Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. 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 356530655 126 LKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILIMF 205
Cdd:cd04128    1 LKIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVNFMEKTISIRGTEITFSIWDLGGQREFINMLPLVCKDAVAILFMF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 206 DLTSRCTLNSVVGWYSKARKWNQTAIPILIGTKFDDFVKLPPDVQWTIVTQARAYARAMKATLFFSSASHNINVNKIFKF 285
Cdd:cd04128   81 DLTRKSTLNSIKEWYRQARGFNKTAIPILVGTKYDLFADLPPEEQEEITKQARKYAKAMKAPLIFCSTSHSINVQKIFKF 160

                        170       180
                 ....*....|....*....|.
gi 356530655 286 IMAKLFNLPWKVERNLTLGEP 306
Cdd:cd04128  161 VLAKVFDLPLTIPEILTVGEP 181

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. 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 356530655 126 LKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILIMF 205
Cdd:cd04128    1 LKIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVNFMEKTISIRGTEITFSIWDLGGQREFINMLPLVCKDAVAILFMF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 206 DLTSRCTLNSVVGWYSKARKWNQTAIPILIGTKFDDFVKLPPDVQWTIVTQARAYARAMKATLFFSSASHNINVNKIFKF 285
Cdd:cd04128   81 DLTRKSTLNSIKEWYRQARGFNKTAIPILVGTKYDLFADLPPEEQEEITKQARKYAKAMKAPLIFCSTSHSINVQKIFKF 160

                        170       180
                 ....*....|....*....|.
gi 356530655 286 IMAKLFNLPWKVERNLTLGEP 306
Cdd:cd04128  161 VLAKVFDLPLTIPEILTVGEP 181

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655   126 LKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDP--GSIcqIPMACKDSVAILI 203
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSRFTDGKFSEQYKSTIGVDFKTKTIEVDGKRVKLQIWDTAGQErfRSI--TSSYYRGAVGALL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655   204 MFDLTSRCTLNSVVGWYSKARKWNQTAIPI-LIGTKFDdfvkLPPDVQwtiVT--QARAYARAMKATLFFSSASHNINVN 280
Cdd:smart00175  79 VYDITNRESFENLENWLKELREYASPNVVImLVGNKSD----LEEQRQ---VSreEAEAFAEEHGLPFFETSAKTNTNVE 151

                          170
                   ....*....|...
gi 356530655   281 KIFKFIMAKLFNL 293
Cdd:smart00175 152 EAFEELAREILKR 164

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 356530655  127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQmKGLNLMDKTLFVQ--GARISFSIWDVAG----DPGSICQIPMAckdsVA 200
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLLGNKGSITEYY-PGTTRNYVTTVIEedGKTYKFNLLDTAGqedyDAIRRLYYPQV----ER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655  201 ILIMFDLTSRC--TLNSVVGWYSKARKWNQTAIPILI-GTKFD-DFVKLPPDVQwtivtqaRAYARAMKATLFFSSASHN 276
Cdd:TIGR00231  78 SLRVFDIVILVldVEEILEKQTKEIIHHADSGVPIILvGNKIDlKDADLKTHVA-------SEFAKLNGEPIIPLSAETG 150

                         170
                  ....*....|
gi 356530655  277 INVNKIFKFI 286
Cdd:TIGR00231 151 KNIDSAFKIV 160

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. 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 356530655 126 LKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILIMF 205
Cdd:cd04128    1 LKIGLLGDAQIGKTSLMVKYVEGEFDEEYIQTLGVNFMEKTISIRGTEITFSIWDLGGQREFINMLPLVCKDAVAILFMF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 206 DLTSRCTLNSVVGWYSKARKWNQTAIPILIGTKFDDFVKLPPDVQWTIVTQARAYARAMKATLFFSSASHNINVNKIFKF 285
Cdd:cd04128   81 DLTRKSTLNSIKEWYRQARGFNKTAIPILVGTKYDLFADLPPEEQEEITKQARKYAKAMKAPLIFCSTSHSINVQKIFKF 160

                        170       180
                 ....*....|....*....|.
gi 356530655 286 IMAKLFNLPWKVERNLTLGEP 306
Cdd:cd04128  161 VLAKVFDLPLTIPEILTVGEP 181

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 356530655  127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAG--DPGSICqiPMACKDSVAILIM 204
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVDFYTKTIEVDGKTVKLQIWDTAGqeRFRALR--PLYYRGADGFLLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655  205 FDLTSRCTLNSVVGWYSKARKWNQTAIPI-LIGTKFDdfvkLPPDVQwtiVT--QARAYARAMKATLFFSSASHNINVNK 281
Cdd:pfam00071  79 YDITSRDSFENVKKWVEEILRHADENVPIvLVGNKCD----LEDQRV---VSteEGEALAKELGLPFMETSAKTNENVEE 151

                  ..
gi 356530655  282 IF 283
Cdd:pfam00071 152 AF 153

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 356530655 127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGdpgsicQ------IPMACKDSVA 200
Cdd:cd01860    3 KLVLLGDSSVGKSSIVLRFVKNEFSENQESTIGAAFLTQTVNLDDTTVKFEIWDTAG------QeryrslAPMYYRGAAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 201 ILIMFDLTSRCTLnsvvgwySKARKW--------NQTAIPILIGTKFDdfvkLPPDVQwtiVT--QARAYARAMKATLFF 270
Cdd:cd01860   77 AIVVYDITSEESF-------EKAKSWvkelqehgPPNIVIALAGNKAD----LESKRQ---VSteEAQEYADENGLLFME 142

                        170       180
                 ....*....|....*....|
gi 356530655 271 SSASHNINVNKIFKFIMAKL 290
Cdd:cd01860  143 TSAKTGENVNELFTEIARKL 162

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 356530655  127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFV---QGARISFSIWDVAGdpgsicQ------IPMACKD 197
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIGVDFKTKTVLEnddNGKKIKLNIWDTAG------QerfrslHPFYYRG 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 356530655  198 SVAILIMFDLTSRCTLNSvvgWYSKARKWNQTAIPILIGTKFD 240
Cdd:pfam08477  75 AAAALLVYDSRTFSNLKY---WLRELKKYAGNSPVILVGNKID 114

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 356530655 127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGdpgsicQ------IPMACKDSVA 200
Cdd:cd01861    2 KLVFLGDQSVGKTSIITRFMYDTFDNQYQATIGIDFLSKTMYVDDKTVRLQLWDTAG------QerfrslIPSYIRDSSV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 201 ILIMFDLTSRCTLNSVVGWYS--KARKWNQTAIpILIGTKFDdfvkLPPDVQWTIVtQARAYARAMKATLFFSSASHNIN 278
Cdd:cd01861   76 AVVVYDITNRQSFDNTDKWIDdvRDERGNDVII-VLVGNKTD----LSDKRQVSTE-EGEKKAKENNAMFIETSAKAGHN 149

                        170
                 ....*....|..
gi 356530655 279 VNKIFKFIMAKL 290
Cdd:cd01861  150 VKQLFKKIAQAL 161

Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in diverse biological functions, such as nuclear transport, spindle formation during mitosis, DNA replication, and cell division. Among the Ras superfamily, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras superfamily. Ran may therefore interact with a wide range of proteins in various intracellular locations. Like other GTPases, Ran exists in GTP- and GDP-bound conformations that interact differently with effectors. Conversion between these forms and the assembly or disassembly of effector complexes requires the interaction of regulator proteins. The intrinsic GTPase activity of Ran is very low, but it is greatly stimulated by a GTPase-activating protein (RanGAP1) located in the cytoplasm. By contrast, RCC1, a guanine nucleotide exchange factor that generates RanGTP, is bound to chromatin and confined to the nucleus. Ran itself is mobile and is actively imported into the nucleus by a mechanism involving NTF-2. Together with the compartmentalization of its regulators, this is thought to produce a relatively high concentration of RanGTP in the nucleus.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDpgsicQIPMACKD------SVA 200
Cdd:cd00877    2 KLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLDFHTNRGKIRFNVWDTAGQ-----EKFGGLRDgyyiqgQCA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 356530655 201 IlIMFDLTSRCTLNSVVGWYSKARKWNQTaIPI-LIGTKFD 240
Cdd:cd00877   77 I-IMFDVTSRVTYKNVPNWHRDLVRVCEN-IPIvLCGNKVD 115

Rab GTPase-like family 2 (Rab-like2); RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share > 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. The specific functions of RabL2a and RabL2b remain unknown. 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 356530655 126 LKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILIMF 205
Cdd:cd04124    1 VKIILLGDSAVGKSKLVERFLMDGYEPQQLSTYALTLYKHNAKFEGKTILVDFWDTAGQERFQTMHASYYHKAHACILVF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356530655 206 DLTSRCTLNSVVGWYSKARKWNQTAIPILIGTKFDdfvkLPPDVqwtiVTQARAYARAMKATLFFSSASHNINVNKIFK 284
Cdd:cd04124   81 DVTRKITYKNLSKWYEELREYRPEIPCIVVANKID----LDPSV----TQKKFNFAEKHNLPLYYVSAADGTNVVKLFQ 151

Rab family protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 124 VNLKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMkGLNLMDKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILI 203
Cdd:PLN03118  13 LSFKILLIGDSGVGKSSLLVSFISSSVEDLAPTI-GVDFKIKQLTVGGKRLKLTIWDTAGQERFRTLTSSYYRNAQGIIL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 204 MFDLTSRCTLNSVVGWYSKARKW---NQTAIPILIGTKFDdfVKLPPDVQwtiVTQARAYARAMKATLFFSSASHNINVN 280
Cdd:PLN03118  92 VYDVTRRETFTNLSDVWGKEVELystNQDCVKMLVGNKVD--RESERDVS---REEGMALAKEHGCLFLECSAKTRENVE 166

                        170       180
                 ....*....|....*....|....*...
gi 356530655 281 KIFKFIMAKLFNLPWKVERNLTLGEPTI 308
Cdd:PLN03118 167 QCFEELALKIMEVPSLLEEGSTAVKRNI 194

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 356530655 127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGdpgsicQ-----IPMA-CKDSVA 200
Cdd:cd01867    5 KLLLIGDSGVGKSCLLLRFSEDSFNPSFISTIGIDFKIRTIELDGKKIKLQIWDTAG------QerfrtITTSyYRGAMG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 201 ILIMFDLTSRCTLNSVVGWYSKARKW-NQTAIPILIGTKFDdfvkLPPDVQWTIvTQARAYARAMKATLFFSSASHNINV 279
Cdd:cd01867   79 IILVYDITDEKSFENIKNWMRNIDEHaSEDVERMLVGNKCD----MEEKRVVSK-EEGEALAREYGIKFLETSAKANINV 153

                        170
                 ....*....|
gi 356530655 280 NKIFkFIMAK 289
Cdd:cd01867  154 EEAF-LTLAK 162

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 356530655 126 LKISLLGDCHIGKTSFVIKYV-GD--EQEKRSLqmkGLNLMDKTLFVQ--GARISFSIWDVAGDPGSICQIPMACKDSVA 200
Cdd:cd04106    1 IKVIVVGNGNVGKSSMIQRFVkGIftKDYKKTI---GVDFLEKQIFLRqsDEDVRLMLWDTAGQEEFDAITKAYYRGAQA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 201 ILIMFDLTSRCTLNSVVGWYSKARKWNQTAIPILIGTKFDdfvkLPPDVqwTIVTQ-ARAYARAMKATLFFSSASHNINV 279
Cdd:cd04106   78 CILVFSTTDRESFEAIESWKEKVEAECGDIPMVLVQTKID----LLDQA--VITNEeAEALAKRLQLPLFRTSVKDDFNV 151

                        170
                 ....*....|
gi 356530655 280 NKIFKFIMAK 289
Cdd:cd04106  152 TELFEYLAEK 161

Rab GTPase family 19 (Rab19); Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. Similarity analysis indicated that Rab41 is closely related to Rab19. However, the function of these Rabs is not yet characterized. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 127 KISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDP--GSICQipMACKDSVAILIM 204
Cdd:cd01864    5 KIILIGDSNVGKTCVVQRFKSGTFSERQGNTIGVDFTMKTLEIQGKRVKLQIWDTAGQErfRTITQ--SYYRSANGAIIA 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 356530655 205 FDLTSRCTLNSVVGWYSKARKWNQTAI-PILIGTKFD 240
Cdd:cd01864   83 YDITRRSSFESVPHWIEEVEKYGASNVvLLLIGNKCD 119

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 356530655 130 LLGDCHIGKTSFVIKYVGDEQEKRSLQM---KGLNLmdKTLFVQGARISFSIWDVAG-----DPGSICQIPMACKDSVAI 201
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEVSDVPgttRDPDV--YVKELDKGKVKLVLVDTPGldefgGLGREELARLLLRGADLI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 202 LIMFDLTSRCTLNSVVGWYSKARKWNQTAIpILIGTKFDdfvKLPPDVQWTIVTQARAYARAmKATLFFSSASHNINVNK 281
Cdd:cd00882   80 LLVVDSTDRESEEDAKLLILRRLRKEGIPI-ILVGNKID---LLEEREVEELLRLEELAKIL-GVPVFEVSAKTGEGVDE 154

                 ....*.
gi 356530655 282 IFKFIM 287
Cdd:cd00882  155 LFEKLI 160

rab6; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 159 GLNLMDKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILIMFDLTSRCTLNSVVGWYSKA-RKWNQTAIPILIGT 237
Cdd:PTZ00099  14 GIDFLSKTLYLDEGPVRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTKWIQDIlNERGKDVIIALVGN 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356530655 238 KFD--DFVKlppdvqwtiVTQARAYARAMKATLFF----SSASHNINVnkIFKFIMAKLFNL 293
Cdd:PTZ00099  94 KTDlgDLRK---------VTYEEGMQKAQEYNTMFhetsAKAGHNIKV--LFKKIAAKLPNL 144

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 356530655 126 LKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILIMF 205
Cdd:cd04120    1 LQVIIIGSRGVGKTSLMERFTDDTFCEACKSTVGVDFKIKTVELRGKKIRLQIWDTAGQERFNSITSAYYRSAKGIILVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 206 DLTSRCTLNSVVGWYSKARKW-NQTAIPILIGTKFDdfvkLPPDVQWTiVTQARAYARAMKATLFF-SSASHNINVNKIF 283
Cdd:cd04120   81 DITKKETFDDLPKWMKMIDKYaSEDAELLLVGNKLD----CETDREIT-RQQGEKFAQQITGMRFCeASAKDNFNVDEIF 155

                        170
                 ....*....|....*...
gi 356530655 284 -KFIMAKLFNLPWKVERN 300
Cdd:cd04120  156 lKLVDDILKKMPLDILRN 173

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 356530655 125 NLKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLmdKTLF-VQGARISFSIWDVAGDPGSICQIPMACKDSVAILI 203
Cdd:cd04131    1 RCKIVLVGDSQCGKTALLQVFAKDSFPENYVPTVFENY--TASFeVDKQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 204 MFDLTSRCTLNSVV-GWYSKARKWNQTAIPILIGTKFD------DFVKLPPDVQWTIVT-QARAYARAMKATLFF--SSA 273
Cdd:cd04131   79 CFDISRPETLDSVLkKWKGEVREFCPNTPVLLVGCKSDlrtdlsTLTELSNKRQIPVSHeQGRNLAKQIGAAAYVecSAK 158

                        170
                 ....*....|....*..
gi 356530655 274 SHNINVNKIFKfiMAKL 290
Cdd:cd04131  159 TSENSVRDVFE--MATL 173

Rnd3/RhoE/Rho8 GTPases; Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd2/Rho7. Rnd3/RhoE is known to bind the serine-threonine kinase ROCK I. Unphosphorylated Rnd3/RhoE associates primarily with membranes, but ROCK I-phosphorylated Rnd3/RhoE localizes in the cytosol. Phosphorylation of Rnd3/RhoE correlates with its activity in disrupting RhoA-induced stress fibers and inhibiting Ras-induced fibroblast transformation. In cells that lack stress fibers, such as macrophages and monocytes, Rnd3/RhoE induces a redistribution of actin, causing morphological changes in the cell. In addition, Rnd3/RhoE has been shown to inhibit cell cycle progression in G1 phase at a point upstream of the pRb family pocket protein checkpoint. Rnd3/RhoE has also been shown to inhibit Ras- and Raf-induced fibroblast transformation. In mammary epithelial tumor cells, Rnd3/RhoE regulates the assembly of the apical junction complex and tight junction formation. Rnd3/RhoE is underexpressed in prostate cancer cells both in vitro and in vivo; re-expression of Rnd3/RhoE suppresses cell cycle progression and increases apoptosis, suggesting it may play a role in tumor suppression. 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 356530655 124 VNLKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMdKTLFVQGARISFSIWDVAGDPGSICQIPMACKDSVAILI 203
Cdd:cd04172    4 VKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYT-ASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 204 MFDLTSRCTLNSVV-GWYSKARKWNQTAIPILIGTKFD------DFVKLPPDVQWTI-VTQARAYARAMKATLFFS-SAS 274
Cdd:cd04172   83 CFDISRPETLDSVLkKWKGEIQEFCPNTKMLLVGCKSDlrtdvsTLVELSNHRQTPVsYDQGANMAKQIGAATYIEcSAL 162

                        170
                 ....*....|
gi 356530655 275 HNIN-VNKIF 283
Cdd:cd04172  163 QSENsVRDIF 172

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 356530655 126 LKISLLGDCHIGKTSFVIKYVGD--EQEKRS-----LQMKGLNLMDKTLfvqgarISFSIWDVAGDPGSICQIPMACKDS 198
Cdd:cd04107    1 FKVLVIGDLGVGKTSIIKRYVHGvfSQHYKAtigvdFALKVIEWDPNTV------VRLQLWDIAGQERFGGMTRVYYKGA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 199 VAILIMFDLTSRCTLNSVVGWY----SKARKWNQTAIP-ILIGTKFDdfvkLPPDVQWTIVTQARAYARAMKATLFF-SS 272
Cdd:cd04107   75 VGAIIVFDVTRPSTFEAVLKWKadldSKVTLPNGEPIPaLLLANKCD----LKKERLAKDPEQMDQFCKENGFIGWFeTS 150

                        170
                 ....*....|....*....
gi 356530655 273 ASHNINVNKIFKFIMAKLF 291
Cdd:cd04107  151 AKENINIEEAMRFLVKNIL 169

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 356530655 126 LKISLLGDCHIGKTSFVIKYVGDEQEKRSLQMKGLNLMDKTLFVQGA-RISFSIWDVAGDpgsicQI--PMACK---DSV 199
Cdd:cd04109    1 IKIVVLGDGASGKTSLIRRFAQEGFGKSYKQTIGLDFFSRRITLPGSlNVTLQVWDIGGQ-----QIggKMLDKyiyGAQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356530655 200 AILIMFDLTSRCTLNSVVGWYSKARKWNQTAIP----ILIGTKFDdfvkLPPDVQWTIVTQARaYARAMKATLFFSSASH 275
Cdd:cd04109   76 AVCLVYDITNSQSFENLEDWLSVVKKVNEESETkpkmVLVGNKTD----LEHNRQVTAEKHAR-FAQENDMESIFVSAKT 150

                        170
                 ....*....|....*...
gi 356530655 276 NINVNKIFKFIMAKLFNL 293
Cdd:cd04109  151 GDRVFLCFQRIAAELLGV 168