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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  13 KFLIFGGKSVGKKTLLRSFCTEGDNESIWTSLTVD-------------DEKVLIEATVSQKWEEGMSKEH----DAIALV 75
Cdd:cd04106    2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDflekqiflrqsdeDVRLMLWDTAGQEEFDAITKAYyrgaQACILV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  76 FSTTDVYSFEYTLELYNEIQKSTERIPLVFIENKIDIVEDSQMDKGLVEGEMRKKHKRLYRVSALKEFNVMHPFAYLIEK 155
Cdd:cd04106   82 FSTTDRESFEAIESWKEKVEAECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSVKDDFNVTELFEYLAEK 161

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  13 KFLIFGGKSVGKKTLLRSFCTEGDNESIWTSLTVD-------------DEKVLIEATVSQKWEEGMSKEH----DAIALV 75
Cdd:cd04106    2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDflekqiflrqsdeDVRLMLWDTAGQEEFDAITKAYyrgaQACILV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  76 FSTTDVYSFEYTLELYNEIQKSTERIPLVFIENKIDIVEDSQMDKGLVEGEMRKKHKRLYRVSALKEFNVMHPFAYLIEK 155
Cdd:cd04106   82 FSTTDRESFEAIESWKEKVEAECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSVKDDFNVTELFEYLAEK 161

GTP-binding nuclear protein Ran; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115532636  91 YNEIQKSTERIPLVFIENKIDiVEDSQMDKGLVEGEmRKKHKRLYRVSALKEFNVMHPFAYLIEKLT 157
Cdd:PLN03071 108 HRDLCRVCENIPIVLCGNKVD-VKNRQVKAKQVTFH-RKKNLQYYEISAKSNYNFEKPFLYLARKLA 172

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  13 KFLIFGGKSVGKKTLLRSFCTEGDNESIWTSLTVD-------------DEKVLIEATVSQKWEEGMSKEH----DAIALV 75
Cdd:cd04106    2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDflekqiflrqsdeDVRLMLWDTAGQEEFDAITKAYyrgaQACILV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  76 FSTTDVYSFEYTLELYNEIQKSTERIPLVFIENKIDIVEDSQMDKGLVEGEMRKKHKRLYRVSALKEFNVMHPFAYLIEK 155
Cdd:cd04106   82 FSTTDRESFEAIESWKEKVEAECGDIPMVLVQTKIDLLDQAVITNEEAEALAKRLQLPLFRTSVKDDFNVTELFEYLAEK 161

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  13 KFLIFGGKSVGKKTLLRSFCT-------EGDNESIWTS-LTVDDEKVLIEA--TVSQKWEEgmSKEH--------DAIAL 74
Cdd:cd04146    1 KIAVLGASGVGKSALTVRFLTkrfigeyEPNLESLYSRqVTIDGEQVSLEIqdTPGQQQNE--DPESlerslrwaDGFVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  75 VFSTTDVYSFEYTLELYN---EIQKSTERIPLVFIENKIDIVEDSQMDKGlvEGEMRKKHKR--LYRVSALKEFN-VMHP 148
Cdd:cd04146   79 VYSITDRSSFDVVSQLLQlirEIKKRDGEIPVILVGNKADLLHSRQVSTE--EGQKLALELGclFFEVSAAENYLeVQNV 156

                        170
                 ....*....|
gi 115532636 149 FAYLIEKLTR 158
Cdd:cd04146  157 FHELCREVRR 166

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636   9 DR-VFKFLIFGGKSVGKKTLLRSF-----CTEGDNESIWTSLTVDD------EKVLI-----EATVSQKWEEGMSKEHDA 71
Cdd:cd01892    1 QRnVFLCFVLGAKGSGKSALLQAFlgrsfSQNAYSPTIKPRYAVNTvevpgqEKYLIlrevgEDEEAILLNDAELAACDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 115532636  72 IALVFSTTDVYSFEYTLELYNeIQKSTERIPLVFIENKIDIVEDSQM 118
Cdd:cd01892   81 ACLVYDSSDPNSFSYCAEVYK-KYFMLGEIPCLFVAAKADLDEQQQR 126

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 115532636  12 FKFLIFGGKSVGKKTLLRSFCT----------EGDnESIWTSLTVDDEKVLIE-----ATVSQKW-EEGMSKEHDAIALV 75
Cdd:cd04148    1 YRVVLLGDSGVGKSSLANIFTAgvyedsayeaSGD-DTYERTVSVDGEEATLVvydhwEQEDGMWlEDSCMQVGDAYVIV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 115532636  76 FSTTDVYSFEYTLELYNEIQKS--TERIPLVFIENKIDIV 113
Cdd:cd04148   80 YSVTDRSSFEKASELRIQLRRArqAEDIPIILVGNKSDLV 119

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 115532636   7 SYDRVFKFLIFGGKSVGKKTLLRSFcTEGDNESIW----------TSLTVDDEKVLIE----------ATVSQKWEEGMS 66
Cdd:cd04121    2 AYDYLLKFLLVGDSDVGKGEILASL-QDGSTESPYgynmgidyktTTILLDGRRVKLQlwdtsgqgrfCTIFRSYSRGAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  67 kehdAIALVFSTTDVYSFEYTLELYNEIQKSTERIPLVFIENKIDIVEDSQMDKGLVEGEMRKKHKRLYRVSALKEFNVM 146
Cdd:cd04121   81 ----GIILVYDITNRWSFDGIDRWIKEIDEHAPGVPKILVGNRLHLAFKRQVATEQAQAYAERNGMTFFEVSPLCNFNIT 156

                 ....*.
gi 115532636 147 HPFAYL 152
Cdd:cd04121  157 ESFTEL 162

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 115532636   8 YDRVFKFLIFGGKSVGKKTLLRSFCTEGDNESIWTSLTVD---------DEKVLIEA----------TVSQKWEEGMske 68
Cdd:cd04110    3 YDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDfkirtveinGERVKLQIwdtagqerfrTITSTYYRGT--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  69 HDAIaLVFSTTDVYSFEYTLELYNEIQKSTERIPLVFIENKIDivedsQMDKGLVEGEMRKKHK-----RLYRVSALKEF 143
Cdd:cd04110   80 HGVI-VVYDVTNGESFVNVKRWLQEIEQNCDDVCKVLVGNKND-----DPERKVVETEDAYKFAgqmgiSLFETSAKENI 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 115532636 144 NVMHPFAYLIEKLTRQKKDLNANESVsENSLRL 176
Cdd:cd04110  154 NVEEMFNCITELVLRAKKDNLAKQQQ-QQQNDV 185

GTP-binding nuclear protein Ran; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115532636  91 YNEIQKSTERIPLVFIENKIDiVEDSQMDKGLVEGEmRKKHKRLYRVSALKEFNVMHPFAYLIEKLT 157
Cdd:PLN03071 108 HRDLCRVCENIPIVLCGNKVD-VKNRQVKAKQVTFH-RKKNLQYYEISAKSNYNFEKPFLYLARKLA 172

GTP-binding nuclear protein Ran; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115532636  91 YNEIQKSTERIPLVFIENKIDiVEDSQMDKGLVEGEmRKKHKRLYRVSALKEFNVMHPFAYLIEKLTRQKK 161
Cdd:PTZ00132 104 HRDIVRVCENIPIVLVGNKVD-VKDRQVKARQITFH-RKKNLQYYDISAKSNYNFEKPFLWLARRLTNDPN 172

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  10 RVFKFLIFGGKSVGKKTLL-----RSFCTEGD---NESIWTSLTVDDEKVLIEA--TVSQKWEEGMSKEH----DAIALV 75
Cdd:cd04145    1 PTYKLVVVGGGGVGKSALTiqfiqSYFVTDYDptiEDSYTKQCEIDGQWARLDIldTAGQEEFSAMREQYmrtgEGFLLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  76 FSTTDVYSFEYTLELYNEIQ--KSTERIPLVFIENKIDIVEDSQMDKGlvEG-EMRKKHKRLY-RVSALKEFNVMHPFAY 151
Cdd:cd04145   81 FSVTDRGSFEEVDKFHTQILrvKDRDEFPMILVGNKADLEHQRQVSRE--EGqELARQLKIPYiETSAKDRVNVDKAFHD 158

                 ..
gi 115532636 152 LI 153
Cdd:cd04145  159 LV 160

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 115532636    10 RVFKFLIFGGKSVGKKTLLRSFCTEGDNE--------SIWTSLTVDDEKVLIEATVSQKWEE--GM----SKEHDAIALV 75
Cdd:smart00010   1 REYKLVVLGGGGVGKSALTIQFVQGHFVDeydptiedSYRKQIEIDGEVCLLDILDTAGQEEfsAMrdqyMRTGEGFLLV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 115532636    76 FSTTDVYSFEYTLELYNEIQ--KSTERIPLVFIENKIDIVEDSQ 117
Cdd:smart00010  81 YSITDRQSFEEIAKFREQILrvKDRDDVPIVLVGNKCDLENERV 124

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  13 KFLIFGGKSVGKKTLLRSFCTEGDNESIWTSLtvddEKVLIEATV-----------------SQKWEEGMSKEHDAIALV 75
Cdd:cd01893    4 RIVLIGDEGVGKSSLIMSLVSEEFPENVPRVL----PEITIPADVtpervpttivdtssrpqDRANLAAEIRKANVICLV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115532636  76 FSTTDVYSFE----YTLELYNEiqkSTERIPLVFIENKIDIVEDSQ 117
Cdd:cd01893   80 YSVDRPSTLErirtKWLPLIRR---LGVKVPIILVGNKSDLRDGSS 122

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  10 RVFKFLIFGGKSVGKKTLLRSFCTEGDNESIWTSLTVD-DEKVLI---EATVSQKW----EEGMSK---EH-----DAIA 73
Cdd:cd04115    1 RIFKIIVIGDSNVGKTCLTYRFCAGRFPERTEATIGVDfRERTVEidgERIKVQLWdtagQERFRKsmvQHyyrnvHAVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532636  74 LVFSTTDVYSFEYTLELYNEIQKST--ERIPLVFIENKIDIVEDSQMDKGLVEgEMRKKHKR-LYRVSALKEFNVMH--- 147
Cdd:cd04115   81 FVYDVTNMASFHSLPSWIEECEQHSlpNEVPRILVGNKCDLREQIQVPTDLAQ-RFADAHSMpLFETSAKDPSENDHvea 159

                 ....*....
gi 115532636 148 PFAYLIEKL 156
Cdd:cd04115  160 IFMTLAHKL 168