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Conserved domains on  [gi|1039789755|ref|XP_017168230|]
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capping protein, Arp2/3 and myosin-I linker protein 2 isoform X4 [Mus musculus]

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 1.89e-54

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: 192.29  E-value: 1.89e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  783 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 857
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  858 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 935
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  936 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1014
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039789755 1015 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1076
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 299-651 3.55e-19

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: 92.16  E-value: 3.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  299 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 370
Cdd:COG5238     96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  371 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 441
Cdd:COG5238    174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  442 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 521
Cdd:COG5238    251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  522 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 600
Cdd:COG5238    313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039789755  601 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 651
Cdd:COG5238    375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
Carm_PH super family cl39358
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.93e-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: 68.85  E-value: 5.93e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789755   43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKKVFP 119
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKKIFP 94
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 221-347 1.04e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 55.44  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  221 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 300
Cdd:cd00116    140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789755  301 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 347
Cdd:cd00116    218 AS-LKSLEVLNLGDNNLTDAGAAALASALLSPNI---SLLTLSLSCN 260
 
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 1.89e-54

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: 192.29  E-value: 1.89e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  783 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 857
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  858 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 935
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  936 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1014
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039789755 1015 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1076
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 299-651 3.55e-19

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: 92.16  E-value: 3.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  299 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 370
Cdd:COG5238     96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  371 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 441
Cdd:COG5238    174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  442 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 521
Cdd:COG5238    251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  522 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 600
Cdd:COG5238    313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039789755  601 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 651
Cdd:COG5238    375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 280-645 5.11e-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: 77.78  E-value: 5.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  280 ELSLSGNLLDDRGMAALSRHLeHCPGALRrlsLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgg 359
Cdd:cd00116      2 QLSLKGELLKTERATELLPKL-LCLQVLR---LEGNTLGEEAAKALASALRPQ----PSLKELCLSLN------------ 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  360 lytflsrpnvlaylNLAGTDATLGTLFTALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKL 439
Cdd:cd00116     62 --------------ETGRIPRGLQSLLQGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGL 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  440 PPEALRALLEGLalntqihdlhldlsacelrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVA 518
Cdd:cd00116    121 GDRGLRLLAKGL--------------------------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELN 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  519 LGRNfnvrckETLDDVLHRIAQLMQDDdCPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKA 597
Cdd:cd00116    172 LANN------GIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTdEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1039789755  598 LR-VNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQA 645
Cdd:cd00116    245 LLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.93e-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: 68.85  E-value: 5.93e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789755   43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKKVFP 119
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKKIFP 94
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 221-347 1.04e-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: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  221 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 300
Cdd:cd00116    140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789755  301 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 347
Cdd:cd00116    218 AS-LKSLEVLNLGDNNLTDAGAAALASALLSPNI---SLLTLSLSCN 260
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
573-599 7.97e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 7.97e-05
                            10        20
                    ....*....|....*....|....*..
gi 1039789755   573 NPKLTALDISGNAIGDAGAKMLAKALR 599
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
572-595 9.51e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 9.51e-05
                           10        20
                   ....*....|....*....|....
gi 1039789755  572 TNPKLTALDISGNAIGDAGAKMLA 595
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 1.89e-54

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: 192.29  E-value: 1.89e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  783 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 857
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  858 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 935
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  936 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1014
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039789755 1015 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1076
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 299-651 3.55e-19

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: 92.16  E-value: 3.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  299 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 370
Cdd:COG5238     96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  371 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 441
Cdd:COG5238    174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  442 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 521
Cdd:COG5238    251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  522 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 600
Cdd:COG5238    313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039789755  601 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 651
Cdd:COG5238    375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 280-645 5.11e-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: 77.78  E-value: 5.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  280 ELSLSGNLLDDRGMAALSRHLeHCPGALRrlsLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgg 359
Cdd:cd00116      2 QLSLKGELLKTERATELLPKL-LCLQVLR---LEGNTLGEEAAKALASALRPQ----PSLKELCLSLN------------ 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  360 lytflsrpnvlaylNLAGTDATLGTLFTALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKL 439
Cdd:cd00116     62 --------------ETGRIPRGLQSLLQGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGL 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  440 PPEALRALLEGLalntqihdlhldlsacelrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVA 518
Cdd:cd00116    121 GDRGLRLLAKGL--------------------------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELN 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  519 LGRNfnvrckETLDDVLHRIAQLMQDDdCPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKA 597
Cdd:cd00116    172 LANN------GIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTdEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1039789755  598 LR-VNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQA 645
Cdd:cd00116    245 LLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 167-464 2.66e-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: 76.75  E-value: 2.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  167 YNGFPFREEIQWVRDVDTIYHR-QGCRHFCLGDFSHFGSRDLALSVAALSYNLWFRRLSCEDMKLSLEVSEQILHMTSQS 245
Cdd:COG5238    128 EDSLILYLALPRRINLIQVLKDpLGGNAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQN 207

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  246 SYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHLEHcPGALRRLSLAQTGLTPRGMRAL 325
Cdd:COG5238    208 TTVTTLWLKRNPIGDEGAEILAEALKG--NKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIAL 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  326 GRALATNatfdSTLTHLDLSGN----PGALgpsqdsgGLYTFLSRPNVLAYLNLAG---TDATLGTLFTALAGGccSSLT 398
Cdd:COG5238    285 AKALQGN----TTLTSLDLSVNrigdEGAI-------ALAEGLQGNKTLHTLNLAYngiGAQGAIALAKALQEN--TTLH 351

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039789755  399 HLEASRNifsRMKSQAApAALQRFLGGTRMLRHLGLAGCKLPPEALRALLEGLALNtQIHDLHLDL 464
Cdd:COG5238    352 SLDLSDN---QIGDEGA-IALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDG 412
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 278-609 3.36e-14

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 75.47  E-value: 3.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  278 LRELSLSGNLLDDRGMAALSRHLEHCPGALR-RLSLAQTGLTPRGMRALGRALATNATfdstLTHLDLSGNpgALGPSQd 356
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCG----LQELDLSDN--ALGPDG- 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  357 SGGLYTFLSRPNV-LAYLNLAGTDATLGTLFTALAGGCCSSLTHLEASRNIFSRMKSQAAPAALQRflggTRMLRHLGLA 435
Cdd:cd00116     98 CGVLESLLRSSSLqELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA----NRDLKELNLA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  436 GCKLPPEALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGS-DMVTLVLAigrsrsL 514
Cdd:cd00116    174 NNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGAAALASA------L 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  515 KHVAlgrnfnvrcketlddvlhriaqlmqdddCPLQSLSVAESRLKQ-GASILIRALGTNPKLTALDISGNAIGDAGAKM 593
Cdd:cd00116    246 LSPN----------------------------ISLLTLSLSCNDITDdGAKDLAEVLAEKESLLELDLRGNKFGEEGAQL 297

                          330
                   ....*....|....*.
gi 1039789755  594 LAKALRVNTRLRSVIW 609
Cdd:cd00116    298 LAESLLEPGNELESLW 313
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.93e-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: 68.85  E-value: 5.93e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039789755   43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKKVFP 119
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKKIFP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 444-723 7.97e-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: 75.60  E-value: 7.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  444 LRALLEGLALNTQIHDLHLDLSACELrSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVT-LVLAIGRSRSLKHVALGRN 522
Cdd:COG5238    140 RINLIQVLKDPLGGNAVHLLGLAARL-GLLAAISMAKALQNNSVETVYLGCNQIGDEGIEeLAEALTQNTTVTTLWLKRN 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  523 fnvrckETLDDVLHRIAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRVN 601
Cdd:COG5238    219 ------PIGDEGAEILAEALKGNK-SLTTLDLSNNQIGdEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGN 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  602 TRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQAhrsrpelttrAVHQIQACLWRNNQVdSTSDLKPclq 681
Cdd:COG5238    292 TTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQ----------GAIALAKALQENTTL-HSLDLSD--- 357

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789755  682 plGLISDHSeqeVNELCQSVQEHMELL-----GCGAGPQGEVAVHQA 723
Cdd:COG5238    358 --NQIGDEG---AIALAKYLEGNTTLRelnlgKNNIGKQGAEALIDA 399
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 248-505 1.91e-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: 60.83  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  248 LEELVLEACGLRGDFVRRLAQALAghfNSGLRELSLSGNLLDDRGMAALSRHLEHCPGALRRLSLAQTGLTPRGMRALGR 327
Cdd:cd00116     83 LQELDLSDNALGPDGCGVLESLLR---SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAK 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  328 ALATNatfdSTLTHLDLSGNPgalgpsqdsgglytflsrpnvlayLNLAGTDAtlgtLFTALAGGCcsSLTHLEASRNIF 407
Cdd:cd00116    160 ALRAN----RDLKELNLANNG------------------------IGDAGIRA----LAEGLKANC--NLEVLDLNNNGL 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  408 SRMKSQAAPAALQRflggTRMLRHLGLAGCKLPPEALRALLEGL-ALNTQIhdLHLDLSACELRSVGA----QVIQDLVC 482
Cdd:cd00116    206 TDEGASALAETLAS----LKSLEVLNLGDNNLTDAGAAALASALlSPNISL--LTLSLSCNDITDDGAkdlaEVLAEKES 279

                          250       260
                   ....*....|....*....|...
gi 1039789755  483 dagaLSSLDLSDNGFGSDMVTLV 505
Cdd:cd00116    280 ----LLELDLRGNKFGEEGAQLL 298
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
339-633 8.93e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.56  E-value: 8.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  339 LTHLDLSGNPGalgpsqdsgglytfLSRPNVLAYLNLAGTDatLGTLFTALAGgcCSSLTHLEASRNIFSrmksqaapaA 418
Cdd:COG4886     98 LTELDLSGNEE--------------LSNLTNLESLDLSGNQ--LTDLPEELAN--LTNLKELDLSNNQLT---------D 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  419 LQRFLGGTRMLRHLGLAGCKLP--PEALRAL--LEGLAL-NTQIHDLHLDLSACElrsvgaqviqdlvcdagALSSLDLS 493
Cdd:COG4886    151 LPEPLGNLTNLKSLDLSNNQLTdlPEELGNLtnLKELDLsNNQITDLPEPLGNLT-----------------NLEELDLS 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  494 DNGFGSdmvtLVLAIGRSRSLKHVALGRNfnvrckeTLDDvLHRIAQLMQdddcpLQSLSVAESRLKQgasilIRALGTN 573
Cdd:COG4886    214 GNQLTD----LPEPLANLTNLETLDLSNN-------QLTD-LPELGNLTN-----LEELDLSNNQLTD-----LPPLANL 271

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  574 PKLTALDISGNAIGDAGAKMLAKALRVNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLK 633
Cdd:COG4886    272 TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLK 331
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 221-347 1.04e-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: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  221 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 300
Cdd:cd00116    140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789755  301 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 347
Cdd:cd00116    218 AS-LKSLEVLNLGDNNLTDAGAAALASALLSPNI---SLLTLSLSCN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
198-464 6.31e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.24  E-value: 6.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  198 DFSHFGSRDLALSVAALSyNLwfRRLSCEDMKLSlEVSEQILHMTSqssyLEELVLEACGLRGdfvrrLAQALAGhfNSG 277
Cdd:COG4886    119 DLSGNQLTDLPEELANLT-NL--KELDLSNNQLT-DLPEPLGNLTN----LKSLDLSNNQLTD-----LPEELGN--LTN 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  278 LRELSLSGNLLDDrgmaaLSRHLEHCPgALRRLSLAQTGLTprgmrALGRALATNatfdSTLTHLDLSGNPgalgpsqds 357
Cdd:COG4886    184 LKELDLSNNQITD-----LPEPLGNLT-NLEELDLSGNQLT-----DLPEPLANL----TNLETLDLSNNQ--------- 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  358 ggLYTF--LSRPNVLAYLNLAGTDatlgtlFTAL-AGGCCSSLTHLEASRNIFSRMKSQAAPAALQRFLGGTRMLRHLGL 434
Cdd:COG4886    240 --LTDLpeLGNLTNLEELDLSNNQ------LTDLpPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLL 311

                          250       260       270
                   ....*....|....*....|....*....|
gi 1039789755  435 AGCKLPPEALRALLEGLALNTQIHDLHLDL 464
Cdd:COG4886    312 ELLILLLLLTTLLLLLLLLKGLLVTLTTLA 341
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
573-599 7.97e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 7.97e-05
                            10        20
                    ....*....|....*....|....*..
gi 1039789755   573 NPKLTALDISGNAIGDAGAKMLAKALR 599
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
276-495 8.99e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.47  E-value: 8.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  276 SGLRELSLSGNLLDDrgmaaLSRHLEHCPgALRRLSLAQTGLTprgmrALGRALATNatfdSTLTHLDLSGN-----PGA 350
Cdd:COG4886    113 TNLESLDLSGNQLTD-----LPEELANLT-NLKELDLSNNQLT-----DLPEPLGNL----TNLKSLDLSNNqltdlPEE 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  351 LGPsqdsgglytfLSRpnvLAYLNLAGTDatLGTLFTALAGgcCSSLTHLEASRNIFSRMksqaaPAALQRFlggtRMLR 430
Cdd:COG4886    178 LGN----------LTN---LKELDLSNNQ--ITDLPEPLGN--LTNLEELDLSGNQLTDL-----PEPLANL----TNLE 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789755  431 HLGLAGCKLppEALRAL-----LEGLAL-NTQIHDL----------HLDLSACELRSVGAQVIQDLVCDAGALSSLDLSD 494
Cdd:COG4886    232 TLDLSNNQL--TDLPELgnltnLEELDLsNNQLTDLpplanltnlkTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309


                   .
gi 1039789755  495 N 495
Cdd:COG4886    310 L 310
LRR_6 pfam13516
Leucine Rich repeat;
572-595 9.51e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 9.51e-05
                           10        20
                   ....*....|....*....|....
gi 1039789755  572 TNPKLTALDISGNAIGDAGAKMLA 595
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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