| Analysis | Hit | start | end | length | Note | Hit coverage | Hit length | Hit pident | Hit pcons | eValue | Hit description |
| blastp_kegg | bfu:BC1G_04296 | 1 | 623 | 623 | n/a | 97.80 | 637 | 91.81 | 0.00 | 0.0 | hypothetical protein K06883 |
| ssl:SS1G_02199 | 1 | 604 | 604 | n/a | 97.73 | 618 | 91.56 | 0.99 | 0.0 | hypothetical protein K06883 |
| ncr:NCU03966 | 4 | 623 | 620 | n/a | 98.57 | 629 | 71.45 | 10.16 | 0.0 | similar to mitochondrial GTPase Miro-2 K06883 |
| fgr:FG08446.1 | 1 | 622 | 622 | n/a | 99.20 | 627 | 71.06 | 9.16 | 0.0 | hypothetical protein K06883 |
| mgr:MGG_01044 | 1 | 623 | 623 | Gaps:7 | 99.37 | 634 | 70.00 | 9.21 | 0.0 | MG01044.4 hypothetical protein K06883 |
| pan:PODANSg3192 | 4 | 623 | 620 | Gaps:2 | 98.72 | 626 | 70.71 | 10.19 | 0.0 | hypothetical protein K06883 |
| pno:SNOG_13056 | 1 | 622 | 622 | Gaps:1 | 98.26 | 632 | 67.79 | 11.59 | 0.0 | hypothetical protein K06883 |
| afm:AFUA_6G07870 | 1 | 622 | 622 | Gaps:5 | 99.21 | 632 | 67.30 | 10.21 | 0.0 | mitochondrial GTPase (Miro-2) K06883 |
| nfi:NFIA_053560 | 1 | 622 | 622 | Gaps:5 | 99.21 | 632 | 66.99 | 10.53 | 0.0 | mitochondrial GTPase (Miro-2) putative K06883 |
| afv:AFLA_036590 | 1 | 622 | 622 | Gaps:5 | 99.05 | 633 | 66.35 | 10.85 | 0.0 | mitochondrial GTPase (Miro-2) putative K06883 |
| blastp_uniprot_sprot | sp|Q7RZA2|GEM1_NEUCR | 4 | 623 | 620 | n/a | 98.57 | 629 | 71.45 | 10.16 | 0.0 | Mitochondrial Rho GTPase 1 OS Neurospora crassa GN gem-1 PE 3 SV 1 |
| sp|Q4I2W2|GEM1_GIBZE | 1 | 622 | 622 | n/a | 99.20 | 627 | 71.06 | 9.16 | 0.0 | Mitochondrial Rho GTPase 1 OS Gibberella zeae GN GEM1 PE 3 SV 1 |
| sp|Q4WN24|GEM1_ASPFU | 1 | 622 | 622 | Gaps:5 | 99.21 | 632 | 67.30 | 10.21 | 0.0 | Mitochondrial Rho GTPase 1 OS Aspergillus fumigatus GN gem1 PE 3 SV 1 |
| sp|Q2UM43|GEM1_ASPOR | 1 | 622 | 622 | Gaps:5 | 99.05 | 633 | 66.35 | 10.85 | 0.0 | Mitochondrial Rho GTPase 1 OS Aspergillus oryzae GN gem1 PE 3 SV 1 |
| sp|Q5B5L3|GEM1_EMENI | 1 | 622 | 622 | Gaps:5 | 98.90 | 634 | 65.71 | 10.85 | 0.0 | Mitochondrial Rho GTPase 1 OS Emericella nidulans GN gem1 PE 3 SV 1 |
| sp|Q6C2J1|GEM1_YARLI | 4 | 600 | 597 | Gaps:34 | 94.59 | 665 | 50.56 | 15.58 | 0.0 | Mitochondrial Rho GTPase 1 OS Yarrowia lipolytica GN GEM1 PE 3 SV 1 |
| sp|Q758X6|GEM1_ASHGO | 4 | 591 | 588 | Gaps:32 | 92.28 | 661 | 48.03 | 15.57 | 1e-157 | Mitochondrial Rho GTPase 1 OS Ashbya gossypii GN GEM1 PE 3 SV 1 |
| sp|Q6CY37|GEM1_KLULA | 4 | 585 | 582 | Gaps:33 | 91.81 | 659 | 47.93 | 16.20 | 1e-156 | Mitochondrial Rho GTPase 1 OS Kluyveromyces lactis GN GEM1 PE 3 SV 1 |
| sp|P39722|GEM1_YEAST | 3 | 596 | 594 | Gaps:35 | 93.50 | 662 | 47.50 | 15.02 | 1e-156 | Mitochondrial Rho GTPase 1 OS Saccharomyces cerevisiae GN GEM1 PE 1 SV 1 |
| sp|Q6FIR8|GEM1_CANGA | 3 | 590 | 588 | Gaps:27 | 92.91 | 649 | 45.77 | 20.07 | 1e-154 | Mitochondrial Rho GTPase 1 OS Candida glabrata GN GEM1 PE 3 SV 1 |
| blastp_pdb | no results |
| rpsblast_cdd | gnl|CDD|133292 | 419 | 586 | 168 | Gaps:3 | 100.00 | 169 | 52.66 | 13.61 | 1e-65 | cd01892 Miro2 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. |
| gnl|CDD|133293 | 4 | 170 | 167 | Gaps:5 | 100.00 | 166 | 54.82 | 14.46 | 3e-65 | cd01893 Miro1 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. |
| gnl|CDD|149425 | 219 | 307 | 89 | n/a | 100.00 | 89 | 60.67 | 10.11 | 2e-39 | pfam08356 EF_assoc_2 EF hand associated. This region predominantly appears near EF-hands (pfam00036) in GTP-binding proteins. It is found in all three eukaryotic kingdoms. |
| gnl|CDD|149424 | 343 | 418 | 76 | Gaps:1 | 100.00 | 75 | 52.00 | 18.67 | 7e-29 | pfam08355 EF_assoc_1 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. |
| gnl|CDD|133251 | 4 | 160 | 157 | Gaps:12 | 96.49 | 171 | 29.09 | 15.76 | 2e-16 | cd00157 Rho Rho (Ras homology) family. Members of the Rho 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. |
| gnl|CDD|31297 | 1 | 185 | 185 | Gaps:15 | 91.32 | 219 | 22.50 | 18.00 | 4e-16 | COG1100 COG1100 GTPase SAR1 and related small G proteins [General function prediction only]. |
| gnl|CDD|133258 | 8 | 160 | 153 | Gaps:13 | 96.82 | 157 | 30.26 | 19.08 | 1e-15 | cd00882 Ras_like_GTPase 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 regulate 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. |
| gnl|CDD|133252 | 5 | 162 | 158 | Gaps:25 | 96.88 | 160 | 35.48 | 16.13 | 4e-15 | cd00876 Ras Ras family. 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. |
| gnl|CDD|149505 | 5 | 537 | 533 | Gaps:25 | 100.00 | 118 | 43.22 | 22.88 | 8e-15 | pfam08477 Miro Miro-like protein. Mitochondrial Rho proteins (Miro-1 and Miro-2) are atypical Rho GTPases. They have a unique domain organisation with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis. |
| gnl|CDD|133250 | 4 | 160 | 157 | Gaps:25 | 96.86 | 159 | 28.57 | 16.88 | 7e-14 | cd00154 Rab Rab family. 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. |
| rpsblast_kog | gnl|CDD|36919 | 1 | 618 | 618 | Gaps:19 | 97.44 | 625 | 45.81 | 17.08 | 1e-178 | KOG1707 KOG1707 KOG1707 Predicted Ras related/Rac-GTP binding protein [Defense mechanisms]. |
| gnl|CDD|35614 | 1 | 170 | 170 | Gaps:12 | 90.91 | 198 | 26.11 | 18.89 | 5e-12 | KOG0393 KOG0393 KOG0393 Ras-related small GTPase Rho type [General function prediction only]. |
| gnl|CDD|35616 | 1 | 161 | 161 | Gaps:13 | 80.61 | 196 | 29.11 | 17.09 | 2e-11 | KOG0395 KOG0395 KOG0395 Ras-related GTPase [General function prediction only]. |
| gnl|CDD|35301 | 3 | 161 | 159 | Gaps:19 | 75.36 | 207 | 25.64 | 17.95 | 2e-09 | KOG0078 KOG0078 KOG0078 GTP-binding protein SEC4 small G protein superfamily and related Ras family GTP-binding proteins [Signal transduction mechanisms Intracellular trafficking secretion and vesicular transport]. |
| gnl|CDD|35315 | 1 | 160 | 160 | Gaps:19 | 78.50 | 200 | 29.94 | 17.20 | 3e-08 | KOG0092 KOG0092 KOG0092 GTPase Rab5/YPT51 and related small G protein superfamily GTPases [Intracellular trafficking secretion and vesicular transport]. |
| gnl|CDD|35302 | 5 | 160 | 156 | Gaps:8 | 76.77 | 198 | 28.29 | 18.42 | 6e-08 | KOG0079 KOG0079 KOG0079 GTP-binding protein H-ray small G protein superfamily [General function prediction only]. |
| gnl|CDD|35307 | 5 | 161 | 157 | Gaps:6 | 75.61 | 205 | 27.10 | 16.13 | 2e-07 | KOG0084 KOG0084 KOG0084 GTPase Rab1/YPT1 small G protein superfamily and related GTP-binding proteins [Signal transduction mechanisms Intracellular trafficking secretion and vesicular transport]. |
Gene Identifier
Genome Report System - copyright INRA 2011