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Conserved domains on  [gi|568956593|ref|XP_006530961|]
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capping protein, Arp2/3 and myosin-I linker protein 2 isoform X6 [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 ...
 781-1074 2.29e-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: 2.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   781 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 855
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   856 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 933
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   934 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1012
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956593  1013 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1074
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 297-649 2.47e-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: 92.55  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  297 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 368
Cdd:COG5238    96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  369 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 439
Cdd:COG5238   174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  440 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 519
Cdd:COG5238   251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  520 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 598
Cdd:COG5238   313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568956593  599 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 649
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 5.88e-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: 5.88e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956593    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 ...
 219-345 8.24e-08

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: 55.82  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  219 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 298
Cdd:cd00116   140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568956593  299 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 345
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 ...
 781-1074 2.29e-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: 2.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   781 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 855
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   856 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 933
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   934 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1012
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956593  1013 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1074
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 297-649 2.47e-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: 92.55  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  297 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 368
Cdd:COG5238    96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  369 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 439
Cdd:COG5238   174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  440 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 519
Cdd:COG5238   251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  520 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 598
Cdd:COG5238   313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568956593  599 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 649
Cdd:COG5238   375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 278-643 2.91e-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: 78.55  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  278 ELSLSGNLLDDRGMAALSRHLeHCPGALRrlsLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgg 357
Cdd:cd00116     2 QLSLKGELLKTERATELLPKL-LCLQVLR---LEGNTLGEEAAKALASALRPQ----PSLKELCLSLN------------ 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  358 lytflsrpnvlaylNLAGTDATLGTLFTALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKL 437
Cdd:cd00116    62 --------------ETGRIPRGLQSLLQGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  438 PPEALRALLEGLalntqihdlhldlsacelrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVA 516
Cdd:cd00116   121 GDRGLRLLAKGL--------------------------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELN 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  517 LGRNfnvrckETLDDVLHRIAQLMQDDdCPLQSLSVAESRL-KQGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKA 595
Cdd:cd00116   172 LANN------GIGDAGIRALAEGLKAN-CNLEVLDLNNNGLtDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568956593  596 LR-VNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQA 643
Cdd:cd00116   245 LLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.88e-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: 5.88e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956593    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 ...
 219-345 8.24e-08

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: 55.82  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  219 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 298
Cdd:cd00116   140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568956593  299 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 345
Cdd:cd00116   218 AS-LKSLEVLNLGDNNLTDAGAAALASALLSPNI---SLLTLSLSCN 260
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
571-597 7.30e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 7.30e-05
                            10        20
                    ....*....|....*....|....*..
gi 568956593    571 NPKLTALDISGNAIGDAGAKMLAKALR 597
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
570-593 8.63e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 8.63e-05
                           10        20
                   ....*....|....*....|....
gi 568956593   570 TNPKLTALDISGNAIGDAGAKMLA 593
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 ...
 781-1074 2.29e-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: 2.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   781 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 855
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   856 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 933
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593   934 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1012
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956593  1013 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1074
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 297-649 2.47e-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: 92.55  E-value: 2.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  297 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 368
Cdd:COG5238    96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  369 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 439
Cdd:COG5238   174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  440 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 519
Cdd:COG5238   251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  520 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 598
Cdd:COG5238   313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568956593  599 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 649
Cdd:COG5238   375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 278-643 2.91e-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: 78.55  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  278 ELSLSGNLLDDRGMAALSRHLeHCPGALRrlsLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgg 357
Cdd:cd00116     2 QLSLKGELLKTERATELLPKL-LCLQVLR---LEGNTLGEEAAKALASALRPQ----PSLKELCLSLN------------ 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  358 lytflsrpnvlaylNLAGTDATLGTLFTALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKL 437
Cdd:cd00116    62 --------------ETGRIPRGLQSLLQGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  438 PPEALRALLEGLalntqihdlhldlsacelrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVA 516
Cdd:cd00116   121 GDRGLRLLAKGL--------------------------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELN 171

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  517 LGRNfnvrckETLDDVLHRIAQLMQDDdCPLQSLSVAESRL-KQGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKA 595
Cdd:cd00116   172 LANN------GIGDAGIRALAEGLKAN-CNLEVLDLNNNGLtDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 568956593  596 LR-VNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQA 643
Cdd:cd00116   245 LLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 202-462 2.11e-14

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 77.14  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  202 SRDLALSVAALSYNLWFRRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSL 281
Cdd:COG5238   166 GLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG--NKSLTTLDL 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  282 SGNLLDDRGMAALSRHLEHcPGALRRLSLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGN----PGALgpsqdsgG 357
Cdd:COG5238   244 SNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGN----TTLTSLDLSVNrigdEGAI-------A 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  358 LYTFLSRPNVLAYLNLAG---TDATLGTLFTALAGGccSSLTHLEASRNifsRMKSQAApAALQRFLGGTRMLRHLGLAG 434
Cdd:COG5238   312 LAEGLQGNKTLHTLNLAYngiGAQGAIALAKALQEN--TTLHSLDLSDN---QIGDEGA-IALAKYLEGNTTLRELNLGK 385

                         250       260
                  ....*....|....*....|....*...
gi 568956593  435 CKLPPEALRALLEGLALNtQIHDLHLDL 462
Cdd:COG5238   386 NNIGKQGAEALIDALQTN-RLHTLILDG 412
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 276-607 2.32e-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: 75.85  E-value: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  276 LRELSLSGNLLDDRGMAALSRHLEHCPGALR-RLSLAQTGLTPRGMRALGRALATNATfdstLTHLDLSGNpgALGPSQd 354
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCG----LQELDLSDN--ALGPDG- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  355 SGGLYTFLSRPNV-LAYLNLAGTDATLGTLFTALAGGCCSSLTHLEASRNIFSRMKSQAAPAALQRflggTRMLRHLGLA 433
Cdd:cd00116    98 CGVLESLLRSSSLqELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA----NRDLKELNLA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  434 GCKLPPEALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGS-DMVTLVLAigrsrsL 512
Cdd:cd00116   174 NNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGAAALASA------L 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  513 KHVAlgrnfnvrcketlddvlhriaqlmqdddCPLQSLSVAESRLKQ-GASILIRALGTNPKLTALDISGNAIGDAGAKM 591
Cdd:cd00116   246 LSPN----------------------------ISLLTLSLSCNDITDdGAKDLAEVLAEKESLLELDLRGNKFGEEGAQL 297

                         330
                  ....*....|....*.
gi 568956593  592 LAKALRVNTRLRSVIW 607
Cdd:cd00116   298 LAESLLEPGNELESLW 313
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.88e-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: 5.88e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568956593    43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKKVFP 119
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKKIFP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 442-721 6.60e-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: 6.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  442 LRALLEGLALNTQIHDLHLDLSACELrSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVT-LVLAIGRSRSLKHVALGRN 520
Cdd:COG5238   140 RINLIQVLKDPLGGNAVHLLGLAARL-GLLAAISMAKALQNNSVETVYLGCNQIGDEGIEeLAEALTQNTTVTTLWLKRN 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  521 fnvrckETLDDVLHRIAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRVN 599
Cdd:COG5238   219 ------PIGDEGAEILAEALKGNK-SLTTLDLSNNQIGdEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGN 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  600 TRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQAhrsrpelttrAVHQIQACLWRNNQVdSTSDLKPclq 679
Cdd:COG5238   292 TTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQ----------GAIALAKALQENTTL-HSLDLSD--- 357

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 568956593  680 plGLISDHSeqeVNELCQSVQEHMELL-----GCGAGPQGEVAVHQA 721
Cdd:COG5238   358 --NQIGDEG---AIALAKYLEGNTTLRelnlgKNNIGKQGAEALIDA 399
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 246-503 1.30e-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: 61.22  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  246 LEELVLEACGLRGDFVRRLAQALAghfNSGLRELSLSGNLLDDRGMAALSRHLEHCPGALRRLSLAQTGLTPRGMRALGR 325
Cdd:cd00116    83 LQELDLSDNALGPDGCGVLESLLR---SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAK 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  326 ALATNatfdSTLTHLDLSGNPgalgpsqdsgglytflsrpnvlayLNLAGTDAtlgtLFTALAGGCcsSLTHLEASRNIF 405
Cdd:cd00116   160 ALRAN----RDLKELNLANNG------------------------IGDAGIRA----LAEGLKANC--NLEVLDLNNNGL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  406 SRMKSQAAPAALQRflggTRMLRHLGLAGCKLPPEALRALLEGL-ALNTQIhdLHLDLSACELRSVGA----QVIQDLVC 480
Cdd:cd00116   206 TDEGASALAETLAS----LKSLEVLNLGDNNLTDAGAAALASALlSPNISL--LTLSLSCNDITDDGAkdlaEVLAEKES 279

                         250       260
                  ....*....|....*....|...
gi 568956593  481 dagaLSSLDLSDNGFGSDMVTLV 503
Cdd:cd00116   280 ----LLELDLRGNKFGEEGAQLL 298
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
337-631 4.80e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.33  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  337 LTHLDLSGNPGalgpsqdsgglytfLSRPNVLAYLNLAGTDatLGTLFTALAGgcCSSLTHLEASRNIFSrmksqaapaA 416
Cdd:COG4886    98 LTELDLSGNEE--------------LSNLTNLESLDLSGNQ--LTDLPEELAN--LTNLKELDLSNNQLT---------D 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  417 LQRFLGGTRMLRHLGLAGCKLP--PEALRAL--LEGLAL-NTQIHDLHLDLSACElrsvgaqviqdlvcdagALSSLDLS 491
Cdd:COG4886   151 LPEPLGNLTNLKSLDLSNNQLTdlPEELGNLtnLKELDLsNNQITDLPEPLGNLT-----------------NLEELDLS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  492 DNGFGSdmvtLVLAIGRSRSLKHVALGRNfnvrckeTLDDvLHRIAQLMQdddcpLQSLSVAESRLKQgasilIRALGTN 571
Cdd:COG4886   214 GNQLTD----LPEPLANLTNLETLDLSNN-------QLTD-LPELGNLTN-----LEELDLSNNQLTD-----LPPLANL 271

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  572 PKLTALDISGNAIGDAGAKMLAKALRVNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLK 631
Cdd:COG4886   272 TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLK 331
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 219-345 8.24e-08

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: 55.82  E-value: 8.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  219 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 298
Cdd:cd00116   140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568956593  299 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 345
Cdd:cd00116   218 AS-LKSLEVLNLGDNNLTDAGAAALASALLSPNI---SLLTLSLSCN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
196-462 3.75e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.01  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  196 DFSHFGSRDLALSVAALSyNLwfRRLSCEDMKLSlEVSEQILHMTSqssyLEELVLEACGLRGdfvrrLAQALAGhfNSG 275
Cdd:COG4886   119 DLSGNQLTDLPEELANLT-NL--KELDLSNNQLT-DLPEPLGNLTN----LKSLDLSNNQLTD-----LPEELGN--LTN 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  276 LRELSLSGNLLDDrgmaaLSRHLEHCPgALRRLSLAQTGLTprgmrALGRALATNatfdSTLTHLDLSGNPgalgpsqds 355
Cdd:COG4886   184 LKELDLSNNQITD-----LPEPLGNLT-NLEELDLSGNQLT-----DLPEPLANL----TNLETLDLSNNQ--------- 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  356 ggLYTF--LSRPNVLAYLNLAGTDatlgtlFTAL-AGGCCSSLTHLEASRNIFSRMKSQAAPAALQRFLGGTRMLRHLGL 432
Cdd:COG4886   240 --LTDLpeLGNLTNLEELDLSNNQ------LTDLpPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLL 311

                         250       260       270
                  ....*....|....*....|....*....|
gi 568956593  433 AGCKLPPEALRALLEGLALNTQIHDLHLDL 462
Cdd:COG4886   312 ELLILLLLLTTLLLLLLLLKGLLVTLTTLA 341
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
274-493 5.16e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.24  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  274 SGLRELSLSGNLLDDrgmaaLSRHLEHCPgALRRLSLAQTGLTprgmrALGRALATNatfdSTLTHLDLSGN-----PGA 348
Cdd:COG4886   113 TNLESLDLSGNQLTD-----LPEELANLT-NLKELDLSNNQLT-----DLPEPLGNL----TNLKSLDLSNNqltdlPEE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  349 LGPsqdsgglytfLSRpnvLAYLNLAGTDatLGTLFTALAGgcCSSLTHLEASRNIFSRMksqaaPAALQRFlggtRMLR 428
Cdd:COG4886   178 LGN----------LTN---LKELDLSNNQ--ITDLPEPLGN--LTNLEELDLSGNQLTDL-----PEPLANL----TNLE 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956593  429 HLGLAGCKLppEALRAL-----LEGLAL-NTQIHDL----------HLDLSACELRSVGAQVIQDLVCDAGALSSLDLSD 492
Cdd:COG4886   232 TLDLSNNQL--TDLPELgnltnLEELDLsNNQLTDLpplanltnlkTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309


                  .
gi 568956593  493 N 493
Cdd:COG4886   310 L 310
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
571-597 7.30e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 7.30e-05
                            10        20
                    ....*....|....*....|....*..
gi 568956593    571 NPKLTALDISGNAIGDAGAKMLAKALR 597
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
570-593 8.63e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 8.63e-05
                           10        20
                   ....*....|....*....|....
gi 568956593   570 TNPKLTALDISGNAIGDAGAKMLA 593
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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