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Conserved domains on  [gi|15240531|ref|NP_200365|]
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tornado 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
250-466 7.00e-20

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: 94.09  E-value: 7.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  250 QIDISGSCRVAAALGMNTTVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKSLQSLY 329
Cdd:COG5238  191 QIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLY 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  330 VDGNRFGSVGVEDLlcplsrfsALQLQANITLRSIVFGGSNtkIGRDGLTAVLKMVTTNETVVHLGIhddAS--LGPDDF 407
Cdd:COG5238  271 LSGNQIGAEGAIAL--------AKALQGNTTLTSLDLSVNR--IGDEGAIALAEGLQGNKTLHTLNL---AYngIGAQGA 337
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  408 IHIFKSLQKNASLRRFSLQGCKgvRGDRVLEAITETLQINPLIEEIDLARTPLQDSGKA 466
Cdd:COG5238  338 IALAKALQENTTLHSLDLSDNQ--IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAE 394
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
104-336 2.05e-15

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: 80.22  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  104 NTSkIKQLAFRKNRFSEQCLNELSEILKRNRFLKEVMFLESSIGYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEELS 183
Cdd:COG5238  207 NTT-VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALA 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  184 RMIEMNSSLKlfsifdsspftatpliSAVLGMNRemevhmwsgdhKRDRSLK-LVEFLPESKTLRIY-----QIDISGSC 257
Cdd:COG5238  286 KALQGNTTLT----------------SLDLSVNR-----------IGDEGAIaLAEGLQGNKTLHTLnlaynGIGAQGAI 338
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  258 RVAAALGMNTTVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKsLQSLYVDGNRFG 336
Cdd:COG5238  339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIG 416
COR super family cl24610
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
724-930 2.32e-14

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


The actual alignment was detected with superfamily member pfam16095:

Pssm-ID: 406489  Cd Length: 196  Bit Score: 73.05  E-value: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531    724 RSENSNKPIMRWKAFADLCQfkvpslriksrNENIQIVETRRHAIATcLHQMGEVIYFDDLGFL----ILDYEWfcgevL 799
Cdd:pfam16095   12 EKERQKKPYISYEEYRKICA-----------ENGIDDEEDQDTLLEF-LHDLGVLLYFQDDPGLrdivILNPQW-----L 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531    800 TQLIK--LDVRKQStgERNGFVSRKELEKTLRSSLQSPipgmtskvlEHFDAcdLVKMMKKVELCYEQDPSSPDSSLlVP 877
Cdd:pfam16095   75 TNAVYrvLDSKHVL--NNNGILTHEDLEQIWKDPGYPR---------ELHPY--LLRLMEKFELCYELPGDEEGTYL-VP 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15240531    878 SILEEGRGKTQKWQI-NTHDCVYSgrhlqcddssHMFLTAGFFPRLQVHLHNRI 930
Cdd:pfam16095  141 QLLPENPPELYDWDEeNNLELRYQ----------YDFLPKGIFSRLIVRLHKFI 184
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
504-695 3.92e-05

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd09914:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 161  Bit Score: 45.40  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  504 LCGQNYAGKTTLCNSILqsssasGFPYVENVrnlmnpveqvVKTVGgMKIKTFK-----DEETKISMWNLAGQHEFFALH 578
Cdd:cd09914    6 LVGQGGVGKTSLCKQLI------GEKFDGDE----------SSTHG-INVQDWKipapeRKKIRLNVWDFGGQEIYHATH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  579 DLMFPSPCFFLIVLslfrkpsnkEPKTPAEvEEELEYWLRFIVSNSRkaiqqcmKPNVTIVLTH-----SEKINLQSesf 653
Cdd:cd09914   69 QFFLTSRSLYLLVF---------DLRTGDE-VSRVPYWLRQIKAFGG-------VSPVILVGTHidescDEDILKKA--- 128
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15240531  654 qatvgciqrLRDKFQALVEFYptvFTVDARSSPSVSKLTHHI 695
Cdd:cd09914  129 ---------LNKKFPAIINDI---HFVSCKNGKGIAELKKAI 158
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
250-466 7.00e-20

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: 94.09  E-value: 7.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  250 QIDISGSCRVAAALGMNTTVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKSLQSLY 329
Cdd:COG5238  191 QIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLY 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  330 VDGNRFGSVGVEDLlcplsrfsALQLQANITLRSIVFGGSNtkIGRDGLTAVLKMVTTNETVVHLGIhddAS--LGPDDF 407
Cdd:COG5238  271 LSGNQIGAEGAIAL--------AKALQGNTTLTSLDLSVNR--IGDEGAIALAEGLQGNKTLHTLNL---AYngIGAQGA 337
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  408 IHIFKSLQKNASLRRFSLQGCKgvRGDRVLEAITETLQINPLIEEIDLARTPLQDSGKA 466
Cdd:COG5238  338 IALAKALQENTTLHSLDLSDNQ--IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAE 394
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
104-336 2.05e-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: 80.22  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  104 NTSkIKQLAFRKNRFSEQCLNELSEILKRNRFLKEVMFLESSIGYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEELS 183
Cdd:COG5238  207 NTT-VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALA 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  184 RMIEMNSSLKlfsifdsspftatpliSAVLGMNRemevhmwsgdhKRDRSLK-LVEFLPESKTLRIY-----QIDISGSC 257
Cdd:COG5238  286 KALQGNTTLT----------------SLDLSVNR-----------IGDEGAIaLAEGLQGNKTLHTLnlaynGIGAQGAI 338
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  258 RVAAALGMNTTVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKsLQSLYVDGNRFG 336
Cdd:COG5238  339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIG 416
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
724-930 2.32e-14

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 73.05  E-value: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531    724 RSENSNKPIMRWKAFADLCQfkvpslriksrNENIQIVETRRHAIATcLHQMGEVIYFDDLGFL----ILDYEWfcgevL 799
Cdd:pfam16095   12 EKERQKKPYISYEEYRKICA-----------ENGIDDEEDQDTLLEF-LHDLGVLLYFQDDPGLrdivILNPQW-----L 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531    800 TQLIK--LDVRKQStgERNGFVSRKELEKTLRSSLQSPipgmtskvlEHFDAcdLVKMMKKVELCYEQDPSSPDSSLlVP 877
Cdd:pfam16095   75 TNAVYrvLDSKHVL--NNNGILTHEDLEQIWKDPGYPR---------ELHPY--LLRLMEKFELCYELPGDEEGTYL-VP 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15240531    878 SILEEGRGKTQKWQI-NTHDCVYSgrhlqcddssHMFLTAGFFPRLQVHLHNRI 930
Cdd:pfam16095  141 QLLPENPPELYDWDEeNNLELRYQ----------YDFLPKGIFSRLIVRLHKFI 184
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
103-257 4.64e-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: 53.51  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  103 DNTSKIKQLAFRKNRFSEQCLNELSEILKRNRFLKEVMFLESSIGYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEEL 182
Cdd:cd00116  134 DLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASAL 213
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  183 SRMIEMNSSLKLFSiFDSSPFTATP---LISAVLGMNREM-EVHMWSGDHKRDRSLKLVEFLPESKTLRiyQIDISGSC 257
Cdd:cd00116  214 AETLASLKSLEVLN-LGDNNLTDAGaaaLASALLSPNISLlTLSLSCNDITDDGAKDLAEVLAEKESLL--ELDLRGNK 289
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
164-451 5.95e-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: 53.13  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  164 LEELQIWEDSIGSKGAEELSRMIEMNSSLKLFSIfdSSPFTA-TPLISAVLGMNREMEVHMWSGDHkRDRSL-----KLV 237
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCL--SLNETGrIPRGLQSLLQGLTKGCGLQELDL-SDNALgpdgcGVL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  238 EFLPESKTLRIYQ-----IDISGSCRVAAALGMNT-TVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKA 311
Cdd:cd00116  102 ESLLRSSSLQELKlnnngLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  312 VVYIAAGLFKNKSLQSLYVDGNRFGSVGVEDLlcplsrfsALQLQANITLRSIVFGGSNtkIGRDGLTAVLK-MVTTNET 390
Cdd:cd00116  182 IRALAEGLKANCNLEVLDLNNNGLTDEGASAL--------AETLASLKSLEVLNLGDNN--LTDAGAAALASaLLSPNIS 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240531  391 VVHLGIHDDaSLGPDDFIHIFKSLQKNASLRRFSLQGCK-GVRGDRVLEAITETLQINPLIE 451
Cdd:cd00116  252 LLTLSLSCN-DITDDGAKDLAEVLAEKESLLELDLRGNKfGEEGAQLLAESLLEPGNELESL 312
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
504-695 3.92e-05

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 45.40  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  504 LCGQNYAGKTTLCNSILqsssasGFPYVENVrnlmnpveqvVKTVGgMKIKTFK-----DEETKISMWNLAGQHEFFALH 578
Cdd:cd09914    6 LVGQGGVGKTSLCKQLI------GEKFDGDE----------SSTHG-INVQDWKipapeRKKIRLNVWDFGGQEIYHATH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  579 DLMFPSPCFFLIVLslfrkpsnkEPKTPAEvEEELEYWLRFIVSNSRkaiqqcmKPNVTIVLTH-----SEKINLQSesf 653
Cdd:cd09914   69 QFFLTSRSLYLLVF---------DLRTGDE-VSRVPYWLRQIKAFGG-------VSPVILVGTHidescDEDILKKA--- 128
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15240531  654 qatvgciqrLRDKFQALVEFYptvFTVDARSSPSVSKLTHHI 695
Cdd:cd09914  129 ---------LNKKFPAIINDI---HFVSCKNGKGIAELKKAI 158
 
Name Accession Description Interval E-value
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
250-466 7.00e-20

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: 94.09  E-value: 7.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  250 QIDISGSCRVAAALGMNTTVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKSLQSLY 329
Cdd:COG5238  191 QIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLY 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  330 VDGNRFGSVGVEDLlcplsrfsALQLQANITLRSIVFGGSNtkIGRDGLTAVLKMVTTNETVVHLGIhddAS--LGPDDF 407
Cdd:COG5238  271 LSGNQIGAEGAIAL--------AKALQGNTTLTSLDLSVNR--IGDEGAIALAEGLQGNKTLHTLNL---AYngIGAQGA 337
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  408 IHIFKSLQKNASLRRFSLQGCKgvRGDRVLEAITETLQINPLIEEIDLARTPLQDSGKA 466
Cdd:COG5238  338 IALAKALQENTTLHSLDLSDNQ--IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAE 394
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
116-415 3.87e-16

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: 82.53  E-value: 3.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  116 NRFSEQCLNELSEILKRNRFLKEVMFLESSIGYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEELSRMIEMNSSLKlf 195
Cdd:COG5238  190 NQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE-- 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  196 sifdsspftatpliSAVLGMNremevhmwsgdhkrdrslklveflpesktlriyQIDISGSCRVAAALGMNTTVRSLDMT 275
Cdd:COG5238  268 --------------TLYLSGN---------------------------------QIGAEGAIALAKALQGNTTLTSLDLS 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  276 GAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKSLQSLYVDGNRFGSVGVEDLlcplsrfsALQL 355
Cdd:COG5238  301 VNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIAL--------AKYL 372
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  356 QANITLRSIVFGGSNtkIGRDGLTAVLKMVTTNEtvVHLGIHDDASLGPDDFIHIFKSLQ 415
Cdd:COG5238  373 EGNTTLRELNLGKNN--IGKQGAEALIDALQTNR--LHTLILDGNLIGAEAQQRLEQLLE 428
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
104-336 2.05e-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: 80.22  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  104 NTSkIKQLAFRKNRFSEQCLNELSEILKRNRFLKEVMFLESSIGYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEELS 183
Cdd:COG5238  207 NTT-VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALA 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  184 RMIEMNSSLKlfsifdsspftatpliSAVLGMNRemevhmwsgdhKRDRSLK-LVEFLPESKTLRIY-----QIDISGSC 257
Cdd:COG5238  286 KALQGNTTLT----------------SLDLSVNR-----------IGDEGAIaLAEGLQGNKTLHTLnlaynGIGAQGAI 338
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  258 RVAAALGMNTTVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKsLQSLYVDGNRFG 336
Cdd:COG5238  339 ALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIG 416
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
264-481 7.82e-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: 78.68  E-value: 7.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  264 GMNTTVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKSLQSLYVDGNRFGSVGVEDL 343
Cdd:COG5238  177 LQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  344 lcplsrfsALQLQANITLRSIVFGGSntKIGRDGLTAVLKMVTTNETV--VHLGIHDdasLGPDDFIHIFKSLQKNASLR 421
Cdd:COG5238  257 --------AEALKNNTTVETLYLSGN--QIGAEGAIALAKALQGNTTLtsLDLSVNR---IGDEGAIALAEGLQGNKTLH 323
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240531  422 RFSLQGCKgvRGDRVLEAITETLQINPLIEEIDLARTPLQDSGkADEIYQKLGHNG--RKID 481
Cdd:COG5238  324 TLNLAYNG--IGAQGAIALAKALQENTTLHSLDLSDNQIGDEG-AIALAKYLEGNTtlRELN 382
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
724-930 2.32e-14

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 73.05  E-value: 2.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531    724 RSENSNKPIMRWKAFADLCQfkvpslriksrNENIQIVETRRHAIATcLHQMGEVIYFDDLGFL----ILDYEWfcgevL 799
Cdd:pfam16095   12 EKERQKKPYISYEEYRKICA-----------ENGIDDEEDQDTLLEF-LHDLGVLLYFQDDPGLrdivILNPQW-----L 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531    800 TQLIK--LDVRKQStgERNGFVSRKELEKTLRSSLQSPipgmtskvlEHFDAcdLVKMMKKVELCYEQDPSSPDSSLlVP 877
Cdd:pfam16095   75 TNAVYrvLDSKHVL--NNNGILTHEDLEQIWKDPGYPR---------ELHPY--LLRLMEKFELCYELPGDEEGTYL-VP 140
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15240531    878 SILEEGRGKTQKWQI-NTHDCVYSgrhlqcddssHMFLTAGFFPRLQVHLHNRI 930
Cdd:pfam16095  141 QLLPENPPELYDWDEeNNLELRYQ----------YDFLPKGIFSRLIVRLHKFI 184
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
67-192 1.69e-07

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: 55.57  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531   67 FIELATSLETQTSLRNLEFEGIFWEIELLQSLGLLLDNTSKIKQLAFRKNRFSEQCLNELSEILKRNRFLKEVMFLESSI 146
Cdd:COG5238  253 VIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGI 332
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15240531  147 GYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEELSRMIEMNSSL 192
Cdd:COG5238  333 GAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTL 378
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
103-257 4.64e-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: 53.51  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  103 DNTSKIKQLAFRKNRFSEQCLNELSEILKRNRFLKEVMFLESSIGYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEEL 182
Cdd:cd00116  134 DLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASAL 213
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240531  183 SRMIEMNSSLKLFSiFDSSPFTATP---LISAVLGMNREM-EVHMWSGDHKRDRSLKLVEFLPESKTLRiyQIDISGSC 257
Cdd:cd00116  214 AETLASLKSLEVLN-LGDNNLTDAGaaaLASALLSPNISLlTLSLSCNDITDDGAKDLAEVLAEKESLL--ELDLRGNK 289
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
164-451 5.95e-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: 53.13  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  164 LEELQIWEDSIGSKGAEELSRMIEMNSSLKLFSIfdSSPFTA-TPLISAVLGMNREMEVHMWSGDHkRDRSL-----KLV 237
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCL--SLNETGrIPRGLQSLLQGLTKGCGLQELDL-SDNALgpdgcGVL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  238 EFLPESKTLRIYQ-----IDISGSCRVAAALGMNT-TVRSLDMTGAKLNSRWAKEFRWVLEQNKTLREVKLSKTGLKDKA 311
Cdd:cd00116  102 ESLLRSSSLQELKlnnngLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  312 VVYIAAGLFKNKSLQSLYVDGNRFGSVGVEDLlcplsrfsALQLQANITLRSIVFGGSNtkIGRDGLTAVLK-MVTTNET 390
Cdd:cd00116  182 IRALAEGLKANCNLEVLDLNNNGLTDEGASAL--------AETLASLKSLEVLNLGDNN--LTDAGAAALASaLLSPNIS 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240531  391 VVHLGIHDDaSLGPDDFIHIFKSLQKNASLRRFSLQGCK-GVRGDRVLEAITETLQINPLIE 451
Cdd:cd00116  252 LLTLSLSCN-DITDDGAKDLAEVLAEKESLLELDLRGNKfGEEGAQLLAESLLEPGNELESL 312
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
104-347 2.03e-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: 51.59  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  104 NTSKIKQLAFRKNRFSEQcLNELSEILKRNRFLKEVMFLESSIGYRGATLLGSALQ-VNDSLEELQIWEDSIGSKGAEEL 182
Cdd:cd00116   79 KGCGLQELDLSDNALGPD-GCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKdLPPALEKLVLGRNRLEGASCEAL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  183 SRMIEMNSSLKlfsifdsspftatplisavlgmnremEVHMwSGDHKRDRSL-KLVEFLPESKTLRIYQIDISGSCR--- 258
Cdd:cd00116  158 AKALRANRDLK--------------------------ELNL-ANNGIGDAGIrALAEGLKANCNLEVLDLNNNGLTDega 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  259 --VAAALGMNTTVRSLDMTGAKLNSRWAKEF-RWVLEQNKTLREVKLSKTGLKDKAVVYIAAGLFKNKSLQSLYVDGNRF 335
Cdd:cd00116  211 saLAETLASLKSLEVLNLGDNNLTDAGAAALaSALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKF 290
                        250
                 ....*....|..
gi 15240531  336 GSVGvEDLLCPL 347
Cdd:cd00116  291 GEEG-AQLLAES 301
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
271-464 8.21e-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: 49.66  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  271 SLDMTGAKLN-SRWAKEFRWVLEqnktLREVKLSKTGLKDKAVVYIAAGLFKNKSLQSLYVDGNRFGSV--GVEDLLCPL 347
Cdd:cd00116    2 QLSLKGELLKtERATELLPKLLC----LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIprGLQSLLQGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  348 SRFSALQlqaniTLRSivfggSNTKIGRDGlTAVLKMVTTNETVVHLGIHDdASLGPDDFIHIFKSLQKNA-SLRRFSLQ 426
Cdd:cd00116   78 TKGCGLQ-----ELDL-----SDNALGPDG-CGVLESLLRSSSLQELKLNN-NGLGDRGLRLLAKGLKDLPpALEKLVLG 145
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15240531  427 GCKgvRGDRVLEAITETLQINPLIEEIDLARTPLQDSG 464
Cdd:cd00116  146 RNR--LEGASCEALAKALRANRDLKELNLANNGIGDAG 181
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
504-695 3.92e-05

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 45.40  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  504 LCGQNYAGKTTLCNSILqsssasGFPYVENVrnlmnpveqvVKTVGgMKIKTFK-----DEETKISMWNLAGQHEFFALH 578
Cdd:cd09914    6 LVGQGGVGKTSLCKQLI------GEKFDGDE----------SSTHG-INVQDWKipapeRKKIRLNVWDFGGQEIYHATH 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531  579 DLMFPSPCFFLIVLslfrkpsnkEPKTPAEvEEELEYWLRFIVSNSRkaiqqcmKPNVTIVLTH-----SEKINLQSesf 653
Cdd:cd09914   69 QFFLTSRSLYLLVF---------DLRTGDE-VSRVPYWLRQIKAFGG-------VSPVILVGTHidescDEDILKKA--- 128
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15240531  654 qatvgciqrLRDKFQALVEFYptvFTVDARSSPSVSKLTHHI 695
Cdd:cd09914  129 ---------LNKKFPAIINDI---HFVSCKNGKGIAELKKAI 158
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
52-194 6.55e-05

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: 47.09  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240531   52 NINVTRDNLtSLSQI----FIELATSLETQTSLRNLEFEGIFWEIELLQSLGLLLDNTSKIKQLAFRKNRFSEQCLNELS 127
Cdd:COG5238  263 NTTVETLYL-SGNQIgaegAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALA 341
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240531  128 EILKRNRFLKEVMFLESSIGYRGATLLGSALQVNDSLEELQIWEDSIGSKGAEELSRMIEMNSSLKL 194
Cdd:COG5238  342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTL 408
 
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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