NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|830197378|ref|XP_012588408|]
View 

PREDICTED: leucine-rich repeat-containing protein 16A isoform X2 [Condylura cristata]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 786-1077 5.32e-120

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: 376.80  E-value: 5.32e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   786 AESLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSNCHHKLA 865
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   866 DHFSRRGKALPQHESL-EIELAEEKPVKRSVITMEeltEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEM-EFDLD 943
Cdd:pfam16000   81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPMATLKSKRKSIHSRKLRPVSVAFSVsELDLD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   944 KALEEVPIHIED----PPFPSTRQEK------RSSGFISELPSeEGRKLEHFTKLRPKRNKKQQPTQAAVRavSIISQDG 1013
Cdd:pfam16000  158 KAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGK--VGPAQDG 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 830197378  1014 EQNGLMGRVDEGVDEFFTKKVTKMDSKRSagRGSECHELGEGGDEKKKRDSRKSAFLNLIKSRS 1077
Cdd:pfam16000  235 EQNGLSGRVDEGLEDFFSKKVIKLSTPTS--PTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRS 296
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 38-119 1.89e-34

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: 127.40  E-value: 1.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378    38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVLCSKSAQMVVETEKCSICMKMASPEDVNDVLAHIGTCLRRI 117
Cdd:pfam17888   13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92


                   ..
gi 830197378   118 FP 119
Cdd:pfam17888   93 FP 94
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 429-658 1.09e-17

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: 87.54  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  429 INLSGTKLSPEPLKALLLGLACNHNLKGvsLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSK 507
Cdd:COG5238   185 VYLGCNQIGDEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  508 NRSIQHLALGKN---------FNNM--KSKNLTPVLDNLVQmIQDE-----------ESPLQSLSLADSKLKTEVTI-II 564
Cdd:COG5238   263 NTTVETLYLSGNqigaegaiaLAKAlqGNTTLTSLDLSVNR-IGDEgaialaeglqgNKTLHTLNLAYNGIGAQGAIaLA 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  565 NALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVALEKN--YTLRFMPIPMYDASQA 642
Cdd:COG5238   342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ 421

                         250
                  ....*....|....*.
gi 830197378  643 lktnpeKTEEALQKIE 658
Cdd:COG5238   422 ------RLEQLLERIK 431
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 223-595 1.34e-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: 58.14  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  223 LSSKDLKLSTDVCEQILRVVSRsnrLEELVLENAGLRADFAQKLASALAHNPNSG---FHTINLAGNPledRGVSSLSIQ 299
Cdd:cd00116     3 LSLKGELLKTERATELLPKLLC---LQVLRLEGNTLGEEAAKALASALRPQPSLKelcLSLNETGRIP---RGLQSLLQG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  300 FAKLPKgLKHLNLSKTSLSPKGVNSLSqslsanlltattlthldlsgNILRGDDLsymysflaqpnaiAHLDLSNteCSL 379
Cdd:cd00116    77 LTKGCG-LQELDLSDNALGPDGCGVLE--------------------SLLRSSSL-------------QELKLNN--NGL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  380 DMVCGALLRGCLQYLAvLNVSRTVFSHRKgKEVPPSFK--QFFSSSLALMQINLSGTKLSPEPLKALLLGLACNHNLKgv 457
Cdd:cd00116   121 GDRGLRLLAKGLKDLP-PALEKLVLGRNR-LEGASCEAlaKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLE-- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  458 SLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKNRSIQHLALGknfnnMKSKNLTpvldnlvq 537
Cdd:cd00116   197 VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL------------TDAGAAALASA-----LLSPNIS-------- 251

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 830197378  538 miqdeespLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKAL 595
Cdd:cd00116   252 --------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1062-1327 1.40e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1062 RDSRKSAFLNLIKSRSKAERPPTVLITEEPSSPKGAVRSPAMDIPRKDTKPAEHNSSSERTEEVKTPDSLEEGQGEDmgk 1141
Cdd:pfam03154   44 RNSPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREKGASDTEEPERATAKKSKTQEISRPNSPSEGEGES--- 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1142 ldrSDSRSspqggrrygVQVMGSGLMAEMKAKQEKRAACAQKKLGNETISQDSSSLTLSSTERP----DGGGAVPKLHPG 1217
Cdd:pfam03154  121 ---SDGRS---------VNDEGSSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPvlqaQSGAASPPSPPP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1218 LPESRFSVGTPEKNAKVESRVEVGSRSRSPSGTLTSSKP--LLQS---------PKPSLAARPTIPQKPRSTSRPEDLPD 1286
Cdd:pfam03154  189 PGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhtLIQQtptlhpqrlPSPHPPLQPMTQPPPPSQVSPQPLPQ 268

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 830197378  1287 SPSGPSspkvalLPPL---LKKVPSDKERDGQHSPQPNPRTFSQ 1327
Cdd:pfam03154  269 PSLHGQ------MPPMphsLQTGPSHMQHPVPPQPFPLTPQSSQ 306
 
Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 786-1077 5.32e-120

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: 376.80  E-value: 5.32e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   786 AESLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSNCHHKLA 865
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   866 DHFSRRGKALPQHESL-EIELAEEKPVKRSVITMEeltEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEM-EFDLD 943
Cdd:pfam16000   81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPMATLKSKRKSIHSRKLRPVSVAFSVsELDLD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   944 KALEEVPIHIED----PPFPSTRQEK------RSSGFISELPSeEGRKLEHFTKLRPKRNKKQQPTQAAVRavSIISQDG 1013
Cdd:pfam16000  158 KAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGK--VGPAQDG 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 830197378  1014 EQNGLMGRVDEGVDEFFTKKVTKMDSKRSagRGSECHELGEGGDEKKKRDSRKSAFLNLIKSRS 1077
Cdd:pfam16000  235 EQNGLSGRVDEGLEDFFSKKVIKLSTPTS--PTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRS 296
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 38-119 1.89e-34

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: 127.40  E-value: 1.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378    38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVLCSKSAQMVVETEKCSICMKMASPEDVNDVLAHIGTCLRRI 117
Cdd:pfam17888   13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92


                   ..
gi 830197378   118 FP 119
Cdd:pfam17888   93 FP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 429-658 1.09e-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: 87.54  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  429 INLSGTKLSPEPLKALLLGLACNHNLKGvsLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSK 507
Cdd:COG5238   185 VYLGCNQIGDEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  508 NRSIQHLALGKN---------FNNM--KSKNLTPVLDNLVQmIQDE-----------ESPLQSLSLADSKLKTEVTI-II 564
Cdd:COG5238   263 NTTVETLYLSGNqigaegaiaLAKAlqGNTTLTSLDLSVNR-IGDEgaialaeglqgNKTLHTLNLAYNGIGAQGAIaLA 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  565 NALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVALEKN--YTLRFMPIPMYDASQA 642
Cdd:COG5238   342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ 421

                         250
                  ....*....|....*.
gi 830197378  643 lktnpeKTEEALQKIE 658
Cdd:COG5238   422 ------RLEQLLERIK 431
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 417-630 2.48e-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: 60.45  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  417 KQFFSSSLALMQINLSGTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELRSGGAQV---LEGCIAeIHNITSLDISDNG 493
Cdd:cd00116    16 TELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLK--ELCLSLNETGRIPRGLqslLQGLTK-GCGLQELDLSDNA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  494 LESDLSTLIVWLSKNRSIQHL-----ALGKNFNNMKSKNLTPVldnlvqmiqdeESPLQSLSLADSKLKTEVTI-IINAL 567
Cdd:cd00116    93 LGPDGCGVLESLLRSSSLQELklnnnGLGDRGLRLLAKGLKDL-----------PPALEKLVLGRNRLEGASCEaLAKAL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 830197378  568 GSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVALEKNYTLR 630
Cdd:cd00116   162 RANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLE 224
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 223-595 1.34e-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: 58.14  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  223 LSSKDLKLSTDVCEQILRVVSRsnrLEELVLENAGLRADFAQKLASALAHNPNSG---FHTINLAGNPledRGVSSLSIQ 299
Cdd:cd00116     3 LSLKGELLKTERATELLPKLLC---LQVLRLEGNTLGEEAAKALASALRPQPSLKelcLSLNETGRIP---RGLQSLLQG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  300 FAKLPKgLKHLNLSKTSLSPKGVNSLSqslsanlltattlthldlsgNILRGDDLsymysflaqpnaiAHLDLSNteCSL 379
Cdd:cd00116    77 LTKGCG-LQELDLSDNALGPDGCGVLE--------------------SLLRSSSL-------------QELKLNN--NGL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  380 DMVCGALLRGCLQYLAvLNVSRTVFSHRKgKEVPPSFK--QFFSSSLALMQINLSGTKLSPEPLKALLLGLACNHNLKgv 457
Cdd:cd00116   121 GDRGLRLLAKGLKDLP-PALEKLVLGRNR-LEGASCEAlaKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLE-- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  458 SLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKNRSIQHLALGknfnnMKSKNLTpvldnlvq 537
Cdd:cd00116   197 VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL------------TDAGAAALASA-----LLSPNIS-------- 251

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 830197378  538 miqdeespLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKAL 595
Cdd:cd00116   252 --------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 244-332 7.19e-08

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: 56.72  E-value: 7.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  244 RSNRLEELVLENAGLRADFAQKLASALAHNPNsgFHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVN 323
Cdd:COG5238   318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIAL-AKYLEGNTTLRELNLGKNNIGKQGAE 394


                  ....*....
gi 830197378  324 SLSQSLSAN 332
Cdd:COG5238   395 ALIDALQTN 403
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1062-1327 1.40e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1062 RDSRKSAFLNLIKSRSKAERPPTVLITEEPSSPKGAVRSPAMDIPRKDTKPAEHNSSSERTEEVKTPDSLEEGQGEDmgk 1141
Cdd:pfam03154   44 RNSPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREKGASDTEEPERATAKKSKTQEISRPNSPSEGEGES--- 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1142 ldrSDSRSspqggrrygVQVMGSGLMAEMKAKQEKRAACAQKKLGNETISQDSSSLTLSSTERP----DGGGAVPKLHPG 1217
Cdd:pfam03154  121 ---SDGRS---------VNDEGSSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPvlqaQSGAASPPSPPP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1218 LPESRFSVGTPEKNAKVESRVEVGSRSRSPSGTLTSSKP--LLQS---------PKPSLAARPTIPQKPRSTSRPEDLPD 1286
Cdd:pfam03154  189 PGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhtLIQQtptlhpqrlPSPHPPLQPMTQPPPPSQVSPQPLPQ 268

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 830197378  1287 SPSGPSspkvalLPPL---LKKVPSDKERDGQHSPQPNPRTFSQ 1327
Cdd:pfam03154  269 PSLHGQ------MPPMphsLQTGPSHMQHPVPPQPFPLTPQSSQ 306
 
Name Accession Description Interval E-value
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 786-1077 5.32e-120

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: 376.80  E-value: 5.32e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   786 AESLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSNCHHKLA 865
Cdd:pfam16000    1 AESLCPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLLEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   866 DHFSRRGKALPQHESL-EIELAEEKPVKRSVITMEeltEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEM-EFDLD 943
Cdd:pfam16000   81 RHLSQRGRTLLEPESLpDGDRPESSPLGPGKRHEG---EIERLEELETPMATLKSKRKSIHSRKLRPVSVAFSVsELDLD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378   944 KALEEVPIHIED----PPFPSTRQEK------RSSGFISELPSeEGRKLEHFTKLRPKRNKKQQPTQAAVRavSIISQDG 1013
Cdd:pfam16000  158 KAPEEVPIHVEDassgPPLPSSSPSEpelsasESLDSLSELPT-EGQKLQHLTKGRPKRNKTRAPTRPPGK--VGPAQDG 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 830197378  1014 EQNGLMGRVDEGVDEFFTKKVTKMDSKRSagRGSECHELGEGGDEKKKRDSRKSAFLNLIKSRS 1077
Cdd:pfam16000  235 EQNGLSGRVDEGLEDFFSKKVIKLSTPTS--PTSEPSSSSLFPDSPKKRKKRKSGFFNFIKPRS 296
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 38-119 1.89e-34

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: 127.40  E-value: 1.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378    38 GDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVLCSKSAQMVVETEKCSICMKMASPEDVNDVLAHIGTCLRRI 117
Cdd:pfam17888   13 GDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDHVVGHILTALKKI 92


                   ..
gi 830197378   118 FP 119
Cdd:pfam17888   93 FP 94
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 429-658 1.09e-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: 87.54  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  429 INLSGTKLSPEPLKALLLGLACNHNLKGvsLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSK 507
Cdd:COG5238   185 VYLGCNQIGDEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  508 NRSIQHLALGKN---------FNNM--KSKNLTPVLDNLVQmIQDE-----------ESPLQSLSLADSKLKTEVTI-II 564
Cdd:COG5238   263 NTTVETLYLSGNqigaegaiaLAKAlqGNTTLTSLDLSVNR-IGDEgaialaeglqgNKTLHTLNLAYNGIGAQGAIaLA 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  565 NALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVALEKN--YTLRFMPIPMYDASQA 642
Cdd:COG5238   342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNrlHTLILDGNLIGAEAQQ 421

                         250
                  ....*....|....*.
gi 830197378  643 lktnpeKTEEALQKIE 658
Cdd:COG5238   422 ------RLEQLLERIK 431
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 441-651 9.27e-15

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: 78.29  E-value: 9.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  441 LKALLLGLACNHNLKGV------SLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGL-ESDLSTLIVWLSKNRSIQH 513
Cdd:COG5238   161 LAARLGLLAAISMAKALqnnsveTVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIgDEGAEILAEALKGNKSLTT 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  514 LALGKNfnNMKSKNLTPVLDNLvqmiqDEESPLQSLSLADSKLKTEVTI-IINALGSNTSLTKVDISGNGMGDMGAKMLA 592
Cdd:COG5238   241 LDLSNN--QIGDEGVIALAEAL-----KNNTTVETLYLSGNQIGAEGAIaLAKALQGNTTLTSLDLSVNRIGDEGAIALA 313

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 830197378  593 KALQINTKLRTVIWDKNNITAQGFQDIAVALEKNYTLRF---MPIPMYDAS-----QALKTNPEKTE 651
Cdd:COG5238   314 EGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSldlSDNQIGDEGaialaKYLEGNTTLRE 380
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 393-630 9.76e-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: 75.21  E-value: 9.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  393 YLAVLNVSRTvFSHRKGKEVPpSFKQFFSSSLALMQINLSGTKLSPEPLKALLLGlacNHNLKGV-SLDLSNCELRSGGA 471
Cdd:COG5238    94 WEGAEEVSPV-ALAETATAVA-TPPPDLRRIMAKTLEDSLILYLALPRRINLIQV---LKDPLGGnAVHLLGLAARLGLL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  472 QVLEGCIAEI-HNITSLDISDNGLESD-LSTLIVWLSKNRSIQHLALGKNfnNMKSKNLtpvlDNLVQMIQDEESpLQSL 549
Cdd:COG5238   169 AAISMAKALQnNSVETVYLGCNQIGDEgIEELAEALTQNTTVTTLWLKRN--PIGDEGA----EILAEALKGNKS-LTTL 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  550 SLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVALEKNYT 628
Cdd:COG5238   242 DLSNNQIGDEgVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKT 321


                  ..
gi 830197378  629 LR 630
Cdd:COG5238   322 LH 323
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
310-612 1.39e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  310 LNLSKTSLSPKGVNSLSQSLSANLLTATTLTHLDLSGNILRGDDLSYMYSFLAQPNAIAHLDLSNTECSLDmvcgallrg 389
Cdd:COG4886    41 SLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN--------- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  390 cLQYLAVLNVSRTvfshrKGKEVPPSFKQFFSsslaLMQINLSGTKLS--PEPLKALllglacnHNLKgvSLDLSNCELR 467
Cdd:COG4886   112 -LTNLESLDLSGN-----QLTDLPEELANLTN----LKELDLSNNQLTdlPEPLGNL-------TNLK--SLDLSNNQLT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  468 SggaqvLEGCIAEIHNITSLDISDNGLeSDLSTlivWLSKNRSIQHLALGKNfnnmkskNLTPVLDNLVQMIQdeespLQ 547
Cdd:COG4886   173 D-----LPEELGNLTNLKELDLSNNQI-TDLPE---PLGNLTNLEELDLSGN-------QLTDLPEPLANLTN-----LE 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830197378  548 SLSLADSKLKTevtiiINALGSNTSLTKVDISGNGMGDmgakmLAKALQInTKLRTVIWDKNNIT 612
Cdd:COG4886   232 TLDLSNNQLTD-----LPELGNLTNLEELDLSNNQLTD-----LPPLANL-TNLKTLDLSNNQLT 285
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 273-624 2.20e-09

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: 61.34  E-value: 2.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  273 NPNSGFHTINLAGNPLEDRGVSSLSIQFAKlPKGLKHLNLSKTSLSPKGVNSLSQSLSANLLTATTlthlDLSGNILrGD 352
Cdd:COG5238   177 LQNNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTL----DLSNNQI-GD 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  353 DlsymysflaqpnaiahldlsntecsldmvcgallrGCLQYLAVLNVSRTVfsHRkgkevppsfkqffssslalmqINLS 432
Cdd:COG5238   251 E-----------------------------------GVIALAEALKNNTTV--ET---------------------LYLS 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  433 GTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIvwlsknrsIQ 512
Cdd:COG5238   273 GNQIGAEGAIALAKALQGNTTLT--SLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIAL--------AK 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  513 HLALGKNfnnmksknltpvldnlvqmiqdeespLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKML 591
Cdd:COG5238   343 ALQENTT--------------------------LHSLDLSDNQIGDEgAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                         330       340       350
                  ....*....|....*....|....*....|...
gi 830197378  592 AKALQINtKLRTVIWDKNNITAQGFQDIAVALE 624
Cdd:COG5238   397 IDALQTN-RLHTLILDGNLIGAEAQQRLEQLLE 428
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 417-630 2.48e-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: 60.45  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  417 KQFFSSSLALMQINLSGTKLSPEPLKALLLGLACNHNLKgvSLDLSNCELRSGGAQV---LEGCIAeIHNITSLDISDNG 493
Cdd:cd00116    16 TELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLK--ELCLSLNETGRIPRGLqslLQGLTK-GCGLQELDLSDNA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  494 LESDLSTLIVWLSKNRSIQHL-----ALGKNFNNMKSKNLTPVldnlvqmiqdeESPLQSLSLADSKLKTEVTI-IINAL 567
Cdd:cd00116    93 LGPDGCGVLESLLRSSSLQELklnnnGLGDRGLRLLAKGLKDL-----------PPALEKLVLGRNRLEGASCEaLAKAL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 830197378  568 GSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVALEKNYTLR 630
Cdd:cd00116   162 RANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLE 224
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 223-595 1.34e-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: 58.14  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  223 LSSKDLKLSTDVCEQILRVVSRsnrLEELVLENAGLRADFAQKLASALAHNPNSG---FHTINLAGNPledRGVSSLSIQ 299
Cdd:cd00116     3 LSLKGELLKTERATELLPKLLC---LQVLRLEGNTLGEEAAKALASALRPQPSLKelcLSLNETGRIP---RGLQSLLQG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  300 FAKLPKgLKHLNLSKTSLSPKGVNSLSqslsanlltattlthldlsgNILRGDDLsymysflaqpnaiAHLDLSNteCSL 379
Cdd:cd00116    77 LTKGCG-LQELDLSDNALGPDGCGVLE--------------------SLLRSSSL-------------QELKLNN--NGL 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  380 DMVCGALLRGCLQYLAvLNVSRTVFSHRKgKEVPPSFK--QFFSSSLALMQINLSGTKLSPEPLKALLLGLACNHNLKgv 457
Cdd:cd00116   121 GDRGLRLLAKGLKDLP-PALEKLVLGRNR-LEGASCEAlaKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLE-- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  458 SLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLesdlstlivwlsKNRSIQHLALGknfnnMKSKNLTpvldnlvq 537
Cdd:cd00116   197 VLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL------------TDAGAAALASA-----LLSPNIS-------- 251

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 830197378  538 miqdeespLQSLSLADSKLKTE-VTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKAL 595
Cdd:cd00116   252 --------LLTLSLSCNDITDDgAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESL 302
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 457-647 2.46e-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: 57.37  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  457 VSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLS---KNRSIQHLALgknFNNMKSKNLTPVLD 533
Cdd:cd00116    26 QVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQgltKGCGLQELDL---SDNALGPDGCGVLE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  534 NLVQmiqdeESPLQSLSLADSKL-KTEVTIIINALGSNT-SLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNI 611
Cdd:cd00116   103 SLLR-----SSSLQELKLNNNGLgDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGI 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 830197378  612 TAQGFQDIAVALEKNYTLR--------FMPIPMYDASQALKTNP 647
Cdd:cd00116   178 GDAGIRALAEGLKANCNLEvldlnnngLTDEGASALAETLASLK 221
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 418-632 5.81e-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: 56.21  E-value: 5.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  418 QFFSSSLALMQINLSGTKLSPE---PLKALLLGLACNHnlkgvsLDLSNCELRSGGAQVLEGCIAEI-HNITSLDISDNG 493
Cdd:cd00116    75 QGLTKGCGLQELDLSDNALGPDgcgVLESLLRSSSLQE------LKLNNNGLGDRGLRLLAKGLKDLpPALEKLVLGRNR 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  494 LESDLST-LIVWLSKNRSIQHLALGKNfnnmksknltPVLDNLVQMIQD---EESPLQSLSLADSKLK-TEVTIIINALG 568
Cdd:cd00116   149 LEGASCEaLAKALRANRDLKELNLANN----------GIGDAGIRALAEglkANCNLEVLDLNNNGLTdEGASALAETLA 218

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 830197378  569 SNTSLTKVDISGNGMGDMGAKMLAKAL-QINTKLRTVIWDKNNITAQGFQDIAVALEKNYTLRFM 632
Cdd:cd00116   219 SLKSLEVLNLGDNNLTDAGAAALASALlSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLEL 283
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 244-332 7.19e-08

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: 56.72  E-value: 7.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  244 RSNRLEELVLENAGLRADFAQKLASALAHNPNsgFHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVN 323
Cdd:COG5238   318 GNKTLHTLNLAYNGIGAQGAIALAKALQENTT--LHSLDLSDNQIGDEGAIAL-AKYLEGNTTLRELNLGKNNIGKQGAE 394


                  ....*....
gi 830197378  324 SLSQSLSAN 332
Cdd:COG5238   395 ALIDALQTN 403
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 280-624 8.64e-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: 52.74  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  280 TINLAGNPLEDRGVSSLsiqFAKLPKgLKHLNLSKTSLSPKGVNSLSQSLSANLLTATTLTHLDLSGNILRGddLSYMYS 359
Cdd:cd00116     2 QLSLKGELLKTERATEL---LPKLLC-LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRG--LQSLLQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  360 FLAQPNAIAHLDLSNTECSLDMVcgALLRGCLQ--YLAVLNVSRTVFSHRKGKEVPPSFKqffSSSLALMQINLSGTKLS 437
Cdd:cd00116    76 GLTKGCGLQELDLSDNALGPDGC--GVLESLLRssSLQELKLNNNGLGDRGLRLLAKGLK---DLPPALEKLVLGRNRLE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  438 PEPLKALLLGLACNHNLKgvSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLE----SDLSTLivwLSKNRSIQH 513
Cdd:cd00116   151 GASCEALAKALRANRDLK--ELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTdegaSALAET---LASLKSLEV 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  514 LALGKNfnnmkskNLTpvldnlvqmiqdeESPLQSLSLADSKLktevtiiinalgsNTSLTKVDISGNGMGDMGAKMLAK 593
Cdd:cd00116   226 LNLGDN-------NLT-------------DAGAAALASALLSP-------------NISLLTLSLSCNDITDDGAKDLAE 272

                         330       340       350
                  ....*....|....*....|....*....|.
gi 830197378  594 ALQINTKLRTVIWDKNNITAQGFQDIAVALE 624
Cdd:cd00116   273 VLAEKESLLELDLRGNKFGEEGAQLLAESLL 303
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 221-502 1.02e-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: 52.36  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  221 TKLSSKDLKLSTDVCeQILRVVSRSNRLEELVLENAGLRADFAQKLASALAHNPnSGFHTINLAGNPLEDRGVSSLSIQF 300
Cdd:cd00116    84 QELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLP-PALEKLVLGRNRLEGASCEALAKAL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  301 AKLPKgLKHLNLSKTSLSPKGVNSLSQSLSANLLtattlthldlsgniLRGDDLSymysflaqpnaiahldlSNTECSLD 380
Cdd:cd00116   162 RANRD-LKELNLANNGIGDAGIRALAEGLKANCN--------------LEVLDLN-----------------NNGLTDEG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  381 MVcgaLLRGCLQYLAVLNVsrtvfshrkgkevppsfkqffssslalmqINLSGTKLSPEPLKALLLGL-ACNHNLKgvSL 459
Cdd:cd00116   210 AS---ALAETLASLKSLEV-----------------------------LNLGDNNLTDAGAAALASALlSPNISLL--TL 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 830197378  460 DLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLI 502
Cdd:cd00116   256 SLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLL 298
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 187-332 1.12e-04

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: 46.32  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  187 LTQDT--RELNLQDfSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRADFAQ 264
Cdd:COG5238   204 LTQNTtvTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAI 282

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 830197378  265 KLASALAHNPNsgFHTINLAGNPLEDRGVSSLsIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSAN 332
Cdd:COG5238   283 ALAKALQGNTT--LTSLDLSVNRIGDEGAIAL-AEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQEN 347
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
418-612 2.04e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 45.69  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  418 QFFSSSLALMQINLSGTKLSPEPLKALLLGLACNHNLKGVSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESD 497
Cdd:COG4886    32 LLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  498 LSTLivwlsknrsiQHLALGKNfnnmKSKNLTPVLDNLVQmiqdeespLQSLSLADSKLKTevtiIINALGSNTSLTKVD 577
Cdd:COG4886   112 LTNL----------ESLDLSGN----QLTDLPEELANLTN--------LKELDLSNNQLTD----LPEPLGNLTNLKSLD 165

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 830197378  578 ISGNGMGDmgakmLAKALQINTKLRTVIWDKNNIT 612
Cdd:COG4886   166 LSNNQLTD-----LPEELGNLTNLKELDLSNNQIT 195
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1062-1327 1.40e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1062 RDSRKSAFLNLIKSRSKAERPPTVLITEEPSSPKGAVRSPAMDIPRKDTKPAEHNSSSERTEEVKTPDSLEEGQGEDmgk 1141
Cdd:pfam03154   44 RNSPSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREKGASDTEEPERATAKKSKTQEISRPNSPSEGEGES--- 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1142 ldrSDSRSspqggrrygVQVMGSGLMAEMKAKQEKRAACAQKKLGNETISQDSSSLTLSSTERP----DGGGAVPKLHPG 1217
Cdd:pfam03154  121 ---SDGRS---------VNDEGSSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQQILQTQPPvlqaQSGAASPPSPPP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830197378  1218 LPESRFSVGTPEKNAKVESRVEVGSRSRSPSGTLTSSKP--LLQS---------PKPSLAARPTIPQKPRSTSRPEDLPD 1286
Cdd:pfam03154  189 PGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPhtLIQQtptlhpqrlPSPHPPLQPMTQPPPPSQVSPQPLPQ 268

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 830197378  1287 SPSGPSspkvalLPPL---LKKVPSDKERDGQHSPQPNPRTFSQ 1327
Cdd:pfam03154  269 PSLHGQ------MPPMphsLQTGPSHMQHPVPPQPFPLTPQSSQ 306
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH