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Conserved domains on  [gi|145558869|sp|Q9BU20|]
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RecName: Full=Ciliogenesis and planar polarity effector 2; AltName: Full=REM2- and Rab-like small GTPase 1

Protein Classification

GTPase domain-containing protein( domain architecture ID 10096372)

GTPase domain-containing protein with a Ras-like GTPase domain, similar to human interferon-induced protein 44-like, which exhibits antiviral activity against hepatitis C virus

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
62-180 1.77e-09

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: 55.16  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  62 GKSGVGKTALVAKLAGLEVPVV---HHETTGIQTTVVFWPAKLqassrvvmFRFEFWDC---GESALKKFDHMLLACMEN 135
Cdd:cd00882    4 GRGGVGKSSLLNALLGGEVGEVsdvPGTTRDPDVYVKELDKGK--------VKLVLVDTpglDEFGGLGREELARLLLRG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 145558869 136 TDAFLFLFSFTDRASFEDLPGQLARIAgEAPGVVRMVIGSKFDQY 180
Cdd:cd00882   76 ADLILLVVDSTDRESEEDAKLLILRRL-RKEGIPIILVGNKIDLL 119
 
Name Accession Description Interval E-value
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
62-180 1.77e-09

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: 55.16  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  62 GKSGVGKTALVAKLAGLEVPVV---HHETTGIQTTVVFWPAKLqassrvvmFRFEFWDC---GESALKKFDHMLLACMEN 135
Cdd:cd00882    4 GRGGVGKSSLLNALLGGEVGEVsdvPGTTRDPDVYVKELDKGK--------VKLVLVDTpglDEFGGLGREELARLLLRG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 145558869 136 TDAFLFLFSFTDRASFEDLPGQLARIAgEAPGVVRMVIGSKFDQY 180
Cdd:cd00882   76 ADLILLVVDSTDRESEEDAKLLILRRL-RKEGIPIILVGNKIDLL 119
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
57-178 1.53e-07

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 49.82  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869   57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQttvvFWPAKLQASSRVVmfRFEFWDcgeSA-LKKFDHMLLACMEN 135
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVD----FYTKTIEVDGKTV--KLQIWD---TAgQERFRALRPLYYRG 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 145558869  136 TDAFLFLFSFTDRASFEDLP---GQLARIAGEapGVVRMVIGSKFD 178
Cdd:pfam00071  72 ADGFLLVYDITSRDSFENVKkwvEEILRHADE--NVPIVLVGNKCD 115
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
57-189 7.23e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 48.05  E-value: 7.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETT-GIQttvvFWPAKLQASSrvVMFRFEFWDC-GESALKKFDHMLLACME 134
Cdd:COG1100    5 KIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTnGVT----IDKKELKLDG--LDVDLVIWDTpGQDEFRETRQFYARQLT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145558869 135 NTDAFLFLFSFTDRASFEDLP---GQLARIAGEAPGVvrmVIGSKFDQYMHTDVPERD 189
Cdd:COG1100   79 GASLYLFVVDGTREETLQSLYellESLRRLGKKSPII---LVLNKIDLYDEEEIEDEE 133
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
56-179 2.24e-04

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: 40.82  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869   56 YKIFVSGKSGVGKTALVAKLAGLEVPVVhheTTGIQTTVVFWPAKLQASSrvVMFRFEFWDCGESAlkKFDHMLLACMEN 135
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSIT---EYYPGTTRNYVTTVIEEDG--KTYKFNLLDTAGQE--DYDAIRRLYYPQ 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 145558869  136 TDAFLFLFSFTDRA-SFED-LPGQLARIAGEAP-GVVRMVIGSKFDQ 179
Cdd:TIGR00231  75 VERSLRVFDIVILVlDVEEiLEKQTKEIIHHADsGVPIILVGNKIDL 121
PLN03110 PLN03110
Rab GTPase; Provisional
56-250 2.34e-03

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 38.37  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  56 YKIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQttvvFWPAKLQASSRVVmfRFEFWDcgESALKKFDHMLLACMEN 135
Cdd:PLN03110  13 FKIVLIGDSGVGKSNILSRFTRNEFCLESKSTIGVE----FATRTLQVEGKTV--KAQIWD--TAGQERYRAITSAYYRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869 136 TDAFLFLFSFTDRASFEDLPGQLARIAGEA-PGVVRMVIGSKFDQYMHTDVPERDLTAFRQAWELPLLRVKSVPGRRLAD 214
Cdd:PLN03110  85 AVGALLVYDITKRQTFDNVQRWLRELRDHAdSNIVIMMAGNKSDLNHLRSVAEEDGQALAEKEGLSFLETSALEATNVEK 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145558869 215 G-RTLdgragLADVAHILNGLAeqLWHQDQVAAGLLP 250
Cdd:PLN03110 165 AfQTI-----LLEIYHIISKKA--LAAQEAAANSGLP 194
 
Name Accession Description Interval E-value
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
62-180 1.77e-09

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: 55.16  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  62 GKSGVGKTALVAKLAGLEVPVV---HHETTGIQTTVVFWPAKLqassrvvmFRFEFWDC---GESALKKFDHMLLACMEN 135
Cdd:cd00882    4 GRGGVGKSSLLNALLGGEVGEVsdvPGTTRDPDVYVKELDKGK--------VKLVLVDTpglDEFGGLGREELARLLLRG 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 145558869 136 TDAFLFLFSFTDRASFEDLPGQLARIAgEAPGVVRMVIGSKFDQY 180
Cdd:cd00882   76 ADLILLVVDSTDRESEEDAKLLILRRL-RKEGIPIILVGNKIDLL 119
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
57-178 1.53e-07

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 49.82  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869   57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQttvvFWPAKLQASSRVVmfRFEFWDcgeSA-LKKFDHMLLACMEN 135
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVD----FYTKTIEVDGKTV--KLQIWD---TAgQERFRALRPLYYRG 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 145558869  136 TDAFLFLFSFTDRASFEDLP---GQLARIAGEapGVVRMVIGSKFD 178
Cdd:pfam00071  72 ADGFLLVYDITSRDSFENVKkwvEEILRHADE--NVPIVLVGNKCD 115
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
56-152 7.16e-07

Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, Gem/Kir) subfamily of Ras GTPases are expressed in a tissue-specific manner and are dynamically regulated by transcriptional and posttranscriptional mechanisms in response to environmental cues. RGK proteins bind to the beta subunit of L-type calcium channels, causing functional down-regulation of these voltage-dependent calcium channels, and either termination of calcium-dependent secretion or modulation of electrical conduction and contractile function. Inhibition of L-type calcium channels by Rem2 may provide a mechanism for modulating calcium-triggered exocytosis in hormone-secreting cells, and has been proposed to influence the secretion of insulin in pancreatic beta cells. RGK proteins also interact with and inhibit the Rho/Rho kinase pathway to modulate remodeling of the cytoskeleton. Two characteristics of RGK proteins cited in the literature are N-terminal and C-terminal extensions beyond the GTPase domain typical of Ras superfamily members. The N-terminal extension is not conserved among family members; the C-terminal extension is reported to be conserved among the family and lack the CaaX prenylation motif typical of membrane-associated Ras proteins. However, a putative CaaX motif has been identified in the alignment of the C-terminal residues of this CD.


Pssm-ID: 206715 [Multi-domain]  Cd Length: 219  Bit Score: 48.55  E-value: 7.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  56 YKIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQT---TVVfwpAKLQASSRVVMfrfEFWDCGESALKKfDHmllaC 132
Cdd:cd04148    1 YRVVLLGDSGVGKSSLANIFTAGVYEDSAYEASGDDTyerTVS---VDGEEATLVVY---DHWEQEDGMWLE-DS----C 69
                         90       100
                 ....*....|....*....|
gi 145558869 133 MENTDAFLFLFSFTDRASFE 152
Cdd:cd04148   70 MQVGDAYVIVYSVTDRSSFE 89
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
57-189 7.23e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 48.05  E-value: 7.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETT-GIQttvvFWPAKLQASSrvVMFRFEFWDC-GESALKKFDHMLLACME 134
Cdd:COG1100    5 KIVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTnGVT----IDKKELKLDG--LDVDLVIWDTpGQDEFRETRQFYARQLT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145558869 135 NTDAFLFLFSFTDRASFEDLP---GQLARIAGEAPGVvrmVIGSKFDQYMHTDVPERD 189
Cdd:COG1100   79 GASLYLFVVDGTREETLQSLYellESLRRLGKKSPII---LVLNKIDLYDEEEIEDEE 133
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
56-200 1.08e-05

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 44.37  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  56 YKIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGI--QTTVVFWPAKlqassrvvMFRFEFWD-CG-EsalkKFDHMLLA 131
Cdd:cd00154    1 FKIVLIGDSGVGKTSLLLRFVDNKFSENYKSTIGVdfKSKTIEVDGK--------KVKLQIWDtAGqE----RFRSITSS 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869 132 CMENTDAFLFLFSFTDRASFEDLPGQLARIAGEAPG-VVRMVIGSKFDQYMHTDVPERDLTAFRQAWELP 200
Cdd:cd00154   69 YYRGAHGAILVYDVTNRESFENLDKWLNELKEYAPPnIPIILVGNKSDLEDERQVSTEEAQQFAKENGLL 138
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
57-196 1.30e-05

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 206701 [Multi-domain]  Cd Length: 182  Bit Score: 44.69  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQttvvFWPAKLQASSRVVMfrFEFWDCGESalKKFDHMLLACMENT 136
Cdd:cd04128    2 KIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVN----FMEKTISIRGTEIT--FSIWDLGGQ--REFINMLPLVCKDA 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869 137 DAFLFLFSFTDRASFEDLPGQLARIAGEAPGVVRMVIGSKFDQYMHTDvPERDLTAFRQA 196
Cdd:cd04128   74 VAILFMFDLTRKSTLNSIKEWYRQARGFNKTAIPILVGTKYDLFADLP-PEEQEEITKQA 132
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
57-196 7.92e-05

Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown.


Pssm-ID: 206688 [Multi-domain]  Cd Length: 167  Bit Score: 42.13  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLA--GLEVPVVHHETTGIQTTVVFWPAKLQASSrVVMFRFEfwdcgESALKKFDHMLLACME 134
Cdd:cd04101    2 QCAVVGDPAVGKSALVQMFHsdGATFQKNYTMTTGCDLVVKTVPVPDTSDS-VELFIFD-----SAGQELFSDMVENVWE 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145558869 135 NTDAFLFLFSFTDRASFEDLPGQLARIAGEAPGV--VRMVIGSKFDQYMHTDVPERDLTAFRQA 196
Cdd:cd04101   76 QPAVVCVVYDVTNEVSFNNCSRWINRVRTHSHGLhtPGVLVGNKCDLTDRREVDAAQAQALAQA 139
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
56-179 2.24e-04

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: 40.82  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869   56 YKIFVSGKSGVGKTALVAKLAGLEVPVVhheTTGIQTTVVFWPAKLQASSrvVMFRFEFWDCGESAlkKFDHMLLACMEN 135
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSIT---EYYPGTTRNYVTTVIEEDG--KTYKFNLLDTAGQE--DYDAIRRLYYPQ 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 145558869  136 TDAFLFLFSFTDRA-SFED-LPGQLARIAGEAP-GVVRMVIGSKFDQ 179
Cdd:TIGR00231  75 VERSLRVFDIVILVlDVEEiLEKQTKEIIHHADsGVPIILVGNKIDL 121
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
57-206 6.60e-04

Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signaling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133306 [Multi-domain]  Cd Length: 162  Bit Score: 39.35  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQttvvFWPAKLQASSRVVMFRFEFWDCgeSALKKFDHMLLACMENT 136
Cdd:cd04106    2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVD----FLEKQIFLRQSDEDVRLMLWDT--AGQEEFDAITKAYYRGA 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869 137 DAFLFLFSFTDRASFEDLPGQLARIAGEAPGVVRMVIGSKFDQYMHTDVPERDLTAFRQAWELPLLRVKS 206
Cdd:cd04106   76 QACILVFSTTDRESFEAIESWKEKVEAECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSV 145
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
57-202 1.58e-03

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 38.28  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETtgIQ----TTVVFwpaklqaSSRVVMFRF-------EFwdcgeSALKkf 125
Cdd:cd00876    1 KLVVLGAGGVGKSALTIRFVSGEFVEEYDPT--IEdsyrKQIVV-------DGETYTLDIldtagqeEF-----SAMR-- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869 126 DHmllaCMENTDAFLFLFSFTDRASFEDLPG---QLARIAGeaPGVVRMVI-GSKFDQYMHTDVPERDLTAFRQAWELPL 201
Cdd:cd00876   65 DQ----YIRNGDGFILVYSITSRESFEEIKNireQILRVKD--KEDVPIVLvGNKCDLENERQVSTEEGEALAEEWGCPF 138

                 .
gi 145558869 202 L 202
Cdd:cd00876  139 L 139
PLN03110 PLN03110
Rab GTPase; Provisional
56-250 2.34e-03

Rab GTPase; Provisional


Pssm-ID: 178657 [Multi-domain]  Cd Length: 216  Bit Score: 38.37  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  56 YKIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQttvvFWPAKLQASSRVVmfRFEFWDcgESALKKFDHMLLACMEN 135
Cdd:PLN03110  13 FKIVLIGDSGVGKSNILSRFTRNEFCLESKSTIGVE----FATRTLQVEGKTV--KAQIWD--TAGQERYRAITSAYYRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869 136 TDAFLFLFSFTDRASFEDLPGQLARIAGEA-PGVVRMVIGSKFDQYMHTDVPERDLTAFRQAWELPLLRVKSVPGRRLAD 214
Cdd:PLN03110  85 AVGALLVYDITKRQTFDNVQRWLRELRDHAdSNIVIMMAGNKSDLNHLRSVAEEDGQALAEKEGLSFLETSALEATNVEK 164
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 145558869 215 G-RTLdgragLADVAHILNGLAeqLWHQDQVAAGLLP 250
Cdd:PLN03110 165 AfQTI-----LLEIYHIISKKA--LAAQEAAANSGLP 194
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
57-213 3.23e-03

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: 37.32  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGLEVPVVHHETTGIQttVVFWPAKLQASSRvvmFRFEFWDCGESALKKFDHMLLacMENT 136
Cdd:cd09914    3 KLMLVGQGGVGKTSLCKQLIGEKFDGDESSTHGIN--VQDWKIPAPERKK---IRLNVWDFGGQEIYHATHQFF--LTSR 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145558869 137 DAFLFLFSFTDRASFEDLPGQLARIagEAPGVVRMVI--GSKFDQYMHTDVPERDLTAFRQAWELPLLRVKSVPGRRLA 213
Cdd:cd09914   76 SLYLLVFDLRTGDEVSRVPYWLRQI--KAFGGVSPVIlvGTHIDESCDEDILKKALNKKFPAIINDIHFVSCKNGKGIA 152
Rab40 cd04121
Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains ...
57-193 4.10e-03

Rab GTPase family 40 (Rab40) contains Rab40a, Rab40b and Rab40c; The Rab40 subfamily contains Rab40a, Rab40b, and Rab40c, which are all highly homologous. In rat, Rab40c is localized to the perinuclear recycling compartment (PRC), and is distributed in a tissue-specific manor, with high expression in brain, heart, kidney, and testis, low expression in lung and liver, and no expression in spleen and skeletal muscle. Rab40c is highly expressed in differentiated oligodendrocytes but minimally expressed in oligodendrocyte progenitors, suggesting a role in the vesicular transport of myelin components. Unlike most other Ras-superfamily proteins, Rab40c was shown to have a much lower affinity for GTP, and an affinity for GDP that is lower than for GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133321 [Multi-domain]  Cd Length: 189  Bit Score: 37.22  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKL--AGLEVPVVHHETTGIQTTVVFWPAKlqassRVvmfRFEFWDCgeSALKKFDHMLLACME 134
Cdd:cd04121    8 KFLLVGDSDVGKGEILASLqdGSTESPYGYNMGIDYKTTTILLDGR-----RV---KLQLWDT--SGQGRFCTIFRSYSR 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145558869 135 NTDAFLFLFSFTDRASFEDLPGQLARIAGEAPGVVRMVIGSKFDQYMHTDVPERDLTAF 193
Cdd:cd04121   78 GAQGIILVYDITNRWSFDGIDRWIKEIDEHAPGVPKILVGNRLHLAFKRQVATEQAQAY 136
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
56-178 4.16e-03

Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, and RSR1. Rap subfamily proteins perform different cellular functions, depending on the isoform and its subcellular localization. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and microsomal membrane of the pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. Rap1 localizes in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap2 is involved in multiple functions, including activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton and activation of the Wnt/beta-catenin signaling pathway in embryonic Xenopus. A number of effector proteins for Rap2 have been identified, including isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK), and the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. RSR1 is the fungal homolog of Rap1 and Rap2. In budding yeasts, it is involved in selecting a site for bud growth, which directs the establishment of cell polarization. The Rho family GTPase Cdc42 and its GEF, Cdc24, then establish an axis of polarized growth. It is believed that Cdc42 interacts directly with RSR1 in vivo. In filamentous fungi such as Ashbya gossypii, RSR1 is a key regulator of polar growth in the hypha. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206708 [Multi-domain]  Cd Length: 164  Bit Score: 37.15  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  56 YKIFVSGKSGVGKTALVAKLagleVPVVHHETTGiQTTVVFWPAKLQASSRVVMFrfEFWDCgeSALKKFDHMLLACMEN 135
Cdd:cd04136    2 YKLVVLGSGGVGKSALTVQF----VQGIFVDKYD-PTIEDSYRKQIEVDCQQCML--EILDT--AGTEQFTAMRDLYIKN 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145558869 136 TDAFLFLFSFTDRASFEDLP---GQLARIAgEAPGVVRMVIGSKFD 178
Cdd:cd04136   73 GQGFALVYSITAQQSFNDLQdlrEQILRVK-DTEDVPMILVGNKCD 117
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
57-154 7.91e-03

Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho (Ras homology) family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Since crystal structures often lack C-terminal residues, this feature is not available for annotation in many of the CDs in the hierarchy.


Pssm-ID: 206641 [Multi-domain]  Cd Length: 171  Bit Score: 36.37  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGLEVPvvhheTTGIQTtvVF--WPAKLQASSRvvMFRFEFWDcgESALKKFDHMLLACME 134
Cdd:cd00157    2 KIVVVGDGAVGKTCLLISYTTNKFP-----TEYVPT--VFdnYSANVTVDGK--QVNLGLWD--TAGQEEYDRLRPLSYP 70
                         90       100
                 ....*....|....*....|
gi 145558869 135 NTDAFLFLFSFTDRASFEDL 154
Cdd:cd00157   71 QTDVFLLCFSVDSPSSFENV 90
PRK13695 PRK13695
NTPase;
57-78 9.65e-03

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 36.04  E-value: 9.65e-03
                         10        20
                 ....*....|....*....|..
gi 145558869  57 KIFVSGKSGVGKTALVAKLAGL 78
Cdd:PRK13695   2 KIGITGPPGVGKTTLVLKIAEL 23
 
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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