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Conserved domains on  [gi|1859470408|ref|NP_001035114|]
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ADP-ribosylation factor-like protein 16 isoform 1 [Homo sapiens]

Protein Classification

Arf family protein( domain architecture ID 10096325)

Arf (ADP-ribosylation factor) family protein similar to Homo sapiens ARF-like protein 16 isoform (Arl16), which inhibits retinoic acid-inducible gene I (RIG-I) by binding with its C-terminal domain in a GTP-dependent manner

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924
SCOP:  4004043

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 1-166 9.30e-48

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.


:

Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 152.35  E-value: 9.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   1 MCLLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQ-RKITIRELGGCMG--PIWSSYYGNCRSL 77
Cdd:cd00878     1 RILMLGLDGAGKTTILYKLK----------LGEVVTTIPTIGFNVETVEYKnVKFTVWDVGGQDKirPLWKHYYENTDGL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  78 LFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTG 157
Cdd:cd00878    71 IFVVDSSDRERIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLESI---KGRRWHIQPCSAVTGDG 147


                  ....*....
gi 1859470408 158 LAGVLAWLQ 166
Cdd:cd00878   148 LDEGLDWLI 156
 
Name Accession Description Interval E-value
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 1-166 9.30e-48

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.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 152.35  E-value: 9.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   1 MCLLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQ-RKITIRELGGCMG--PIWSSYYGNCRSL 77
Cdd:cd00878     1 RILMLGLDGAGKTTILYKLK----------LGEVVTTIPTIGFNVETVEYKnVKFTVWDVGGQDKirPLWKHYYENTDGL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  78 LFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTG 157
Cdd:cd00878    71 IFVVDSSDRERIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLESI---KGRRWHIQPCSAVTGDG 147


                  ....*....
gi 1859470408 158 LAGVLAWLQ 166
Cdd:cd00878   148 LDEGLDWLI 156
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 2-165 1.34e-22

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 88.05  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   2 CLLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDI-VAQRKITIRELGG--CMGPIWSSYYGNCRSLL 78
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLK----------LGEIVTTIPTIGFNVETVtYKNVKFTVWDVGGqeSLRPLWRNYFPNTDAVI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  79 FVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGL 158
Cdd:pfam00025  73 FVVDSADRDRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHEL---KDRPWEIQGCSAVTGEGL 149


                  ....*..
gi 1859470408 159 AGVLAWL 165
Cdd:pfam00025 150 DEGLDWL 156
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 3-168 4.07e-17

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 74.50  E-value: 4.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQR-KITIRELGG--CMGPIWSSYYGNCRSLLF 79
Cdd:PTZ00133   21 LMVGLDAAGKTTILYKLK----------LGEVVTTIPTIGFNVETVEYKNlKFTMWDVGGqdKLRPLWRHYYQNTNGLIF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGLA 159
Cdd:PTZ00133   91 VVDSNDRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGLHSV---RQRNWYIQGCCATTAQGLY 167


                  ....*....
gi 1859470408 160 GVLAWLQAT 168
Cdd:PTZ00133  168 EGLDWLSAN 176
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 3-170 1.60e-16

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).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 72.65  E-value: 1.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408    3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQR-KITIRELGGC--MGPIWSSYYGNCRSLLF 79
Cdd:smart00177  17 LMVGLDAAGKTTILYKLK----------LGESVTTIPTIGFNVETVTYKNiSFTVWDVGGQdkIRPLWRHYYTNTQGLIF 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGLA 159
Cdd:smart00177  87 VVDSNDRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSI---RDRNWYIQPTCATSGDGLY 163

                          170
                   ....*....|.
gi 1859470408  160 GVLAWLQATHR 170
Cdd:smart00177 164 EGLTWLSNNLK 174
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
3-158 9.10e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.51  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRL--QEVSSRDGKGdlgeppptrpTVGTnltdIVAQRKITIREL---------GGCM-----GPI 66
Cdd:COG1100     7 VVVGTGGVGKTSLVNRLvgDIFSLEKYLS----------TNGV----TIDKKELKLDGLdvdlviwdtPGQDefretRQF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  67 WSSYYGNCRSLLFVMDASDPTQLsasCVQLLGLLSAEQLAEAS-VLILFNKIDLpcyMSTEEMKSLIRLPDIIAcAKQNI 145
Cdd:COG1100    73 YARQLTGASLYLFVVDGTREETL---QSLYELLESLRRLGKKSpIILVLNKIDL---YDEEEIEDEERLKEALS-EDNIV 145

                         170
                  ....*....|...
gi 1859470408 146 TTAEISAREGTGL 158
Cdd:COG1100   146 EVVATSAKTGEGV 158
 
Name Accession Description Interval E-value
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 1-166 9.30e-48

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.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 152.35  E-value: 9.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   1 MCLLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQ-RKITIRELGGCMG--PIWSSYYGNCRSL 77
Cdd:cd00878     1 RILMLGLDGAGKTTILYKLK----------LGEVVTTIPTIGFNVETVEYKnVKFTVWDVGGQDKirPLWKHYYENTDGL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  78 LFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTG 157
Cdd:cd00878    71 IFVVDSSDRERIEEAKNELHKLLNEEELKGAPLLILANKQDLPGALTESELIELLGLESI---KGRRWHIQPCSAVTGDG 147


                  ....*....
gi 1859470408 158 LAGVLAWLQ 166
Cdd:cd00878   148 LDEGLDWLI 156
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 2-165 1.34e-22

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 88.05  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   2 CLLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDI-VAQRKITIRELGG--CMGPIWSSYYGNCRSLL 78
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLK----------LGEIVTTIPTIGFNVETVtYKNVKFTVWDVGGqeSLRPLWRNYFPNTDAVI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  79 FVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGL 158
Cdd:pfam00025  73 FVVDSADRDRIEEAKEELHALLNEEELADAPLLILANKQDLPGAMSEAEIRELLGLHEL---KDRPWEIQGCSAVTGEGL 149


                  ....*..
gi 1859470408 159 AGVLAWL 165
Cdd:pfam00025 150 DEGLDWL 156
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
 3-165 8.43e-22

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.


Pssm-ID: 206718 [Multi-domain]  Cd Length: 158  Bit Score: 85.92  E-value: 8.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQR-KITIRELGGCMG--PIWSSYYGNCRSLLF 79
Cdd:cd04151     3 LILGLDGAGKTTILYRLQ----------VGEVVTTIPTIGFNVETVTYKNlKFQVWDLGGQTSirPYWRCYYSNTDAIIY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGLA 159
Cdd:cd04151    73 VVDSTDRDRLGISKSELHAMLEEEELKDAVLLVFANKQDMPGALSEAEVAEKLGLSEL---KDRTWQIFKTSATKGEGLD 149


                  ....*.
gi 1859470408 160 GVLAWL 165
Cdd:cd04151   150 EGMDWL 155
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
 3-165 4.42e-21

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.


Pssm-ID: 206725 [Multi-domain]  Cd Length: 168  Bit Score: 84.32  E-value: 4.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQEVSSRDGKGdlgePPPTR--PTVGTNLTDI-VAQRKITIRELGGCMG--PIWSSYYGNCRSL 77
Cdd:cd04160     3 LILGLDNAGKTTFLEQTKTKFSKNYKG----LNPSKitPTVGLNIGTIeVGKARLMFWDLGGQEElrSLWDKYYAESHGV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  78 LFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLpDIIACAKQNITTAEISAREGTG 157
Cdd:cd04160    79 IYVIDSTDRERFNESKSAFEKVINNEALEGVPLLVLANKQDLPDALSVAEIKEVFDD-CIALIGRRDCLVQPVSALEGEG 157


                  ....*...
gi 1859470408 158 LAGVLAWL 165
Cdd:cd04160   158 VEEGIEWL 165
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 3-165 1.99e-19

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.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 80.52  E-value: 1.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRL--QEVSsrdgkgdlgeppPTRPTVGTNLTDIVAQ-RKITIRELGG--CMGPIWSSYYGNCRSL 77
Cdd:cd04155    19 LLLGLDNAGKTTILKQLasEDIS------------HITPTQGFNIKNVQADgFKLNVWDIGGqrKIRPYWRNYFENTDVL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  78 LFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDII-------ACakqnittaei 150
Cdd:cd04155    87 IYVIDSADRKRFEEAGQELVELLEEEKLAGVPVLVFANKQDLLTAAPAEEVAEALNLHDIRdrswhiqAC---------- 156

                         170
                  ....*....|....*
gi 1859470408 151 SAREGTGLAGVLAWL 165
Cdd:cd04155   157 SAKTGEGLQEGMNWV 171
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
 3-165 2.95e-18

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 77.39  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQR-KITIRELGG--CMGPIWSSYYGNCRSLLF 79
Cdd:cd04153    19 IIVGLDNAGKTTILYQFL----------LGEVVHTSPTIGSNVEEIVYKNiRFLMWDIGGqeSLRSSWNTYYTNTDAVIL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPD-------IIACakqnittaeiSA 152
Cdd:cd04153    89 VIDSTDRERLPLTKEELYKMLAHEDLRKAVLLVLANKQDLKGAMTPAEISESLGLTSirdhtwhIQGC----------CA 158

                         170
                  ....*....|...
gi 1859470408 153 REGTGLAGVLAWL 165
Cdd:cd04153   159 LTGEGLPEGLDWI 171
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 3-159 3.06e-17

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 74.37  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQRKI--TIRELGG--CMGPIWSSYYGNCRSLL 78
Cdd:cd04156     3 LLLGLDSAGKSTLLYKLK----------HAELVTTIPTVGFNVEMLQLEKHLslTVWDVGGqeKMRTVWKCYLENTDGLV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  79 FVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiaCAKQNITTAEISAREGTGL 158
Cdd:cd04156    73 YVVDSSDEARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEITRRFKLKKY--CSDRDWYVQPCSAVTGEGL 150


                  .
gi 1859470408 159 A 159
Cdd:cd04156   151 A 151
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 3-168 4.07e-17

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 74.50  E-value: 4.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQR-KITIRELGG--CMGPIWSSYYGNCRSLLF 79
Cdd:PTZ00133   21 LMVGLDAAGKTTILYKLK----------LGEVVTTIPTIGFNVETVEYKNlKFTMWDVGGqdKLRPLWRHYYQNTNGLIF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGLA 159
Cdd:PTZ00133   91 VVDSNDRERIGDAREELERMLSEDELRDAVLLVFANKQDLPNAMSTTEVTEKLGLHSV---RQRNWYIQGCCATTAQGLY 167


                  ....*....
gi 1859470408 160 GVLAWLQAT 168
Cdd:PTZ00133  168 EGLDWLSAN 176
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 4-165 6.05e-17

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 73.51  E-value: 6.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   4 LLGATGVGKTLLVKRLqevssrdgkGDLGEPPPTRPTVGTNLTDIVAQR-KITIRELGGC--MGPIWSSYYGNCRSLLFV 80
Cdd:cd04159     4 LVGLQNSGKTTLVNVI---------ASGQFSEDTIPTVGFNMRKVTKGNvTIKVWDLGGQprFRSMWERYCRGVNAIVYV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  81 MDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGLAG 160
Cdd:cd04159    75 VDAADREKLEVAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALSVDELIEQMNLKSI---TDREVSCYSISAKEKTNIDI 151


                  ....*
gi 1859470408 161 VLAWL 165
Cdd:cd04159   152 VLDWL 156
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 3-170 1.60e-16

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).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 72.65  E-value: 1.60e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408    3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQR-KITIRELGGC--MGPIWSSYYGNCRSLLF 79
Cdd:smart00177  17 LMVGLDAAGKTTILYKLK----------LGESVTTIPTIGFNVETVTYKNiSFTVWDVGGQdkIRPLWRHYYTNTQGLIF 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGLA 159
Cdd:smart00177  87 VVDSNDRDRIDEAREELHRMLNEDELRDAVILVFANKQDLPDAMKAAEITEKLGLHSI---RDRNWYIQPTCATSGDGLY 163

                          170
                   ....*....|.
gi 1859470408  160 GVLAWLQATHR 170
Cdd:smart00177 164 EGLTWLSNNLK 174
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
 3-168 3.57e-16

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 71.92  E-value: 3.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLtDIVAQRKI--TIRELGGC--MGPIWSSYYGNCRSLL 78
Cdd:PLN00223   21 LMVGLDAAGKTTILYKLK----------LGEIVTTIPTIGFNV-ETVEYKNIsfTVWDVGGQdkIRPLWRHYFQNTQGLI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  79 FVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiacAKQNITTAEISAREGTGL 158
Cdd:PLN00223   90 FVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSL---RQRHWYIQSTCATSGEGL 166

                         170
                  ....*....|
gi 1859470408 159 AGVLAWLQAT 168
Cdd:PLN00223  167 YEGLDWLSNN 176
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
 3-168 7.60e-16

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).


Pssm-ID: 206717 [Multi-domain]  Cd Length: 159  Bit Score: 70.51  E-value: 7.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLtDIVAQRKI--TIRELGG--CMGPIWSSYYGNCRSLL 78
Cdd:cd04150     4 LMVGLDAAGKTTILYKLK----------LGEIVTTIPTIGFNV-ETVEYKNIsfTVWDVGGqdKIRPLWRHYFQNTQGLI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  79 FVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDiiaCAKQNITTAEISAREGTGL 158
Cdd:cd04150    73 FVVDSNDRERIGEAREELQRMLNEDELRDAVLLVFANKQDLPNAMSAAEVTDKLGLHS---LRNRNWYIQATCATSGDGL 149

                         170
                  ....*....|
gi 1859470408 159 AGVLAWLQAT 168
Cdd:cd04150   150 YEGLDWLSNN 159
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
 3-165 3.12e-15

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.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 69.42  E-value: 3.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIVAQR-KITIRELGGC--MGPIWSSYYGNCRSLLF 79
Cdd:cd04149    13 LMLGLDAAGKTTILYKLK----------LGQSVTTIPTVGFNVETVTYKNvKFNVWDVGGQdkIRPLWRHYYTGTQGLIF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKS---LIRLPDIIACAKQNIttaeisAREGT 156
Cdd:cd04149    83 VVDSADRDRIDEARQELHRIINDREMRDALLLVFANKQDLPDAMKPHEIQEklgLTRIRDRNWYVQPSC------ATSGD 156


                  ....*....
gi 1859470408 157 GLAGVLAWL 165
Cdd:cd04149   157 GLYEGLTWL 165
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 3-135 1.47e-14

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.


Pssm-ID: 206645 [Multi-domain]  Cd Length: 191  Bit Score: 68.07  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQEvssrdgkGDLGEPPPT-RPTvGTNLTdiVAQRKITIRELGG--CMGPIWSSYYGNCRSLLF 79
Cdd:cd00879    23 VFLGLDNAGKTTLLHMLKD-------DRLAQHVPTlHPT-SEELT--IGNVKFTTFDLGGheQARRVWKDYFPEVDGIVF 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1859470408  80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLP 135
Cdd:cd00879    93 LVDAADPERFQESKEELDSLLNDEELANVPILILGNKIDKPGAVSEEELREALGLY 148
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
 5-165 2.63e-14

(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein 1) is an unusual member of the Arf family. In addition to the C-terminal Arf domain, ARD1 has an additional 46-kDa N-terminal domain that contains a RING finger domain, two predicted B-Boxes, and a coiled-coil protein interaction motif. This domain belongs to the TRIM (tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. Like most Arfs, the ARD1 Arf domain lacks detectable GTPase activity. However, unlike most Arfs, the full-length ARD1 protein has significant GTPase activity due to the GAP (GTPase-activating protein) activity exhibited by the 46-kDa N-terminal domain. The GAP domain of ARD1 is specific for its own Arf domain and does not bind other Arfs. The rate of GDP dissociation from the ARD1 Arf domain is slowed by the adjacent 15 amino acids, which act as a GDI (GDP-dissociation inhibitor) domain. ARD1 is ubiquitously expressed in cells and localizes to the Golgi and to the lysosomal membrane. Two Tyr-based motifs in the Arf domain are responsible for Golgi localization, while the GAP domain controls lysosomal localization.


Pssm-ID: 206723 [Multi-domain]  Cd Length: 169  Bit Score: 66.98  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   5 LGATGVGKTLLVKRLQEvssrdgkGDLGEPPPTrptVGTNLTDIVAQR-KITIRELGGC--MGPIWSSYYGNCRSLLFVM 81
Cdd:cd04158     5 LGLDGAGKTTILFKLKQ-------DEFMQPIPT---IGFNVETVEYKNlKFTIWDVGGKhkLRPLWKHYYLNTQAVVFVI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  82 DASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIiaCAKQNITTAEISAREGTGLAGV 161
Cdd:cd04158    75 DSSHRDRVSEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEMTELLSLHKL--CCGRSWYIQGCDARSGMGLYEG 152


                  ....
gi 1859470408 162 LAWL 165
Cdd:cd04158   153 LDWL 156
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 3-134 1.62e-12

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.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 62.26  E-value: 1.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408    3 LLLGATGVGKTLLVKRLqevssrdgKGD-LGEPPPTRPTVGTNLTdiVAQRKITIRELGGCMGP--IWSSYYGNCRSLLF 79
Cdd:smart00178  21 LFLGLDNAGKTTLLHML--------KNDrLAQHQPTQHPTSEELA--IGNIKFTTFDLGGHQQArrLWKDYFPEVNGIVY 90

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1859470408   80 VMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRL 134
Cdd:smart00178  91 LVDAYDKERFAESKRELDALLSDEELATVPFLILGNKIDAPYAASEDELRYALGL 145
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
 3-168 3.90e-11

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. 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.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 58.21  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdlgePPPTR-----PTVGTNLTDIVAQR-KITIRELGGCMG--PIWSSYYGNC 74
Cdd:cd04157     3 LVLGLDNSGKTTIINQLK-------------PSNAQsqnivPTVGFNVESFKKGNlSFTAFDMSGQGKyrGLWEHYYKNI 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  75 RSLLFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILF--NKIDLPCYMSTEEMKSLIRLpDIIACAKQNITTAeiSA 152
Cdd:cd04157    70 QGIIFVIDSSDRLRMVVAKDELELLLNHPDIKHRRIPILFyaNKMDLPDALTAVKITQLLCL-ENIKDKPWHIFAS--SA 146

                         170
                  ....*....|....*.
gi 1859470408 153 REGTGLAGVLAWLQAT 168
Cdd:cd04157   147 LTGEGLDEGVDWLQAQ 162
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
 11-120 2.02e-09

Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene.


Pssm-ID: 133361 [Multi-domain]  Cd Length: 167  Bit Score: 53.55  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  11 GKTLLVKRLQEVSSRDgkgdlgepppTRPTVGTNLTDIVAQR-KITIRELGGCMG--PIWSSYYGNCRSLLFVMDASDPT 87
Cdd:cd04161    11 GKTTLVSALQGEIPKK----------VAPTVGFTPTKLRLDKyEVCIFDLGGGANfrGIWVNYYAEAHGLVFVVDSSDDD 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1859470408  88 QLSASCVQLLGLLSAEQLAEASVLILFNKIDLP 120
Cdd:cd04161    81 RVQEVKEILRELLQHPRVSGKPILVLANKQDKK 113
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 3-165 3.15e-09

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.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 53.23  E-value: 3.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRL--QEVSSRDGkgdlgEPPPTRPTVGTNLTDIVAQRKITIRELGG-----CMGPIWSS--YYGN 73
Cdd:cd00882     1 VVVGRGGVGKSSLLNALlgGEVGEVSD-----VPGTTRDPDVYVKELDKGKVKLVLVDTPGldefgGLGREELArlLLRG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  74 CRSLLFVMDASDPTQLSASCVQLLGLLSAEQLAeasVLILFNKIDLPcymSTEEMKSLIRLpdIIACAKQNITTAEISAR 153
Cdd:cd00882    76 ADLILLVVDSTDRESEEDAKLLILRRLRKEGIP---IILVGNKIDLL---EEREVEELLRL--EELAKILGVPVFEVSAK 147

                         170
                  ....*....|..
gi 1859470408 154 EGTGLAGVLAWL 165
Cdd:cd00882   148 TGEGVDELFEKL 159
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 3-137 5.24e-08

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 49.75  E-value: 5.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQEVSSRDGkgdlgepppTRPTVGTNLTDIVAQR-KITIRELGGC--MGPIWSSYYGNCRSLLF 79
Cdd:cd04162     3 LVLGLDGAGKTSLLHSLSSERSLES---------VVPTTGFNSVAIPTQDaIMELLEIGGSqnLRKYWKRYLSGSQGLIF 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1859470408  80 VMDASDPTQLSASCVQLLGLLSAEqlAEASVLILFNKIDLPCYMSTEEMKSLIRLPDI 137
Cdd:cd04162    74 VVDSADSERLPLARQELHQLLQHP--PDLPLVVLANKQDLPAARSVQEIHKELELEPI 129
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
3-158 9.10e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.51  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRL--QEVSSRDGKGdlgeppptrpTVGTnltdIVAQRKITIREL---------GGCM-----GPI 66
Cdd:COG1100     7 VVVGTGGVGKTSLVNRLvgDIFSLEKYLS----------TNGV----TIDKKELKLDGLdvdlviwdtPGQDefretRQF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  67 WSSYYGNCRSLLFVMDASDPTQLsasCVQLLGLLSAEQLAEAS-VLILFNKIDLpcyMSTEEMKSLIRLPDIIAcAKQNI 145
Cdd:COG1100    73 YARQLTGASLYLFVVDGTREETL---QSLYELLESLRRLGKKSpIILVLNKIDL---YDEEEIEDEERLKEALS-EDNIV 145

                         170
                  ....*....|...
gi 1859470408 146 TTAEISAREGTGL 158
Cdd:COG1100   146 EVVATSAKTGEGV 158
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 3-157 3.16e-06

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.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 44.75  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQEvssrdgkgdlGE-PPPTRPTVGTNL---TDIVAQRKITIRelggcmgpIW----------- 67
Cdd:cd00154     4 VLIGDSGVGKTSLLLRFVD----------NKfSENYKSTIGVDFkskTIEVDGKKVKLQ--------IWdtagqerfrsi 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  68 -SSYYGNCRSLLFVMDASDPTQLSaSCVQLLGLLSAEQLAEASVLILFNKIDLPC--YMSTEEMKSLirlpdiiaCAKQN 144
Cdd:cd00154    66 tSSYYRGAHGAILVYDVTNRESFE-NLDKWLNELKEYAPPNIPIILVGNKSDLEDerQVSTEEAQQF--------AKENG 136

                         170
                  ....*....|...
gi 1859470408 145 ITTAEISAREGTG 157
Cdd:cd00154   137 LLFFETSAKTGEN 149
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
 3-158 9.38e-06

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.


Pssm-ID: 206719 [Multi-domain]  Cd Length: 183  Bit Score: 43.64  E-value: 9.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrdgkgdLGEPPPTRPTVGTNLTDIV----AQRKITIR--ELGGC--MGPIWSSYYGNC 74
Cdd:cd04152     7 VMLGLDSAGKTTVLYRLK----------FNEFVNTVPTKGFNTEKIKvslgNAKGVTFHfwDVGGQekLRPLWKSYTRCT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  75 RSLLFVMDASDPTQLSASCVQLLGLLSAEQLAEASVLILFNKIDLPCYMSTEEMKSLIRLPDIIACAKQNITTAeiSARE 154
Cdd:cd04152    77 DGIVFVVDSVDVERMEEAKTELHKITKFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSSTPWHVQPA--CAII 154


                  ....
gi 1859470408 155 GTGL 158
Cdd:cd04152   155 GEGL 158
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 4-158 2.10e-05

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 42.62  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   4 LLGATGVGKTLLVKRL--QEVSS--------RDGKGDLGEPPPTRP-----TVGtnLTDIVAQRKITIRElggcmgpIWS 68
Cdd:cd00880     2 IFGRPNVGKSSLLNALlgQNVGIvspipgttRDPVRKEWELLPLGPvvlidTPG--LDEEGGLGRERVEE-------ARQ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  69 SYYGnCRSLLFVMDAsdpTQLSASCVQLLGLLSAEQLAeasVLILFNKIDLPcymSTEEMKSLIRlpDIIACAKQNITTA 148
Cdd:cd00880    73 VADR-ADLVLLVVDS---DLTPVEEEAKLGLLRERGKP---VLLVLNKIDLV---PESEEEELLR--ERKLELLPDLPVI 140

                         170
                  ....*....|
gi 1859470408 149 EISAREGTGL 158
Cdd:cd00880   141 AVSALPGEGI 150
PRK10463 PRK10463
hydrogenase nickel incorporation protein HypB; Provisional
 108-171 1.85e-04

hydrogenase nickel incorporation protein HypB; Provisional


Pssm-ID: 182479  Cd Length: 290  Bit Score: 40.56  E-value: 1.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859470408 108 ASVLILFNKIDLPCYMSTEEMKSlirlpdiIACAKQ---NITTAEISAREGTGLAGVLAWLQATHRA 171
Cdd:PRK10463  231 AASLMLLNKVDLLPYLNFDVEKC-------IACAREvnpEIEIILISATSGEGMDQWLNWLETQRCA 290
HflX COG2262
50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis]; ...
 77-163 5.60e-04

50S ribosomal subunit-associated GTPase HflX [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441863 [Multi-domain]  Cd Length: 419  Bit Score: 39.30  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  77 LLFVMDASDP---TQLSASCvQLLGLLSAEqlaEASVLILFNKIDLpcyMSTEEMKSL-IRLPDIIAcakqnittaeISA 152
Cdd:COG2262   282 LLHVVDASDPdfeEQIETVN-EVLEELGAD---DKPIILVFNKIDL---LDDEELERLrAGYPDAVF----------ISA 344

                          90
                  ....*....|.
gi 1859470408 153 REGTGLAGVLA 163
Cdd:COG2262   345 KTGEGIDELLE 355
HflX cd01878
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ...
 77-165 6.79e-04

HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.


Pssm-ID: 206666 [Multi-domain]  Cd Length: 204  Bit Score: 38.59  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  77 LLFVMDASDPT---QLSAScVQLLGLLSAEqlaEASVLILFNKIDLpcyMSTEEMKSLIR--LPDIIAcakqnittaeIS 151
Cdd:cd01878   124 LLHVVDASDPDreeQIETV-EEVLKELGAD---DIPIILVLNKIDL---LDDEELEERLRagRPDAVF----------IS 186

                          90
                  ....*....|....
gi 1859470408 152 AREGTGLAGVLAWL 165
Cdd:cd01878   187 AKTGEGLDLLKEAI 200
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 78-158 1.77e-03

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 37.73  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  78 LFVMDASDPtqLSASCVQLLgllsaEQLAEASVLILFNKIDLPCyMSTEEMKSLIRLPDIiacakqnittaEISAREGTG 157
Cdd:COG0486   297 LLLLDASEP--LTEEDEEIL-----EKLKDKPVIVVLNKIDLPS-EADGELKSLPGEPVI-----------AISAKTGEG 357


                  .
gi 1859470408 158 L 158
Cdd:COG0486   358 I 358
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 74-158 2.11e-03

Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.


Pssm-ID: 206685 [Multi-domain]  Cd Length: 170  Bit Score: 37.02  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  74 CRSLLFVMDASDPTQLSASCVQLLGLLSA--EQLAEASVLILFNKIDLPcymSTEEMKSLIRlpdIIACAKQNITTAEIS 151
Cdd:cd01898    79 TRVLLHVIDLSGEDDPVEDYETIRNELEAynPGLAEKPRIVVLNKIDLL---DAEERFEKLK---ELLKELKGKKVFPIS 152


                  ....*..
gi 1859470408 152 AREGTGL 158
Cdd:cd01898   153 ALTGEGL 159
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 99-166 2.88e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 36.99  E-value: 2.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1859470408  99 LLSAEQlAEASVLILFNKIDLpcyMSTEEMKSLIRlpdiiACAKQNITTAEISAREGTGLAGVLAWLQ 166
Cdd:cd01854    26 LVAAEA-SGIEPVIVLNKADL---VDDEELEELLE-----IYEKLGYPVLAVSAKTGEGLDELRELLK 84
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 78-158 4.80e-03

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 35.93  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408  78 LFVMDASDPTQLSAscvqllgLLSAEQLAEASVLILFNKIDLpcyMSTEEMKSLIRLPDIIAcakqnittaeISAREGTG 157
Cdd:cd04164    87 LLVVDASEGLDEED-------LEILELPAKKPVIVVLNKSDL---LSDAEGISELNGKPIIA----------ISAKTGEG 146


                  .
gi 1859470408 158 L 158
Cdd:cd04164   147 I 147
PRK00098 PRK00098
GTPase RsgA; Reviewed
 105-166 5.38e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 36.34  E-value: 5.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1859470408 105 LAEA---SVLILFNKIDLpcYMSTEEMKSLIRLpdiiacaKQNI--TTAEISAREGTGLAGVLAWLQ 166
Cdd:PRK00098  106 LAEAngiKPIIVLNKIDL--LDDLEEARELLAL-------YRAIgyDVLELSAKEGEGLDELKPLLA 163
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 3-118 5.95e-03

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.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 34.79  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470408   3 LLLGATGVGKTLLVKRLQevssrDGKGDlgepPPTRPTVG------TNLTDIVAQRKITIRelggcmgpIW--------- 67
Cdd:pfam08477   3 VLLGDSGVGKTSLLKRFV-----DDTFD----PKYKSTIGvdfktkTVLENDDNGKKIKLN--------IWdtagqerfr 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1859470408  68 ---SSYYGNCRSLLFVMDASdptqlSASCVQLLgLLSAEQLAEASVLILF-NKID 118
Cdd:pfam08477  66 slhPFYYRGAAAALLVYDSR-----TFSNLKYW-LRELKKYAGNSPVILVgNKID 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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