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Conserved domains on  [gi|42573277|ref|NP_974735|]
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signal recognition particle binding protein [Arabidopsis thaliana]

Protein Classification

signal recognition particle receptor subunit beta( domain architecture ID 10134869)

signal recognition particle (SRP) receptor subunit beta, together with SRP subunit alpha, forms the heterodimeric SRP receptor that binds SRP to regulate protein translocation across the ER membrane

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
57-257 4.29e-70

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


:

Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 214.11  E-value: 4.29e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  57 NTVLLSGLTGSGKTVLFYQLRDGSsHQGTVTSMEPNEGTFVLHSentkkGKIKPVHLVDVPGHSRLRPKLEEFLPQAA-A 135
Cdd:cd04105   1 PTVLLLGPSDSGKTALFTKLTTGK-VRSTVTSIEPNVASFYSNS-----SKGKKLTLVDVPGHEKLRDKLLEYLKASLkA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277 136 IVFVVDALEFLPNCRAASEYLYEILTNANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEKEIEKLRASRSAVSTADIAN 215
Cdd:cd04105  75 IVFVVDSATFQKNIRDVAEFLYDILTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGD 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42573277 216 DFTI----GIEGEVFSFTHCSNKVTVAE--ASGLTGETIQIEDFIREY 257
Cdd:cd04105 155 DGSKdtlgDKGGKDFEFDQLEGEVDFVEgsVKKSKGGIDDIEEWIDEL 202
 
Name Accession Description Interval E-value
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
57-257 4.29e-70

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 214.11  E-value: 4.29e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  57 NTVLLSGLTGSGKTVLFYQLRDGSsHQGTVTSMEPNEGTFVLHSentkkGKIKPVHLVDVPGHSRLRPKLEEFLPQAA-A 135
Cdd:cd04105   1 PTVLLLGPSDSGKTALFTKLTTGK-VRSTVTSIEPNVASFYSNS-----SKGKKLTLVDVPGHEKLRDKLLEYLKASLkA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277 136 IVFVVDALEFLPNCRAASEYLYEILTNANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEKEIEKLRASRSAVSTADIAN 215
Cdd:cd04105  75 IVFVVDSATFQKNIRDVAEFLYDILTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGD 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42573277 216 DFTI----GIEGEVFSFTHCSNKVTVAE--ASGLTGETIQIEDFIREY 257
Cdd:cd04105 155 DGSKdtlgDKGGKDFEFDQLEGEVDFVEgsVKKSKGGIDDIEEWIDEL 202
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
54-235 7.08e-37

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 128.71  E-value: 7.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277    54 TKSNTVLLSGLTGSGKTVLFYQLRDGSSHQgTVTSMEPNegtFVLHSENTKKGKIKpvhLVDVPGHSRLRPKLEE---FL 130
Cdd:pfam09439   1 SSQPAVIIAGLCDSGKTSLFTLLTTDSVRP-TVTSQEPS---AAYRYMLNKGNSFT---LIDFPGHVKLRYKLLEtlkDS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277   131 PQAAAIVFVVDALEFLPNCRAASEYLYEILTNANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEKEIEKLRASRS-AVS 209
Cdd:pfam09439  74 SSLKGIVFVVDSTIFPKEVTDTAEFLYDILSITELLKNGIDILIACNKQESFTARPPKKIKQALEKEINTIRERRSkALS 153
                         170       180
                  ....*....|....*....|....*...
gi 42573277   210 TADIAND--FTIGIEGEVFSFTHCSNKV 235
Cdd:pfam09439 154 GLDGSEDlsAVLGKKGKGFKFDQLEANV 181
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
59-196 1.76e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 46.60  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277    59 VLLSGLTGSGKTVLFYQLRDgssHQGTVTSMEPNEGTFVLHSENTKKGKIKPVHLVDVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLG---NKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573277   139 VVDALefLPNCRAAS---EYLYEIltnANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEK 196
Cdd:TIGR00231  81 VFDIV--ILVLDVEEileKQTKEI---IHHADSGVPIILVGNKIDLKDADLKTHVASEFAK 136
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
55-191 1.57e-05

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 44.54  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277     55 KSNTVLLSGLTGSGKTVLFYQLRDGSshqgtVTSMEPnegTFVLHSENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQAA 134
Cdd:smart00178  16 KHAKILFLGLDNAGKTTLLHMLKNDR-----LAQHQP---TQHPTSEELAIGNIK-FTTFDLGGHQQARRLWKDYFPEVN 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 42573277    135 AIVFVVDALEFLPNCRAASEyLYEILTNANVvkKKIPVLLCCNKTDKLTAHTKEFIR 191
Cdd:smart00178  87 GIVYLVDAYDKERFAESKRE-LDALLSDEEL--ATVPFLILGNKIDAPYAASEDELR 140
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
113-203 8.25e-04

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.97  E-value: 8.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277 113 LVDVPG-HsrlRPK--LEEFLPQAA--------AIVFVVDALEFLpncRAASEYLYEILTNAnvvkkKIPVLLCCNKTDK 181
Cdd:COG1159  55 FVDTPGiH---KPKrkLGRRMNKAAwsaledvdVILFVVDATEKI---GEGDEFILELLKKL-----KTPVILVINKIDL 123
                        90       100
                ....*....|....*....|..
gi 42573277 182 LTahtkefiRKQMEKEIEKLRA 203
Cdd:COG1159 124 VK-------KEELLPLLAEYSE 138
era PRK00089
GTPase Era; Reviewed
113-196 8.41e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.03  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  113 LVDVPG-HSRLRpKLEEFLPQAA--------AIVFVVDALEFLpncraaSEYLYEILtnANVVKKKIPVLLCCNKTDKLt 183
Cdd:PRK00089  57 FVDTPGiHKPKR-ALNRAMNKAAwsslkdvdLVLFVVDADEKI------GPGDEFIL--EKLKKVKTPVILVLNKIDLV- 126
                         90
                 ....*....|...
gi 42573277  184 aHTKEFIRKQMEK 196
Cdd:PRK00089 127 -KDKEELLPLLEE 138
 
Name Accession Description Interval E-value
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
57-257 4.29e-70

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 214.11  E-value: 4.29e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  57 NTVLLSGLTGSGKTVLFYQLRDGSsHQGTVTSMEPNEGTFVLHSentkkGKIKPVHLVDVPGHSRLRPKLEEFLPQAA-A 135
Cdd:cd04105   1 PTVLLLGPSDSGKTALFTKLTTGK-VRSTVTSIEPNVASFYSNS-----SKGKKLTLVDVPGHEKLRDKLLEYLKASLkA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277 136 IVFVVDALEFLPNCRAASEYLYEILTNANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEKEIEKLRASRSAVSTADIAN 215
Cdd:cd04105  75 IVFVVDSATFQKNIRDVAEFLYDILTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGD 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42573277 216 DFTI----GIEGEVFSFTHCSNKVTVAE--ASGLTGETIQIEDFIREY 257
Cdd:cd04105 155 DGSKdtlgDKGGKDFEFDQLEGEVDFVEgsVKKSKGGIDDIEEWIDEL 202
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
54-235 7.08e-37

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 128.71  E-value: 7.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277    54 TKSNTVLLSGLTGSGKTVLFYQLRDGSSHQgTVTSMEPNegtFVLHSENTKKGKIKpvhLVDVPGHSRLRPKLEE---FL 130
Cdd:pfam09439   1 SSQPAVIIAGLCDSGKTSLFTLLTTDSVRP-TVTSQEPS---AAYRYMLNKGNSFT---LIDFPGHVKLRYKLLEtlkDS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277   131 PQAAAIVFVVDALEFLPNCRAASEYLYEILTNANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEKEIEKLRASRS-AVS 209
Cdd:pfam09439  74 SSLKGIVFVVDSTIFPKEVTDTAEFLYDILSITELLKNGIDILIACNKQESFTARPPKKIKQALEKEINTIRERRSkALS 153
                         170       180
                  ....*....|....*....|....*...
gi 42573277   210 TADIAND--FTIGIEGEVFSFTHCSNKV 235
Cdd:pfam09439 154 GLDGSEDlsAVLGKKGKGFKFDQLEANV 181
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
55-194 1.39e-11

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.


Pssm-ID: 206645 [Multi-domain]  Cd Length: 191  Bit Score: 61.91  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  55 KSNTVLLSGLTGSGKTVLFYQLRDGSSHQgTVTSMEPnegtfvlHSENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQAA 134
Cdd:cd00879  18 KEAKIVFLGLDNAGKTTLLHMLKDDRLAQ-HVPTLHP-------TSEELTIGNVK-FTTFDLGGHEQARRVWKDYFPEVD 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42573277 135 AIVFVVDAL--EFLPNCRAASEYLYEILTNANVvkkkiPVLLCCNKTDKLTAHTKEFIRKQM 194
Cdd:cd00879  89 GIVFLVDAAdpERFQESKEELDSLLNDEELANV-----PILILGNKIDKPGAVSEEELREAL 145
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
63-200 1.55e-11

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 60.93  E-value: 1.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  63 GLTGSGKTVLFYQLRDGS---SHQGTVTSMEPNEGTFVLHsentkkGKIKPVHLVDVPGH-----SRLRPKLEEFLPQAA 134
Cdd:cd00882   4 GRGGVGKSSLLNALLGGEvgeVSDVPGTTRDPDVYVKELD------KGKVKLVLVDTPGLdefggLGREELARLLLRGAD 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42573277 135 AIVFVVDAleflpnCRAASEYLYEILTNANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEKEIEK 200
Cdd:cd00882  78 LILLVVDS------TDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKIL 137
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
59-195 3.15e-11

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 59.90  E-value: 3.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  59 VLLSGLTGSGKTVLFYQLRdgsshQGTVTSMEPNEGTFVlhsENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:cd00878   2 ILMLGLDGAGKTTILYKLK-----LGEVVTTIPTIGFNV---ETVEYKNVK-FTVWDVGGQDKIRPLWKHYYENTDGLIF 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42573277 139 VVDAL--EFLPncrAASEYLYEILTNANVvkKKIPVLLCCNKTDKLTAHTKEFIRKQME 195
Cdd:cd00878  73 VVDSSdrERIE---EAKNELHKLLNEEEL--KGAPLLILANKQDLPGALTESELIELLG 126
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
59-203 2.58e-08

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 51.84  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277    59 VLLSGLTGSGKTVLFYQLRDGSSHQgTVTSMEPNegtfvlhSENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLKLGEIVT-TIPTIGFN-------VETVTYKNVK-FTVWDVGGQESLRPLWRNYFPNTDAVIF 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573277   139 VVDA--LEFLPNCRAASEYLYEILTNANVvkkkiPVLLCCNKTDKLTAHTKEFIRKQMekEIEKLRA 203
Cdd:pfam00025  74 VVDSadRDRIEEAKEELHALLNEEELADA-----PLLILANKQDLPGAMSEAEIRELL--GLHELKD 133
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
61-194 8.16e-08

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 50.39  E-value: 8.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  61 LSGLTGSGKTVLFYQLRDGsshqGTVTSMEPNEGTfvlhseNTKKGKIKPVHLV--DVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:cd04159   4 LVGLQNSGKTTLVNVIASG----QFSEDTIPTVGF------NMRKVTKGNVTIKvwDLGGQPRFRSMWERYCRGVNAIVY 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42573277 139 VVDALEFLpNCRAASEYLYEILTNANVvkKKIPVLLCCNKTDKLTAHTKEFIRKQM 194
Cdd:cd04159  74 VVDAADRE-KLEVAKNELHDLLEKPSL--EGIPLLVLGNKNDLPGALSVDELIEQM 126
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
59-205 1.45e-07

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 49.72  E-value: 1.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  59 VLLSGLTGSGKTVLFYQLRdgssHQGTVTSMePNEGTFVlhsENTKKGKIKPVHLVDVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:cd04156   2 VLLLGLDSAGKSTLLYKLK----HAELVTTI-PTVGFNV---EMLQLEKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVY 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573277 139 VVDALEF--LPNCRAAseyLYEILTNANVvkKKIPVLLCCNKTDKLTAHTKEFIRKQMekEIEKLRASR 205
Cdd:cd04156  74 VVDSSDEarLDESQKE---LKHILKNEHI--KGVPVVLLANKQDLPGALTAEEITRRF--KLKKYCSDR 135
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
48-195 3.09e-07

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 49.32  E-value: 3.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  48 IRLVRRTKSNT-----VLLSGLTGSGKTVLFYQLrdGSSHQGTVTsmePNEGtFVLHSENTKKGKIKpvhLVDVPGHSRL 122
Cdd:cd04155   2 LSILRKLKPSSrqevrILLLGLDNAGKTTILKQL--ASEDISHIT---PTQG-FNIKNVQADGFKLN---VWDIGGQRKI 72
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42573277 123 RPKLEEFLPQAAAIVFVVDALEfLPNCRAASEYLYEILTNANvvKKKIPVLLCCNKTDKLTAHTKEFIRKQME 195
Cdd:cd04155  73 RPYWRNYFENTDVLIYVIDSAD-RKRFEEAGQELVELLEEEK--LAGVPVLVFANKQDLLTAAPAEEVAEALN 142
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
58-190 3.47e-07

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 48.96  E-value: 3.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  58 TVLLSGLTGSGKTVLFYQLRDGSSHQGTVTsmePNEGTFVlhsENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQAAAIV 137
Cdd:cd04157   1 NILVLGLDNSGKTTIINQLKPSNAQSQNIV---PTVGFNV---ESFKKGNLS-FTAFDMSGQGKYRGLWEHYYKNIQGII 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42573277 138 FVVDALEFLPNCRAASEyLYEILTNANVVKKKIPVLLCCNKTDKLTAHTKEFI 190
Cdd:cd04157  74 FVIDSSDRLRMVVAKDE-LELLLNHPDIKHRRIPILFYANKMDLPDALTAVKI 125
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
59-196 1.76e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 46.60  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277    59 VLLSGLTGSGKTVLFYQLRDgssHQGTVTSMEPNEGTFVLHSENTKKGKIKPVHLVDVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLG---NKGSITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLR 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573277   139 VVDALefLPNCRAAS---EYLYEIltnANVVKKKIPVLLCCNKTDKLTAHTKEFIRKQMEK 196
Cdd:TIGR00231  81 VFDIV--ILVLDVEEileKQTKEI---IHHADSGVPIILVGNKIDLKDADLKTHVASEFAK 136
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
59-197 2.63e-06

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 46.29  E-value: 2.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  59 VLLSGLTGSGKTVLFYQLRDGSSHQGTVtsmePNEGtFVLHSENTKKGKikpVHLVDVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:cd04162   2 ILVLGLDGAGKTSLLHSLSSERSLESVV----PTTG-FNSVAIPTQDAI---MELLEIGGSQNLRKYWKRYLSGSQGLIF 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42573277 139 VVDAL--EFLPNCRaasEYLYEILTNANVvkkkIPVLLCCNKTDKLTAHTKEFIRKQMEKE 197
Cdd:cd04162  74 VVDSAdsERLPLAR---QELHQLLQHPPD----LPLVVLANKQDLPAARSVQEIHKELELE 127
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
59-180 5.70e-06

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 45.42  E-value: 5.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  59 VLLSGLTGSGKTVLFYQLrdgssHQGTVTSMEPNEGTfvlhseNTKKGKIKPVHLV--DVPGHSRLRPKLEEFLPQAAAI 136
Cdd:cd04153  18 VIIVGLDNAGKTTILYQF-----LLGEVVHTSPTIGS------NVEEIVYKNIRFLmwDIGGQESLRSSWNTYYTNTDAV 86
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42573277 137 VFVVDAL--EFLPncrAASEYLYEILTNANVvkKKIPVLLCCNKTD 180
Cdd:cd04153  87 ILVIDSTdrERLP---LTKEELYKMLAHEDL--RKAVLLVLANKQD 127
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
55-191 1.57e-05

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 44.54  E-value: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277     55 KSNTVLLSGLTGSGKTVLFYQLRDGSshqgtVTSMEPnegTFVLHSENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQAA 134
Cdd:smart00178  16 KHAKILFLGLDNAGKTTLLHMLKNDR-----LAQHQP---TQHPTSEELAIGNIK-FTTFDLGGHQQARRLWKDYFPEVN 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 42573277    135 AIVFVVDALEFLPNCRAASEyLYEILTNANVvkKKIPVLLCCNKTDKLTAHTKEFIR 191
Cdd:smart00178  87 GIVYLVDAYDKERFAESKRE-LDALLSDEEL--ATVPFLILGNKIDAPYAASEDELR 140
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
59-180 3.20e-05

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 42.11  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277    59 VLLSGLTGSGKTVLFYQLRDG--SSHQGTVTSMEPNEGTFVlhsENTKKGKIKPVHLVDVPGHSRLRPKLEEFLPQAAAI 136
Cdd:pfam08477   2 VVLLGDSGVGKTSLLKRFVDDtfDPKYKSTIGVDFKTKTVL---ENDDNGKKIKLNIWDTAGQERFRSLHPFYYRGAAAA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 42573277   137 VFVVDALEFlpncRAASEYLYEILTNANvvkkKIPVLLCCNKTD 180
Cdd:pfam08477  79 LLVYDSRTF----SNLKYWLRELKKYAG----NSPVILVGNKID 114
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
59-202 9.10e-05

ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability.


Pssm-ID: 206718 [Multi-domain]  Cd Length: 158  Bit Score: 41.63  E-value: 9.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  59 VLLSGLTGSGKTVLFYQLrdgssHQGTVTSMEPNEGtFVLHSENTKKGKIKpvhLVDVPGHSRLRPKLEEFLPQAAAIVF 138
Cdd:cd04151   2 ILILGLDGAGKTTILYRL-----QVGEVVTTIPTIG-FNVETVTYKNLKFQ---VWDLGGQTSIRPYWRCYYSNTDAIIY 72
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42573277 139 VVDALEfLPNCRAASEYLYEILTNANVvkKKIPVLLCCNKTDKLTAHTKEFIRKQMEKEIEKLR 202
Cdd:cd04151  73 VVDSTD-RDRLGISKSELHAMLEEEEL--KDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDR 133
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
113-203 1.38e-04

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 41.29  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277 113 LVDVPG-HSRlRPKLEEFLPQAA--------AIVFVVDALEFLpncraaSEYLYEILtnANVVKKKIPVLLCCNKTDKLT 183
Cdd:cd04163  55 FVDTPGiHKP-KKKLGERMVKAAwsalkdvdLVLFVVDASEWI------GEGDEFIL--ELLKKSKTPVILVLNKIDLVK 125
                        90       100
                ....*....|....*....|
gi 42573277 184 AhtkefiRKQMEKEIEKLRA 203
Cdd:cd04163 126 D------KEDLLPLLEKLKE 139
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
54-142 2.67e-04

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 40.53  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  54 TKSNTVLLSGLTGSGKTVLFYQLRDGSShqgtVTSMePNEGTFVlhsENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQA 133
Cdd:cd04149   7 NKEMRILMLGLDAAGKTTILYKLKLGQS----VTTI-PTVGFNV---ETVTYKNVK-FNVWDVGGQDKIRPLWRHYYTGT 77

                ....*....
gi 42573277 134 AAIVFVVDA 142
Cdd:cd04149  78 QGLIFVVDS 86
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
113-203 8.25e-04

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.97  E-value: 8.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277 113 LVDVPG-HsrlRPK--LEEFLPQAA--------AIVFVVDALEFLpncRAASEYLYEILTNAnvvkkKIPVLLCCNKTDK 181
Cdd:COG1159  55 FVDTPGiH---KPKrkLGRRMNKAAwsaledvdVILFVVDATEKI---GEGDEFILELLKKL-----KTPVILVINKIDL 123
                        90       100
                ....*....|....*....|..
gi 42573277 182 LTahtkefiRKQMEKEIEKLRA 203
Cdd:COG1159 124 VK-------KEELLPLLAEYSE 138
era PRK00089
GTPase Era; Reviewed
113-196 8.41e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 40.03  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  113 LVDVPG-HSRLRpKLEEFLPQAA--------AIVFVVDALEFLpncraaSEYLYEILtnANVVKKKIPVLLCCNKTDKLt 183
Cdd:PRK00089  57 FVDTPGiHKPKR-ALNRAMNKAAwsslkdvdLVLFVVDADEKI------GPGDEFIL--EKLKKVKTPVILVLNKIDLV- 126
                         90
                 ....*....|...
gi 42573277  184 aHTKEFIRKQMEK 196
Cdd:PRK00089 127 -KDKEELLPLLEE 138
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
55-142 1.54e-03

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 38.36  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277     55 KSNTVLLSGLTGSGKTVLFYQLRDGSShqgtVTSMePNEGTFVlhsENTKKGKIKpVHLVDVPGHSRLRPKLEEFLPQAA 134
Cdd:smart00177  12 KEMRILMVGLDAAGKTTILYKLKLGES----VTTI-PTIGFNV---ETVTYKNIS-FTVWDVGGQDKIRPLWRHYYTNTQ 82

                   ....*...
gi 42573277    135 AIVFVVDA 142
Cdd:smart00177  83 GLIFVVDS 90
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
59-180 2.24e-03

Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206719 [Multi-domain]  Cd Length: 183  Bit Score: 37.86  E-value: 2.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  59 VLLSGLTGSGKTVLFYQLRdGSSHQGTVtsmePNEGTfvlhseNTKK-----GKIKPV--HLVDVPGHSRLRPKLEEFLP 131
Cdd:cd04152   6 IVMLGLDSAGKTTVLYRLK-FNEFVNTV----PTKGF------NTEKikvslGNAKGVtfHFWDVGGQEKLRPLWKSYTR 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42573277 132 QAAAIVFVVDALEflpncraaSEYLYEILTNANVVKK-----KIPVLLCCNKTD 180
Cdd:cd04152  75 CTDGIVFVVDSVD--------VERMEEAKTELHKITKfsenqGVPVLVLANKQD 120
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
63-197 4.57e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 36.84  E-value: 4.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573277  63 GLTGSGKTVLFYQLRDgsSHQGTV-----TSMEPNEGTFVLHsentkkgKIKPVHLVDVPG------HSRLRPKL-EEFL 130
Cdd:cd00880   4 GRPNVGKSSLLNALLG--QNVGIVspipgTTRDPVRKEWELL-------PLGPVVLIDTPGldeeggLGRERVEEaRQVA 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573277 131 PQAAAIVFVVDAlEFLPncraasEYLYEILTNANvvKKKIPVLLCCNKTDKLTAHTKEFIRKQMEKE 197
Cdd:cd00880  75 DRADLVLLVVDS-DLTP------VEEEAKLGLLR--ERGKPVLLVLNKIDLVPESEEEELLRERKLE 132
 
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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