMGDAGAKLLAKALR 598
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
571-594 1.05e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 37.60  E-value: 1.05e-03
                           10        20
                   ....*....|....*....|....
gi 949474729   571 TNPNLTALDISGNAMGDAGAKLLA 594
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 ...
 783-1076 7.59e-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: 7.59e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   783 ARSLCPQMLQGSSWREQLEGVLAGSRGLPELLPEQ-----LLQDAFTRLRDMRLSITGTLAESIVAQALAGLSAARDQLV 857
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   858 ESLAQQ-ATVTMPPALPAPDGGEPSLLEPG-----------ELEGLFFPEEKE--EEKEKDDSPPQKWPE-----LSHGL 918
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGkrhegeierleELETPMATLKSKrkSIHSRKLRPVSVAFSvseldLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729   919 HLVPfIHsaaeeaepepelaapGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPLAGQPLRHPTRARPRPRRQHHHRP 998
Cdd:pfam16000  161 EEVP-IH---------------VEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTR 223

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 949474729   999 PPGGPQVppALPQEGNGLSARVDEGVEEFFSKRLIQQDRLWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1076
Cdd:pfam16000  224 PPGKVGP--AQDGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 250-650 1.17e-16

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 84.07  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  250 LVLETCSLRGDFVRRLAQALAGHSssgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALA 329
Cdd:COG5238   158 LLGLAARLGLLAAISMAKALQNNS---VETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  330 TNAafdsTLTHLDLSGNPgaLGaseDSGglysflsrpnvlsFLNLAgtdtaldtlfaavsrgccTSLTHldasrnvfsrt 409
Cdd:COG5238   234 GNK----SLTTLDLSNNQ--IG---DEG-------------VIALA------------------EALKN----------- 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  410 ksraapaalqlflsrARTLRHLGLAGCKLPPDALRALLDGLALNTHLRDLhlDLSACELRSAGAQVIQDLVCDAGAVSSL 489
Cdd:COG5238   263 ---------------NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL--DLSVNRIGDEGAIALAEGLQGNKTLHTL 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  490 DLADNGFGSDmvtlvlaigrsrslrhvalgrnfnvrcketlddvlhrivqlmqdddcplqslsvaesrlklGASVLLRAL 569
Cdd:COG5238   326 NLAYNGIGAQ-------------------------------------------------------------GAIALAKAL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  570 ATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNhSLKAMPLPLNDVAQAQRSRP 649
Cdd:COG5238   345 QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRL 423


                  .
gi 949474729  650 E 650
Cdd:COG5238   424 E 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 277-608 1.45e-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: 82.40  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  277 LRELSLAGNLLDDRGMTALSRHLERCPGALR-RLSLAQTGLTPRGMRALGRALATNAAfdstLTHLDLSGNpgALGAsED 355
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCG----LQELDLSDN--ALGP-DG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  356 SGGLYSFLSRPN--VLSFLNLAGTDTALDTLfAAVSRGCCTSLTHLDASRNVFSRTKSRAAPAALQLflsrARTLRHLGL 433
Cdd:cd00116    98 CGVLESLLRSSSlqELKLNNNGLGDRGLRLL-AKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA----NRDLKELNL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  434 AGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDLVCDAGAVSSLDLADNGFGS-DMVTLVLA-IGRSR 511
Cdd:cd00116   173 ANNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGAAALASAlLSPNI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  512 SLRHVALGRNfNVRCKetlddvlhrivqlmqdddcplqslsvaesrlklGASVLLRALATNPNLTALDISGNAMGDAGAK 591
Cdd:cd00116   251 SLLTLSLSCN-DITDD---------------------------------GAKDLAEVLAEKESLLELDLRGNKFGEEGAQ 296

                         330
                  ....*....|....*..
gi 949474729  592 LLAKALRVNSRLRSVVW 608
Cdd:cd00116   297 LLAESLLEPGNELESLW 313
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 279-644 6.32e-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: 77.40  E-value: 6.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  279 ELSLAGNLLDDRGMTALSRHLeRCPGALRrlsLAQTGLTPRGMRALGRALATNAAfdstLTHLDLSGNpgalgasedsgg 358
Cdd:cd00116     2 QLSLKGELLKTERATELLPKL-LCLQVLR---LEGNTLGEEAAKALASALRPQPS----LKELCLSLN------------ 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  359 lysflsrpnvlsflNLAGTDTALDTLFAAVSRGCCtsLTHLDASRNVFSRTKSRAAPAALQLFlsrarTLRHLGLAGCKL 438
Cdd:cd00116    62 --------------ETGRIPRGLQSLLQGLTKGCG--LQELDLSDNALGPDGCGVLESLLRSS-----SLQELKLNNNGL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  439 PPDALRALLDGL-ALNTHLRDLhlDLSACELRSAGAQVIQDLVCDAGAVSSLDLADNGFGSDMVTlvlaigrsrslrhvA 517
Cdd:cd00116   121 GDRGLRLLAKGLkDLPPALEKL--VLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIR--------------A 184

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  518 LGRNFNVRCKetlddvLHRIVqlmqdddcpLQSLSVAEsrlkLGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKAL 597
Cdd:cd00116   185 LAEGLKANCN------LEVLD---------LNNNGLTD----EGASALAETLASLKSLEVLNLGDNNLTDAGAAALASAL 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 949474729  598 R-VNSRLRSVVWDRNHTSALGLLDVAQALEQNHSLKAMPLPLNDVAQA 644
Cdd:cd00116   246 LsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 37-120 1.54e-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: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729    37 GAVQNHVLALLRWRAYLLHTTcLPLRVDCTFSYLEVQAMALQeTPPQVTFELEsLRELVLEFPGVAALEQLAQHVAAAIK 116
Cdd:pfam17888   14 DKVEDRILVLTPWRLFLLSAK-VPTKVERTFHFLEIRAINSR-NPNQVIVETD-KSNYSLKLASEEDVDHVVGHILTALK 90


                   ....
gi 949474729   117 KVFP 120
Cdd:pfam17888   91 KIFP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 188-479 1.96e-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: 74.06  E-value: 1.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  188 QGCRHFSLGDFSHLGSRDLALSVAALSYNLWFRCLSCVDMKLSLEVSEQILHMMSQSSHLEELVLETCSLRGDFVRRLAQ 267
Cdd:COG5238   151 LGGNAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAE 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  268 ALAGHSSsgLRELSLAGNLLDDRGMTALSRHLERcPGALRRLSLAQTGLTPRGMRALGRALATNaafdSTLTHLDLSGNP 347
Cdd:COG5238   231 ALKGNKS--LTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGN----TTLTSLDLSVNR 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  348 -GALGASedsgGLYSFLSRPNVLSFLNLAG---TDTALDTLFAAVSRGccTSLTHLDASRNVFSRtksrAAPAALQLFLS 423
Cdd:COG5238   304 iGDEGAI----ALAEGLQGNKTLHTLNLAYngiGAQGAIALAKALQEN--TTLHSLDLSDNQIGD----EGAIALAKYLE 373

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 949474729  424 RARTLRHLGLAGCKLPPDALRALLDGLALNThlrdLH-LDLSACELRSAGAQVIQDL 479
Cdd:COG5238   374 GNTTLRELNLGKNNIGKQGAEALIDALQTNR----LHtLILDGNLIGAEAQQRLEQL 426
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 238-479 7.57e-11

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 65.07  E-value: 7.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  238 LHMMSQSSHLEELVLETCSLRGDFVRRLaQALagHSSSGLRELSLAGNLLDDRGMTALSRHLERCPGALRRLSLAQTGLT 317
Cdd:cd00116    74 LQGLTKGCGLQELDLSDNALGPDGCGVL-ESL--LRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  318 PRGMRALGRALATNaafdSTLTHLDLSGNP-GALGASEDSGGLYSFlSRPNVLSFLNLAGTDTALDTLFAAVSRGCCtsL 396
Cdd:cd00116   151 GASCEALAKALRAN----RDLKELNLANNGiGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKS--L 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  397 THLDASRNVFSrtkSRAAPAALQLFLSRARTLRHLGLAGCKLPPDALRALLDGLALNTHLRdlHLDLSACELRSAGAQVI 476
Cdd:cd00116   224 EVLNLGDNNLT---DAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLL--ELDLRGNKFGEEGAQLL 298


                  ...
gi 949474729  477 QDL 479
Cdd:cd00116   299 AES 301
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 440-652 1.66e-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: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  440 PDALRALLDGLALNTHLRdlHLDLSACELRSAGAQVIQDLVcDAGAVSSLDLADNGFGSDMVTLVLAIGRSRSLR---HV 516
Cdd:cd00116    67 PRGLQSLLQGLTKGCGLQ--ELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPAlekLV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  517 ALGRNFNVRCKETLDDVLHRIvqlmqdddCPLQSLSVAESRLKL-GASVLLRALATNPNLTALDISGNAMGDAGAKLLAK 595
Cdd:cd00116   144 LGRNRLEGASCEALAKALRAN--------RDLKELNLANNGIGDaGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAE 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949474729  596 ALRVNSRLRSVVWDRNHTSALGLLDVAQAL-EQNHSLKAMPLPLN--------DVAQAQRSRPELT 652
Cdd:cd00116   216 TLASLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNditddgakDLAEVLAEKESLL 281
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 561-704 7.94e-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: 62.89  E-value: 7.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  561 GASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNHSLKAMPLPLND 640
Cdd:COG5238   196 GIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQ 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949474729  641 V-AQAQRSRPELTARAVHqIQACLLRNNRADPASS-------DHTTRLQPLGLVSDP-SEQEVNELCQSVQEH 704
Cdd:COG5238   276 IgAEGAIALAKALQGNTT-LTSLDLSVNRIGDEGAialaeglQGNKTLHTLNLAYNGiGAQGAIALAKALQEN 347
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
338-639 1.71e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.24  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  338 LTHLDLSGNPGalgasedsgglysfLSRPNVLSFLNLAGTdtALDTLFAAVSRgcCTSLTHLDASRNVFSrtksraapaA 417
Cdd:COG4886    98 LTELDLSGNEE--------------LSNLTNLESLDLSGN--QLTDLPEELAN--LTNLKELDLSNNQLT---------D 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  418 LQLFLSRARTLRHLGLAGCKLP--PDALRAL--LDGLAL-NTHLRDLHLDLSACElrsagaqviqdlvcdagAVSSLDLA 492
Cdd:COG4886   151 LPEPLGNLTNLKSLDLSNNQLTdlPEELGNLtnLKELDLsNNQITDLPEPLGNLT-----------------NLEELDLS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  493 DNGFGSdmvtLVLAIGRSRSLRHVALGRNfnvrckeTLDDvLHRIVQLMQdddcpLQSLSVAESRLKLgasvlLRALATN 572
Cdd:COG4886   214 GNQLTD----LPEPLANLTNLETLDLSNN-------QLTD-LPELGNLTN-----LEELDLSNNQLTD-----LPPLANL 271

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 949474729  573 PNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNHSLKAMPLPLN 639
Cdd:COG4886   272 TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLT 338
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 201-346 2.32e-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: 51.20  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  201 LGSRDLALSVAALSYNlwfrclscvdmKLSLEVSEQILHMMSQSSHLEELVLETCSLRGDFVRRLAQALAghSSSGLREL 280
Cdd:cd00116   132 LKDLPPALEKLVLGRN-----------RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK--ANCNLEVL 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 949474729  281 SLAGNLLDDRGMTALSrHLERCPGALRRLSLAQTGLTPRGMRALGRALATNAafdSTLTHLDLSGN 346
Cdd:cd00116   199 DLNNNGLTDEGASALA-ETLASLKSLEVLNLGDNNLTDAGAAALASALLSPN---ISLLTLSLSCN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
242-463 3.72e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.01  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  242 SQSSHLEELVLETCSLRGdfvrrLAQALAGHSSsgLRELSLAGNLLDDrgmtaLSRHLERCPgALRRLSLAQTGLTprgm 321
Cdd:COG4886   156 GNLTNLKSLDLSNNQLTD-----LPEELGNLTN--LKELDLSNNQITD-----LPEPLGNLT-NLEELDLSGNQLT---- 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 949474729  322 rALGRALATNaafdSTLTHLDLSGNPgaLGAsedsggLYSFLSRPNvLSFLNLAGTD-TALDTLfaavsrGCCTSLTHLD 400
Cdd:COG4886   219 -DLPEPLANL----TNLETLDLSNNQ--LTD------LPELGNLTN-LEELDLSNNQlTDLPPL------ANLTNLKTLD 278

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 949474729  401 ASRNVFSRTKSRAAPAALQLFLSRARTLRHLGLAGCKLPPDALRALLDGLALNTHLRDLHLDL 463
Cdd:COG4886   279 LSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLA 341
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
572-598 3.84e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.93  E-value: 3.84e-04
                            10        20
                    ....*....|....*....|....*..
gi 949474729    572 NPNLTALDISGNAMGDAGAKLLAKALR 598
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
571-594 1.05e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 37.60  E-value: 1.05e-03
                           10        20
                   ....*....|....*....|....
gi 949474729   571 TNPNLTALDISGNAMGDAGAKLLA 594
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
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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