ADP-ribosylation factor family; Pfam combines a number of different Prosite families together

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315   80 VLVLGLDGAGKSTFLRVLSGKPpLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLKLGE-IVTTIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADRD 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 767938315  160 RLPWARQELHKLLDKDP--DLPVVVVANKQ 187
Cdd:pfam00025  82 RIEEAKEELHALLNEEElaDAPLLILANKQ 111

ADP-ribosylation factor; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFLRVLS-GKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:PTZ00133  20 ILMVGLDAAGKTTILYKLKlGE--VVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDSNDR 97

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767938315 159 LRLPWARQELHKLLDKDP--DLPVVVVANKQ 187
Cdd:PTZ00133  98 ERIGDAREELERMLSEDElrDAVLLVFANKQ 128

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 767938315   80 VLVLGLDGAGKSTFLRVLSGKPPLEGHI-PTWGFN----SVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVD 154
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYyPGTTRNyvttVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767938315  155 ------SADRLRLPWaRQELHKLLDKdpDLPVVVVANKQ 187
Cdd:TIGR00231  84 ivilvlDVEEILEKQ-TKEIIHHADS--GVPIILVGNKI 119

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFLRVLSGKPPlEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:cd00878    2 ILMLGLDGAGKTTILYKLKLGEV-VTTIPTIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSDRE 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 767938315 160 RLPWARQELHKLLDKDP--DLPVVVVANKQ 187
Cdd:cd00878   81 RIEEAKNELHKLLNEEElkGAPLLILANKQ 110

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  77 QREVLVLGLDGAGKSTFLRVLSGKPplEGHI-PTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDS 155
Cdd:cd04155   15 EVRILLLGLDNAGKTTILKQLASED--ISHItPTQGFNIKNVQADGFKLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDS 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767938315 156 ADRLRLPWARQELHKLLDKDP--DLPVVVVANKQ 187
Cdd:cd04155   93 ADRKRFEEAGQELVELLEEEKlaGVPVLVFANKQ 126

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFLRVLSGKPpLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:cd04154   17 ILMLGLDNAGKTTILKKFNGED-ISTISPTLGFNIKTLEYNGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVVDSSDRA 95

                         90       100       110
                 ....*....|....*....|....*....|
gi 767938315 160 RLPWARQELHKLL--DKDPDLPVVVVANKQ 187
Cdd:cd04154   96 RLEDCKRELQKLLveERLAGATLLIFANKQ 125

ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFL-RVLSGKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04151    2 ILILGLDGAGKTTILyRLQVGE--VVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767938315 159 LRLPWARQELHKLLDKDP--DLPVVVVANKQ--TGSHSAAQ 195
Cdd:cd04151   80 DRLGISKSELHAMLEEEElkDAVLLVFANKQdmPGALSEAE 120

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  78 REVLVLGLDGAGKSTFLRVL-SGKppLEGHIPTWGFNS-------VRLPTKDfevdlleIGGSQNLRFYWKEFVSEVDVL 149
Cdd:cd00879   20 AKIVFLGLDNAGKTTLLHMLkDDR--LAQHVPTLHPTSeeltignVKFTTFD-------LGGHEQARRVWKDYFPEVDGI 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767938315 150 VFVVDSADRLRLPWARQELHKLLDKD--PDLPVVVVANK--QTGSHSAAQ 195
Cdd:cd00879   91 VFLVDAADPERFQESKEELDSLLNDEelANVPILILGNKidKPGAVSEEE 140

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315    80 VLVLGLDGAGKSTFLRVLSGKPPLEGhIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:smart00177  16 ILMVGLDAAGKTTILYKLKLGESVTT-IPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSNDRD 94

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767938315   160 RLPWARQELHKLLDKDP--DLPVVVVANKQTGSHSAAQAGVQRR--DHSTR-RPTY 210
Cdd:smart00177  95 RIDEAREELHRMLNEDElrDAVILVFANKQDLPDAMKAAEITEKlgLHSIRdRNWY 150

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFLRVLSgkppLEGH---IPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSA 156
Cdd:cd04149   12 ILMLGLDAAGKTTILYKLK----LGQSvttIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSA 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767938315 157 DRLRLPWARQELHKLL-DKD-PDLPVVVVANKQ 187
Cdd:cd04149   88 DRDRIDEARQELHRIInDREmRDALLLVFANKQ 120

Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFLRVLSGKPPLEGhIPTWGFNSVRL-----PTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVD 154
Cdd:cd04152    6 IVMLGLDSAGKTTVLYRLKFNEFVNT-VPTKGFNTEKIkvslgNAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767938315 155 SADRLRLPWARQELHKL--LDKDPDLPVVVVANKQ 187
Cdd:cd04152   85 SVDVERMEEAKTELHKItkFSENQGVPVLVLANKQ 119

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFLRVLS-GKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04150    3 ILMVGLDAAGKTTILYKLKlGE--IVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767938315 159 LRLPWARQELHKLLDKDP--DLPVVVVANKQ 187
Cdd:cd04150   81 ERIGEAREELQRMLNEDElrDAVLLVFANKQ 111

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315    79 EVLVLGLDGAGKSTFLRVLSGKPpLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:smart00178  19 KILFLGLDNAGKTTLLHMLKNDR-LAQHQPTQHPTSEELAIGNIKFTTFDLGGHQQARRLWKDYFPEVNGIVYLVDAYDK 97

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767938315   159 LRLPWARQELHKLLDKD--PDLPVVVVANKQTGSHSAAQA 196
Cdd:smart00178  98 ERFAESKRELDALLSDEelATVPFLILGNKIDAPYAASED 137

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 767938315  81 LVLGLDGAGKSTFLRVLSGKPPLEG---HIPTWGFNSVRLPTKDFEVDL-------LEIGGSQNLRFYWKEFVSEVDVLV 150
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVsdvPGTTRDPDVYVKELDKGKVKLvlvdtpgLDEFGGLGREELARLLLRGADLIL 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767938315 151 FVVDSADRLRLPWARQELHKLLDKDpDLPVVVVANKQ 187
Cdd:cd00882   81 LVVDSTDRESEEDAKLLILRRLRKE-GIPIILVGNKI 116

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315   79 EVLVLGLDGAGKSTFLRVLSGKPPLEGHIP--TWGFNSVRLPTKDFEVDLLEIGGS-QNLRFYW---KEFVS--EVDVLV 150
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPgtTRDPNEGRLELKGKQIILVDTPGLiEGASEGEglgRAFLAiiEADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767938315  151 FVVDSADRLRLpwARQELHKLLDKDpDLPVVVVANK 186
Cdd:pfam01926  81 FVVDSEEGITP--LDEELLELLREN-KKPIILVLNK 113

GTPase SAR1 family domain [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKSTFLRVLSGKP-PLEGHIPTWGFN----SVRLPTKDFEVDLLEIGGS---QNLRFYWKEFVSEVDVLVF 151
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIfSLEKYLSTNGVTidkkELKLDGLDVDLVIWDTPGQdefRETRQFYARQLTGASLYLF 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767938315 152 VVDSADRLRLPWARQELHKLLDKDPDLPVVVVANK 186
Cdd:COG1100   86 VVDGTREETLQSLYELLESLRRLGKKSPIILVLNK 120

Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  77 QREVL---VLGLDGAGKSTFLRVLSGKPP-LEGHIPTWG----FNSVRLPTKD-----FEVDLLEIGGSQNlrfywKEFV 143
Cdd:cd01892    1 QRNVFlcfVLGAKGSGKSALLQAFLGRSFsQNAYSPTIKpryaVNTVEVPGQEkylilREVGEDEEAILLN-----DAEL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767938315 144 SEVDVLVFVVDSADrlrlP--WAR-QELHKLLDKDPDLPVVVVANK 186
Cdd:cd01892   76 AACDVACLVYDSSD----PnsFSYcAEVYKKYFMLGEIPCLFVAAK 117

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.

                         10        20
                 ....*....|....*....|....*....
gi 767938315  80 VLVLGLDGAGKSTFLRVLSG-KPPLEGHI 107
Cdd:cd03225   30 VLIVGPNGSGKSTLLRLLNGlLGPTSGEV 58

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767938315  80 VLVLGLDGAGKST-FLRVLSGKPP-----LEGHIPTWGFNSVrlptKDFEVDLLEIGGSQNLRF-YWKEFVSEVDVLVFV 152
Cdd:cd04105    3 VLLLGPSDSGKTAlFTKLTTGKVRstvtsIEPNVASFYSNSS----KGKKLTLVDVPGHEKLRDkLLEYLKASLKAIVFV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767938315 153 VDSADRLRLpwARQE---LHKLL----DKDPDLPVVVVANKQ 187
Cdd:cd04105   79 VDSATFQKN--IRDVaefLYDILtdleKIKNKIPILIACNKQ 118

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767938315  82 VLGLDGAGKSTFLRVLSG-KPPLEGHIPTWGfnsvRLPTkdfevdLLEIG--------GSQNLRFY 138
Cdd:COG1134   57 IIGRNGAGKSTLLKLIAGiLEPTSGRVEVNG----RVSA------LLELGagfhpeltGRENIYLN 112

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                         10        20
                 ....*....|....*....|....*....
gi 767938315  80 VLVLGLDGAGKSTFLRVLSG-KPPLEGHI 107
Cdd:cd00267   28 VALVGPNGSGKSTLLRAIAGlLKPTSGEI 56

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.

                         10        20
                 ....*....|....*....|....*..
gi 767938315  82 VLGLDGAGKSTFLRVLSG-KPPLEGHI 107
Cdd:cd03220   53 LIGRNGAGKSTLLRLLAGiYPPDSGTV 79

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 767938315  80 VLVLGLDGAGKSTFLRVLSGKPP----LEGHI 107
Cdd:cd03233   36 VLVLGRPGSGCSTLLKALANRTEgnvsVEGDI 67