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Conserved domains on  [gi|172045698|sp|Q3V3V9|]
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RecName: Full=Capping protein, Arp2/3 and myosin-I linker protein 2; AltName: Full=Capping protein regulator and myosin 1 linker 2; AltName: Full=F-actin-uncapping protein RLTPR; AltName: Full=Leucine-rich repeat-containing protein 16C; AltName: Full=RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein

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 ...
 752-1000 3.07e-47

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: 171.49  E-value: 3.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   752 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 826
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   827 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEE---------REKVLLRK-RNGTPSWQLRGKMQSRRL 895
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELEtpmatlkskRKSIHSRKlRPVSVAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   896 GRLHAVAEKHWAAGPRDTPASAVY------------------QRVDVCV----------------GWVPPALLQEGNGLT 941
Cdd:pfam16000  161 EEVPIHVEDASSGPPLPSSSPSEPelsasesldslselptegQKLQHLTkgrpkrnktraptrppGKVGPAQDGEQNGLS 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 172045698   942 ARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1000
Cdd:pfam16000  241 GRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 235-620 2.93e-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: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  235 QILHMTSQSSYLEELVLEACGLRGDFVR--RLAQALAGHFNSG--LRELSLSGNLLDDRGMRALGRALATNATfdstLTH 310
Cdd:COG5238   137 LPRRINLIQVLKDPLGGNAVHLLGLAARlgLLAAISMAKALQNnsVETVYLGCNQIGDEGIEELAEALTQNTT----VTT 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  311 LDLSGNPgaLGPSQDSGglytflsrpnvlaylnlagtdatlgtLFTALAGGccSSLTHLEASRNifsRMKSQAApAALQR 390
Cdd:COG5238   213 LWLKRNP--IGDEGAEI--------------------------LAEALKGN--KSLTTLDLSNN---QIGDEGV-IALAE 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  391 FLGGTRMLRHLGLAGCKLPPEALRALLEGLALNTQIHDLhlDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSdm 470
Cdd:COG5238   259 ALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL--DLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGA-- 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  471 vtlvlaigrsrslkhvalgrnfnvrcketlddvlhriaqlmqdddcplqslsvaesrlkQGASILIRALGTNPKLTALDI 550
Cdd:COG5238   335 -----------------------------------------------------------QGAIALAKALQENTTLHSLDL 355

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  551 SGNAIGDAGAKMLAKALRVNTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 620
Cdd:COG5238   356 SDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
Carm_PH super family cl39358
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.55e-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: 5.55e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 172045698    43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKKVFP 119
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKKIFP 94
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 964-1296 8.85e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  964 APEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRGPRPDLETSPGA-----AARARKSTLGDLLRPPArPGRGEEPGG 1038
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrrAARPTVGSLTSLADPPP-PPPTPEPAP 2712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1039 AEGGTSSPDPARRNRPRYTRESKAYSMILLPAEEEAAV--GTRPDKRRPLERGDTELAPSFEQRV--QVMLQRIGVSRAS 1114
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpgGPARPARPPTTAGPPAPAPPAAPAAgpPRRLTRPAVASLS 2792

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1115 GGAESKRKQSKDGEIKKAGSDGDIMDSSTETPPISIKSRTHSVSADPSCRPGPggqgpeSATWKTLGQQL--NAELRGRG 1192
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVapGGDVRRRP 2866

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1193 WGQQDGPGPPSPCPSPSPRRTSPAPDilSLPEDPCLGPRNEERPLRLQRSPVLKRRPKLEAPPSPSLGSGLGSKPLPPY- 1271
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVS--RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLa 2944

                         330       340
                  ....*....|....*....|....*
gi 172045698 1272 PTEPSSPERSPPSPATDQRGGGPNP 1296
Cdd:PHA03247 2945 PTTDPAGAGEPSGAVPQPWLGALVP 2969
 
Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 752-1000 3.07e-47

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: 171.49  E-value: 3.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   752 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 826
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   827 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEE---------REKVLLRK-RNGTPSWQLRGKMQSRRL 895
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELEtpmatlkskRKSIHSRKlRPVSVAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   896 GRLHAVAEKHWAAGPRDTPASAVY------------------QRVDVCV----------------GWVPPALLQEGNGLT 941
Cdd:pfam16000  161 EEVPIHVEDASSGPPLPSSSPSEPelsasesldslselptegQKLQHLTkgrpkrnktraptrppGKVGPAQDGEQNGLS 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 172045698   942 ARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1000
Cdd:pfam16000  241 GRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 235-620 2.93e-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: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  235 QILHMTSQSSYLEELVLEACGLRGDFVR--RLAQALAGHFNSG--LRELSLSGNLLDDRGMRALGRALATNATfdstLTH 310
Cdd:COG5238   137 LPRRINLIQVLKDPLGGNAVHLLGLAARlgLLAAISMAKALQNnsVETVYLGCNQIGDEGIEELAEALTQNTT----VTT 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  311 LDLSGNPgaLGPSQDSGglytflsrpnvlaylnlagtdatlgtLFTALAGGccSSLTHLEASRNifsRMKSQAApAALQR 390
Cdd:COG5238   213 LWLKRNP--IGDEGAEI--------------------------LAEALKGN--KSLTTLDLSNN---QIGDEGV-IALAE 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  391 FLGGTRMLRHLGLAGCKLPPEALRALLEGLALNTQIHDLhlDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSdm 470
Cdd:COG5238   259 ALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL--DLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGA-- 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  471 vtlvlaigrsrslkhvalgrnfnvrcketlddvlhriaqlmqdddcplqslsvaesrlkQGASILIRALGTNPKLTALDI 550
Cdd:COG5238   335 -----------------------------------------------------------QGAIALAKALQENTTLHSLDL 355

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  551 SGNAIGDAGAKMLAKALRVNTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 620
Cdd:COG5238   356 SDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 276-614 1.96e-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: 78.94  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  276 LRELSLSGNLLDDRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgglytflsrpnvlaylNLAGTDATLGTLF 355
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQ----PSLKELCLSLN--------------------------ETGRIPRGLQSLL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  356 TALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKLPPEALRALLEGLalntqihdlhldlsa 435
Cdd:cd00116    75 QGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLAKGL--------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  436 celrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVALGRNfnvrckETLDDVLHRIAQLMQDD 514
Cdd:cd00116   133 -----------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELNLANN------GIGDAGIRALAEGLKAN 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  515 dCPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALR-VNTRLRSVIWDRNNTSALGLLDVA 592
Cdd:cd00116   193 -CNLEVLDLNNNGLTdEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLsPNISLLTLSLSCNDITDDGAKDLA 271

                         330       340
                  ....*....|....*....|..
gi 172045698  593 QALEQNHSLKSMPLPLNDVTQA 614
Cdd:cd00116   272 EVLAEKESLLELDLRGNKFGEE 293
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.55e-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: 5.55e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 172045698    43 ILALLRWRAYLLHTCLPLRVDCTFSYLEVQAMALQeTPPRVTFELESLPeLVLEFPCVAALEQLAQHVAAAIKKVFP 119
Cdd:pfam17888   20 ILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSR-NPNQVIVETDKSN-YSLKLASEEDVDHVVGHILTALKKIFP 94
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
542-568 5.68e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 41.24  E-value: 5.68e-05
                            10        20
                    ....*....|....*....|....*..
gi 172045698    542 NPKLTALDISGNAIGDAGAKMLAKALR 568
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
541-564 7.19e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 7.19e-05
                           10        20
                   ....*....|....*....|....
gi 172045698   541 TNPKLTALDISGNAIGDAGAKMLA 564
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
PHA03247 PHA03247
large tegument protein UL36; Provisional
 964-1296 8.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  964 APEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRGPRPDLETSPGA-----AARARKSTLGDLLRPPArPGRGEEPGG 1038
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrrAARPTVGSLTSLADPPP-PPPTPEPAP 2712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1039 AEGGTSSPDPARRNRPRYTRESKAYSMILLPAEEEAAV--GTRPDKRRPLERGDTELAPSFEQRV--QVMLQRIGVSRAS 1114
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpgGPARPARPPTTAGPPAPAPPAAPAAgpPRRLTRPAVASLS 2792

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1115 GGAESKRKQSKDGEIKKAGSDGDIMDSSTETPPISIKSRTHSVSADPSCRPGPggqgpeSATWKTLGQQL--NAELRGRG 1192
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVapGGDVRRRP 2866

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1193 WGQQDGPGPPSPCPSPSPRRTSPAPDilSLPEDPCLGPRNEERPLRLQRSPVLKRRPKLEAPPSPSLGSGLGSKPLPPY- 1271
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVS--RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLa 2944

                         330       340
                  ....*....|....*....|....*
gi 172045698 1272 PTEPSSPERSPPSPATDQRGGGPNP 1296
Cdd:PHA03247 2945 PTTDPAGAGEPSGAVPQPWLGALVP 2969
 
Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 752-1000 3.07e-47

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: 171.49  E-value: 3.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   752 TRSLCPQMLQTPGWRKQLEGVLVGSGGLPELLPEH-----LLQDAFSRLRDMRLSITGTLAESIVAQALAGLHAARDRLV 826
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKStlleqAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   827 ERLTQQ-APVTMAPAVPPLGGNELSPLETGGLEELFFPTEKEEE---------REKVLLRK-RNGTPSWQLRGKMQSRRL 895
Cdd:pfam16000   81 RHLSQRgRTLLEPESLPDGDRPESSPLGPGKRHEGEIERLEELEtpmatlkskRKSIHSRKlRPVSVAFSVSELDLDKAP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698   896 GRLHAVAEKHWAAGPRDTPASAVY------------------QRVDVCV----------------GWVPPALLQEGNGLT 941
Cdd:pfam16000  161 EEVPIHVEDASSGPPLPSSSPSEPelsasesldslselptegQKLQHLTkgrpkrnktraptrppGKVGPAQDGEQNGLS 240

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 172045698   942 ARVDEGVEEFFSKRLIQQDHFWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRG 1000
Cdd:pfam16000  241 GRVDEGLEDFFSKKVIKLSTPTSPTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 235-620 2.93e-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: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  235 QILHMTSQSSYLEELVLEACGLRGDFVR--RLAQALAGHFNSG--LRELSLSGNLLDDRGMRALGRALATNATfdstLTH 310
Cdd:COG5238   137 LPRRINLIQVLKDPLGGNAVHLLGLAARlgLLAAISMAKALQNnsVETVYLGCNQIGDEGIEELAEALTQNTT----VTT 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  311 LDLSGNPgaLGPSQDSGglytflsrpnvlaylnlagtdatlgtLFTALAGGccSSLTHLEASRNifsRMKSQAApAALQR 390
Cdd:COG5238   213 LWLKRNP--IGDEGAEI--------------------------LAEALKGN--KSLTTLDLSNN---QIGDEGV-IALAE 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  391 FLGGTRMLRHLGLAGCKLPPEALRALLEGLALNTQIHDLhlDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGSdm 470
Cdd:COG5238   259 ALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL--DLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGA-- 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  471 vtlvlaigrsrslkhvalgrnfnvrcketlddvlhriaqlmqdddcplqslsvaesrlkQGASILIRALGTNPKLTALDI 550
Cdd:COG5238   335 -----------------------------------------------------------QGAIALAKALQENTTLHSLDL 355

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  551 SGNAIGDAGAKMLAKALRVNTRLRSVIWDRNNTSALGLLDVAQALEQNhSLKSMPLPLNDVTQAHRSRPE 620
Cdd:COG5238   356 SDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLE 424
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 230-469 8.58e-17

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 84.46  E-value: 8.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  230 LEVSEQILHMTSQSSYLEELVLEACGLRgdfvrRLAQALAGhfNSGLRELSLSGNLLDDRGMRALGRALATNATfdstLT 309
Cdd:COG5238   171 ISMAKALQNNSVETVYLGCNQIGDEGIE-----ELAEALTQ--NTTVTTLWLKRNPIGDEGAEILAEALKGNKS----LT 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  310 HLDLSGNPgaLGpsqDSG--GLYTFLSRPNVLAYLNLAG---TDATLGTLFTALAGGccSSLTHLEASRNifsRMKSQAA 384
Cdd:COG5238   240 TLDLSNNQ--IG---DEGviALAEALKNNTTVETLYLSGnqiGAEGAIALAKALQGN--TTLTSLDLSVN---RIGDEGA 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  385 pAALQRFLGGTRMLRHLGLAGCKLPPEALRALLEGLALNTQIHDlhLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDN 464
Cdd:COG5238   310 -IALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHS--LDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN 386


                  ....*
gi 172045698  465 GFGSD 469
Cdd:COG5238   387 NIGKQ 391
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 276-614 1.96e-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: 78.94  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  276 LRELSLSGNLLDDRGMRALGRALATNatfdSTLTHLDLSGNpgalgpsqdsgglytflsrpnvlaylNLAGTDATLGTLF 355
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQ----PSLKELCLSLN--------------------------ETGRIPRGLQSLL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  356 TALAGGCCssLTHLEASRNIFSrmksQAAPAALQRFLGGTrMLRHLGLAGCKLPPEALRALLEGLalntqihdlhldlsa 435
Cdd:cd00116    75 QGLTKGCG--LQELDLSDNALG----PDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLAKGL--------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  436 celrsvgaqviQDLVCdagALSSLDLSDNGFGSD-MVTLVLAIGRSRSLKHVALGRNfnvrckETLDDVLHRIAQLMQDD 514
Cdd:cd00116   133 -----------KDLPP---ALEKLVLGRNRLEGAsCEALAKALRANRDLKELNLANN------GIGDAGIRALAEGLKAN 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  515 dCPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALR-VNTRLRSVIWDRNNTSALGLLDVA 592
Cdd:cd00116   193 -CNLEVLDLNNNGLTdEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLsPNISLLTLSLSCNDITDDGAKDLA 271

                         330       340
                  ....*....|....*....|..
gi 172045698  593 QALEQNHSLKSMPLPLNDVTQA 614
Cdd:cd00116   272 EVLAEKESLLELDLRGNKFGEE 293
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 413-692 3.59e-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: 76.37  E-value: 3.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  413 LRALLEGLALNTQIHDLHLDLSACELrSVGAQVIQDLVCDAGALSSLDLSDNGFGSDMVT-LVLAIGRSRSLKHVALGRN 491
Cdd:COG5238   140 RINLIQVLKDPLGGNAVHLLGLAARL-GLLAAISMAKALQNNSVETVYLGCNQIGDEGIEeLAEALTQNTTVTTLWLKRN 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  492 fnvrckETLDDVLHRIAQLMQDDDcPLQSLSVAESRLK-QGASILIRALGTNPKLTALDISGNAIGDAGAKMLAKALRVN 570
Cdd:COG5238   219 ------PIGDEGAEILAEALKGNK-SLTTLDLSNNQIGdEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGN 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  571 TRLRSVIWDRNNTSALGLLDVAQALEQNHSLKSMPLPLNDVTQAhrsrpelttrAVHQIQACLWRNNQVdSTSDLKPclq 650
Cdd:COG5238   292 TTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQ----------GAIALAKALQENTTL-HSLDLSD--- 357

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 172045698  651 plGLISDHSeqeVNELCQSVQEHMELL-----GCGAGPQGEVAVHQA 692
Cdd:COG5238   358 --NQIGDEG---AIALAKYLEGNTTLRelnlgKNNIGKQGAEALIDA 399
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 43-119 5.55e-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: 5.55e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 172045698    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 ...
 246-578 1.10e-13

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: 73.54  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  246 LEELVLEACGLRGDFVRRLAQALagHFNSGLRELSLSGNLL--DDRGMRALGRALATNATfdstLTHLDLSGNpgALGPS 323
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASAL--RPQPSLKELCLSLNETgrIPRGLQSLLQGLTKGCG----LQELDLSDN--ALGPD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  324 QdSGGLYTFLSRPNV-LAYLNLAGTDATLGTLFTALAGGCCSSLTHLEASRNIFSRMKSQAAPAALQRflggTRMLRHLG 402
Cdd:cd00116    97 G-CGVLESLLRSSSLqELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRA----NRDLKELN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  403 LAGCKLPPEALRALLEGLALNTQIHdlHLDLSACELRSVGAQVIQDLVCDAGALSSLDLSDNGFGS-DMVTLVLAigrsr 481
Cdd:cd00116   172 LANNGIGDAGIRALAEGLKANCNLE--VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDaGAAALASA----- 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  482 sLKHVAlgrnfnvrcketlddvlhriaqlmqdddCPLQSLSVAESRLKQ-GASILIRALGTNPKLTALDISGNAIGDAGA 560
Cdd:cd00116   245 -LLSPN----------------------------ISLLTLSLSCNDITDdGAKDLAEVLAEKESLLELDLRGNKFGEEGA 295

                         330
                  ....*....|....*...
gi 172045698  561 KMLAKALRVNTRLRSVIW 578
Cdd:cd00116   296 QLLAESLLEPGNELESLW 313
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 396-614 1.42e-12

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 70.08  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  396 RMLRHLGLAGCKLPPEALRALLEglALNTQIHDLHLDLSACELRSVGAQViQDLVCDAGA---LSSLDLSDNGFGSDMVT 472
Cdd:cd00116    23 LCLQVLRLEGNTLGEEAAKALAS--ALRPQPSLKELCLSLNETGRIPRGL-QSLLQGLTKgcgLQELDLSDNALGPDGCG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  473 LVLAIGRSRSLKHVALGRNfnvrckETLDDVLHRIAQLMQDDDCPLQSLSVAESRLKQGASI-LIRALGTNPKLTALDIS 551
Cdd:cd00116   100 VLESLLRSSSLQELKLNNN------GLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEaLAKALRANRDLKELNLA 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 172045698  552 GNAIGDAGAKMLAKALRVNTRLRsVIWDRNNT-SALGLLDVAQALEQNHSLKSMPLPLNDVTQA 614
Cdd:cd00116   174 NNGIGDAGIRALAEGLKANCNLE-VLDLNNNGlTDEGASALAETLASLKSLEVLNLGDNNLTDA 236
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
308-602 2.50e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.10  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  308 LTHLDLSGNPGalgpsqdsgglytfLSRPNVLAYLNLAGTDatLGTLFTALAGgcCSSLTHLEASRNIFSrmksqaapaA 387
Cdd:COG4886    98 LTELDLSGNEE--------------LSNLTNLESLDLSGNQ--LTDLPEELAN--LTNLKELDLSNNQLT---------D 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  388 LQRFLGGTRMLRHLGLAGCKLP--PEALRAL--LEGLAL-NTQIHDLHLDLSACElrsvgaqviqdlvcdagALSSLDLS 462
Cdd:COG4886   151 LPEPLGNLTNLKSLDLSNNQLTdlPEELGNLtnLKELDLsNNQITDLPEPLGNLT-----------------NLEELDLS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  463 DNGFGSdmvtLVLAIGRSRSLKHVALGRNfnvrckeTLDDvLHRIAQLMQdddcpLQSLSVAESRLKQgasilIRALGTN 542
Cdd:COG4886   214 GNQLTD----LPEPLANLTNLETLDLSNN-------QLTD-LPELGNLTN-----LEELDLSNNQLTD-----LPPLANL 271

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  543 PKLTALDISGNAIGDAGAKMLAKALRVNTRLRSVIWDRNNTSALGLLDVAQALEQNHSLK 602
Cdd:COG4886   272 TNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLK 331
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 240-474 4.33e-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: 56.59  E-value: 4.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  240 TSQSSYLEELVLEACGLRGDFVRRLAQALaGHFNSGLRELSLSGNLLDDRGMRALGRALATNatfdSTLTHLDLSGNPga 319
Cdd:cd00116   104 LLRSSSLQELKLNNNGLGDRGLRLLAKGL-KDLPPALEKLVLGRNRLEGASCEALAKALRAN----RDLKELNLANNG-- 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  320 lgpsqdsgglytflsrpnvlayLNLAGTDAtlgtLFTALAGGCcsSLTHLEASRNIFSRMKSQAAPAALQRflggTRMLR 399
Cdd:cd00116   177 ----------------------IGDAGIRA----LAEGLKANC--NLEVLDLNNNGLTDEGASALAETLAS----LKSLE 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  400 HLGLAGCKLPPEALRALLEGL-ALNTQIhdLHLDLSACELRSVGA----QVIQDLVCdagaLSSLDLSDNGFGSDMVTLV 474
Cdd:cd00116   225 VLNLGDNNLTDAGAAALASALlSPNISL--LTLSLSCNDITDDGAkdlaEVLAEKES----LLELDLRGNKFGEEGAQLL 298
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 219-317 2.60e-06

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 50.82  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  219 RRLSCEDMKLSLEVSEQILHMTSQSSYLEELVLEACGLRGDFVRRLAQALAGhfNSGLRELSLSGNLLDDRGMRALGRAL 298
Cdd:cd00116   140 EKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA--NCNLEVLDLNNNGLTDEGASALAETL 217

                          90
                  ....*....|....*....
gi 172045698  299 ATNAtfdsTLTHLDLSGNP 317
Cdd:cd00116   218 ASLK----SLEVLNLGDNN 232
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
542-568 5.68e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 41.24  E-value: 5.68e-05
                            10        20
                    ....*....|....*....|....*..
gi 172045698    542 NPKLTALDISGNAIGDAGAKMLAKALR 568
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
LRR_6 pfam13516
Leucine Rich repeat;
541-564 7.19e-05

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 40.68  E-value: 7.19e-05
                           10        20
                   ....*....|....*....|....
gi 172045698   541 TNPKLTALDISGNAIGDAGAKMLA 564
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
196-449 6.36e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.77  E-value: 6.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  196 DFSHFGSRDLALSVAALSyNLwfRRLSCEDMKLSlEVSEQILHMTSqssyLEELVLEACGLRGdfvrrLAQALAGhfNSG 275
Cdd:COG4886   119 DLSGNQLTDLPEELANLT-NL--KELDLSNNQLT-DLPEPLGNLTN----LKSLDLSNNQLTD-----LPEELGN--LTN 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  276 LRELSLSGNLLDDrgmraLGRALATNatfdSTLTHLDLSGNP-GALGPSqdsgglytfLSRPNVLAYLNLAGTDatlgtl 354
Cdd:COG4886   184 LKELDLSNNQITD-----LPEPLGNL----TNLEELDLSGNQlTDLPEP---------LANLTNLETLDLSNNQ------ 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  355 FTALAG-GCCSSLTHLEASRNIFSRMKSqaapaalqrfLGGTRMLRHLGLAGCKLPPEALRALLEGLALNTQIHDLHLDL 433
Cdd:COG4886   240 LTDLPElGNLTNLEELDLSNNQLTDLPP----------LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLN 309

                         250
                  ....*....|....*.
gi 172045698  434 SACELRSVGAQVIQDL 449
Cdd:COG4886   310 LLELLILLLLLTTLLL 325
PHA03247 PHA03247
large tegument protein UL36; Provisional
 964-1296 8.85e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698  964 APEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRGPRPDLETSPGA-----AARARKSTLGDLLRPPArPGRGEEPGG 1038
Cdd:PHA03247 2634 AANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQrprrrAARPTVGSLTSLADPPP-PPPTPEPAP 2712

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1039 AEGGTSSPDPARRNRPRYTRESKAYSMILLPAEEEAAV--GTRPDKRRPLERGDTELAPSFEQRV--QVMLQRIGVSRAS 1114
Cdd:PHA03247 2713 HALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpgGPARPARPPTTAGPPAPAPPAAPAAgpPRRLTRPAVASLS 2792

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1115 GGAESKRKQSKDGEIKKAGSDGDIMDSSTETPPISIKSRTHSVSADPSCRPGPggqgpeSATWKTLGQQL--NAELRGRG 1192
Cdd:PHA03247 2793 ESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVapGGDVRRRP 2866

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 172045698 1193 WGQQDGPGPPSPCPSPSPRRTSPAPDilSLPEDPCLGPRNEERPLRLQRSPVLKRRPKLEAPPSPSLGSGLGSKPLPPY- 1271
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVS--RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLa 2944

                         330       340
                  ....*....|....*....|....*
gi 172045698 1272 PTEPSSPERSPPSPATDQRGGGPNP 1296
Cdd:PHA03247 2945 PTTDPAGAGEPSGAVPQPWLGALVP 2969
 
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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