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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560    1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:smart00010  66 MRDQYMRTGEGFLLVYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETS 145

                           90       100
                   ....*....|....*....|.
gi 1335348560   81 AKLRLNVDEAFEQLVRAVRKY 101
Cdd:smart00010 146 AKERINVDEAFYDLVREIRKS 166

Ras-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:PTZ00369   69 MRDQYMRTGQGFLCVYSITSRSSFEEIASFREQILRVKDKDRVPMILVGNKCDLDSERQVSTGEGQELAKSFGIPFLETS 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1335348560  81 AKLRLNVDEAFEQLVRAVRKYQEQelpPSPPSAPRKKDGGC 121
Cdd:PTZ00369  149 AKQRVNVDEAFYELVREIRKYLKE---DMPSQKQKKKGGLC 186

GTPase SAR1 family domain [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   2 REQYMRAGNG---FLLVFA---INDRQSFNEvgkLFTQILRVKDrdDFPIVLVGNKADL--ENQRQVLRSEASSFSASHH 73
Cdd:COG1100    70 RQFYARQLTGaslYLFVVDgtrEETLQSLYE---LLESLRRLGK--KSPIILVLNKIDLydEEEIEDEERLKEALSEDNI 144

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1335348560  74 MTYFEASAKLRLNVDEAFEQLVRAVRKYQEQEL 106
Cdd:COG1100   145 VEVVATSAKTGEGVEELFAALAEILRGEGDSLD 177

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560    1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:smart00010  66 MRDQYMRTGEGFLLVYSITDRQSFEEIAKFREQILRVKDRDDVPIVLVGNKCDLENERVVSTEEGKELARQWGCPFLETS 145

                           90       100
                   ....*....|....*....|.
gi 1335348560   81 AKLRLNVDEAFEQLVRAVRKY 101
Cdd:smart00010 146 AKERINVDEAFYDLVREIRKS 166

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:cd00876    63 MRDQYIRNGDGFILVYSITSRESFEEIKNIREQILRVKDKEDVPIVLVGNKCDLENERQVSTEEGEALAEEWGCPFLETS 142

                          90
                  ....*....|....*.
gi 1335348560  81 AKLRLNVDEAFEQLVR 96
Cdd:cd00876   143 AKTNINIDELFNTLVR 158

Ras GTPase family containing H-Ras,N-Ras and K-Ras4A/4B; H-Ras/N-Ras/K-Ras subfamily. H-Ras, N-Ras, and K-Ras4A/4B are the prototypical members of the Ras family. These isoforms generate distinct signal outputs despite interacting with a common set of activators and effectors, and are strongly associated with oncogenic progression in tumor initiation. Mutated versions of Ras that are insensitive to GAP stimulation (and are therefore constitutively active) are found in a significant fraction of human cancers. Many Ras guanine nucleotide exchange factors (GEFs) have been identified. They 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 that stimulate a variety of diverse cytoplasmic signaling activities. Some are known to positively mediate the oncogenic properties of Ras, including Raf, phosphatidylinositol 3-kinase (PI3K), RalGEFs, and Tiam1. Others are proposed to play negative regulatory roles in oncogenesis, including RASSF 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENqRQVLRSEASSFSASHHMTYFEAS 80
Cdd:cd04138    65 MRDQYMRTGEGFLCVFAINSRKSFEDIHTYREQIKRVKDSDDVPMVLVGNKCDLAA-RTVSTRQGQDLAKSYGIPYIETS 143

                          90
                  ....*....|....*....
gi 1335348560  81 AKLRLNVDEAFEQLVRAVR 99
Cdd:cd04138   144 AKTRQGVEEAFYTLVREIR 162

RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that is found in fungi. In budding yeasts, RSR1 is involved in selecting a site for bud growth on the cell cortex, which directs the establishment of cell polarization. The Rho family GTPase cdc42 and its GEF, cdc24, then establish an axis of polarized growth by organizing the actin cytoskeleton and secretory apparatus at the bud site. It is believed that cdc42 interacts directly with RSR1 in vivo. In filamentous fungi, polar growth occurs at the tips of hypha and at novel growth sites along the extending hypha. In Ashbya gossypii, RSR1 is a key regulator of hyphal growth, localizing at the tip region and regulating in apical polarization of the actin cytoskeleton. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSAS-HHMTYFEA 79
Cdd:cd04177    65 MRELYIKSGQGFLLVYSVTSEASLNELGELREQVLRIKDSDNVPMVLVGNKADLEDDRQVSREDGVSLSQQwGNVPFYET 144

                          90       100
                  ....*....|....*....|
gi 1335348560  80 SAKLRLNVDEAFEQLVRAVR 99
Cdd:cd04177   145 SARKRTNVDEVFIDLVRQII 164

Rat sarcoma (Ras) family 2 of small guanosine triphosphatases (GTPases); The Ras2 subfamily, found exclusively in fungi, was first identified in Ustilago maydis. In U. maydis, Ras2 is regulated by Sql2, a protein that is homologous to GEFs (guanine nucleotide exchange factors) of the CDC25 family. Ras2 has been shown to induce filamentous growth, but the signaling cascade through which Ras2 and Sql2 regulate cell morphology is not known. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRD--DFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFE 78
Cdd:cd04144    63 LRDQWIREGEGFILVYSITSRSTFERVERFREQIQRVKDESaaDVPIMIVGNKCDKVYEREVSTEEGAALARRLGCEFIE 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1335348560  79 ASAKLRLNVDEAFEQLVRAVRKYQEQELPP--SPPSAPRKKDGGC 121
Cdd:cd04144   143 ASAKTNVNVERAFYTLVRALRQQRQGGQGPkgGPTKKKEKKKRKC 187

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSAS-HHMTYFEA 79
Cdd:cd04136    65 MRDLYIKNGQGFALVYSITAQQSFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVSKEEGQNLARQwGNCPFLET 144

                          90
                  ....*....|....*....
gi 1335348560  80 SAKLRLNVDEAFEQLVRAV 98
Cdd:cd04136   145 SAKSKINVDEIFYDLVRQI 163

Ras-like protein in all tissues (Rit), Ras-like protein in neurons (Rin) and Ras-related protein which interacts with calmodulin (Ric); Rit (Ras-like protein in all tissues), Rin (Ras-like protein in neurons) and Ric (Ras-related protein which interacts with calmodulin) form a subfamily with several unique structural and functional characteristics. These proteins all lack a the C-terminal CaaX lipid-binding motif typical of Ras family proteins, and Rin and Ric contain calmodulin-binding domains. Rin, which is expressed only in neurons, induces neurite outgrowth in rat pheochromocytoma cells through its association with calmodulin and its activation of endogenous Rac/cdc42. Rit, which is ubiquitously expressed in mammals, inhibits growth-factor withdrawl-mediated apoptosis and induces neurite extension in pheochromocytoma cells. Rit and Rin are both able to form a ternary complex with PAR6, a cell polarity-regulating protein, and Rac/cdc42. This ternary complex is proposed to have physiological function in processes such as tumorigenesis. Activated Ric is likely to signal in parallel with the Ras pathway or stimulate the Ras pathway at some upstream point, and binding of calmodulin to Ric may negatively regulate Ric activity.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:cd04141    66 MRDQYMRCGEGFIICYSVTDRHSFQEASEFKELITRVRLTEDIPLVLVGNKVDLEQQRQVTTEEGRNLAREFNCPFFETS 145

                          90       100
                  ....*....|....*....|
gi 1335348560  81 AKLRLNVDEAFEQLVRAVRK 100
Cdd:cd04141   146 AALRFYIDDAFHGLVREIRR 165

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:cd04176    65 MRDLYIKNGQGFIVVYSLVNQQTFQDIKPMRDQIVRVKGYEKVPIILVGNKVDLESEREVSSAEGRALAEEWGCPFMETS 144

                          90
                  ....*....|....*.
gi 1335348560  81 AKLRLNVDEAFEQLVR 96
Cdd:cd04176   145 AKSKTMVNELFAEIVR 160

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   2 REQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASA 81
Cdd:cd04148    66 EDSCMQVGDAYVIVYSVTDRSSFEKASELRIQLRRARQAEDIPIILVGNKSDLVRSREVSVQEGRACAVVFDCKFIETSA 145

                          90
                  ....*....|....*...
gi 1335348560  82 KLRLNVDEAFEQLVRAVR 99
Cdd:cd04148   146 ALQHNVDELFEGIVRQVR 163

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDrDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAKLR 84
Cdd:cd01867    72 YYRGAMGIILVYDITDEKSFENIKNWMRNIDEHAS-EDVERMLVGNKCDMEEKRVVSKEEGEALAREYGIKFLETSAKAN 150

                          90
                  ....*....|....*.
gi 1335348560  85 LNVDEAFEQLVRAVRK 100
Cdd:cd01867   151 INVEEAFLTLAKDILK 166

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:cd04137    65 LPQKYSIGIHGYILVYSVTSRKSFEVVKVIYDKILDMLGKESVPIVLVGNKSDLHMERQVSAEEGKKLAESWGAAFLESS 144

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1335348560  81 AKLRLNVDEAFEQLVRAVRKYQEqelpPSPPSAPRK 116
Cdd:cd04137   145 AKENENVEEAFELLIEEIEKVEN----PLPPGQKSK 176

Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENqRQVLRSEASSFSASHHMTYFEASAKLR 84
Cdd:cd01863    69 YYRGAQGVILVYDVTRRDTFDNLDTWLNELDTYSTNPDAVKMLVGNKIDKEN-REVTREEGQKFARKHNMLFIETSAKTR 147

                          90
                  ....*....|....
gi 1335348560  85 LNVDEAFEQLVRAV 98
Cdd:cd01863   148 IGVQQAFEELVEKI 161

Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRD--------DFPIVLVGNKADLENQRQVLRSEASSF-SAS 71
Cdd:cd04143    64 MRRLSILTGDVFILVFSLDNRESFEEVCRLREQILETKSCLknktkenvKIPMVICGNKADRDFPREVQRDEVEQLvGGD 143

                          90       100
                  ....*....|....*....|...
gi 1335348560  72 HHMTYFEASAKLRLNVDEAFEQL 94
Cdd:cd04143   144 ENCAYFEVSAKKNSNLDEMFRAL 166

Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVgKLFTQILRVKDRDDFPI-VLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAKL 83
Cdd:cd04111    72 YYRNSVGVLLVFDITNRESFEHV-HDWLEEARSHIQPHRPVfILVGHKCDLESQRQVTREEAEKLAKDLGMKYIETSART 150

                          90       100
                  ....*....|....*....|....*...
gi 1335348560  84 RLNVDEAFEQLVRAVrkYQEQELPPSPP 111
Cdd:cd04111   151 GDNVEEAFELLTQEI--YERIKRGELCA 176

Rab GTPase family 4 (Rab4); Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQIlRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:cd04113    65 VTRSYYRGAAGALLVYDITSRESFNALTNWLTDA-RTLASPDIVIILVGNKKDLEDDREVTFLEASRFAQENGLLFLETS 143

                          90
                  ....*....|....*...
gi 1335348560  81 AKLRLNVDEAFEQLVRAV 98
Cdd:cd04113   144 ALTGENVEEAFLKCARSI 161

Rab GTPase family 9 (Rab9); Rab9 is found in late endosomes, together with mannose 6-phosphate receptors (MPRs) and the tail-interacting protein of 47 kD (TIP47). Rab9 is a key mediator of vesicular transport from late endosomes to the trans-Golgi network (TGN) by redirecting the MPRs. Rab9 has been identified as a key component for the replication of several viruses, including HIV1, Ebola, Marburg, and measles, making it a potential target for inhibiting a variety of viruses. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVG---KLFTQILRVKDRDDFPIVLVGNKADLEnQRQVLRSEASSFSASHHMT-Y 76
Cdd:cd04116    70 LRTPFYRGSDCCLLTFSVDDSQSFQNLSnwkKEFIYYADVKEPESFPFVILGNKIDIP-ERQVSTEEAQAWCRDNGDYpY 148

                          90       100
                  ....*....|....*....|..
gi 1335348560  77 FEASAKLRLNVDEAFEQLVRAV 98
Cdd:cd04116   149 FETSAKDATNVAAAFEEAVRRV 170

Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVGKLFTQIlRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAKLR 84
Cdd:cd01865    70 YYRGAMGFILMYDITNEESFNAVQDWSTQI-KTYSWDNAQVILVGNKCDMEDERVVSAERGRQLADQLGFEFFEASAKEN 148

                          90
                  ....*....|.
gi 1335348560  85 LNVDEAFEQLV 95
Cdd:cd01865   149 INVKQVFERLV 159

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAgNGFLLVFAINDRQSFNEVGklfTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASH-HMTYFEA 79
Cdd:cd00882    69 ARLLLRGA-DLILLVVDSTDRESEEDAK---LLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKIlGVPVFEV 144

                          90
                  ....*....|....*..
gi 1335348560  80 SAKLRLNVDEAFEQLVR 96
Cdd:cd00882   145 SAKTGEGVDELFEKLIE 161

Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was localized to the Golgi complex. The specific function of Rab12 remains unknown, and inconsistent results about its cellular localization have been reported. More recent studies have identified Rab12 associated with post-Golgi vesicles, or with other small vesicle-like structures but not with the Golgi complex. 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. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDrDDFPIVLVGNKADLENQRQVLRSEASSFSAS-HHMTYFEASAKL 83
Cdd:cd04120    69 YYRSAKGIILVYDITKKETFDDLPKWMKMIDKYAS-EDAELLLVGNKLDCETDREITRQQGEKFAQQiTGMRFCEASAKD 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1335348560  84 RLNVDEAFEQLVRAVRKYQ------------------EQELPPS-PPSAP 114
Cdd:cd04120   148 NFNVDEIFLKLVDDILKKMpldilrnelsnsilslqpEPEIPPElPPPRP 197

Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with C-terminal DNAJ domains in deuterostome metazoa. They are not found in plants, fungi, and protostome metazoa, suggesting a horizontal gene transfer between protists and deuterostome metazoa. RJLs lack any known membrane targeting signal and contain a degenerate phosphate/magnesium-binding 3 (PM3) motif, suggesting an impaired ability to hydrolyze GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   2 REQYMRAGNGFLLVFAINDRQSF---NEVGKLFTQ-ILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYF 77
Cdd:cd04119    66 RNEFYKDTQGVLLVYDVTDRQSFealDSWLKEMKQeGGPHGNMENIVVVVCANKIDLTKHRAVSEDEGRLWAESKGFKYF 145

                          90       100
                  ....*....|....*....|.
gi 1335348560  78 EASAKLRLNVDEAFEQLVRAV 98
Cdd:cd04119   146 ETSACTGEGVNEMFQTLFSSI 166

Rab family protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVGKlFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAKLR 84
Cdd:PLN03108   75 YYRGAAGALLVYDITRRETFNHLAS-WLEDARQHANANMTIMLIGNKCDLAHRRAVSTEEGEQFAKEHGLIFMEASAKTA 153

                  ....*..
gi 1335348560  85 LNVDEAF 91
Cdd:PLN03108  154 QNVEEAF 160

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVGKLFTQIlrVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAKLR 84
Cdd:cd04121    75 YSRGAQGIILVYDITNRWSFDGIDRWIKEI--DEHAPGVPKILVGNRLHLAFKRQVATEQAQAYAERNGMTFFEVSPLCN 152

                          90       100
                  ....*....|....*....|....*...
gi 1335348560  85 LNVDEAFEQLVRAVRkYQEQELPPSPPS 112
Cdd:cd04121   153 FNITESFTELARIVL-MRHGRPPQSPPQ 179

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   1 MREQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEAS 80
Cdd:cd04101    69 MVENVWEQPAVVCVVYDVTNEVSFNNCSRWINRVRTHSHGLHTPGVLVGNKCDLTDRREVDAAQAQALAQANTLKFYETS 148

                          90
                  ....*....|....*..
gi 1335348560  81 AKLRLNVDEAFEQLVRA 97
Cdd:cd04101   149 AKEGVGYEAPFLSLARA 165

Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   5 YMRAGNGFLLVFAINDRQSFNEVGKLFTQIlrVKDRDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAKLR 84
Cdd:cd04110    75 YYRGTHGVIVVYDVTNGESFVNVKRWLQEI--EQNCDDVCKVLVGNKNDDPERKVVETEDAYKFAGQMGISLFETSAKEN 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1335348560  85 LNVDEAFEQLVRAV-----------RKYQEQELPPSPPSAPRKK 117
Cdd:cd04110   153 INVEEMFNCITELVlrakkdnlakqQQQQQNDVVKLPKNSKRKK 196

Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560   3 EQYMRAGNGFLLVFAINDRQSFNEVGKLFTQILRVKDrDDFPIVLVGNKADLENQRQVLRSEASSFSASHHMTYFEASAK 82
Cdd:cd04117    67 KQYYRRAQGIFLVYDISSERSYQHIMKWVSDVDEYAP-EGVQKILIGNKADEEQKRQVGDEQGNKLAKEYGMDFFETSAC 145

                          90
                  ....*....|....*.
gi 1335348560  83 LRLNVDEAFEQLVRAV 98
Cdd:cd04117   146 TNKNIKESFTRLTELV 161

Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are members of the Rab family of small GTPases. Human Rab32 was first identified in platelets but it is expressed in a variety of cell types, where it functions as an A-kinase anchoring protein (AKAP). Rab38 has been shown to be melanocyte-specific. 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335348560  43 FPIVLVGNKADLENQR-QVLRSEASSFSASHHMT-YFEASAKLRLNVDEAFEQLVRAVRKyQEQELPPSPP--------- 111
Cdd:cd04107   111 IPALLLANKCDLKKERlAKDPEQMDQFCKENGFIgWFETSAKENINIEEAMRFLVKNILK-NDKGLQSPEPdednvidlk 189