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Conserved domains on  [gi|571026635|ref|NP_001275684|]
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mitochondrial Rho GTPase 1 isoform 6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Miro2 cd01892
Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) ...
 394-571 2.17e-91

Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


:

Pssm-ID: 206679  Cd Length: 180  Bit Score: 279.13  E-value: 2.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 394 QRNVFRCNVIGVKNCGKSGVLQALLGRNLMrQKKIREDHKSYYAINTVYVYGQEKYLLLHDISESEFLTEAEII----CD 469
Cdd:cd01892    1 QRNVFLCFVLGAKGSGKSALLQAFLGRSFS-QNAYSPTIKPRYAVNTVEVPGQEKYLILREVGEDEEAILLNDAelaaCD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 470 VVCLVYDVSNPKSFEYCARIFKQHFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKMPPPQAFTCNTADaPSKDIF 549
Cdd:cd01892   80 VACLVYDSSDPNSFSYCAEVYKKYFMLGEIPCLFVAAKADLDEQQQRAEVQPDEFCRKLGLPPPLHFSSRLGD-SSNELF 158

                        170       180
                 ....*....|....*....|..
gi 571026635 550 VKLTTMAMYPHVTQADLKSSTF 571
Cdd:cd01892  159 TKLATAAQYPHLSIPELESGKT 180
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 1-148 5.22e-80

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 cd01893:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 168  Bit Score: 249.18  E-value: 5.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   1 MSLVSEEFPEEVPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLI 80
Cdd:cd01893   20 MSLVSEEFPENVPRVLPEITIPADVTPERVPTTIVDTSSRPQDRANLAAEIRKANVICLVYSVDRPSTLERIRTKWLPLI 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571026635  81 NERTDkdsRLPLILVGNKSDLVEYSS----METILPIMNQYTEIETCVECSAKNLKNISELFYYAQKAVLHP 148
Cdd:cd01893  100 RRLGV---KVPIILVGNKSDLRDGSSqaglEEEMLPIMNEFREIETCVECSAKTLINVSEVFYYAQKAVLHP 168
EF_assoc_2 pfam08356
EF hand associated; This region predominantly appears near EF-hands (pfam00036) in GTP-binding ...
 198-282 3.36e-50

EF hand associated; This region predominantly appears near EF-hands (pfam00036) in GTP-binding proteins. It is found in all three eukaryotic kingdoms.


:

Pssm-ID: 462444  Cd Length: 85  Bit Score: 168.04  E-value: 3.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  198 TPLAPQALEDVKNVVRKHISDGVADSGLTLKGFLFLHTLFIQRGRHETTWTVLRRFGYDDDLDLTPEYLFPLLKIPPDCT 277
Cdd:pfam08356   1 KPLSPQELEDIKSVVQKNLPDGVSDNGLTLKGFLFLNKLFIEKGRHETTWTILRKFGYTDSLSLKDDYLHPKFDVPPDSS 80


                  ....*
gi 571026635  278 TELNH 282
Cdd:pfam08356  81 VELSP 85
EF_assoc_1 pfam08355
EF hand associated; This region typically appears on the C-terminus of EF hands in GTP-binding ...
 320-389 1.49e-34

EF hand associated; This region typically appears on the C-terminus of EF hands in GTP-binding proteins such as Arht/Rhot (may be involved in mitochondrial homeostasis and apoptosis). The EF hand associated region is found in yeast, vertebrates and plants.


:

Pssm-ID: 462443  Cd Length: 70  Bit Score: 124.96  E-value: 1.49e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571026635  320 W-GPDVNNTVCTNERGWITYQGFLSQWTLTTYLDVQRCLEYLGYLGYSILTEQESQaSAVTVTRDKKIDLQ 389
Cdd:pfam08355   1 WlEPDFPDTVVTNEKGWLTLQGFLAQWSLTTLLDPKRTLEYLAYLGYPGDLGSQSQ-SAIKVTRPRKLDRK 70
 
Name Accession Description Interval E-value
Miro2 cd01892
Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) ...
 394-571 2.17e-91

Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206679  Cd Length: 180  Bit Score: 279.13  E-value: 2.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 394 QRNVFRCNVIGVKNCGKSGVLQALLGRNLMrQKKIREDHKSYYAINTVYVYGQEKYLLLHDISESEFLTEAEII----CD 469
Cdd:cd01892    1 QRNVFLCFVLGAKGSGKSALLQAFLGRSFS-QNAYSPTIKPRYAVNTVEVPGQEKYLILREVGEDEEAILLNDAelaaCD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 470 VVCLVYDVSNPKSFEYCARIFKQHFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKMPPPQAFTCNTADaPSKDIF 549
Cdd:cd01892   80 VACLVYDSSDPNSFSYCAEVYKKYFMLGEIPCLFVAAKADLDEQQQRAEVQPDEFCRKLGLPPPLHFSSRLGD-SSNELF 158

                        170       180
                 ....*....|....*....|..
gi 571026635 550 VKLTTMAMYPHVTQADLKSSTF 571
Cdd:cd01892  159 TKLATAAQYPHLSIPELESGKT 180
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
 1-148 5.22e-80

Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206680 [Multi-domain]  Cd Length: 168  Bit Score: 249.18  E-value: 5.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   1 MSLVSEEFPEEVPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLI 80
Cdd:cd01893   20 MSLVSEEFPENVPRVLPEITIPADVTPERVPTTIVDTSSRPQDRANLAAEIRKANVICLVYSVDRPSTLERIRTKWLPLI 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571026635  81 NERTDkdsRLPLILVGNKSDLVEYSS----METILPIMNQYTEIETCVECSAKNLKNISELFYYAQKAVLHP 148
Cdd:cd01893  100 RRLGV---KVPIILVGNKSDLRDGSSqaglEEEMLPIMNEFREIETCVECSAKTLINVSEVFYYAQKAVLHP 168
EF_assoc_2 pfam08356
EF hand associated; This region predominantly appears near EF-hands (pfam00036) in GTP-binding ...
 198-282 3.36e-50

EF hand associated; This region predominantly appears near EF-hands (pfam00036) in GTP-binding proteins. It is found in all three eukaryotic kingdoms.


Pssm-ID: 462444  Cd Length: 85  Bit Score: 168.04  E-value: 3.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  198 TPLAPQALEDVKNVVRKHISDGVADSGLTLKGFLFLHTLFIQRGRHETTWTVLRRFGYDDDLDLTPEYLFPLLKIPPDCT 277
Cdd:pfam08356   1 KPLSPQELEDIKSVVQKNLPDGVSDNGLTLKGFLFLNKLFIEKGRHETTWTILRKFGYTDSLSLKDDYLHPKFDVPPDSS 80


                  ....*
gi 571026635  278 TELNH 282
Cdd:pfam08356  81 VELSP 85
EF_assoc_1 pfam08355
EF hand associated; This region typically appears on the C-terminus of EF hands in GTP-binding ...
 320-389 1.49e-34

EF hand associated; This region typically appears on the C-terminus of EF hands in GTP-binding proteins such as Arht/Rhot (may be involved in mitochondrial homeostasis and apoptosis). The EF hand associated region is found in yeast, vertebrates and plants.


Pssm-ID: 462443  Cd Length: 70  Bit Score: 124.96  E-value: 1.49e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571026635  320 W-GPDVNNTVCTNERGWITYQGFLSQWTLTTYLDVQRCLEYLGYLGYSILTEQESQaSAVTVTRDKKIDLQ 389
Cdd:pfam08355   1 WlEPDFPDTVVTNEKGWLTLQGFLAQWSLTTLLDPKRTLEYLAYLGYPGDLGSQSQ-SAIKVTRPRKLDRK 70
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
 52-148 2.35e-11

Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.


Pssm-ID: 197554 [Multi-domain]  Cd Length: 174  Bit Score: 62.63  E-value: 2.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635    52 SQANVICIVYAVNNKHSIDKVTSRWIPLINERTDKdsrLPLILVGNKSDLVEYSSMETILPIMNQ--YTEIETC------ 123
Cdd:smart00174  68 PDTDVFLICFSVDSPASFENVKEKWYPEVKHFCPN---VPIILVGTKLDLRNDKSTLEELSKKKQepVTYEQGQalakri 144

                           90       100       110
                   ....*....|....*....|....*....|
gi 571026635   124 -----VECSAKNLKNISELFYYAQKAVLHP 148
Cdd:smart00174 145 gavkyLECSALTQEGVREVFEEAIRAALNK 174
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 53-146 1.67e-09

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: 57.14  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   53 QANVICIVYAVNNKHSIDKVTsRWIPLINERTDKDsrLPLILVGNKSDL-----VEYSSMETI-----LPIMnqyteiet 122
Cdd:pfam00071  71 GADGFLLVYDITSRDSFENVK-KWVEEILRHADEN--VPIVLVGNKCDLedqrvVSTEEGEALakelgLPFM-------- 139

                          90       100
                  ....*....|....*....|....
gi 571026635  123 cvECSAKNLKNISELFYYAQKAVL 146
Cdd:pfam00071 140 --ETSAKTNENVEEAFEELAREIL 161
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 445-531 9.58e-05

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: 43.27  E-value: 9.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  445 GQEKYlllHDISESEFLTeaeiiCDVVCLVYDVSNPKSFEYCARIFKQ--HFMDSRIPCLIVAAKSDLHEVKQeysISPT 522
Cdd:pfam00071  57 GQERF---RALRPLYYRG-----ADGFLLVYDITSRDSFENVKKWVEEilRHADENVPIVLVGNKCDLEDQRV---VSTE 125

                          90
                  ....*....|..
gi 571026635  523 D---FCRKHKMP 531
Cdd:pfam00071 126 EgeaLAKELGLP 137
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 473-531 1.64e-04

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 42.50  E-value: 1.64e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 571026635   473 LVYDVSNPKSFEYCARIFK--QHFMDSRIPCLIVAAKSDL---HEVKQEysiSPTDFCRKHKMP 531
Cdd:smart00175  78 LVYDITNRESFENLENWLKelREYASPNVVIMLVGNKSDLeeqRQVSRE---EAEAFAEEHGLP 138
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
86-157 2.98e-04

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 43.05  E-value: 2.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 571026635  86 KDSRLPLILVGNKSDLVeysSMETILPIMNQYTEI---ETCVECSAKNLKNISELFyyaqKAVLH--PTGPLYCPEE 157
Cdd:COG1159  108 KKLKTPVILVINKIDLV---KKEELLPLLAEYSELldfAEIVPISALKGDNVDELL----DEIAKllPEGPPYYPED 177
era PRK00089
GTPase Era; Reviewed
 86-157 3.35e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 42.73  E-value: 3.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 571026635  86 KDSRLPLILVGNKSDLVeySSMETILPIMNQYTE----IETcVECSAKNLKNISELFYYAQKAVlhPTGPLYCPEE 157
Cdd:PRK00089 110 KKVKTPVILVLNKIDLV--KDKEELLPLLEELSElmdfAEI-VPISALKGDNVDELLDVIAKYL--PEGPPYYPED 180
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
168-323 3.31e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 168 LTRIFKISDQDNDGTLNDAELNFFqricfntplapqALEDVKNVVRKHISDGvaDSGLTLKGFLFLHTLFIQRGRHETTW 247
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDFEAL------------FRRLWATLFSEADTDG--DGRISREEFVAGMESLFEATVEPFAR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 248 TVLRRFgyDDDLD--LTPEYLFPLLK---IPPDCTTELnhhaylflqstFDKHDLDRDCALSPDELKDLFKVFpyipWGP 322
Cdd:COG5126   73 AAFDLL--DTDGDgkISADEFRRLLTalgVSEEEADEL-----------FARLDTDGDGKISFEEFVAAVRDY----YTP 135


                 .
gi 571026635 323 D 323
Cdd:COG5126  136 D 136
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 56-140 4.64e-03

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: 38.12  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   56 VICIVYAVNNKHSIDKVTSRWIPLINERTDKDSrlPLILVGNKSDLVEYSSME---TILPIMNQYTEIETcvecSAKNLK 132
Cdd:TIGR00231  78 SLRVFDIVILVLDVEEILEKQTKEIIHHADSGV--PIILVGNKIDLKDADLKThvaSEFAKLNGEPIIPL----SAETGK 151


                  ....*...
gi 571026635  133 NISELFYY 140
Cdd:TIGR00231 152 NIDSAFKI 159
 
Name Accession Description Interval E-value
Miro2 cd01892
Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) ...
 394-571 2.17e-91

Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206679  Cd Length: 180  Bit Score: 279.13  E-value: 2.17e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 394 QRNVFRCNVIGVKNCGKSGVLQALLGRNLMrQKKIREDHKSYYAINTVYVYGQEKYLLLHDISESEFLTEAEII----CD 469
Cdd:cd01892    1 QRNVFLCFVLGAKGSGKSALLQAFLGRSFS-QNAYSPTIKPRYAVNTVEVPGQEKYLILREVGEDEEAILLNDAelaaCD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 470 VVCLVYDVSNPKSFEYCARIFKQHFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKMPPPQAFTCNTADaPSKDIF 549
Cdd:cd01892   80 VACLVYDSSDPNSFSYCAEVYKKYFMLGEIPCLFVAAKADLDEQQQRAEVQPDEFCRKLGLPPPLHFSSRLGD-SSNELF 158

                        170       180
                 ....*....|....*....|..
gi 571026635 550 VKLTTMAMYPHVTQADLKSSTF 571
Cdd:cd01892  159 TKLATAAQYPHLSIPELESGKT 180
Miro1 cd01893
Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) ...
 1-148 5.22e-80

Mitochondrial Rho family 1 (Miro1), N-terminal; Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.


Pssm-ID: 206680 [Multi-domain]  Cd Length: 168  Bit Score: 249.18  E-value: 5.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   1 MSLVSEEFPEEVPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLI 80
Cdd:cd01893   20 MSLVSEEFPENVPRVLPEITIPADVTPERVPTTIVDTSSRPQDRANLAAEIRKANVICLVYSVDRPSTLERIRTKWLPLI 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 571026635  81 NERTDkdsRLPLILVGNKSDLVEYSS----METILPIMNQYTEIETCVECSAKNLKNISELFYYAQKAVLHP 148
Cdd:cd01893  100 RRLGV---KVPIILVGNKSDLRDGSSqaglEEEMLPIMNEFREIETCVECSAKTLINVSEVFYYAQKAVLHP 168
EF_assoc_2 pfam08356
EF hand associated; This region predominantly appears near EF-hands (pfam00036) in GTP-binding ...
 198-282 3.36e-50

EF hand associated; This region predominantly appears near EF-hands (pfam00036) in GTP-binding proteins. It is found in all three eukaryotic kingdoms.


Pssm-ID: 462444  Cd Length: 85  Bit Score: 168.04  E-value: 3.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  198 TPLAPQALEDVKNVVRKHISDGVADSGLTLKGFLFLHTLFIQRGRHETTWTVLRRFGYDDDLDLTPEYLFPLLKIPPDCT 277
Cdd:pfam08356   1 KPLSPQELEDIKSVVQKNLPDGVSDNGLTLKGFLFLNKLFIEKGRHETTWTILRKFGYTDSLSLKDDYLHPKFDVPPDSS 80


                  ....*
gi 571026635  278 TELNH 282
Cdd:pfam08356  81 VELSP 85
EF_assoc_1 pfam08355
EF hand associated; This region typically appears on the C-terminus of EF hands in GTP-binding ...
 320-389 1.49e-34

EF hand associated; This region typically appears on the C-terminus of EF hands in GTP-binding proteins such as Arht/Rhot (may be involved in mitochondrial homeostasis and apoptosis). The EF hand associated region is found in yeast, vertebrates and plants.


Pssm-ID: 462443  Cd Length: 70  Bit Score: 124.96  E-value: 1.49e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571026635  320 W-GPDVNNTVCTNERGWITYQGFLSQWTLTTYLDVQRCLEYLGYLGYSILTEQESQaSAVTVTRDKKIDLQ 389
Cdd:pfam08355   1 WlEPDFPDTVVTNEKGWLTLQGFLAQWSLTTLLDPKRTLEYLAYLGYPGDLGSQSQ-SAIKVTRPRKLDRK 70
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 54-141 4.12e-12

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: 64.40  E-value: 4.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  54 ANVICIVYAVNNKHSIDKVtSRWIPLINERTDKDsrLPLILVGNKSDLVEYS--SMETILPIMNQYteIETCVECSAKNL 131
Cdd:cd00154   73 AHGAILVYDVTNRESFENL-DKWLNELKEYAPPN--IPIILVGNKSDLEDERqvSTEEAQQFAKEN--GLLFFETSAKTG 147

                         90
                 ....*....|
gi 571026635 132 KNISELFYYA 141
Cdd:cd00154  148 ENVDEAFESL 157
RHO smart00174
Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like ...
 52-148 2.35e-11

Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms.


Pssm-ID: 197554 [Multi-domain]  Cd Length: 174  Bit Score: 62.63  E-value: 2.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635    52 SQANVICIVYAVNNKHSIDKVTSRWIPLINERTDKdsrLPLILVGNKSDLVEYSSMETILPIMNQ--YTEIETC------ 123
Cdd:smart00174  68 PDTDVFLICFSVDSPASFENVKEKWYPEVKHFCPN---VPIILVGTKLDLRNDKSTLEELSKKKQepVTYEQGQalakri 144

                           90       100       110
                   ....*....|....*....|....*....|
gi 571026635   124 -----VECSAKNLKNISELFYYAQKAVLHP 148
Cdd:smart00174 145 gavkyLECSALTQEGVREVFEEAIRAALNK 174
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
 1-170 7.67e-11

Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a GTPase that controls septum degradation by regulating secretion of Eng1 or Agn1 during cytokinesis. Rho4 also plays a role in cell morphogenesis. Rho4 regulates septation and cell morphology by controlling the actin cytoskeleton and cytoplasmic microtubules. The localization of Rho4 is modulated by Rdi1, which may function as a GDI, and by Rga9, which is believed to function as a GAP. In S. pombe, both Rho4 deletion and Rho4 overexpression result in a defective cell wall, suggesting a role for Rho4 in maintaining cell wall integrity. 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.


Pssm-ID: 206704 [Multi-domain]  Cd Length: 197  Bit Score: 61.59  E-value: 7.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   1 MSLVSEEFPEEVPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEIS--QANVICIVYAVNNKHSIDKVTSRWIP 78
Cdd:cd04132   21 MVYAQGSFPEEYVPTVFENYVTTLQVPNGKIIELALWDTAGQEDYDRLRPLSypDVDVILICYSVDNPTSLDNVEDKWYP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  79 LINERTDKdsrLPLILVGNKSDLveYSSMETILPIMNQYTEIETC---------------VECSAKNLKNISELFYYAQK 143
Cdd:cd04132  101 EVNHFCPG---TPIVLVGLKTDL--RKDKNSVSKLRAQGLEPVTPeqgesvaksigavayIECSAKLMENVDEVFDAAIN 175

                        170       180
                 ....*....|....*....|....*..
gi 571026635 144 AVLhptgplycpeeKEMKPACIKALTR 170
Cdd:cd04132  176 VAL-----------SKSGRAARKKKKK 191
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 2-143 1.28e-10

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: 60.16  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   2 SLVSEEFPEEVPPR---AEEITIPADVTPERVPTHIVD-----YSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVT 73
Cdd:cd00882   16 ALLGGEVGEVSDVPgttRDPDVYVKELDKGKVKLVLVDtpgldEFGGLGREELARLLLRGADLILLVVDSTDRESEEDAK 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571026635  74 SRWIplineRTDKDSRLPLILVGNKSDLVEYSSMETILP-IMNQYTEIETCVECSAKNLKNISELFYYAQK 143
Cdd:cd00882   96 LLIL-----RRLRKEGIPIILVGNKIDLLEEREVEELLRlEELAKILGVPVFEVSAKTGEGVDELFEKLIE 161
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 3-140 1.38e-10

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: 59.85  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   3 LVSEEFPEEVPPRAEEI-TIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVtSRWIPLIN 81
Cdd:cd00876   19 FVSGEFVEEYDPTIEDSyRKQIVVDGETYTLDILDTAGQEEFSAMRDQYIRNGDGFILVYSITSRESFEEI-KNIREQIL 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 571026635  82 ERTDKDsRLPLILVGNKSDLVEYSSMetilpimnQYTEIETCV--------ECSAKNLKNISELFYY 140
Cdd:cd00876   98 RVKDKE-DVPIVLVGNKCDLENERQV--------STEEGEALAeewgcpflETSAKTNINIDELFNT 155
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 402-540 7.61e-10

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: 57.85  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 402 VIGVKNCGKSGVLQALLGRNLMRQKKIRE--DHKSYYAINTVYVYGQekyLLLHD---ISESEFLTEAEII------CDV 470
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGttRDPDVYVKELDKGKVK---LVLVDtpgLDEFGGLGREELArlllrgADL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 471 VCLVYDVSNPKSFEYCARIFKQHFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKMPPPQAFTCNT 540
Cdd:cd00882   79 ILLVVDSTDRESEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGVPVFEVSAKT 148
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 53-146 1.67e-09

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: 57.14  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   53 QANVICIVYAVNNKHSIDKVTsRWIPLINERTDKDsrLPLILVGNKSDL-----VEYSSMETI-----LPIMnqyteiet 122
Cdd:pfam00071  71 GADGFLLVYDITSRDSFENVK-KWVEEILRHADEN--VPIVLVGNKCDLedqrvVSTEEGEALakelgLPFM-------- 139

                          90       100
                  ....*....|....*....|....
gi 571026635  123 cvECSAKNLKNISELFYYAQKAVL 146
Cdd:pfam00071 140 --ETSAKTNENVEEAFEELAREIL 161
Rho cd00157
Ras homology family (Rho) of small guanosine triphosphatases (GTPases); Members of the Rho ...
 53-138 6.05e-09

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: 55.63  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  53 QANVICIVYAVNNKHSIDKVTSRWIPLINERTdkdSRLPLILVGNKSDLVEYSSMETILPIMN---QYTEIETC------ 123
Cdd:cd00157   71 QTDVFLLCFSVDSPSSFENVKTKWYPEIKHYC---PNVPIILVGTKIDLRDDGNTLKKLEKKQkpiTPEEGEKLakeiga 147

                         90
                 ....*....|....*...
gi 571026635 124 ---VECSAKNLKNISELF 138
Cdd:cd00157  148 vkyMECSALTQEGLKEVF 165
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
 20-138 1.62e-08

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: 54.07  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  20 TIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVtSRWIPLINERTdKDSRLPLILVGNKS 99
Cdd:cd04101   43 TVPVPDTSDSVELFIFDSAGQELFSDMVENVWEQPAVVCVVYDVTNEVSFNNC-SRWINRVRTHS-HGLHTPGVLVGNKC 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 571026635 100 DLVEYSSME----TILPIMNQYteieTCVECSAKNLKNISELF 138
Cdd:cd04101  121 DLTDRREVDaaqaQALAQANTL----KFYETSAKEGVGYEAPF 159
RhoG cd01875
Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a ...
 1-149 1.38e-07

Ras homolog family, member G (RhoG) of small guanosine triphosphatases (GTPases); RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. RhoG has also been shown to play a role in caveolar trafficking and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists. 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.


Pssm-ID: 133277 [Multi-domain]  Cd Length: 191  Bit Score: 51.93  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   1 MSLVSEEFPEE-VPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPl 79
Cdd:cd01875   21 ICYTTNAFPKEyIPTVFDNYSAQTAVDGRTVSLNLWDTAGQEEYDRLRTLSYPQTNVFIICFSIASPSSYENVRHKWHP- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  80 inERTDKDSRLPLILVGNKSDL------VEYSSMETILPIMNQY-----TEIETC--VECSAKNLKNISELFYYAQKAVL 146
Cdd:cd01875  100 --EVCHHCPNVPILLVGTKKDLrndadtLKKLKEQGQAPITPQQggalaKQIHAVkyLECSALNQDGVKEVFAEAVRAVL 177


                 ...
gi 571026635 147 HPT 149
Cdd:cd01875  178 NPT 180
Rho2 cd04129
Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal ...
 7-146 2.25e-07

Ras homology family 2 (Rho2) of small guanosine triphosphatases (GTPases); Rho2 is a fungal GTPase that plays a role in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Rho2 activates the protein kinase C homolog Pck2, and Pck2 controls Mok1, the major (1-3) alpha-D-glucan synthase. Together with Rho1 (RhoA), Rho2 regulates the construction of the cell wall. Unlike Rho1, Rho2 is not an essential protein, but its overexpression is lethal. 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 proper intracellular localization via membrane attachment. As with other Rho family GTPases, the GDP/GTP cycling is regulated by GEFs (guanine nucleotide exchange factors), GAPs (GTPase-activating proteins) and GDIs (guanine nucleotide dissociation inhibitors).


Pssm-ID: 206702 [Multi-domain]  Cd Length: 190  Bit Score: 51.37  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   7 EFPEEVPPRAEEITIpADVTPERVPTHIVDYSEAEQSD-EQLHQ-EISQANVICIVYAVNNKHSIDKVTSRWIPLINERT 84
Cdd:cd04129   25 EFPEEYHPTVFENYV-TDCRVDGKPVQLALWDTAGQEEyERLRPlSYSKAHVILIGFAIDTPDSLENVRTKWIEEVRRYC 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 571026635  85 DKdsrLPLILVGNKSDL-VEYSSMETilPIMNQYTEIETC------------VECSAKNLKNISELFYYAQKAVL 146
Cdd:cd04129  104 PN---VPVILVGLKKDLrQEAVAKGN--YATDEFVPIQQAklvaraigakkyMECSALTGEGVDDVFEAATRAAL 173
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
 49-139 8.60e-07

Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small GTPases of the ARF, RAB, RAN, RAS, and SAR subfamilies. Others that could not be classified in this way are predicted to be members of the small GTPase superfamily without predictions of the subfamily.


Pssm-ID: 197466 [Multi-domain]  Cd Length: 166  Bit Score: 49.10  E-value: 8.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635    49 QEISQANVICIVYAVNNKHSIDKVTSRWIPLIneRTDKDSRLPLILVGNKSDLVEYS--SMETILPIMNQYteieTC--V 124
Cdd:smart00010  69 QYMRTGEGFLLVYSITDRQSFEEIAKFREQIL--RVKDRDDVPIVLVGNKCDLENERvvSTEEGKELARQW----GCpfL 142

                           90
                   ....*....|....*
gi 571026635   125 ECSAKNLKNISELFY 139
Cdd:smart00010 143 ETSAKERINVDEAFY 157
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
 51-138 1.67e-06

Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways through the Golgi and from endosomes to the Golgi. Rab6A of mammals is implicated in retrograde transport through the Golgi stack, and is also required for a slow, COPI-independent, retrograde transport pathway from the Golgi to the endoplasmic reticulum (ER). This pathway may allow Golgi residents to be recycled through the ER for scrutiny by ER quality-control systems. Yeast Ypt6p, the homolog of the mammalian Rab6 GTPase, is not essential for cell viability. Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. 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: 206654 [Multi-domain]  Cd Length: 161  Bit Score: 48.39  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  51 ISQANVICIVYAVNNKHSIDKVTsRWIPLINERTDKDSRLplILVGNKSDL-----VEYSSMETILPIMNQYTeIETcve 125
Cdd:cd01861   70 IRDSSVAVVVYDITNRQSFDNTD-KWIDDVRDERGNDVII--VLVGNKTDLsdkrqVSTEEGEKKAKENNAMF-IET--- 142

                         90
                 ....*....|...
gi 571026635 126 cSAKNLKNISELF 138
Cdd:cd01861  143 -SAKAGHNVKQLF 154
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
 49-139 2.02e-06

Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades


Pssm-ID: 214541 [Multi-domain]  Cd Length: 164  Bit Score: 47.94  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635    49 QEISQANVICIVYAVNNKHSIDKVtSRWIPLINERTDKDSrLPLILVGNKSDLVEYS--SMETILPIMNQYteieTC--V 124
Cdd:smart00173  67 QYMRTGEGFLLVYSITDRQSFEEI-KKFREQILRVKDRDD-VPIVLVGNKCDLESERvvSTEEGKELARQW----GCpfL 140

                           90
                   ....*....|....*
gi 571026635   125 ECSAKNLKNISELFY 139
Cdd:smart00173 141 ETSAKERVNVDEAFY 155
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
 3-139 3.37e-06

Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. 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: 206710 [Multi-domain]  Cd Length: 163  Bit Score: 47.42  E-value: 3.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   3 LVSEEFPEEVPP-----RAEEITipadVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWI 77
Cdd:cd04139   20 FMYDEFVEDYEPtkadsYRKKVV----LDGEEVQLNILDTAGQEDYAAIRDNYFRSGEGFLLVFSITDMESFTALAEFRE 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 571026635  78 PLIneRTDKDSRLPLILVGNKSDLVEYSSMetilPIMNQYTEIETC----VECSAKNLKNISELFY 139
Cdd:cd04139   96 QIL--RVKEDDNVPLLLVGNKCDLEDKRQV----SVEEAANLAEQWgvnyVETSAKTRANVDKVFF 155
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
 399-530 4.20e-06

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: 47.14  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 399 RCNVIGVKNCGKSGVLQALLGRNLMRQKKIREDHKSYYAINTVYVYGQEKY--LLLHDISESEfltEAEIICD------- 469
Cdd:cd04101    2 QCAVVGDPAVGKSALVQMFHSDGATFQKNYTMTTGCDLVVKTVPVPDTSDSveLFIFDSAGQE---LFSDMVEnvweqpa 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 571026635 470 VVCLVYDVSNPKSFEYCARIFKQ---HFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKM 530
Cdd:cd04101   79 VVCVVYDVTNEVSFNNCSRWINRvrtHSHGLHTPGVLVGNKCDLTDRREVDAAQAQALAQANTL 142
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 468-531 4.47e-06

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: 47.07  E-value: 4.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 571026635 468 CDVVCLVYDVSNPKSFEYCARIFKQ--HFMDSRIPCLIVAAKSDLHEVKQeysISPTD---FCRKHKMP 531
Cdd:cd00154   73 AHGAILVYDVTNRESFENLDKWLNElkEYAPPNIPIILVGNKSDLEDERQ---VSTEEaqqFAKENGLL 138
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
 8-138 1.52e-05

Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 responsive Cdc42 homolog) is a Rho family GTPase that shares significant sequence and functional similarity with Cdc42. Wrch-1 was first identified in mouse mammary epithelial cells, where its transcription is upregulated in Wnt-1 transformation. Wrch-1 contains N- and C-terminal extensions relative to cdc42, suggesting potential differences in cellular localization and function. The Wrch-1 N-terminal extension contains putative SH3 domain-binding motifs and has been shown to bind the SH3 domain-containing protein Grb2, which increases the level of active Wrch-1 in cells. Unlike Cdc42, which localizes to the cytosol and perinuclear membranes, Wrch-1 localizes extensively with the plasma membrane and endosomes. The membrane association, localization, and biological activity of Wrch-1 indicate an atypical model of regulation distinct from other Rho family GTPases. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133330 [Multi-domain]  Cd Length: 173  Bit Score: 45.86  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   8 FPEEVPPRAEEiTIPADVTPERVPTHI--VDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLINERTD 85
Cdd:cd04130   25 YPTEYVPTAFD-NFSVVVLVDGKPVRLqlCDTAGQDEFDKLRPLCYPDTDVFLLCFSVVNPSSFQNISEKWIPEIRKHNP 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 571026635  86 KdsrLPLILVGNKSDLVEYSSmetILPIMNQY--------------TEIETC--VECSAKNLKNISELF 138
Cdd:cd04130  104 K---APIILVGTQADLRTDVN---VLIQLARYgekpvsqsrakalaEKIGACeyIECSALTQKNLKEVF 166
Rab5_related cd01860
Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The ...
 54-143 2.64e-05

Rab-related GTPase family includes Rab5 and Rab22; regulates early endosome fusion; The Rab5-related subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. 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: 206653 [Multi-domain]  Cd Length: 163  Bit Score: 44.85  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  54 ANVICIVYAVNNKHSIDKVTSrWIpliNE-RTDKDSRLPLILVGNKSDLVeySSMETILPIMNQYTEIETC--VECSAKN 130
Cdd:cd01860   74 AAAAIVVYDITSEESFEKAKS-WV---KElQEHGPPNIVIALAGNKADLE--SKRQVSTEEAQEYADENGLlfMETSAKT 147

                         90
                 ....*....|....
gi 571026635 131 LKNISELFYY-AQK 143
Cdd:cd01860  148 GENVNELFTEiARK 161
M_R_Ras_like cd04145
R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, ...
 59-139 3.78e-05

R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, and related members of the Ras family. M-Ras is expressed in lympho-hematopoetic cells. It interacts with some of the known Ras effectors, but appears to also have its own effectors. Expression of mutated M-Ras leads to transformation of several types of cell lines, including hematopoietic cells, mammary epithelial cells, and fibroblasts. Overexpression of M-Ras is observed in carcinomas from breast, uterus, thyroid, stomach, colon, kidney, lung, and rectum. In addition, expression of a constitutively active M-Ras mutant in murine bone marrow induces a malignant mast cell leukemia that is distinct from the monocytic leukemia induced by H-Ras. TC21, along with H-Ras, has been shown to regulate the branching morphogenesis of ureteric bud cell branching in mice. 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: 133345 [Multi-domain]  Cd Length: 164  Bit Score: 44.32  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  59 IVYAVNNKHSIDKVtSRWIPLINERTDKDSrLPLILVGNKSDLV--------EYSSMETILPIMnqYteietcVECSAKN 130
Cdd:cd04145   79 LVFSVTDRGSFEEV-DKFHTQILRVKDRDE-FPMILVGNKADLEhqrqvsreEGQELARQLKIP--Y------IETSAKD 148


                 ....*....
gi 571026635 131 LKNISELFY 139
Cdd:cd04145  149 RVNVDKAFH 157
RalA_RalB cd04139
Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily ...
 468-531 5.48e-05

Ral (Ras-like) family containing highly homologous RalA and RalB; The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (>80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exocyst and for localizing the exocyst to the leading edge of migrating cells. In human cancer cells, RalA is required to support anchorage-independent proliferation and RalB is required to suppress apoptosis. RalA has been shown to localize to the plasma membrane while RalB is localized to the intracellular vesicles. 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: 206710 [Multi-domain]  Cd Length: 163  Bit Score: 43.95  E-value: 5.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 571026635 468 CDVVCLVYDVSNPKSFEYCARIFKQ---HFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKMP 531
Cdd:cd04139   72 GEGFLLVFSITDMESFTALAEFREQilrVKEDDNVPLLLVGNKCDLEDKRQVSVEEAANLAEQWGVN 138
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
 55-146 7.98e-05

Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. 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. RhoA and RhoC are observed only in geranylgeranylated forms; however, RhoB can be present in palmitoylated, farnesylated, and geranylgeranylated forms. RhoA and RhoC are highly relevant for tumor progression and invasiveness; however, RhoB has recently been suggested to be a tumor suppressor. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206662 [Multi-domain]  Cd Length: 175  Bit Score: 43.57  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  55 NVICIVYAVNNKHSIDKVTSRWIPLINERTdkdSRLPLILVGNKSDLVEYSSMETILPIMNQyTEIET------------ 122
Cdd:cd01870   74 DVILMCFSIDSPDSLENIPEKWTPEVKHFC---PNVPIILVGNKKDLRNDEHTIRELAKMKQ-EPVKPeegramaekiga 149

                         90       100
                 ....*....|....*....|....*.
gi 571026635 123 --CVECSAKNLKNISELFYYAQKAVL 146
Cdd:cd01870  150 fgYLECSAKTKEGVREVFEMATRAAL 175
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 445-531 9.58e-05

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: 43.27  E-value: 9.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  445 GQEKYlllHDISESEFLTeaeiiCDVVCLVYDVSNPKSFEYCARIFKQ--HFMDSRIPCLIVAAKSDLHEVKQeysISPT 522
Cdd:pfam00071  57 GQERF---RALRPLYYRG-----ADGFLLVYDITSRDSFENVKKWVEEilRHADENVPIVLVGNKCDLEDQRV---VSTE 125

                          90
                  ....*....|..
gi 571026635  523 D---FCRKHKMP 531
Cdd:pfam00071 126 EgeaLAKELGLP 137
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 473-531 1.64e-04

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 42.50  E-value: 1.64e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 571026635   473 LVYDVSNPKSFEYCARIFK--QHFMDSRIPCLIVAAKSDL---HEVKQEysiSPTDFCRKHKMP 531
Cdd:smart00175  78 LVYDITNRESFENLENWLKelREYASPNVVIMLVGNKSDLeeqRQVSRE---EAEAFAEEHGLP 138
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
 39-101 1.85e-04

Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like families; RERG (Ras-related and Estrogen- Regulated Growth inhibitor) and Ras-like 11 are members of a novel subfamily of Ras that were identified based on their behavior in breast and prostate tumors, respectively. RERG expression was decreased or lost in a significant fraction of primary human breast tumors that lack estrogen receptor and are correlated with poor clinical prognosis. Elevated RERG expression correlated with favorable patient outcome in a breast tumor subtype that is positive for estrogen receptor expression. In contrast to most Ras proteins, RERG overexpression inhibited the growth of breast tumor cells in vitro and in vivo. RasL11 was found to be ubiquitously expressed in human tissue, but down-regulated in prostate tumors. Both RERG and RasL11 lack the C-terminal CaaX prenylation motif, where a = an aliphatic amino acid and X = any amino acid, and are localized primarily in the cytoplasm. Both are believed to have tumor suppressor activity.


Pssm-ID: 206713 [Multi-domain]  Cd Length: 166  Bit Score: 42.26  E-value: 1.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 571026635  39 EAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVtSRWIPLINERTDKDSRLPLILVGNKSDL 101
Cdd:cd04146   58 QQNEDPESLERSLRWADGFVLVYSITDRSSFDVV-SQLLQLIREIKKRDGEIPVILVGNKADL 119
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 54-138 2.24e-04

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 42.11  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635    54 ANVICIVYAVNNKHSIDKVTsRWIPLINERTDKDsrLPLILVGNKSDL-----VEYSSMEtilpimnQYTEIETC--VEC 126
Cdd:smart00175  73 AVGALLVYDITNRESFENLE-NWLKELREYASPN--VVIMLVGNKSDLeeqrqVSREEAE-------AFAEEHGLpfFET 142

                           90
                   ....*....|..
gi 571026635   127 SAKNLKNISELF 138
Cdd:smart00175 143 SAKTNTNVEEAF 154
ARHI_like cd04140
A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family ...
 33-138 2.33e-04

A Ras homolog member I (ARHI); ARHI (A Ras homolog member I) is a member of the Ras family with several unique structural and functional properties. ARHI is expressed in normal human ovarian and breast tissue, but its expression is decreased or eliminated in breast and ovarian cancer. ARHI contains an N-terminal extension of 34 residues (human) that is required to retain its tumor suppressive activity. Unlike most other Ras family members, ARHI is maintained in the constitutively active (GTP-bound) state in resting cells and has modest GTPase activity. ARHI inhibits STAT3 (signal transducers and activators of transcription 3), a latent transcription factor whose abnormal activation plays a critical role in oncogenesis. 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: 206711 [Multi-domain]  Cd Length: 165  Bit Score: 42.12  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  33 HIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLINERTDKDSRLPLILVGNKSDlvEYSSMETILP 112
Cdd:cd04140   52 QITDTTGSHQFPAMQRLSISKGHAFILVYSITSKQSLEELKPIYELICEIKGNNLEKIPIMLVGNKCD--ESPSREVSSS 129

                         90       100
                 ....*....|....*....|....*...
gi 571026635 113 IMNQYTEIETC--VECSAKNLKNISELF 138
Cdd:cd04140  130 EGAALARTWNCafMETSAKTNHNVQELF 157
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
 52-146 2.46e-04

Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. 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.


Pssm-ID: 206706 [Multi-domain]  Cd Length: 185  Bit Score: 42.15  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  52 SQANVICIVYAVNNKHSIDKVTSRWIPlinERTDKDSRLPLILVGNKSDLVEYSSMETILPIMNQYTE-------IETC- 123
Cdd:cd04134   70 ADTHVIMLCFSVDNPDSLENVESKWLA---EIRHHCPGVKLVLVALKCDLREPRNERDRGTHTISYEEglavakrINACr 146

                         90       100
                 ....*....|....*....|....
gi 571026635 124 -VECSAKNLKNISELFYYAQKAVL 146
Cdd:cd04134  147 yLECSAKLNRGVNEAFTEAARVAL 170
Rab21 cd04123
Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, ...
 54-146 2.96e-04

Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate phagocytosis. 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: 133323 [Multi-domain]  Cd Length: 162  Bit Score: 41.83  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  54 ANVICIVYAVNNKHSIDKVTSrWI-PLINERTDKDSrlpLILVGNKSDLVEYS--SMETILPIMNQYTEIEtcVECSAKN 130
Cdd:cd04123   73 ADGAILVYDITDADSFQKVKK-WIkELKQMRGNNIS---LVIVGNKIDLERQRvvSKSEAEEYAKSVGAKH--FETSAKT 146

                         90
                 ....*....|....*.
gi 571026635 131 LKNISELFYYAQKAVL 146
Cdd:cd04123  147 GKGIEELFLSLAKRMI 162
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
86-157 2.98e-04

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


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 43.05  E-value: 2.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 571026635  86 KDSRLPLILVGNKSDLVeysSMETILPIMNQYTEI---ETCVECSAKNLKNISELFyyaqKAVLH--PTGPLYCPEE 157
Cdd:COG1159  108 KKLKTPVILVINKIDLV---KKEELLPLLAEYSELldfAEIVPISALKGDNVDELL----DEIAKllPEGPPYYPED 177
era PRK00089
GTPase Era; Reviewed
 86-157 3.35e-04

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 42.73  E-value: 3.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 571026635  86 KDSRLPLILVGNKSDLVeySSMETILPIMNQYTE----IETcVECSAKNLKNISELFYYAQKAVlhPTGPLYCPEE 157
Cdd:PRK00089 110 KKVKTPVILVLNKIDLV--KDKEELLPLLEELSElmdfAEI-VPISALKGDNVDELLDVIAKYL--PEGPPYYPED 180
RGK cd04148
Rem, Rem2, Rad, Gem/Kir (RGK) subfamily of Ras GTPases; RGK subfamily. The RGK (Rem, Rem2, Rad, ...
 34-102 4.29e-04

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: 42.01  E-value: 4.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  34 IVDYSEAEQSDeQLHQEISQ-ANVICIVYAVNNKHSIDKVTSRWIPLINERTDKDsrLPLILVGNKSDLV 102
Cdd:cd04148   53 VYDHWEQEDGM-WLEDSCMQvGDAYVIVYSVTDRSSFEKASELRIQLRRARQAED--IPIILVGNKSDLV 119
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
 3-146 5.67e-04

Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206703 [Multi-domain]  Cd Length: 176  Bit Score: 41.26  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   3 LVSEEFPEE-VPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPlin 81
Cdd:cd04131   21 FAKDSFPENyVPTVFENYTASFEVDKQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVLKKWKG--- 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 571026635  82 ERTDKDSRLPLILVGNKSDL-------VEYSSMETILPIMNQYTEI------ETCVECSAKNLKN-ISELFYYAQKAVL 146
Cdd:cd04131   98 EVREFCPNTPVLLVGCKSDLrtdlstlTELSNKRQIPVSHEQGRNLakqigaAAYVECSAKTSENsVRDVFEMATLACL 176
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
 54-147 9.16e-04

Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. 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: 206659 [Multi-domain]  Cd Length: 167  Bit Score: 40.33  E-value: 9.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  54 ANVICIVYAVNNKHSIDKVtSRWIPLINERTDKDsrLPLILVGNKSDLVEYS--SMETILPIMNQY--TEIETcvecSAK 129
Cdd:cd01867   76 AMGIILVYDITDEKSFENI-KNWMRNIDEHASED--VERMLVGNKCDMEEKRvvSKEEGEALAREYgiKFLET----SAK 148

                         90
                 ....*....|....*...
gi 571026635 130 NLKNISELFYYAQKAVLH 147
Cdd:cd01867  149 ANINVEEAFLTLAKDILK 166
Rab19 cd01864
Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. ...
 54-138 1.06e-03

Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. Similarity analysis indicated that Rab41 is closely related to Rab19. However, the function of these Rabs is not yet characterized. 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: 133267 [Multi-domain]  Cd Length: 165  Bit Score: 40.11  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  54 ANVICIVYAVNNKHSIDKVtSRWIPLINERTDkdSRLPLILVGNKSDL-----VEYSSMETilpiMNQYTEIETCVECSA 128
Cdd:cd01864   76 ANGAIIAYDITRRSSFESV-PHWIEEVEKYGA--SNVVLLLIGNKCDLeeqreVLFEEACT----LAEHYGILAVLETSA 148

                         90
                 ....*....|
gi 571026635 129 KNLKNISELF 138
Cdd:cd01864  149 KESSNVEEAF 158
RERG_RasL11_like cd04146
Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like ...
 402-515 1.33e-03

Ras-related and Estrogen-Regulated Growth inhibitor (RERG) and Ras-like 11 (RasL11)-like families; RERG (Ras-related and Estrogen- Regulated Growth inhibitor) and Ras-like 11 are members of a novel subfamily of Ras that were identified based on their behavior in breast and prostate tumors, respectively. RERG expression was decreased or lost in a significant fraction of primary human breast tumors that lack estrogen receptor and are correlated with poor clinical prognosis. Elevated RERG expression correlated with favorable patient outcome in a breast tumor subtype that is positive for estrogen receptor expression. In contrast to most Ras proteins, RERG overexpression inhibited the growth of breast tumor cells in vitro and in vivo. RasL11 was found to be ubiquitously expressed in human tissue, but down-regulated in prostate tumors. Both RERG and RasL11 lack the C-terminal CaaX prenylation motif, where a = an aliphatic amino acid and X = any amino acid, and are localized primarily in the cytoplasm. Both are believed to have tumor suppressor activity.


Pssm-ID: 206713 [Multi-domain]  Cd Length: 166  Bit Score: 39.95  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 402 VIGVKNCGKSgvlqALLGRNLMRqKKIREdhksyYAINT-------VYVYGQEKYLLLHD-----ISESEFLTEAEI-IC 468
Cdd:cd04146    4 VLGASGVGKS----ALTVRFLTK-RFIGE-----YEPNLeslysrqVTIDGEQVSLEIQDtpgqqQNEDPESLERSLrWA 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 571026635 469 DVVCLVYDVSNPKSFEYCARIFKQ----HFMDSRIPCLIVAAKSDLHEVKQ 515
Cdd:cd04146   74 DGFVLVYSITDRSSFDVVSQLLQLireiKKRDGEIPVILVGNKADLLHSRQ 124
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 445-512 1.90e-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: 39.43  E-value: 1.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571026635 445 GQEKYLLLHDISESEflteaeiiCDVVCLVYDVSNPKSFEYCARIFKQHFM---DSRIPCLIVAAKSDLHE 512
Cdd:cd00876   56 GQEEFSAMRDQYIRN--------GDGFILVYSITSRESFEEIKNIREQILRvkdKEDVPIVLVGNKCDLEN 118
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
 471-552 2.24e-03

Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ubiquitously expressed in mouse tissues and cells, where it is localized to the medial Golgi cisternae. It colocalizes with alpha-mannose II. Together with the other cisternal Rabs, Rab6A and Rab6A', it is believed to regulate the Golgi response to stress and is likely a molecular target in stress-activated signaling pathways. Rab33A (previously known as S10) is expressed primarily in the brain and immune system cells. In humans, it is located on the X chromosome at Xq26 and its expression is down-regulated in tuberculosis patients. Experimental evidence suggests that Rab33A is a novel CD8+ T cell factor that likely plays a role in tuberculosis disease processes. 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: 133315 [Multi-domain]  Cd Length: 170  Bit Score: 39.34  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 471 VCLVYDVSNPKSF-------EYCarifKQHFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKMPPpqaFTCNTADA 543
Cdd:cd04115   79 VVFVYDVTNMASFhslpswiEEC----EQHSLPNEVPRILVGNKCDLREQIQVPTDLAQRFADAHSMPL---FETSAKDP 151

                         90
                 ....*....|...
gi 571026635 544 PSKD----IFVKL 552
Cdd:cd04115  152 SENDhveaIFMTL 164
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
2-138 2.51e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.19  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   2 SLVSEEFPEEVPPRAEEITIPADVTPERVPT-------HIVD---YSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDK 71
Cdd:COG1100   18 SLVNRLVGDIFSLEKYLSTNGVTIDKKELKLdgldvdlVIWDtpgQDEFRETRQFYARQLTGASLYLFVVDGTREETLQS 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 571026635  72 VTSrWIPLInERTDKDSrlPLILVGNKSDLVEYSSMETILPIMNQYTE--IETCVECSAKNLKNISELF 138
Cdd:COG1100   98 LYE-LLESL-RRLGKKS--PIILVLNKIDLYDEEEIEDEERLKEALSEdnIVEVVATSAKTGEGVEELF 162
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 86-138 2.61e-03

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: 38.98  E-value: 2.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 571026635  86 KDSRLPLILVGNKSDLVeySSMETILPIMNQYTE---IETCVECSAKNLKNISELF 138
Cdd:cd04163  108 KKSKTPVILVLNKIDLV--KDKEDLLPLLEKLKElhpFAEIFPISALKGENVDELL 161
Rab1_Ypt1 cd01869
Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in ...
 54-138 3.23e-03

Rab GTPase family 1 includes the yeast homolog Ypt1; Rab1/Ypt1 subfamily. Rab1 is found in every eukaryote and is a key regulatory component for the transport of vesicles from the ER to the Golgi apparatus. Studies on mutations of Ypt1, the yeast homolog of Rab1, showed that this protein is necessary for the budding of vesicles of the ER as well as for their transport to, and fusion with, the Golgi apparatus. 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: 206661 [Multi-domain]  Cd Length: 166  Bit Score: 38.85  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  54 ANVICIVYAVNNKHSIDKVtSRWIPLINERTDKDSRLplILVGNKSDL-----VEYS-----SMETILPIMnqyteietc 123
Cdd:cd01869   75 AHGIIIVYDVTDQESFNNV-KQWLQEIDRYASENVNK--LLVGNKCDLtdkkvVDYTeakefADELGIPFL--------- 142

                         90
                 ....*....|....*
gi 571026635 124 vECSAKNLKNISELF 138
Cdd:cd01869  143 -ETSAKNATNVEEAF 156
RheB cd04137
Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) ...
 59-138 3.24e-03

Ras Homolog Enriched in Brain (RheB) is a small GTPase; Rheb (Ras Homolog Enriched in Brain) subfamily. Rheb was initially identified in rat brain, where its expression is elevated by seizures or by long-term potentiation. It is expressed ubiquitously, with elevated levels in muscle and brain. Rheb functions as an important mediator between the tuberous sclerosis complex proteins, TSC1 and TSC2, and the mammalian target of rapamycin (TOR) kinase to stimulate cell growth. TOR kinase regulates cell growth by controlling nutrient availability, growth factors, and the energy status of the cell. TSC1 and TSC2 form a dimeric complex that has tumor suppressor activity, and TSC2 is a GTPase activating protein (GAP) for Rheb. The TSC1/TSC2 complex inhibits the activation of TOR kinase through Rheb. Rheb has also been shown to induce the formation of large cytoplasmic vacuoles in a process that is dependent on the GTPase cycle of Rheb, but independent of the TOR kinase, suggesting Rheb plays a role in endocytic trafficking that leads to cell growth and cell-cycle progression. 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.


Pssm-ID: 206709 [Multi-domain]  Cd Length: 180  Bit Score: 38.77  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  59 IVYAVNNKHSIDKVTSRWIPLINERtdKDSRLPLILVGNKSDLveysSMETILpimnQYTEIE--------TCVECSAKN 130
Cdd:cd04137   78 LVYSVTSRKSFEVVKVIYDKILDML--GKESVPIVLVGNKSDL----HMERQV----SAEEGKklaeswgaAFLESSAKE 147


                 ....*...
gi 571026635 131 LKNISELF 138
Cdd:cd04137  148 NENVEEAF 155
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
 473-530 3.26e-03

Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and Rab25 are closely related, evolutionary conserved Rab proteins that are differentially expressed. Rab11a is ubiquitously synthesized, Rab11b is enriched in brain and heart and Rab25 is only found in epithelia. Rab11/25 proteins seem to regulate recycling pathways from endosomes to the plasma membrane and to the trans-Golgi network. Furthermore, Rab11a is thought to function in the histamine-induced fusion of tubulovesicles containing H+, K+ ATPase with the plasma membrane in gastric parietal cells and in insulin-stimulated insertion of GLUT4 in the plasma membrane of cardiomyocytes. Overexpression of Rab25 has recently been observed in ovarian cancer and breast cancer, and has been correlated with worsened outcomes in both diseases. In addition, Rab25 overexpression has also been observed in prostate cancer, transitional cell carcinoma of the bladder, and invasive breast tumor cells. 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: 206660 [Multi-domain]  Cd Length: 165  Bit Score: 38.70  E-value: 3.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 473 LVYDVSNPKSFEYCARIFKQ--HFMDSRIPCLIVAAKSDLHEVKQEYSISPTDFCRKHKM 530
Cdd:cd01868   81 LVYDITKKSTFENVERWLKElrDHADSNIVIMLVGNKSDLRHLRAVPTEEAKAFAEKNGL 140
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
168-323 3.31e-03

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 168 LTRIFKISDQDNDGTLNDAELNFFqricfntplapqALEDVKNVVRKHISDGvaDSGLTLKGFLFLHTLFIQRGRHETTW 247
Cdd:COG5126    7 LDRRFDLLDADGDGVLERDDFEAL------------FRRLWATLFSEADTDG--DGRISREEFVAGMESLFEATVEPFAR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635 248 TVLRRFgyDDDLD--LTPEYLFPLLK---IPPDCTTELnhhaylflqstFDKHDLDRDCALSPDELKDLFKVFpyipWGP 322
Cdd:COG5126   73 AAFDLL--DTDGDgkISADEFRRLLTalgVSEEEADEL-----------FARLDTDGDGKISFEEFVAAVRDY----YTP 135


                 .
gi 571026635 323 D 323
Cdd:COG5126  136 D 136
Rab11_like cd01868
Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and ...
 59-138 3.62e-03

Rab GTPase family 11 (Rab11)-like includes Rab11a, Rab11b, and Rab25; Rab11a, Rab11b, and Rab25 are closely related, evolutionary conserved Rab proteins that are differentially expressed. Rab11a is ubiquitously synthesized, Rab11b is enriched in brain and heart and Rab25 is only found in epithelia. Rab11/25 proteins seem to regulate recycling pathways from endosomes to the plasma membrane and to the trans-Golgi network. Furthermore, Rab11a is thought to function in the histamine-induced fusion of tubulovesicles containing H+, K+ ATPase with the plasma membrane in gastric parietal cells and in insulin-stimulated insertion of GLUT4 in the plasma membrane of cardiomyocytes. Overexpression of Rab25 has recently been observed in ovarian cancer and breast cancer, and has been correlated with worsened outcomes in both diseases. In addition, Rab25 overexpression has also been observed in prostate cancer, transitional cell carcinoma of the bladder, and invasive breast tumor cells. 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: 206660 [Multi-domain]  Cd Length: 165  Bit Score: 38.70  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  59 IVYAVNNKHSIDKVTsRWIPLINERTDKDsrLPLILVGNKSDLVEYSSMET----ILPIMNQYTEIETcvecSAKNLKNI 134
Cdd:cd01868   81 LVYDITKKSTFENVE-RWLKELRDHADSN--IVIMLVGNKSDLRHLRAVPTeeakAFAEKNGLSFIET----SALDGTNV 153


                 ....
gi 571026635 135 SELF 138
Cdd:cd01868  154 EEAF 157
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
 4-138 3.73e-03

Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap subfamily of the Ras family. It consists of Rap2a, Rap2b, and Rap2c. Both isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK) are putative effectors of Rap2 in mediating the activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton. In human platelets, Rap2 was shown to interact with the cytoskeleton by binding the actin filaments. In embryonic Xenopus development, Rap2 is necessary for the Wnt/beta-catenin signaling pathway. The Rap2 interacting protein 9 (RPIP9) is highly expressed in human breast carcinomas and correlates with a poor prognosis, suggesting a role for Rap2 in breast cancer oncogenesis. Rap2b, but not Rap2a, Rap2c, Rap1a, or Rap1b, is expressed in human red blood cells, where it is believed to be involved in vesiculation. A number of additional effector proteins for Rap2 have been identified, including the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. 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: 133376 [Multi-domain]  Cd Length: 163  Bit Score: 38.66  E-value: 3.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   4 VSEEFPEEVPPRAEEI---TIPADVTPERVptHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLI 80
Cdd:cd04176   22 VSGTFIEKYDPTIEDFyrkEIEVDSSPSVL--EILDTAGTEQFASMRDLYIKNGQGFIVVYSLVNQQTFQDIKPMRDQIV 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 571026635  81 neRTDKDSRLPLILVGNKSDLV---EYSSMETilpimNQYTEIETC--VECSAKNLKNISELF 138
Cdd:cd04176  100 --RVKGYEKVPIILVGNKVDLEserEVSSAEG-----RALAEEWGCpfMETSAKSKTMVNELF 155
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 56-140 4.64e-03

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: 38.12  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   56 VICIVYAVNNKHSIDKVTSRWIPLINERTDKDSrlPLILVGNKSDLVEYSSME---TILPIMNQYTEIETcvecSAKNLK 132
Cdd:TIGR00231  78 SLRVFDIVILVLDVEEILEKQTKEIIHHADSGV--PIILVGNKIDLKDADLKThvaSEFAKLNGEPIIPL----SAETGK 151


                  ....*...
gi 571026635  133 NISELFYY 140
Cdd:TIGR00231 152 NIDSAFKI 159
Rab28 cd04109
Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown ...
 469-532 5.21e-03

Rab GTPase family 28 (Rab28); Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumably the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. 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: 206694 [Multi-domain]  Cd Length: 213  Bit Score: 38.62  E-value: 5.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 571026635 469 DVVCLVYDVSNPKSFEYCA---RIFKQHFMDSRIPCLI--VAAKSDLHEVKQEYSISPTDFCRKHKMPP 532
Cdd:cd04109   75 QAVCLVYDITNSQSFENLEdwlSVVKKVNEESETKPKMvlVGNKTDLEHNRQVTAEKHARFAQENDMES 143
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
 1-145 5.93e-03

Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3; The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. 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. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206663 [Multi-domain]  Cd Length: 174  Bit Score: 38.25  E-value: 5.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635   1 MSLVSEEFPEEVPPRAEEiTIPADVTPERVPTHIVDYSEAEQSDEQLHQEIS--QANVICIVYAVNNKHSIDKVTSRWIP 78
Cdd:cd01871   19 ISYTTNAFPGEYIPTVFD-NYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSypQTDVFLICFSLVSPASFENVRAKWYP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  79 LINERTDKdsrLPLILVGNKSDLVEysSMETI--------LPImnQYTEIETC---------VECSAKNLKNISELFYYA 141
Cdd:cd01871   98 EVRHHCPN---TPIILVGTKLDLRD--DKDTIeklkekklTPI--TYPQGLAMakeigavkyLECSALTQRGLKTVFDEA 170


                 ....
gi 571026635 142 QKAV 145
Cdd:cd01871  171 IRAV 174
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 30-137 7.11e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 37.47  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571026635  30 VPTHIVDYS---EAEQSDEQL-----HQEISQANVICIVyavnnkhsIDkVTSRWIPLINERTDKDSRLPLILVGNKSDL 101
Cdd:cd04164   51 IPVRLIDTAglrETEDEIEKIgieraREAIEEADLVLLV--------VD-ASEGLDEEDLEILELPAKKPVIVVLNKSDL 121

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 571026635 102 VEyssMETILPIMNQYTEIETcvecSAKNLKNISEL 137
Cdd:cd04164  122 LS---DAEGISELNGKPIIAI----SAKTGEGIDEL 150
 
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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