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Conserved domains on  [gi|27734809|ref|NP_775935|]
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ADP-ribosylation factor-like protein 10 isoform 2 [Homo sapiens]

Protein Classification

Arl9_Arfrp2_like domain-containing protein( domain architecture ID 10134997)

Arl9_Arfrp2_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 79-237 5.29e-94

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: 272.78  E-value: 5.29e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  79 EVLVLGLDGAGKSTFLRVLSGKPPLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04162   1 QILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809 159 LRLPWARQELHKLLDKDPDLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQREVFLLAASIAPAGP-----TFEEPGTV 233
Cdd:cd04162  81 ERLPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGTSLDDDGSpsrmeAVKDLLSQ 160


                ....
gi 27734809 234 HIWK 237
Cdd:cd04162 161 LINL 164
 
Name Accession Description Interval E-value
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 79-237 5.29e-94

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: 272.78  E-value: 5.29e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  79 EVLVLGLDGAGKSTFLRVLSGKPPLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04162   1 QILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809 159 LRLPWARQELHKLLDKDPDLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQREVFLLAASIAPAGP-----TFEEPGTV 233
Cdd:cd04162  81 ERLPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGTSLDDDGSpsrmeAVKDLLSQ 160


                ....
gi 27734809 234 HIWK 237
Cdd:cd04162 161 LINL 164
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 80-214 4.05e-39

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 133.12  E-value: 4.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    80 VLVLGLDGAGKSTFLRVLSGKPpLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLKLGE-IVTTIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADRD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27734809   160 RLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR-EVF 214
Cdd:pfam00025  82 RIEEAKEELHALLNEEElaDAPLLILANKQDLPGAMSEAEIRELLGLHELKDRPwEIQ 139
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 80-224 2.59e-28

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: 105.77  E-value: 2.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809     80 VLVLGLDGAGKSTFLRVLSGKPPLEGhIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:smart00177  16 ILMVGLDAAGKTTILYKLKLGESVTT-IPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSNDRD 94

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27734809    160 RLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQRevFLLAASIAPAG 224
Cdd:smart00177  95 RIDEAREELHRMLNEDElrDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDRN--WYIQPTCATSG 159
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 80-211 1.78e-26

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 101.08  E-value: 1.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809   80 VLVLGLDGAGKSTFLRVLS-GKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:PTZ00133  20 ILMVGLDAAGKTTILYKLKlGE--VVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDSNDR 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27734809  159 LRLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR 211
Cdd:PTZ00133  98 ERIGDAREELERMLSEDElrDAVLLVFANKQDLPNAMSTTEVTEKLGLHSVRQRN 152
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
 80-206 1.20e-15

Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 72.55  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPPL--EGHIPtwgfnSVRLPTKDFE---VDLLEIGGSQNLRFY-------------WKE 141
Cdd:COG2229  15 IVYAGPFGAGKTTFVRSISEIEPLstEGRLT-----DASLETKTTTtvaFDFGRLTLGDGLRLHlfgtpgqvrfdfmWDI 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27734809 142 FVSEVDVLVFVVDSAdRLRLPWARQELHKLLDKDPDLPVVVVANKQDLSEAMSMGELQRELGLQA 206
Cdd:COG2229  90 LLRGADGVVFLADSR-RLEDSFNAESLDFFEERLEKLPFVVAVNKRDLPDALSLEELREALDLGP 153
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 80-189 2.92e-08

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]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 51.60  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    80 VLVLGLDGAGKSTFLRVLSGKPPLEGHI-PTWGFN----SVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVD 154
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYyPGTTRNyvttVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 27734809   155 ------SADRLRLPWaRQELHKLLDKdpDLPVVVVANKQDL 189
Cdd:TIGR00231  84 ivilvlDVEEILEKQ-TKEIIHHADS--GVPIILVGNKIDL 121
 
Name Accession Description Interval E-value
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 79-237 5.29e-94

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: 272.78  E-value: 5.29e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  79 EVLVLGLDGAGKSTFLRVLSGKPPLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04162   1 QILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809 159 LRLPWARQELHKLLDKDPDLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQREVFLLAASIAPAGP-----TFEEPGTV 233
Cdd:cd04162  81 ERLPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGTSLDDDGSpsrmeAVKDLLSQ 160


                ....
gi 27734809 234 HIWK 237
Cdd:cd04162 161 LINL 164
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 80-211 3.28e-47

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: 153.89  E-value: 3.28e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPPlEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:cd00878   2 ILMLGLDGAGKTTILYKLKLGEV-VTTIPTIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSDRE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 27734809 160 RLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR 211
Cdd:cd00878  81 RIEEAKNELHKLLNEEElkGAPLLILANKQDLPGALTESELIELLGLESIKGRR 134
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 80-214 4.05e-39

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 133.12  E-value: 4.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    80 VLVLGLDGAGKSTFLRVLSGKPpLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLKLGE-IVTTIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADRD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 27734809   160 RLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR-EVF 214
Cdd:pfam00025  82 RIEEAKEELHALLNEEElaDAPLLILANKQDLPGAMSEAEIRELLGLHELKDRPwEIQ 139
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 77-209 2.56e-34

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: 121.35  E-value: 2.56e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  77 QREVLVLGLDGAGKSTFLRVLSGKPplEGHI-PTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDS 155
Cdd:cd04155  15 EVRILLLGLDNAGKTTILKQLASED--ISHItPTQGFNIKNVQADGFKLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDS 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27734809 156 ADRLRLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDN 209
Cdd:cd04155  93 ADRKRFEEAGQELVELLEEEKlaGVPVLVFANKQDLLTAAPAEEVAEALNLHDIRD 148
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 79-213 3.31e-31

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: 112.80  E-value: 3.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  79 EVLVLGLDGAGKSTFLRVLSGKPPLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04159   1 EITLVGLQNSGKTTLVNVIASGQFSEDTIPTVGFNMRKVTKGNVTIKVWDLGGQPRFRSMWERYCRGVNAIVYVVDAADR 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27734809 159 LRLPWARQELHKLLDKdPDL---PVVVVANKQDLSEAMSMGELQRELGLQAIDNqREV 213
Cdd:cd04159  81 EKLEVAKNELHDLLEK-PSLegiPLLVLGNKNDLPGALSVDELIEQMNLKSITD-REV 136
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
 80-211 6.54e-31

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: 111.73  E-value: 6.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFL-RVLSGKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04151   2 ILILGLDGAGKTTILyRLQVGE--VVTTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDR 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27734809 159 LRLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR 211
Cdd:cd04151  80 DRLGISKSELHAMLEEEElkDAVLLVFANKQDMPGALSEAEVAEKLGLSELKDRT 134
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 79-238 1.67e-29

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: 108.27  E-value: 1.67e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  79 EVLVLGLDGAGKSTFLRVLSGKPPLEGhIPTWGFNSVRLPT-KDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSAD 157
Cdd:cd04156   1 QVLLLGLDSAGKSTLLYKLKHAELVTT-IPTVGFNVEMLQLeKHLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809 158 RLRLPWARQELHKLLdKDPDL---PVVVVANKQDLSEAMSMGELQRELGLQAIDNQREVFLLAASiAPAGPTFEEpGTVH 234
Cdd:cd04156  80 EARLDESQKELKHIL-KNEHIkgvPVVLLANKQDLPGALTAEEITRRFKLKKYCSDRDWYVQPCS-AVTGEGLAE-AFRK 156


                ....
gi 27734809 235 IWKL 238
Cdd:cd04156 157 LASF 160
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
 80-211 1.70e-29

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.


Pssm-ID: 206720 [Multi-domain]  Cd Length: 173  Bit Score: 108.57  E-value: 1.70e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPpLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:cd04154  17 ILMLGLDNAGKTTILKKFNGED-ISTISPTLGFNIKTLEYNGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVVDSSDRA 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 27734809 160 RLPWARQELHKLL--DKDPDLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR 211
Cdd:cd04154  96 RLEDCKRELQKLLveERLAGATLLIFANKQDLPGALSPEEIREVLELDSIKSHH 149
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
 80-207 8.34e-29

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: 107.05  E-value: 8.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPPLEGHiPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:cd04153  18 VIIVGLDNAGKTTILYQFLLGEVVHTS-PTIGSNVEEIVYKNIRFLMWDIGGQESLRSSWNTYYTNTDAVILVIDSTDRE 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27734809 160 RLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAI 207
Cdd:cd04153  97 RLPLTKEELYKMLAHEDlrKAVLLVLANKQDLKGAMTPAEISESLGLTSI 146
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 80-224 2.59e-28

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: 105.77  E-value: 2.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809     80 VLVLGLDGAGKSTFLRVLSGKPPLEGhIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:smart00177  16 ILMVGLDAAGKTTILYKLKLGESVTT-IPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSNDRD 94

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27734809    160 RLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQRevFLLAASIAPAG 224
Cdd:smart00177  95 RIDEAREELHRMLNEDElrDAVILVFANKQDLPDAMKAAEITEKLGLHSIRDRN--WYIQPTCATSG 159
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 78-205 7.40e-28

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: 105.05  E-value: 7.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  78 REVLVLGLDGAGKSTFLRVL-SGKppLEGHIPTWGFNS-------VRLPTKDfevdlleIGGSQNLRFYWKEFVSEVDVL 149
Cdd:cd00879  20 AKIVFLGLDNAGKTTLLHMLkDDR--LAQHVPTLHPTSeeltignVKFTTFD-------LGGHEQARRVWKDYFPEVDGI 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 27734809 150 VFVVDSADRLRLPWARQELHKLLDKD--PDLPVVVVANKQDLSEAMSMGELQRELGLQ 205
Cdd:cd00879  91 VFLVDAADPERFQESKEELDSLLNDEelANVPILILGNKIDKPGAVSEEELREALGLY 148
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 80-211 1.78e-26

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 101.08  E-value: 1.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809   80 VLVLGLDGAGKSTFLRVLS-GKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:PTZ00133  20 ILMVGLDAAGKTTILYKLKlGE--VVTTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDSNDR 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27734809  159 LRLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR 211
Cdd:PTZ00133  98 ERIGDAREELERMLSEDElrDAVLLVFANKQDLPNAMSTTEVTEKLGLHSVRQRN 152
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
 80-218 5.77e-26

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 99.66  E-value: 5.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809   80 VLVLGLDGAGKSTFLRVLS-GKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:PLN00223  20 ILMVGLDAAGKTTILYKLKlGE--IVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27734809  159 LRLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIdNQREVFLLAA 218
Cdd:PLN00223  98 DRVVEARDELHRMLNEDElrDAVLLVFANKQDLPNAMNAAEITDKLGLHSL-RQRHWYIQST 158
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
 80-210 8.64e-26

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: 98.63  E-value: 8.64e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLS-GKppLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:cd04150   3 ILMVGLDAAGKTTILYKLKlGE--IVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 27734809 159 LRLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQ 210
Cdd:cd04150  81 ERIGEAREELQRMLNEDElrDAVLLVFANKQDLPNAMSAAEVTDKLGLHSLRNR 134
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
 80-210 5.15e-25

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: 96.77  E-value: 5.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSgkppLEGH---IPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSA 156
Cdd:cd04149  12 ILMLGLDAAGKTTILYKLK----LGQSvttIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSA 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 27734809 157 DRLRLPWARQELHKLL-DKD-PDLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQ 210
Cdd:cd04149  88 DRDRIDEARQELHRIInDREmRDALLLVFANKQDLPDAMKPHEIQEKLGLTRIRDR 143
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
 80-210 6.53e-25

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: 96.69  E-value: 6.53e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPPLEGHiPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:cd04161   2 LLTVGLDNAGKTTLVSALQGEIPKKVA-PTVGFTPTKLRLDKYEVCIFDLGGGANFRGIWVNYYAEAHGLVFVVDSSDDD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 27734809 160 RLPWARQELHKLLdKDPDL---PVVVVANKQDLSEAMSMGELQRELGLQAIDNQ 210
Cdd:cd04161  81 RVQEVKEILRELL-QHPRVsgkPILVLANKQDKKNALLGADVIEYLSLEKLVNE 133
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
 80-211 1.11e-24

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: 96.41  E-value: 1.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPPLEGhIPTWGFNSVRL-----PTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVD 154
Cdd:cd04152   6 IVMLGLDSAGKTTVLYRLKFNEFVNT-VPTKGFNTEKIkvslgNAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27734809 155 SADRLRLPWARQELHKL--LDKDPDLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQR 211
Cdd:cd04152  85 SVDVERMEEAKTELHKItkFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSST 143
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
 80-229 1.43e-22

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: 90.48  E-value: 1.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFL--------RVLSGKPPlEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVF 151
Cdd:cd04160   2 VLILGLDNAGKTTFLeqtktkfsKNYKGLNP-SKITPTVGLNIGTIEVGKARLMFWDLGGQEELRSLWDKYYAESHGVIY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809 152 VVDSADRLRLPWARQELHKLLdKDPDL---PVVVVANKQDLSEAMSMGELQRELGLQAIDNQREVFLLAASIAPAGPTFE 228
Cdd:cd04160  81 VIDSTDRERFNESKSAFEKVI-NNEALegvPLLVLANKQDLPDALSVAEIKEVFDDCIALIGRRDCLVQPVSALEGEGVE 159


                .
gi 27734809 229 E 229
Cdd:cd04160 160 E 160
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
 80-207 1.46e-21

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: 87.48  E-value: 1.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLsgKPPLE--GHI-PTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSA 156
Cdd:cd04157   2 ILVLGLDNSGKTTIINQL--KPSNAqsQNIvPTVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSS 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27734809 157 DRLRLPWARQELHKLLD----KDPDLPVVVVANKQDLSEAMSMGELQRELGLQAI 207
Cdd:cd04157  80 DRLRMVVAKDELELLLNhpdiKHRRIPILFYANKMDLPDALTAVKITQLLCLENI 134
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 79-215 3.58e-20

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: 84.60  E-value: 3.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809     79 EVLVLGLDGAGKSTFLRVLSGKPpLEGHIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADR 158
Cdd:smart00178  19 KILFLGLDNAGKTTLLHMLKNDR-LAQHQPTQHPTSEELAIGNIKFTTFDLGGHQQARRLWKDYFPEVNGIVYLVDAYDK 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27734809    159 LRLPWARQELHKLLDKD--PDLPVVVVANKQDLSEAMSMGELQRELGL------QAIDNQR--EVFL 215
Cdd:smart00178  98 ERFAESKRELDALLSDEelATVPFLILGNKIDAPYAASEDELRYALGLtntttgKGKVGVRpvEVFM 164
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
 80-207 5.30e-17

(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: 75.84  E-value: 5.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPPLEGhIPTWGFNSVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVDSADRL 159
Cdd:cd04158   2 VVTLGLDGAGKTTILFKLKQDEFMQP-IPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVIDSSHRD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 27734809 160 RLPWARQELHKLLDKDP--DLPVVVVANKQDLSEAMSMGELQRELGLQAI 207
Cdd:cd04158  81 RVSEAHSELAKLLTEKElrDALLLIFANKQDVAGALSVEEMTELLSLHKL 130
Srp102 COG2229
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ...
 80-206 1.20e-15

Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441830 [Multi-domain]  Cd Length: 189  Bit Score: 72.55  E-value: 1.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPPL--EGHIPtwgfnSVRLPTKDFE---VDLLEIGGSQNLRFY-------------WKE 141
Cdd:COG2229  15 IVYAGPFGAGKTTFVRSISEIEPLstEGRLT-----DASLETKTTTtvaFDFGRLTLGDGLRLHlfgtpgqvrfdfmWDI 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27734809 142 FVSEVDVLVFVVDSAdRLRLPWARQELHKLLDKDPDLPVVVVANKQDLSEAMSMGELQRELGLQA 206
Cdd:COG2229  90 LLRGADGVVFLADSR-RLEDSFNAESLDFFEERLEKLPFVVAVNKRDLPDALSLEELREALDLGP 153
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 81-222 1.84e-14

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: 68.64  E-value: 1.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  81 LVLGLDGAGKSTFLRVLSGKPPLEG---HIPTWGFNSVRLPTKDFEVDL-------LEIGGSQNLRFYWKEFVSEVDVLV 150
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVsdvPGTTRDPDVYVKELDKGKVKLvlvdtpgLDEFGGLGREELARLLLRGADLIL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27734809 151 FVVDSADRLRLPWARQELHKLLDKDpDLPVVVVANKQDLSEAmsmGELQRELGLQAIDNQREVFLLAASIAP 222
Cdd:cd00882  81 LVVDSTDRESEEDAKLLILRRLRKE-GIPIILVGNKIDLLEE---REVEELLRLEELAKILGVPVFEVSAKT 148
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
80-229 2.83e-11

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 60.38  E-value: 2.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKP-PLEGHIPTWGFN----SVRLPTKDFEVDLLEIGGS---QNLRFYWKEFVSEVDVLVF 151
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIfSLEKYLSTNGVTidkkELKLDGLDVDLVIWDTPGQdefRETRQFYARQLTGASLYLF 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27734809 152 VVDSADRLRLPWARQELHKLLDKDPDLPVVVVANKQDLSEAMSMGELQRELGLQAIDNQREVFLLAasiAPAGPTFEE 229
Cdd:COG1100  86 VVDGTREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEIEDEERLKEALSEDNIVEVVATS---AKTGEGVEE 160
Miro2 cd01892
Mitochondrial Rho family 2 (Miro2), C-terminal; Miro2 subfamily. Miro (mitochondrial Rho) ...
 77-234 8.04e-10

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.


Pssm-ID: 206679  Cd Length: 180  Bit Score: 56.48  E-value: 8.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  77 QREVL---VLGLDGAGKSTFLRVLSGKPP-LEGHIPTWG----FNSVRLPTKD-----FEVDLLEIGGSQNlrfywKEFV 143
Cdd:cd01892   1 QRNVFlcfVLGAKGSGKSALLQAFLGRSFsQNAYSPTIKpryaVNTVEVPGQEkylilREVGEDEEAILLN-----DAEL 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809 144 SEVDVLVFVVDSADrlrlP--WAR-QELHKLLDKDPDLPVVVVANKQDLSEAMSMGELQ-----RELGLQA--------I 207
Cdd:cd01892  76 AACDVACLVYDSSD----PnsFSYcAEVYKKYFMLGEIPCLFVAAKADLDEQQQRAEVQpdefcRKLGLPPplhfssrlG 151

                       170       180
                ....*....|....*....|....*..
gi 27734809 208 DNQREVFLLAASIApagptfEEPGTVH 234
Cdd:cd01892 152 DSSNELFTKLATAA------QYPHLSI 172
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 79-186 2.03e-09

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.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 53.78  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    79 EVLVLGLDGAGKSTFLRVLSGKPPLEGHIP--TWGFNSVRLPTKDFEVDLLEIGGS-QNLRFYW---KEFVS--EVDVLV 150
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPgtTRDPNEGRLELKGKQIILVDTPGLiEGASEGEglgRAFLAiiEADLIL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 27734809   151 FVVDSADRLRLpwARQELHKLLDKDpDLPVVVVANK 186
Cdd:pfam01926  81 FVVDSEEGITP--LDEELLELLREN-KKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 82-192 2.19e-09

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: 54.94  E-value: 2.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  82 VLGLDGAGKSTFLRVLSGKPPLE-GHIP---TWGfNSVR---LPTKDFE-VD---LLEIGGSQNLRF--YWKEFvSEVDV 148
Cdd:cd00880   2 IFGRPNVGKSSLLNALLGQNVGIvSPIPgttRDP-VRKEwelLPLGPVVlIDtpgLDEEGGLGRERVeeARQVA-DRADL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 27734809 149 LVFVVDSaDRLRLPWaRQELHKLLDKdpDLPVVVVANKQDLSEA 192
Cdd:cd00880  80 VLLVVDS-DLTPVEE-EAKLGLLRER--GKPVLLVLNKIDLVPE 119
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 80-189 2.92e-08

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]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 51.60  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    80 VLVLGLDGAGKSTFLRVLSGKPPLEGHI-PTWGFN----SVRLPTKDFEVDLLEIGGSQNLRFYWKEFVSEVDVLVFVVD 154
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSITEYyPGTTRNyvttVIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 27734809   155 ------SADRLRLPWaRQELHKLLDKdpDLPVVVVANKQDL 189
Cdd:TIGR00231  84 ivilvlDVEEILEKQ-TKEIIHHADS--GVPIILVGNKIDL 121
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 80-203 3.06e-06

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.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 46.55  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKST-FLRVLSGKPP-----LEGHIPTWGFNSVrlptKDFEVDLLEIGGSQNLRF-YWKEFVSEVDVLVFV 152
Cdd:cd04105   3 VLLLGPSDSGKTAlFTKLTTGKVRstvtsIEPNVASFYSNSS----KGKKLTLVDVPGHEKLRDkLLEYLKASLKAIVFV 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27734809 153 VDSADRLRLpwARQE---LHKLL----DKDPDLPVVVVANKQDLSEAMSMG----ELQRELG 203
Cdd:cd04105  79 VDSATFQKN--IRDVaefLYDILtdleKIKNKIPILIACNKQDLFTAKPAKkikeLLEKEIN 138
Obg cd01898
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
 83-218 2.05e-05

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: 43.57  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  83 LGLDGAGKSTFLRVLSG-KP-----P---LeghIPTWGFnsVRLP-TKDFEV-D---LLEiGGSQN----LRFYwkEFVS 144
Cdd:cd01898   6 VGLPNAGKSTLLSAISNaKPkiadyPfttL---VPNLGV--VRVDdGRSFVIaDipgLIE-GASEGkglgHRFL--RHIE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809 145 EVDVLVFVVDsADRLRLPWA-----RQEL----HKLLDKdpdlPVVVVANKQDLSEAMSMGELQRElgLQAIDNQREVFL 215
Cdd:cd01898  78 RTRVLLHVID-LSGEDDPVEdyetiRNELeaynPGLAEK----PRIVVLNKIDLLDAEERFEKLKE--LLKELKGKKVFP 150


                ...
gi 27734809 216 LAA 218
Cdd:cd01898 151 ISA 153
SRPRB pfam09439
Signal recognition particle receptor beta subunit; The beta subunit of the signal recognition ...
 77-204 7.97e-04

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


Pssm-ID: 462797 [Multi-domain]  Cd Length: 181  Bit Score: 39.35  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    77 QREVLVLGLDGAGKST-FLRVLSG--KPPLEGHIP--TWGFNSVrlptKDFEVDLLEIGGSQNLRFYWKE---FVSEVDV 148
Cdd:pfam09439   3 QPAVIIAGLCDSGKTSlFTLLTTDsvRPTVTSQEPsaAYRYMLN----KGNSFTLIDFPGHVKLRYKLLEtlkDSSSLKG 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27734809   149 LVFVVDSA-DRLRLPWARQELHKLL---DKDPDLPVVVVA-NKQDLSEAMS----MGELQRELGL 204
Cdd:pfam09439  79 IVFVVDSTiFPKEVTDTAEFLYDILsitELLKNGIDILIAcNKQESFTARPpkkiKQALEKEINT 143
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 79-216 1.07e-03

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 38.40  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    79 EVLVL-GLDGAGKSTFLRVLSGK-PPLEGHIpTWGFNSVRLPTKDFEvdLLEIGG-SQNLRFywKEFVSEVDVLVFVVDS 155
Cdd:pfam00005  12 EILALvGPNGAGKSTLLKLIAGLlSPTEGTI-LLDGQDLTDDERKSL--RKEIGYvFQDPQL--FPRLTVRENLRLGLLL 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27734809   156 ADRLRlPWARQELHKLLDK--DPDLPVVVVANKQDlseAMSMGELQReLGL-QAIDNQREVFLL 216
Cdd:pfam00005  87 KGLSK-REKDARAEEALEKlgLGDLADRPVGERPG---TLSGGQRQR-VAIaRALLTKPKLLLL 145
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 80-111 1.20e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 39.66  E-value: 1.20e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGK-PPLEGHIpTWG 111
Cdd:COG0488 344 IGLIGPNGAGKSTLLKLLAGElEPDSGTV-KLG 375
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 80-218 2.11e-03

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 37.49  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809    80 VLVLGLDGAGKSTFL-RVLSGKPPLEgHIPTWGFNSVrlpTKDFEVD----LLEI---GGSQnlRF------YWKEfvSE 145
Cdd:pfam00071   2 LVLVGDGGVGKSSLLiRFTQNKFPEE-YIPTIGVDFY---TKTIEVDgktvKLQIwdtAGQE--RFralrplYYRG--AD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809   146 VDVLVFVVDSADRL-RLP-WARQELHKlldKDPDLPVVVVANKQDLSE--AMSMGE---LQRELGLQAID-------NQR 211
Cdd:pfam00071  74 GFLLVYDITSRDSFeNVKkWVEEILRH---ADENVPIVLVGNKCDLEDqrVVSTEEgeaLAKELGLPFMEtsaktneNVE 150


                  ....*..
gi 27734809   212 EVFLLAA 218
Cdd:pfam00071 151 EAFEELA 157
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 143-189 3.42e-03

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 37.06  E-value: 3.42e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 27734809 143 VSEVDVLVFVVDSADrlrlpWARQELHKLLD--KDPDLPVVVVANKQDL 189
Cdd:cd04163  80 LKDVDLVLFVVDASE-----WIGEGDEFILEllKKSKTPVILVLNKIDL 123
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 80-138 4.08e-03

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 37.07  E-value: 4.08e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  80 VLVLGLDGAGKSTFLRVLSG-KPPLEGHIpTWGFNSVRLPTKDFEVDLLEIG----------GSQNLRFY 138
Cdd:COG4133  31 LALTGPNGSGKTTLLRILAGlLPPSAGEV-LWNGEPIRDAREDYRRRLAYLGhadglkpeltVRENLRFW 99
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 80-107 4.11e-03

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.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 37.45  E-value: 4.11e-03
                        10        20
                ....*....|....*....|....*....
gi 27734809  80 VLVLGLDGAGKSTFLRVLSG-KPPLEGHI 107
Cdd:cd03225  30 VLIVGPNGSGKSTLLRLLNGlLGPTSGEV 58
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 82-138 5.63e-03

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 36.98  E-value: 5.63e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27734809  82 VLGLDGAGKSTFLRVLSG-KPPLEGHIPTWGfnsvRLPTkdfevdLLEIG--------GSQNLRFY 138
Cdd:COG1134  57 IIGRNGAGKSTLLKLIAGiLEPTSGRVEVNG----RVSA------LLELGagfhpeltGRENIYLN 112
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 140-192 6.09e-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: 37.35  E-value: 6.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 27734809 140 KEFVSEVDVLVFVVDSADRLRlpwarQELHKLLDKDPDLPVVVVANKQDLSEA 192
Cdd:COG0486 287 REAIEEADLVLLLLDASEPLT-----EEDEEILEKLKDKPVIVVLNKIDLPSE 334
RhoA_like cd01870
Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of ...
 78-200 6.71e-03

Ras homology family A (RhoA)-like includes RhoA, RhoB and RhoC; The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. RhoA and RhoC are observed only in geranylgeranylated forms; however, RhoB can be present in palmitoylated, farnesylated, and geranylgeranylated forms. RhoA and RhoC are highly relevant for tumor progression and invasiveness; however, RhoB has recently been suggested to be a tumor suppressor. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206662 [Multi-domain]  Cd Length: 175  Bit Score: 36.25  E-value: 6.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734809  78 REVLVLGLDGA-GKSTFLRVLSGKPPLEGHIPTWGFNSVrlptKDFEVD-------LLEIGGSQN---LR-FYWKEfvSE 145
Cdd:cd01870   1 RKKLVIVGDGAcGKTCLLIVFSKDQFPEVYVPTVFENYV----ADIEVDgkqvelaLWDTAGQEDydrLRpLSYPD--TD 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 27734809 146 VDVLVFVVDSADRL---RLPWARQELHKLldkdPDLPVVVVANKQDL-SEAMSMGELQR 200
Cdd:cd01870  75 VILMCFSIDSPDSLeniPEKWTPEVKHFC----PNVPIILVGNKKDLrNDEHTIRELAK 129
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 80-107 7.59e-03

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.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 36.47  E-value: 7.59e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 27734809  80 VLVLGLDGAGKSTFLRVLSGKPP----LEGHI 107
Cdd:cd03233  36 VLVLGRPGSGCSTLLKALANRTEgnvsVEGDI 67
 
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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