GTP-binding protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   6 RVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYkeGTP----------EEKTYYIELWDVGGSvgsaS 75
Cdd:PLN00023   21 QVRVLVVGDSGVGKSSLVHLIVKGSSIARPPQTIGCTVGVKHITY--GSPgsssnsikgdSERDFFVELWDVSGH----E 94

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1394533545  76 SVKSTRAVFYNSVNGIIFVHDLTNKKSSQNLRRWSLE 112
Cdd:PLN00023   95 RYKDCRSLFYSQINGVIFVHDLSQRRTKTSLQKWASE 131

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGcsVDVRVHDYKEGTPEEKTYYIELWDVGGsvgsASSVKSTRAVFYNS 87
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIG--VDFKTKTVLENDDNGKKIKLNIWDTAG----QERFRSLHPFYYRG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533545  88 VNGIIFVHDltnKKSSQNLRRWSLEAlnrdlvptgvlvtngdydqEQFADNqIPLLVIGTKLD 150
Cdd:pfam08477  75 AAAALLVYD---SRTFSNLKYWLREL-------------------KKYAGN-SPVILVGNKID 114

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   6 RVKVLVLGDSGVGKSSLVhllcqNQVLGNpswtvgcsvDVRVHDYKEGTPEE----------KTYYIELWDVGGSV-GSA 74
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLL-----NSLLGN---------KGSITEYYPGTTRNyvttvieedgKTYKFNLLDTAGQEdYDA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545  75 SSVKSTRAV--FYNSVNGIIFVHDLTNKKSSQnlrrwslealnrdlvptgvlvtngDYDQEQFADNQIPLLVIGTKLDQI 152
Cdd:TIGR00231  67 IRRLYYPQVerSLRVFDIVILVLDVEEILEKQ------------------------TKEIIHHADSGVPIILVGNKIDLK 122

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1394533545 153 HET-KRHEVLTRTAFLAEDFNPEEInLDCTN 182
Cdd:TIGR00231 123 DADlKTHVASEFAKLNGEPIIPLSA-ETGKN 152

GTP-binding protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   6 RVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYkeGTP----------EEKTYYIELWDVGGSvgsaS 75
Cdd:PLN00023   21 QVRVLVVGDSGVGKSSLVHLIVKGSSIARPPQTIGCTVGVKHITY--GSPgsssnsikgdSERDFFVELWDVSGH----E 94

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1394533545  76 SVKSTRAVFYNSVNGIIFVHDLTNKKSSQNLRRWSLE 112
Cdd:PLN00023   95 RYKDCRSLFYSQINGVIFVHDLSQRRTKTSLQKWASE 131

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545    7 VKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGcsVDVRVhdyKEGTPEEKTYYIELWDVGG-----SVGSAssvkstr 81
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSEQYKSTIG--VDFKT---KTIEVDGKRVKLQIWDTAGqerfrSITSS------- 68

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533545   82 avFYNSVNGIIFVHDLTNKKSSQNLRRWSLEAlnrdlvptgvlvtngdydqEQFADNQIPLLVIGTKLDQIHE 154
Cdd:smart00175  69 --YYRGAVGALLVYDITNRESFENLENWLKEL-------------------REYASPNVVIMLVGNKSDLEEQ 120

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 1394533545   7 VKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGcsVDVRVhdyKEGTPEEKTYYIELWDVGGsvgsASSVKSTRAVFYN 86
Cdd:cd01863     1 LKILLIGDSGVGKSSLLLRFTDDTFDEDLSSTIG--VDFKV---KTVTVDGKKVKLAIWDTAG----QERFRTLTSSYYR 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533545  87 SVNGIIFVHDLTNKKSSQNLRRWSLEAlnrdlvptgvlvtngdydqEQFADNQ-IPLLVIGTKLD 150
Cdd:cd01863    72 GAQGVILVYDVTRRDTFDNLDTWLNEL-------------------DTYSTNPdAVKMLVGNKID 117

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVlgNPSW--TVGC---SVDVRVHDykegtpeeKTYYIELWDVGGSvgsaSSVKSTRA 82
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKF--PEEYipTIGVdfyTKTIEVDG--------KTVKLQIWDTAGQ----ERFRALRP 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1394533545  83 VFYNSVNGIIFVHDLTNKKSSQNLRRWslealnrdlvptgvlvtngdYDQ-EQFADNQIPLLVIGTKLD 150
Cdd:pfam00071  67 LYYRGADGFLLVYDITSRDSFENVKKW--------------------VEEiLRHADENVPIVLVGNKCD 115

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 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYkegtpEEKTYYIELWDVGGSvgsaSSVKSTRAVFYNS 87
Cdd:cd04110     8 KLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEI-----NGERVKLQIWDTAGQ----ERFRTITSTYYRG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1394533545  88 VNGIIFVHDLTNKKSSQNLRRWSLEALNRDLVPTGVLVTNGDYDQEQ 134
Cdd:cd04110    79 THGVIVVYDVTNGESFVNVKRWLQEIEQNCDDVCKVLVGNKNDDPER 125

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 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYKEGtpeeKTYYIELWDVGGSvgsaSSVKS-TRAVFYN 86
Cdd:cd04111     4 RLIVIGDSTVGKSSLLKRFTEGRFAEVSDPTVGVDFFSRLIEIEPG----VRIKLQLWDTAGQ----ERFRSiTRSYYRN 75

                          90       100
                  ....*....|....*....|....*..
gi 1394533545  87 SVNGIIfVHDLTNKKSSQNLRRWSLEA 113
Cdd:cd04111    76 SVGVLL-VFDITNRESFEHVHDWLEEA 101

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 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVlgNPSW--TVGCsvdvrvhDYKEGTPE--EKTYYIELWDVGGSvgsaSSVKSTRAV 83
Cdd:cd01867     5 KLLLIGDSGVGKSCLLLRFSEDSF--NPSFisTIGI-------DFKIRTIEldGKKIKLQIWDTAGQ----ERFRTITTS 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533545  84 FYNSVNGIIFVHDLTNKKSSQNLRRWSLEAlnrdlvptgvlvtngdydqEQFADNQIPLLVIGTKLD 150
Cdd:cd01867    72 YYRGAMGIILVYDITDEKSFENIKNWMRNI-------------------DEHASEDVERMLVGNKCD 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   6 RVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGC---SVDVRVHDykegtpeeKTYYIELWDVGGSvgsaSSVKSTRA 82
Cdd:cd01860     1 QFKLVLLGDSSVGKSSIVLRFVKNEFSENQESTIGAaflTQTVNLDD--------TTVKFEIWDTAGQ----ERYRSLAP 68

                          90       100
                  ....*....|....*....|....*..
gi 1394533545  83 VFYNSVNGIIFVHDLTNKKSSQNLRRW 109
Cdd:cd01860    69 MYYRGAAAAIVVYDITSEESFEKAKSW 95

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 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGcsVD--VRVHDYKEGTPEEktyyIELWDVGGSVGSASsvkSTRaVFY 85
Cdd:cd04107     2 KVLVIGDLGVGKTSIIKRYVHGVFSQHYKATIG--VDfaLKVIEWDPNTVVR----LQLWDIAGQERFGG---MTR-VYY 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533545  86 NSVNGIIFVHDLTNKKSSQNLRRWslealnrdlvptgvlvtNGDYDQE-QFADNQ-IPLLVIGTKLDQIHET 155
Cdd:cd04107    72 KGAVGAIIVFDVTRPSTFEAVLKW-----------------KADLDSKvTLPNGEpIPALLLANKCDLKKER 126

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 1394533545   7 VKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYkegtpEEKTYYIELWDVGGSVGSASSVKStravFYN 86
Cdd:cd04113     1 FKFLIIGSAGTGKSCLLHQFIENKFKQDSNHTIGVEFGSRVVNV-----GGKSVKLQIWDTAGQERFRSVTRS----YYR 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1394533545  87 SVNGIIFVHDLTNKKSSQNLRRWSLEAlnRDLVPTGVLV 125
Cdd:cd04113    72 GAAGALLVYDITSRESFNALTNWLTDA--RTLASPDIVI 108

Rab GTPase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYkegtpEEKTYYIELWDVGGSvgsaSSVKSTRAVFYNS 87
Cdd:PLN03110   14 KIVLIGDSGVGKSNILSRFTRNEFCLESKSTIGVEFATRTLQV-----EGKTVKAQIWDTAGQ----ERYRAITSAYYRG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533545  88 VNGIIFVHDLTNKKSSQNLRRWSLEAlnRDlvptgvlvtngdydqeqFADNQIPLLVIGTKLDQIH 153
Cdd:PLN03110   85 AVGALLVYDITKRQTFDNVQRWLREL--RD-----------------HADSNIVIMMAGNKSDLNH 131

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGcsVDVRVHDYKEgtpEEKTYYIELWDVGGSvgsaSSVKSTRAVFYNS 87
Cdd:cd01869     4 KLLLIGDSGVGKSCLLLRFADDTYTESYISTIG--VDFKIRTIEL---DGKTVKLQIWDTAGQ----ERFRTITSSYYRG 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1394533545  88 VNGIIFVHDLTNKKSSQNLRRWsLEALNRdLVPTGV---LVTNG---------DYDQEQ-FAD-NQIPLLVIGTK 148
Cdd:cd01869    75 AHGIIIVYDVTDQESFNNVKQW-LQEIDR-YASENVnklLVGNKcdltdkkvvDYTEAKeFADeLGIPFLETSAK 147

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 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCsvdvrvhDYKEGTPEEK--TYYIELWDVGGSVGSASSVKStravFY 85
Cdd:cd04117     2 RLLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGV-------DFKMKTIEVDgiKVRIQIWDTAGQERYQTITKQ----YY 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533545  86 NSVNGIIFVHDLTNKKSSQNLRRWSlealnrdlvptgvlvtngdYDQEQFADNQIPLLVIGTKLDQihETKR 157
Cdd:cd04117    71 RRAQGIFLVYDISSERSYQHIMKWV-------------------SDVDEYAPEGVQKILIGNKADE--EQKR 121

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   7 VKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRvhdyKEGTPEEKTYYIELWDVGG-SVGSASSVKstravFY 85
Cdd:cd04109     1 IKIVVLGDGASGKTSLIRRFAQEGFGKSYKQTIGLDFFSR----RITLPGSLNVTLQVWDIGGqQIGGKMLDK-----YI 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1394533545  86 NSVNGIIFVHDLTNKKSSQNLRRW--SLEALNRDLV--PTGVLVTN 127
Cdd:cd04109    72 YGAQAVCLVYDITNSQSFENLEDWlsVVKKVNEESEtkPKMVLVGN 117

Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily in the Golgi, interacts with its effector, Rab-interacting lysosomal protein (RILP). This enables its participation in microtubular dynenin-dynactin-mediated repositioning of lysosomes from the cell periphery to the Golgi. A Rab34 (Rah) isoform that lacks the consensus GTP-binding region has been identified in mice. This isoform is associated with membrane ruffles and promotes macropinosome formation. Rab36 has been mapped to human chromosome 22q11.2, a region that is homozygously deleted in malignant rhabdoid tumors (MRTs). However, experimental assessments do not implicate Rab36 as a tumor suppressor that would enable tumor formation through a loss-of-function mechanism. 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 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGcsVDVRVHDYK-EGTPeektYYIELWDVGGSvgsaSSVKSTRAVFYN 86
Cdd:cd04108     2 KVIVVGDLSVGKTCLINRFCKDVFDKNYKATIG--VDFEMERFEvLGVP----FSLQLWDTAGQ----ERFKCIASTYYR 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1394533545  87 SVNGIIFVHDLTNKKSSQNLRRWSLEALnRDLVPTGVLV 125
Cdd:cd04108    72 GAQAIIIVFDLTDVASLEHTRQWLEDAL-KENDPSSVLL 109

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533545   6 RVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGcsvdVRVHDYKEGTPEEKTYYIELWDVGG 69
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLIGEKFDGDESSTHG----INVQDWKIPAPERKKIRLNVWDFGG 60

Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, including the rough ER, the Golgi complex, and the trans-Golgi network, and to endosomal compartments, including early endosomal vacuoles and associated vesicles. Rab14 is believed to function in both the biosynthetic and recycling pathways between the Golgi and endosomal compartments. Rab14 has also been identified on GLUT4 vesicles, and has been suggested to help regulate GLUT4 translocation. In addition, Rab14 is believed to play a role in the regulation of 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCSVDVRVHDYkegtpEEKTYYIELWDVGGSvgsassvKSTRAV---F 84
Cdd:cd04122     4 KYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEV-----NGQKIKLQIWDTAGQ-------ERFRAVtrsY 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1394533545  85 YNSVNGIIFVHDLTNKKSSQNLRRWSLEALN 115
Cdd:cd04122    72 YRGAAGALMVYDITRRSTYNHLSSWLTDARN 102

Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. 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 1394533545   8 KVLVLGDSGVGKSS-LVHLLCQNQVLGNPSWTVGCSVDVRVHdykegTPEEKTYYIELWDVGGSvgsaSSVKSTRAVFYN 86
Cdd:cd04112     2 KVMLVGDSGVGKTClLVRFKDGAFLAGSFIATVGIQFTNKVV-----TVDGVKVKLQIWDTAGQ----ERFRSVTHAYYR 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1394533545  87 SVNGIIFVHDLTNKKSSQNLRRW---SLEALNRDLV 119
Cdd:cd04112    73 DAHALLLLYDVTNKSSFDNIRAWlteILEYAQSDVV 108

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   8 KVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVGCsvdvrvhDY--KEGTPEEKTYYIELWDVGGSVGSASSVKStravFY 85
Cdd:cd01861     2 KLVFLGDQSVGKTSIITRFMYDTFDNQYQATIGI-------DFlsKTMYVDDKTVRLQLWDTAGQERFRSLIPS----YI 70

                          90       100
                  ....*....|....*....|....
gi 1394533545  86 NSVNGIIFVHDLTNKKSSQNLRRW 109
Cdd:cd01861    71 RDSSVAVVVYDITNRQSFDNTDKW 94

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533545   6 RVKVLVLGDSGVGKSSLVHLLCQNQVLGNPSWTVgcsvdvrVHDYKEGTpEEKTYYIEL--WDVGGSvgsaSSVKSTRAV 83
Cdd:cd04131     1 RCKIVLVGDSQCGKTALLQVFAKDSFPENYVPTV-------FENYTASF-EVDKQRIELslWDTSGS----PYYDNVRPL 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533545  84 FYNSVNGIIFVHDLTNKKSSQN-LRRWSLEAlnRDLVPTgvlvtngdydqeqfadnqIPLLVIGTKLD 150
Cdd:cd04131    69 SYPDSDAVLICFDISRPETLDSvLKKWKGEV--REFCPN------------------TPVLLVGCKSD 116

Rab GTPase family 24 (Rab24); Rab24 is distinct from other Rabs in several ways. It exists primarily in the GTP-bound state, having a low intrinsic GTPase activity; it is not efficiently geranyl-geranylated at the C-terminus; it does not form a detectable complex with Rab GDP-dissociation inhibitors (GDIs); and it has recently been shown to undergo tyrosine phosphorylation when overexpressed in vitro. The specific function of Rab24 still remains unknown. It is found in a transport route between ER-cis-Golgi and late endocytic compartments. It is putatively involved in an autophagic pathway, possibly directing misfolded proteins in the ER to degradative pathways. 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 1394533545   7 VKVLVLGDSGVGKSSLVHLLCQNQVLGNPSW-TVGCSVDVrvhdyKEGTPEEKTYYIELWDVGGSvgsaSSVKSTRAVFY 85
Cdd:cd04118     1 VKVVMLGKESVGKTSLVERYVHHRFLVGPYQnTIGAAFVA-----KRMVVGERVVTLGIWDTAGS----ERYEAMSRIYY 71