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 62955735   4 VKILLIGPSECGKTALAN-FLSDTTESigaDYSPTQGVrilEFESHNLHNGNKssSCDVELWDCAGDFKFESCWPALMKD 82
Cdd:cd00154   1 FKIVLIGDSGVGKTSLLLrFVDNKFSE---NYKSTIGV---DFKSKTIEVDGK--KVKLQIWDTAGQERFRSITSSYYRG 72

                        90       100
                ....*....|....*....|....*.
gi 62955735  83 SNGVAVVFnpDVPSH--LKEIETWYS 106
Cdd:cd00154  73 AHGAILVY--DVTNResFENLDKWLN 96

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955735   4 VKILLIGPSECGKTALAN-FLSDTTESigaDYSPTQGVrilEFESHNLHNGNKssSCDVELWDCAGDFKFESCWPALMKD 82
Cdd:cd00154   1 FKIVLIGDSGVGKTSLLLrFVDNKFSE---NYKSTIGV---DFKSKTIEVDGK--KVKLQIWDTAGQERFRSITSSYYRG 72

                        90       100
                ....*....|....*....|....*.
gi 62955735  83 SNGVAVVFnpDVPSH--LKEIETWYS 106
Cdd:cd00154  73 AHGAILVY--DVTNResFENLDKWLN 96

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 62955735     4 VKILLIGPSECGKTALANFLSDTTESIGADYsPTQGVRILEfESHNLhngnKSSSCDVELWDCAGDFKFESCWPALMKDS 83
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYY-PGTTRNYVT-TVIEE----DGKTYKFNLLDTAGQEDYDAIRRLYYPQV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 62955735    84 NGVAVVFNPDVPshlkeietwysaFISSQGLLEGQCLLIAHHKPGS 129
Cdd:TIGR00231  76 ERSLRVFDIVIL------------VLDVEEILEKQTKEIIHHADSG 109

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955735      4 VKILLIGPSECGKTALAN-FLSDTTESigaDYSPTQGVrilEFESHNLHNGNKssSCDVELWDCAGDFKFESCWPALMKD 82
Cdd:smart00175   1 FKIILIGDSGVGKSSLLSrFTDGKFSE---QYKSTIGV---DFKTKTIEVDGK--RVKLQIWDTAGQERFRSITSSYYRG 72

                           90       100
                   ....*....|....*....|....*...
gi 62955735     83 SNGVAVVF---NPD----VPSHLKEIET 103
Cdd:smart00175  73 AVGALLVYditNREsfenLENWLKELRE 100

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955735   4 VKILLIGPSECGKTALAN-FLSDTTESigaDYSPTQGVrilEFESHNLHNGNKssSCDVELWDCAGDFKFESCWPALMKD 82
Cdd:cd00154   1 FKIVLIGDSGVGKTSLLLrFVDNKFSE---NYKSTIGV---DFKSKTIEVDGK--KVKLQIWDTAGQERFRSITSSYYRG 72

                        90       100
                ....*....|....*....|....*.
gi 62955735  83 SNGVAVVFnpDVPSH--LKEIETWYS 106
Cdd:cd00154  73 AHGAILVY--DVTNResFENLDKWLN 96

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 62955735     5 KILLIGPSECGKTALAN-FLSDTTEsigADYSPTQGVrilEFESHN-LHNGNKSSSCDVELWDCAGDFKFESCWPALMKD 82
Cdd:pfam08477   1 KVVLLGDSGVGKTSLLKrFVDDTFD---PKYKSTIGV---DFKTKTvLENDDNGKKIKLNIWDTAGQERFRSLHPFYYRG 74

                          90       100
                  ....*....|....*....|...
gi 62955735    83 SNGVAVVFNPDVpshLKEIETWY 105
Cdd:pfam08477  75 AAAALLVYDSRT---FSNLKYWL 94

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 62955735   3 KVKILLIGPSECGKTALANFLSdtTESIGADYSPTQgvrileFESHNLHNGNKSSSCDVELWDCAGDFKFESCWPALMKD 82
Cdd:cd04172   5 KCKIVVVGDSQCGKTALLHVFA--KDCFPENYVPTV------FENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPD 76

                        90
                ....*....|....*....
gi 62955735  83 SNGVAVVFNPDVPSHLKEI 101
Cdd:cd04172  77 SDAVLICFDISRPETLDSV 95

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 62955735     4 VKILLIGPSECGKTALANFLSDTTESIGADYsPTQGVRILEfESHNLhngnKSSSCDVELWDCAGDFKFESCWPALMKDS 83
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYY-PGTTRNYVT-TVIEE----DGKTYKFNLLDTAGQEDYDAIRRLYYPQV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 62955735    84 NGVAVVFNPDVPshlkeietwysaFISSQGLLEGQCLLIAHHKPGS 129
Cdd:TIGR00231  76 ERSLRVFDIVIL------------VLDVEEILEKQTKEIIHHADSG 109

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 62955735   4 VKILLIGPSECGKTAL-ANFLSDTTESigaDYSPTQGVRILEfESHNLHNGNKSSScdveLWDCAGDFKFESCWPALMKD 82
Cdd:cd04128   1 LKIGLLGDAQIGKTSLmVKYVEGEFDE---EYIQTLGVNFME-KTISIRGTEITFS----IWDLGGQREFINMLPLVCKD 72

                        90       100
                ....*....|....*....|....*.
gi 62955735  83 SngVAVVFNPDV--PSHLKEIETWYS 106
Cdd:cd04128  73 A--VAILFMFDLtrKSTLNSIKEWYR 96

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 62955735   3 KVKILLIGPSECGKTALANFLSdtTESIGADYSPTQgvrileFEshnlhngNKSSSCDVE-------LWDCAGDFKFESC 75
Cdd:cd04131   1 RCKIVLVGDSQCGKTALLQVFA--KDSFPENYVPTV------FE-------NYTASFEVDkqrielsLWDTSGSPYYDNV 65

                        90       100       110
                ....*....|....*....|....*....|
gi 62955735  76 WPALMKDSNGVAVVFNPDVPSHLKEI-ETW 104
Cdd:cd04131  66 RPLSYPDSDAVLICFDISRPETLDSVlKKW 95

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 62955735   7 LLIGPSECGKTALANFLSDTTESI-GADYSPTQGVRILEFEshnlhngNKSSSCDVELWDCAG-----DFKFESCWPALM 80
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEvSDVPGTTRDPDVYVKE-------LDKGKVKLVLVDTPGldefgGLGREELARLLL 73

                        90       100       110
                ....*....|....*....|....*....|...
gi 62955735  81 KDSNGVAVVFNPDVPSHLKEIETWYSAFISSQG 113
Cdd:cd00882  74 RGADLILLVVDSTDRESEEDAKLLILRRLRKEG 106

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 62955735   4 VKILLIGPSECGKTALAN-FLSDttesigaDYSPTQ-GVRILEFESHNLHNGNKSssCDVELWDCAGDFKFESCWPALMK 81
Cdd:cd04124   1 VKIILLGDSAVGKSKLVErFLMD-------GYEPQQlSTYALTLYKHNAKFEGKT--ILVDFWDTAGQERFQTMHASYYH 71

                        90       100
                ....*....|....*....|....
gi 62955735  82 DSNGVAVVFNPDVPSHLKEIETWY 105
Cdd:cd04124  72 KAHACILVFDVTRKITYKNLSKWY 95

Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. 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 62955735   3 KVKILLIGPSECGKTALANFLSdtTESIGADYSPTQgvrileFESHNLHNGNKSSSCDVELWDCAGDFKFESCWPALMKD 82
Cdd:cd04174  13 RCKLVLVGDVQCGKTAMLQVLA--KDCYPETYVPTV------FENYTACLETEEQRVELSLWDTSGSPYYDNVRPLCYSD 84

                        90       100
                ....*....|....*....|....*
gi 62955735  83 SNGVAVVFNPDVPSHLKE-IETWYS 106
Cdd:cd04174  85 SDAVLLCFDISRPEIFDSaLKKWRA 109

Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition particle receptor (SRP) is a transmembrane GTPase which anchors the alpha subunit to the endoplasmic reticulum membrane.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955735     6 ILLIGPSECGKTALANFLsdTTESigadYSPTQGVRILEF-ESHNLHNGNKssscdVELWDCAGDFKFESCWPALMKDSN 84
Cdd:pfam09439   6 VIIAGLCDSGKTSLFTLL--TTDS----VRPTVTSQEPSAaYRYMLNKGNS-----FTLIDFPGHVKLRYKLLETLKDSS 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 62955735    85 GV-AVVFNPDVPSHLKEI----ETWYSAFISSQGLLEGQCLLIAHHK 126
Cdd:pfam09439  75 SLkGIVFVVDSTIFPKEVtdtaEFLYDILSITELLKNGIDILIACNK 121

Rab GTPase family 21 (Rab21); The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate 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 62955735   4 VKILLIGPSECGKTALA-----NFLSDTTES-IGADYsptqgvrileFESHNLHNGNKsssCDVELWDCAGDFKFESCWP 77
Cdd:cd04123   1 FKVVLLGEGRVGKTSLVlryveNKFNEKHEStTQASF----------FQKTVNIGGKR---IDLAIWDTAGQERYHALGP 67

                        90       100
                ....*....|....*....|....*..
gi 62955735  78 ALMKDSNGVAVVFNPDVPSHLKEIETW 104
Cdd:cd04123  68 IYYRDADGAILVYDITDADSFQKVKKW 94

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 62955735   4 VKILLIGPSECGKTAL------ANFLSDTTESIGADYsptqgvriLEfESHNLhngnKSSSCDVE--LWDCAGDFKFESC 75
Cdd:cd04106   1 IKVIVVGNGNVGKSSMiqrfvkGIFTKDYKKTIGVDF--------LE-KQIFL----RQSDEDVRlmLWDTAGQEEFDAI 67

                        90       100
                ....*....|....*....|....*....
gi 62955735  76 WPALMKDSNGVAVVFNPDVPSHLKEIETW 104
Cdd:cd04106  68 TKAYYRGAQACILVFSTTDRESFEAIESW 96