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Conserved domains on  [gi|1039789752|ref|XP_017168229|]
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capping protein, Arp2/3 and myosin-I linker protein 2 isoform X3 [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 ...
 772-1065 2.98e-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: 191.91  E-value: 2.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  772 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 846
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  847 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 924
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  925 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1003
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039789752 1004 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1065
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 288-640 8.18e-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: 91.00  E-value: 8.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  288 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 359
Cdd:COG5238     96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  360 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 430
Cdd:COG5238    174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  431 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 510
Cdd:COG5238    251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  511 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 589
Cdd:COG5238    313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039789752  590 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 640
Cdd:COG5238    375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
Carm_PH super family cl39358
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-116 2.50e-11

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: 61.14  E-value: 2.50e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039789752   43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKK 116
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKK 91
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 210-336 1.08e-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: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  210 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 289
Cdd:cd00116    140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789752  290 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 336
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 ...
 772-1065 2.98e-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: 191.91  E-value: 2.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  772 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 846
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  847 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 924
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  925 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1003
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039789752 1004 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1065
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 288-640 8.18e-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: 91.00  E-value: 8.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  288 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 359
Cdd:COG5238     96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  360 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 430
Cdd:COG5238    174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  431 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 510
Cdd:COG5238    251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  511 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 589
Cdd:COG5238    313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039789752  590 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 640
Cdd:COG5238    375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 269-634 5.63e-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: 5.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  269 ELSLSGNLLDDRGMAALSRHLeHCPGALRrlsLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgg 348
Cdd:cd00116      2 QLSLKGELLKTERATELLPKL-LCLQVLR---LEGNTLGEEAAKALASALRPQ----PSLKELCLSLN------------ 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  349 lytflsrpnvlaylNLAGTDATLGTLFTALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKL 428
Cdd:cd00116     62 --------------ETGRIPRGLQSLLQGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGL 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  429 PPEALRALLEGLalntqihdlhldlsacelrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVA 507
Cdd:cd00116    121 GDRGLRLLAKGL--------------------------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELN 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  508 LGRNfnvrckETLDDVLHRIAQLMQDDdCPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKA 586
Cdd:cd00116    172 LANN------GIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTdEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1039789752  587 LR-VNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQA 634
Cdd:cd00116    245 LLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-116 2.50e-11

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: 61.14  E-value: 2.50e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039789752   43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKK 116
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKK 91
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 210-336 1.08e-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: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  210 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 289
Cdd:cd00116    140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789752  290 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 336
Cdd:cd00116    218 AS-LKSLEVLNLGDNNLTDAGAAALASALLSPNI---SLLTLSLSCN 260
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
562-588 8.30e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 8.30e-05
                            10        20
                    ....*....|....*....|....*..
gi 1039789752   562 NPKLTALDISGNAIGDAGAKMLAKALR 588
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
561-584 1.01e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.30  E-value: 1.01e-04
                           10        20
                   ....*....|....*....|....
gi 1039789752  561 TNPKLTALDISGNAIGDAGAKMLA 584
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 ...
 772-1065 2.98e-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: 191.91  E-value: 2.98e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  772 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 846
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  847 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEEREKDESSSWKWLEPSNCFHLVS-SLHGAAEEAERDP 924
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELETPMATLKSKRKSIHSRKLRPVSvAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  925 ELA-APGEDAEPQAgPSARGSPSPAAPGPPAGPLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQVppALLQEGN 1003
Cdd:pfam16000  161 EEVpIHVEDASSGP-PLPSSSPSEPELSASESLDSLSELPTEGQKLQHLTKGRPKRNKTRAPTRPPGKVGP--AQDGEQN 237

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039789752 1004 GLTARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1065
Cdd:pfam16000  238 GLSGRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 288-640 8.18e-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: 91.00  E-value: 8.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  288 HLEHC-PGALRRLSLAQTGLTPRGMRALGRALAtnATFDSTLTHLDLSGNP-----GALGPSQDSGGLYTFLSRPNVL-- 359
Cdd:COG5238     96 GAEEVsPVALAETATAVATPPPDLRRIMAKTLE--DSLILYLALPRRINLIqvlkdPLGGNAVHLLGLAARLGLLAAIsm 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  360 --AYLNLAGTDATLGTLFTALAGgcCSSLT-HLEASRNI----FSR--MKSQAAPAALQRFLGGTRmLRHLGLAGCKLPP 430
Cdd:COG5238    174 akALQNNSVETVYLGCNQIGDEG--IEELAeALTQNTTVttlwLKRnpIGDEGAEILAEALKGNKS-LTTLDLSNNQIGD 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  431 EALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVtlvlaigrsrslkhVALgr 510
Cdd:COG5238    251 EGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGA--------------IAL-- 312

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  511 nfnvrcketlddvlhriAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRV 589
Cdd:COG5238    313 -----------------AEGLQGNK-TLHTLNLAYNGIGaQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039789752  590 NTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 640
Cdd:COG5238    375 NTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 269-634 5.63e-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: 5.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  269 ELSLSGNLLDDRGMAALSRHLeHCPGALRrlsLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgg 348
Cdd:cd00116      2 QLSLKGELLKTERATELLPKL-LCLQVLR---LEGNTLGEEAAKALASALRPQ----PSLKELCLSLN------------ 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  349 lytflsrpnvlaylNLAGTDATLGTLFTALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKL 428
Cdd:cd00116     62 --------------ETGRIPRGLQSLLQGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGL 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  429 PPEALRALLEGLalntqihdlhldlsacelrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVA 507
Cdd:cd00116    121 GDRGLRLLAKGL--------------------------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELN 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  508 LGRNfnvrckETLDDVLHRIAQLMQDDdCPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKA 586
Cdd:cd00116    172 LANN------GIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTdEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASA 244

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1039789752  587 LR-VNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQA 634
Cdd:cd00116    245 LLsPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEE 293
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 267-598 3.63e-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: 75.08  E-value: 3.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  267 LRELSLSGNLLDDRGMAALSRHLEHCPGALR-RLSLAQTGLTPRGMRALGRALATNATfdstLTHLDLSGNpgALGPSQd 345
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKElCLSLNETGRIPRGLQSLLQGLTKGCG----LQELDLSDN--ALGPDG- 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  346 SGGLYTFLSRPNV-LAYLNLAGTDATLGTLFTALAGGCCSSLTHLEASRNIFSRMKSQAAPAALQRflggTRMLRHLGLA 424
Cdd:cd00116     98 CGVLESLLRSSSLqELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA----NRDLKELNLA 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  425 GCKLPPEALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGS-DMVTLVLAigrsrsL 503
Cdd:cd00116    174 NNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGAAALASA------L 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  504 KHVAlgrnfnvrcketlddvlhriaqlmqdddCPLQSLSVAESRLKQ-GASILIRALGTNPKLTALDISGNAIGDAGAKM 582
Cdd:cd00116    246 LSPN----------------------------ISLLTLSLSCNDITDdGAKDLAEVLAEKESLLELDLRGNKFGEEGAQL 297

                          330
                   ....*....|....*.
gi 1039789752  583 LAKALRVNTRLRSVIW 598
Cdd:cd00116    298 LAESLLEPGNELESLW 313
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 193-453 4.75e-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: 75.98  E-value: 4.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  193 SRDLALSVAALSYNLWFRRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSL 272
Cdd:COG5238    166 GLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG--NKSLTTLDL 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  273 SGNLLDDRGMAALSRHLEHcPGALRRLSLAQTGLTPRGMRALGRALATNatfdSTLTHLDLSGN----PGALgpsqdsgG 348
Cdd:COG5238    244 SNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGN----TTLTSLDLSVNrigdEGAI-------A 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  349 LYTFLSRPNVLAYLNLAG---TDATLGTLFTALAGGccSSLTHLEASRNifsRMKSQAApAALQRFLGGTRMLRHLGLAG 425
Cdd:COG5238    312 LAEGLQGNKTLHTLNLAYngiGAQGAIALAKALQEN--TTLHSLDLSDN---QIGDEGA-IALAKYLEGNTTLRELNLGK 385

                          250       260
                   ....*....|....*....|....*...
gi 1039789752  426 CKLPPEALRALLEGLALNtQIHDLHLDL 453
Cdd:COG5238    386 NNIGKQGAEALIDALQTN-RLHTLILDG 412
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 433-712 1.40e-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: 74.83  E-value: 1.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  433 LRALLEGLALNTQIHDLHLDLSACELrSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVT-LVLAIGRSRSLKHVALGRN 511
Cdd:COG5238    140 RINLIQVLKDPLGGNAVHLLGLAARL-GLLAAISMAKALQNNSVETVYLGCNQIGDEGIEeLAEALTQNTTVTTLWLKRN 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  512 fnvrckETLDDVLHRIAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRVN 590
Cdd:COG5238    219 ------PIGDEGAEILAEALKGNK-SLTTLDLSNNQIGdEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGN 291

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  591 TRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQAhrsrpelttrAVHQIQACLWRNNQVdSTSDLKPclq 670
Cdd:COG5238    292 TTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQ----------GAIALAKALQENTTL-HSLDLSD--- 357

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789752  671 plGLISDHSeqeVNELCQSVQEHMELL-----GCGAGPQGEVAVHQA 712
Cdd:COG5238    358 --NQIGDEG---AIALAKYLEGNTTLRelnlgKNNIGKQGAEALIDA 399
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-116 2.50e-11

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: 61.14  E-value: 2.50e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039789752   43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKK 116
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKK 91
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 237-494 2.01e-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: 2.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  237 LEELVLEACGLRGDFVRRLAQALAghfNSGLRELSLSGNLLDDRGMAALSRHLEHCPGALRRLSLAQTGLTPRGMRALGR 316
Cdd:cd00116     83 LQELDLSDNALGPDGCGVLESLLR---SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAK 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  317 ALATNatfdSTLTHLDLSGNPgalgpsqdsgglytflsrpnvlayLNLAGTDAtlgtLFTALAGGCcsSLTHLEASRNIF 396
Cdd:cd00116    160 ALRAN----RDLKELNLANNG------------------------IGDAGIRA----LAEGLKANC--NLEVLDLNNNGL 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  397 SRMKSQAAPAALQRflggTRMLRHLGLAGCKLPPEALRALLEGL-ALNTQIhdLHLDLSACELRSVGA----QVIQDLVC 471
Cdd:cd00116    206 TDEGASALAETLAS----LKSLEVLNLGDNNLTDAGAAALASALlSPNISL--LTLSLSCNDITDDGAkdlaEVLAEKES 279

                          250       260
                   ....*....|....*....|...
gi 1039789752  472 dagaLSSLDLSDNGFGSDMVTLV 494
Cdd:cd00116    280 ----LLELDLRGNKFGEEGAQLL 298
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
328-622 6.17e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.95  E-value: 6.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  328 LTHLDLSGNPGalgpsqdsgglytfLSRPNVLAYLNLAGTDatLGTLFTALAGgcCSSLTHLEASRNIFSrmksqaapaA 407
Cdd:COG4886     98 LTELDLSGNEE--------------LSNLTNLESLDLSGNQ--LTDLPEELAN--LTNLKELDLSNNQLT---------D 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  408 LQRFLGGTRMLRHLGLAGCKLP--PEALRAL--LEGLAL-NTQIHDLHLDLSACElrsvgaqviqdlvcdagALSSLDLS 482
Cdd:COG4886    151 LPEPLGNLTNLKSLDLSNNQLTdlPEELGNLtnLKELDLsNNQITDLPEPLGNLT-----------------NLEELDLS 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  483 DNGFGSdmvtLVLAIGRSRSLKHVALGRNfnvrckeTLDDvLHRIAQLMQdddcpLQSLSVAESRLKQgasilIRALGTN 562
Cdd:COG4886    214 GNQLTD----LPEPLANLTNLETLDLSNN-------QLTD-LPELGNLTN-----LEELDLSNNQLTD-----LPPLANL 271

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  563 PKLTALDISGNAIGDAGAKMLAKALRVNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLK 622
Cdd:COG4886    272 TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLK 331
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 210-336 1.08e-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: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  210 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMAALSRHL 289
Cdd:cd00116    140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039789752  290 EHcPGALRRLSLAQTGLTPRGMRALGRALATNATfdsTLTHLDLSGN 336
Cdd:cd00116    218 AS-LKSLEVLNLGDNNLTDAGAAALASALLSPNI---SLLTLSLSCN 260
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
187-453 4.56e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.62  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  187 DFSHFGSRDLALSVAALSyNLwfRRLSCEDMKLSlEVSEQILHMTSqssyLEELVLEACGLRGdfvrrLAQALAGhfNSG 266
Cdd:COG4886    119 DLSGNQLTDLPEELANLT-NL--KELDLSNNQLT-DLPEPLGNLTN----LKSLDLSNNQLTD-----LPEELGN--LTN 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  267 LRELSLSGNLLDDrgmaaLSRHLEHCPgALRRLSLAQTGLTprgmrALGRALATNatfdSTLTHLDLSGNPgalgpsqds 346
Cdd:COG4886    184 LKELDLSNNQITD-----LPEPLGNLT-NLEELDLSGNQLT-----DLPEPLANL----TNLETLDLSNNQ--------- 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  347 ggLYTF--LSRPNVLAYLNLAGTDatlgtlFTAL-AGGCCSSLTHLEASRNIFSRMKSQAAPAALQRFLGGTRMLRHLGL 423
Cdd:COG4886    240 --LTDLpeLGNLTNLEELDLSNNQ------LTDLpPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLL 311

                          250       260       270
                   ....*....|....*....|....*....|
gi 1039789752  424 AGCKLPPEALRALLEGLALNTQIHDLHLDL 453
Cdd:COG4886    312 ELLILLLLLTTLLLLLLLLKGLLVTLTTLA 341
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
265-484 6.73e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 6.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  265 SGLRELSLSGNLLDDrgmaaLSRHLEHCPgALRRLSLAQTGLTprgmrALGRALATNatfdSTLTHLDLSGN-----PGA 339
Cdd:COG4886    113 TNLESLDLSGNQLTD-----LPEELANLT-NLKELDLSNNQLT-----DLPEPLGNL----TNLKSLDLSNNqltdlPEE 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  340 LGPsqdsgglytfLSRpnvLAYLNLAGTDatLGTLFTALAGgcCSSLTHLEASRNIFSRMksqaaPAALQRFlggtRMLR 419
Cdd:COG4886    178 LGN----------LTN---LKELDLSNNQ--ITDLPEPLGN--LTNLEELDLSGNQLTDL-----PEPLANL----TNLE 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039789752  420 HLGLAGCKLppEALRAL-----LEGLAL-NTQIHDL----------HLDLSACELRSVGAQVIQDLVCDAGALSSLDLSD 483
Cdd:COG4886    232 TLDLSNNQL--TDLPELgnltnLEELDLsNNQLTDLpplanltnlkTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309


                   .
gi 1039789752  484 N 484
Cdd:COG4886    310 L 310
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
562-588 8.30e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 8.30e-05
                            10        20
                    ....*....|....*....|....*..
gi 1039789752   562 NPKLTALDISGNAIGDAGAKMLAKALR 588
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
561-584 1.01e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.30  E-value: 1.01e-04
                           10        20
                   ....*....|....*....|....
gi 1039789752  561 TNPKLTALDISGNAIGDAGAKMLA 584
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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