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Conserved domains on  [gi|5729999|ref|NP_006561|]
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ras-related GTP-binding protein A [Homo sapiens]

Protein Classification

GTR/RAG family GTP-binding protein( domain architecture ID 10183650)

GTR/RAG family GTP-binding protein similar to yeast GTP-binding protein GTR1, the GTPase component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
 9-292 0e+00

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and B; RagA and RagB are closely related Rag GTPases (ras-related GTP-binding protein A and B) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr1. These domains function by forming heterodimers with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2, through the carboxy-terminal segments. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


:

Pssm-ID: 206744  Cd Length: 286  Bit Score: 586.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:cd11384   1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECACFRTSIWDET 168
Cdd:cd11384  81 IYVFDVESRELEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEVTCFPTSIWDET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999  169 LYKAWSSIVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQ--RDVHRFEKISNIIKQFKLSCSKLA 246
Cdd:cd11384 161 LYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEAsaLDPHRFEKISNIIKQFKLSCSKLQ 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5729999  247 ASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRN 292
Cdd:cd11384 241 ASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
 
Name Accession Description Interval E-value
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
 9-292 0e+00

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and B; RagA and RagB are closely related Rag GTPases (ras-related GTP-binding protein A and B) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr1. These domains function by forming heterodimers with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2, through the carboxy-terminal segments. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206744  Cd Length: 286  Bit Score: 586.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:cd11384   1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECACFRTSIWDET 168
Cdd:cd11384  81 IYVFDVESRELEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEVTCFPTSIWDET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999  169 LYKAWSSIVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQ--RDVHRFEKISNIIKQFKLSCSKLA 246
Cdd:cd11384 161 LYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEAsaLDPHRFEKISNIIKQFKLSCSKLQ 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5729999  247 ASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRN 292
Cdd:cd11384 241 ASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 9-235 1.61e-134

Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a suppressor of a mutation in RCC1. Biochemical analysis revealed that Gtr1 is in fact a G protein of the Ras family. The RagA/B proteins are the human homologs of Gtr1. Included in this family is the human Rag C, a novel protein that has been shown to interact with RagA/B.


Pssm-ID: 398377 [Multi-domain]  Cd Length: 231  Bit Score: 380.77  E-value: 1.61e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999      9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNYLTFQKEHIFSNVGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999     89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLE----CACFRTSI 164
Cdd:pfam04670  81 IYVFDVQSREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGleldLSFFLTSI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5729999    165 WDETLYKAWSSIVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDVHRFEKISNII 235
Cdd:pfam04670 161 WDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVDDMQRYEKCSDII 231
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
7-163 1.15e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 53.83  E-value: 1.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    7 KKKVLLMGKSGSGKTSmrsiiFANYIARDT---RRLGATIDVEHSHVRF---LGNLVLNLWDCGGQDTFMEnyFTSQRDN 80
Cdd:COG1100   3 EKKIVVVGTGGVGKTS-----LVNRLVGDIfslEKYLSTNGVTIDKKELkldGLDVDLVIWDTPGQDEFRE--TRQFYAR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   81 IFRNVEVLIYVFDVesrELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRdlifKEREEDLRRLSRPLECACF 160
Cdd:COG1100  76 QLTGASLYLFVVDG---TREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEI----EDEERLKEALSEDNIVEVV 148


                ...
gi 5729999  161 RTS 163
Cdd:COG1100 149 ATS 151
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 8-135 9.81e-07

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: 47.75  E-value: 9.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999      8 KKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLG-NLVLNLWDCGGQDTF--MENYFTSQRDNIFRN 84
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGkTYKFNLLDTAGQEDYdaIRRLYYPQVERSLRV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5729999     85 VEVLIYVFDVESRELEKDMhyyqsclEAILQNSPDAKIFCLVHKMDLVQED 135
Cdd:TIGR00231  82 FDIVILVLDVEEILEKQTK-------EIIHHADSGVPIILVGNKIDLKDAD 125
PLN03118 PLN03118
Rab family protein; Provisional
 9-163 1.36e-06

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 48.13  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999     9 KVLLMGKSGSGKTSMrsiiFANYIARDTRRLGATIDVEHSHVRFL---GNLVLNLWDCGGQDTFmeNYFTSqrdNIFRNV 85
Cdd:PLN03118  16 KILLIGDSGVGKSSL----LVSFISSSVEDLAPTIGVDFKIKQLTvggKRLKLTIWDTAGQERF--RTLTS---SYYRNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    86 EVLIYVFDVESREL--------EKDMHYY---QSCLEAILQNSPDakifclvhkmdlvQEDQRDLifkEREEDLrRLSRP 154
Cdd:PLN03118  87 QGIILVYDVTRRETftnlsdvwGKEVELYstnQDCVKMLVGNKVD-------------RESERDV---SREEGM-ALAKE 149


                 ....*....
gi 5729999   155 LECACFRTS 163
Cdd:PLN03118 150 HGCLFLECS 158
 
Name Accession Description Interval E-value
RagA_like cd11384
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and ...
 9-292 0e+00

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins A and B; RagA and RagB are closely related Rag GTPases (ras-related GTP-binding protein A and B) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr1. These domains function by forming heterodimers with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2, through the carboxy-terminal segments. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206744  Cd Length: 286  Bit Score: 586.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:cd11384   1 KVLLMGKSGSGKTSMRSIIFANYLARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDAFMENYFTSQRDHIFRNVEVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECACFRTSIWDET 168
Cdd:cd11384  81 IYVFDVESRELEKDLTYFRSCLEALRQNSPDAKVFVLIHKMDLVQEDEREAVFERKEKELRRLSEPLEVTCFPTSIWDET 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999  169 LYKAWSSIVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQ--RDVHRFEKISNIIKQFKLSCSKLA 246
Cdd:cd11384 161 LYKAWSSIVYSLIPNIQVLESNLKKFADICEADEVVLFERATFLVISHSSRKEAsaLDPHRFEKISNIIKQFKLSCSKLQ 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 5729999  247 ASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRN 292
Cdd:cd11384 241 ASFQSMEVRNSNFSAFIDEFTSNTYIMVVMSDPSIESAAILMNIRN 286
Gtr1_RagA pfam04670
Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a ...
 9-235 1.61e-134

Gtr1/RagA G protein conserved region; GTR1 was first identified in S. cerevisiae as a suppressor of a mutation in RCC1. Biochemical analysis revealed that Gtr1 is in fact a G protein of the Ras family. The RagA/B proteins are the human homologs of Gtr1. Included in this family is the human Rag C, a novel protein that has been shown to interact with RagA/B.


Pssm-ID: 398377 [Multi-domain]  Cd Length: 231  Bit Score: 380.77  E-value: 1.61e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999      9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVL 88
Cdd:pfam04670   1 KVLLMGLSGSGKSSMRSVIFSNYSPRDTLRLGATIDVEHSHVRFLGNLVLNLWDCGGQDDFFDNYLTFQKEHIFSNVGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999     89 IYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLE----CACFRTSI 164
Cdd:pfam04670  81 IYVFDVQSREYEEDLARLKETIEALYQYSPDAKVFVLIHKMDLIQEDHREEIFRDRKQEIREESEDLGleldLSFFLTSI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5729999    165 WDETLYKAWSSIVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDVHRFEKISNII 235
Cdd:pfam04670 161 WDESLYKAWSSIVQKLIPNLPTLENLLKVFCSNSDADEVFLFERTTFLVIATDSRSPVDDMQRYEKCSDII 231
Rag cd09915
Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) ...
 9-181 1.15e-50

Rag GTPase subfamily of Ras-related GTPases; Rag GTPases (ras-related GTP-binding proteins) constitute a unique subgroup of the Ras superfamily, playing an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. This subfamily consists of RagA and RagB as well as RagC and RagD that are closely related. Saccharomyces cerevisiae encodes single orthologs of metazoan RagA/B and RagC/D, Gtr1 and Gtr2, respectively. Dimer formation is important for their cellular function; these domains form heterodimers, as RagA or RagB dimerizes with RagC or RagD, and similarly, Gtr1 dimerizes with Gtr2. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206742 [Multi-domain]  Cd Length: 175  Bit Score: 165.43  E-value: 1.15e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMEnyFTSQRDNIFRNVEVL 88
Cdd:cd09915   1 KLLL*GRRRSGKSSIRKVVFHNYSPFDTLRLESTIDVEHSHLSFLGN*TLNLWDCPGQDVFFE--PTKDKEHIFQ*VGAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   89 IYVFDVESrELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQED-----QRDLIFKEREEDLRRLSRPLECACFRTS 163
Cdd:cd09915  79 IYVIDVQD-EYLKAITILAKALKQAYKVNPDANIEVLIHKVDGLSLDkkeelQRDI*QRLSETLSEFGLEFPNLSFYLTS 157

                       170
                ....*....|....*...
gi 5729999  164 IWDETLYKAWSSIVYQLI 181
Cdd:cd09915 158 IWDHSIYEAFSQIVQKLI 175
RagC_like cd11385
Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and ...
 9-181 4.83e-15

Rag GTPase, subfamily of Ras-related GTPases, includes Ras-related GTP-binding proteins C and D; RagC and RagD are closely related Rag GTPases (ras-related GTP-binding protein C and D) that constitute a unique subgroup of the Ras superfamily, and are functional homologs of Saccharomyces cerevisiae Gtr2. These domains form heterodimers with RagA or RagB, and similarly, Gtr2 dimerizes with Gtr1 in order to function. They play an essential role in regulating amino acid-induced target of rapamycin complex 1 (TORC1) kinase signaling, exocytic cargo sorting at endosomes, and epigenetic control of gene expression. In response to amino acids, the Rag GTPases guide the TORC1 complex to activate the platform containing Rheb proto-oncogene by driving the relocalization of mTORC1 from discrete locations in the cytoplasm to a late endosomal and/or lysosomal compartment that is Rheb-enriched and contains Rab-7.


Pssm-ID: 206745 [Multi-domain]  Cd Length: 175  Bit Score: 71.87  E-value: 4.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSqrDNIFRNVEVL 88
Cdd:cd11385   1 RILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKITKDDISNSSFVNFQIWDFPGQLDPFDPTLDP--EMIFSGCGAL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   89 IYVFDVESrelekdmHYYQSC------LEAILQNSPDAKIFCLVHKMDLVQED-----QRDlIFKEREEDLRRLSRP-LE 156
Cdd:cd11385  79 VFVIDAQD-------DYDEAIarlvetVTKAYKVNPNINFEVFIHKVDGLSEDhkietQRD-IQQRVTDELADAGLEdVQ 150

                       170       180
                ....*....|....*....|....*
gi 5729999  157 CACFRTSIWDETLYKAWSSIVYQLI 181
Cdd:cd11385 151 ISFYLTSIYDHSIFEAFSKVVQKLI 175
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 11-163 2.62e-11

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: 60.93  E-value: 2.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   11 LLMGKSGSGKTSmrsiiFANYIARDT-----RRLGATIDVEHSHVRFLGNLV-LNLWDCGGQDTFMENYFTSQRDNIFRN 84
Cdd:cd00882   1 VVVGRGGVGKSS-----LLNALLGGEvgevsDVPGTTRDPDVYVKELDKGKVkLVLVDTPGLDEFGGLGREELARLLLRG 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5729999   85 VEVLIYVFDVESRELEKDMHYyqscLEAILQNSPDAKIFCLVHKMDLVQEDQRdlifkEREEDLRRLSRPLECACFRTS 163
Cdd:cd00882  76 ADLILLVVDSTDRESEEDAKL----LILRRLRKEGIPIILVGNKIDLLEEREV-----EELLRLEELAKILGVPVFEVS 145
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
7-163 1.15e-08

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 53.83  E-value: 1.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    7 KKKVLLMGKSGSGKTSmrsiiFANYIARDT---RRLGATIDVEHSHVRF---LGNLVLNLWDCGGQDTFMEnyFTSQRDN 80
Cdd:COG1100   3 EKKIVVVGTGGVGKTS-----LVNRLVGDIfslEKYLSTNGVTIDKKELkldGLDVDLVIWDTPGQDEFRE--TRQFYAR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   81 IFRNVEVLIYVFDVesrELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRdlifKEREEDLRRLSRPLECACF 160
Cdd:COG1100  76 QLTGASLYLFVVDG---TREETLQSLYELLESLRRLGKKSPIILVLNKIDLYDEEEI----EDEERLKEALSEDNIVEVV 148


                ...
gi 5729999  161 RTS 163
Cdd:COG1100 149 ATS 151
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 9-157 2.73e-07

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: 49.44  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999      9 KVLLMGKSGSGKTSMRS--------------IIFANYIArdtrrlgaTIDVEHSHVRflgnlvLNLWDCGGQDTfmenyF 74
Cdd:pfam00071   1 KLVLVGDGGVGKSSLLIrftqnkfpeeyiptIGVDFYTK--------TIEVDGKTVK------LQIWDTAGQER-----F 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999     75 TSQRDNIFRNVEVLIYVFDVESRE-LEKDMHYYQScleaILQNSPDAKIFCLV-HKMDLvqEDQRDLIFKEREEDLRRLS 152
Cdd:pfam00071  62 RALRPLYYRGADGFLLVYDITSRDsFENVKKWVEE----ILRHADENVPIVLVgNKCDL--EDQRVVSTEEGEALAKELG 135


                  ....*.
gi 5729999    153 RP-LEC 157
Cdd:pfam00071 136 LPfMET 141
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 8-135 9.81e-07

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: 47.75  E-value: 9.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999      8 KKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLG-NLVLNLWDCGGQDTF--MENYFTSQRDNIFRN 84
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNYVTTVIEEDGkTYKFNLLDTAGQEDYdaIRRLYYPQVERSLRV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 5729999     85 VEVLIYVFDVESRELEKDMhyyqsclEAILQNSPDAKIFCLVHKMDLVQED 135
Cdd:TIGR00231  82 FDIVILVLDVEEILEKQTK-------EIIHHADSGVPIILVGNKIDLKDAD 125
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 9-130 1.17e-06

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: 46.73  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999      9 KVLLMGKSGSGKTSmrsiiFANYIARDTR--RLGATIDVEHSHVRFLGN------LVLNLWDCGGQDTF--MENYFtsqr 78
Cdd:pfam08477   1 KVVLLGDSGVGKTS-----LLKRFVDDTFdpKYKSTIGVDFKTKTVLENddngkkIKLNIWDTAGQERFrsLHPFY---- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 5729999     79 dniFRNVEVLIYVFDVESrelEKDMHYYQSCLEAILQNSPdakIFCLVHKMD 130
Cdd:pfam08477  72 ---YRGAAAALLVYDSRT---FSNLKYWLRELKKYAGNSP---VILVGNKID 114
PLN03118 PLN03118
Rab family protein; Provisional
 9-163 1.36e-06

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 48.13  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999     9 KVLLMGKSGSGKTSMrsiiFANYIARDTRRLGATIDVEHSHVRFL---GNLVLNLWDCGGQDTFmeNYFTSqrdNIFRNV 85
Cdd:PLN03118  16 KILLIGDSGVGKSSL----LVSFISSSVEDLAPTIGVDFKIKQLTvggKRLKLTIWDTAGQERF--RTLTS---SYYRNA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    86 EVLIYVFDVESREL--------EKDMHYY---QSCLEAILQNSPDakifclvhkmdlvQEDQRDLifkEREEDLrRLSRP 154
Cdd:PLN03118  87 QGIILVYDVTRRETftnlsdvwGKEVELYstnQDCVKMLVGNKVD-------------RESERDV---SREEGM-ALAKE 149


                 ....*....
gi 5729999   155 LECACFRTS 163
Cdd:PLN03118 150 HGCLFLECS 158
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 9-139 2.97e-06

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: 46.42  E-value: 2.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRsiifaNYIAR-DTRRLGATI-----DVEHSHVRFlgnlvlNLWDCGGQDTFM---ENYftsqrd 79
Cdd:cd00878   1 RILMLGLDGAGKTTIL-----YKLKLgEVVTTIPTIgfnveTVEYKNVKF------TVWDVGGQDKIRplwKHY------ 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5729999   80 niFRNVEVLIYVFDVESRElekdmHYYQSC--LEAILQNSP--DAKIFCLVHKMDL-----VQEDQRDL 139
Cdd:cd00878  64 --YENTDGLIFVVDSSDRE-----RIEEAKneLHKLLNEEElkGAPLLILANKQDLpgaltESELIELL 125
RabL3 cd04102
Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins ...
 9-113 5.18e-06

Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL3 lacks a prenylation site at the C-terminus. The specific function of RabL3 remains unknown.


Pssm-ID: 206689  Cd Length: 204  Bit Score: 46.43  E-value: 5.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFAN-YIARDTRRLGATIDVEHSHVRFLG----NLVLNLWDCGGQDTFMENYfTSQRDNIFR 83
Cdd:cd04102   2 KVLVLGDSGVGKSSLVHLLCKNqVLGNPSWTVGCSVDVRHHTYGEGTpeekTFYVELWDVGGSVGSAESV-KSTRAVFYN 80

                        90       100       110
                ....*....|....*....|....*....|
gi 5729999   84 NVEVLIYVFDVESRELEKDMhyYQSCLEAI 113
Cdd:cd04102  81 QINGIIFVHDLTNKKSSQNL--YRWSLEAL 108
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 1-133 5.07e-05

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: 43.15  E-value: 5.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    1 MPNTAMKKKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATI-DVEHSHVRflgnlvLNLWDCGGQDT---FMENYfts 76
Cdd:cd04155   9 KPSSRQEVRILLLGLDNAGKTTILKQLASEDISHITPTQGFNIkNVQADGFK------LNVWDIGGQRKirpYWRNY--- 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5729999   77 qrdniFRNVEVLIYVFDVESRELEKDMHyyqSCLEAILQNSPDAKIFCLV--HKMDLVQ 133
Cdd:cd04155  80 -----FENTDVLIYVIDSADRKRFEEAG---QELVELLEEEKLAGVPVLVfaNKQDLLT 130
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 11-132 2.10e-04

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They 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. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 40.79  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   11 LLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVeHSHVRFLGNLVLNLWDCGGQDtfmENYFTSQR-----DNIFRNV 85
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFGTEVAAVGDRRPTTRAA-QAYVWQTGGDGLVLLDLPGVG---ERGRRDREyeelyRRLLPEA 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 5729999   86 EVLIYVFDVESRELEKDMHYYQSCLEAilqnsPDAKIFCLVHKMDLV 132
Cdd:cd11383  77 DLVLWLLDADDRALAADHDFYLLPLAG-----HDAPLLFVLNQVDPV 118
YeeP COG3596
Predicted GTPase [General function prediction only];
10-211 2.40e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 42.06  E-value: 2.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   10 VLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQR-DNIFRNVEVL 88
Cdd:COG3596  42 IALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLPGLVLLDTPGLGEVNERDREYRElRELLPEADLI 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   89 IYVFDVESRELEKDMHYYQscleAILQNSPDAKIFCLVHKMDLV---QEDQR--DLIFKEREEDLRRL----SRPLECAC 159
Cdd:COG3596 122 LWVVKADDRALATDEEFLQ----ALRAQYPDPPVLVVLTQVDRLepeREWDPpyNWPSPPKEQNIRRAleaiAEQLGVPI 197

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999  160 FR----TSIWDETLY---KAWSSIVyQLIPNVQQLEMnLRNF-AQIIEADEVLLFERATF 211
Cdd:COG3596 198 DRvipvSAAEDRTGYgleELVDALA-EALPEAKRSRL-ARLLrAKAIDRYTLLAAAAALL 255
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 9-136 3.19e-04

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: 40.52  E-value: 3.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTsmrSII--FANYIARDTRRlgATIDVEHSH--VRFLGNLV-LNLWDCGGQDTFMenyftSQRDNIFR 83
Cdd:cd00154   2 KIVLIGDSGVGKT---SLLlrFVDNKFSENYK--STIGVDFKSktIEVDGKKVkLQIWDTAGQERFR-----SITSSYYR 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5729999   84 NVEVLIYVFDVESRE-LEKDMHYYQsclEAILQNSPDAKIFCLVHKMDLVQEDQ 136
Cdd:cd00154  72 GAHGAILVYDVTNREsFENLDKWLN---ELKEYAPPNIPIILVGNKSDLEDERQ 122
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 9-163 4.33e-04

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras 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 Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 40.20  E-value: 4.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTS-----MRSIIFANYIAR--DTRRLGATIDVEHSHvrflgnlvLNLWDCGGQDTFmenyfTSQRDNI 81
Cdd:cd00876   1 KLVVLGAGGVGKSAltirfVSGEFVEEYDPTieDSYRKQIVVDGETYT--------LDILDTAGQEEF-----SAMRDQY 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   82 FRNVEVLIYVFDVESRE-LEKDMHYYQSCLEAILQNSPdakIFCLV-HKMDLVqedqrdlifKERE---EDLRRLSRPLE 156
Cdd:cd00876  68 IRNGDGFILVYSITSREsFEEIKNIREQILRVKDKEDV---PIVLVgNKCDLE---------NERQvstEEGEALAEEWG 135


                ....*..
gi 5729999  157 CACFRTS 163
Cdd:cd00876 136 CPFLETS 142
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 9-156 4.58e-04

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 40.01  E-value: 4.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTS-----MRSIIFANYIARDtrrlGATIDVEHSHVRFLGNLVLNLWDCGGQDTFmenYFTSQrdnIF- 82
Cdd:cd09914   3 KLMLVGQGGVGKTSlckqlIGEKFDGDESSTH----GINVQDWKIPAPERKKIRLNVWDFGGQEIY---HATHQ---FFl 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5729999   83 RNVEVLIYVFDVESRELEKDMHYYQSCLEAilqNSPDAKIFCLVHKMDlVQEDQRDLifkerEEDLRRLSRPLE 156
Cdd:cd09914  73 TSRSLYLLVFDLRTGDEVSRVPYWLRQIKA---FGGVSPVILVGTHID-ESCDEDIL-----KKALNKKFPAII 137
Rho4_like cd04132
Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a ...
 7-97 6.11e-04

Ras homology family 4 (Rho4) of small guanosine triphosphatases (GTPases)-like; Rho4 is a GTPase that controls septum degradation by regulating secretion of Eng1 or Agn1 during cytokinesis. Rho4 also plays a role in cell morphogenesis. Rho4 regulates septation and cell morphology by controlling the actin cytoskeleton and cytoplasmic microtubules. The localization of Rho4 is modulated by Rdi1, which may function as a GDI, and by Rga9, which is believed to function as a GAP. In S. pombe, both Rho4 deletion and Rho4 overexpression result in a defective cell wall, suggesting a role for Rho4 in maintaining cell wall integrity. 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.


Pssm-ID: 206704 [Multi-domain]  Cd Length: 197  Bit Score: 40.02  E-value: 6.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    7 KKKVLLMGKSGSGKTSMRSI-------------IFANYIArdtrrlgaTIDVEHSHVrflgnLVLNLWDCGGQdtfmENY 73
Cdd:cd04132   3 KVKIVVVGDGGCGKTCLLMVyaqgsfpeeyvptVFENYVT--------TLQVPNGKI-----IELALWDTAGQ----EDY 65

                        90       100
                ....*....|....*....|....
gi 5729999   74 fTSQRDNIFRNVEVLIYVFDVESR 97
Cdd:cd04132  66 -DRLRPLSYPDVDVILICYSVDNP 88
PLN00023 PLN00023
GTP-binding protein; Provisional
 9-97 1.46e-03

GTP-binding protein; Provisional


Pssm-ID: 177661  Cd Length: 334  Bit Score: 39.85  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999     9 KVLLMGKSGSGKTSMRSIIF-ANYIARDTRRLGATIDVEHSHVRFLG------------NLVLNLWDCGGQDTFME--NY 73
Cdd:PLN00023  23 RVLVVGDSGVGKSSLVHLIVkGSSIARPPQTIGCTVGVKHITYGSPGsssnsikgdserDFFVELWDVSGHERYKDcrSL 102

                         90       100
                 ....*....|....*....|....
gi 5729999    74 FTSQRDNIfrnvevlIYVFDVESR 97
Cdd:PLN00023 103 FYSQINGV-------IFVHDLSQR 119
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
 9-167 2.47e-03

Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signaling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133306 [Multi-domain]  Cd Length: 162  Bit Score: 37.81  E-value: 2.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRlgaTIDVEHSH----VRFLGNLV-LNLWDCGGQDTfmenyFTSQRDNIFR 83
Cdd:cd04106   2 KVIVVGNGNVGKSSMIQRFVKGIFTKDYKK---TIGVDFLEkqifLRQSDEDVrLMLWDTAGQEE-----FDAITKAYYR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   84 NVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPDAkifcLVH-KMDLVqeDQRDLIFKEREedlrRLSRPLECACFRT 162
Cdd:cd04106  74 GAQACILVFSTTDRESFEAIESWKEKVEAECGDIPMV----LVQtKIDLL--DQAVITNEEAE----ALAKRLQLPLFRT 143


                ....*
gi 5729999  163 SIWDE 167
Cdd:cd04106 144 SVKDD 148
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
 1-97 3.17e-03

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 38.14  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999     1 MPNTAMKKKVLLMGKSGSGKTSM--RSII--F-ANYIArdtrrlgaTIDVEHSHVRF---LGNLVLNLWDCGGQDTfmen 72
Cdd:PTZ00132   3 QMDEVPEFKLILVGDGGVGKTTFvkRHLTgeFeKKYIP--------TLGVEVHPLKFytnCGPICFNVWDTAGQEK---- 70

                         90       100
                 ....*....|....*....|....*
gi 5729999    73 yFTSQRDNIFRNVEVLIYVFDVESR 97
Cdd:PTZ00132  71 -FGGLRDGYYIKGQCAIIMFDVTSR 94
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 9-98 4.34e-03

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


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 37.20  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999      9 KVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATID-VEHshvrflGNLVLNLWDCGGQDT---FMENYftsqrdniFRN 84
Cdd:pfam00025   2 RILILGLDNAGKTTILYKLKLGEIVTTIPTIGFNVEtVTY------KNVKFTVWDVGGQESlrpLWRNY--------FPN 67

                          90
                  ....*....|....
gi 5729999     85 VEVLIYVFDVESRE 98
Cdd:pfam00025  68 TDAVIFVVDSADRD 81
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
 9-146 4.51e-03

Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206655 [Multi-domain]  Cd Length: 172  Bit Score: 37.26  E-value: 4.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSmrsiIFANYI-ARDTRRLGATI--DVEHSHVRFLGNLV-LNLWDCGGQDTFMenyftSQRDNIFRN 84
Cdd:cd01862   2 KVIILGDSGVGKTS----LMNQYVnKKFSNQYKATIgaDFLTKEVTVDDRLVtLQIWDTAGQERFQ-----SLGVAFYRG 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5729999   85 VEVLIYVFDV------ESRELEKDMHYYQSCleailQNSPDAKIFCLV-HKMDLvqEDQRDLIFKEREE 146
Cdd:cd01862  73 ADCCVLVYDVtnpksfESLDSWRDEFLIQAS-----PRDPENFPFVVLgNKIDL--EEKRQVSTKKAQQ 134
Rab33B_Rab33A cd04115
Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ...
 9-98 5.06e-03

Rab GTPase family 33 includes Rab33A and Rab33B; Rab33B/Rab33A subfamily. Rab33B is ubiquitously expressed in mouse tissues and cells, where it is localized to the medial Golgi cisternae. It colocalizes with alpha-mannose II. Together with the other cisternal Rabs, Rab6A and Rab6A', it is believed to regulate the Golgi response to stress and is likely a molecular target in stress-activated signaling pathways. Rab33A (previously known as S10) is expressed primarily in the brain and immune system cells. In humans, it is located on the X chromosome at Xq26 and its expression is down-regulated in tuberculosis patients. Experimental evidence suggests that Rab33A is a novel CD8+ T cell factor that likely plays a role in tuberculosis disease processes. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133315 [Multi-domain]  Cd Length: 170  Bit Score: 37.03  E-value: 5.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMrsiIFANYIARDTRRLGATIDVEHSH--VRFLG-NLVLNLWDCGGQDTFMEnyftSQRDNIFRNV 85
Cdd:cd04115   4 KIIVIGDSNVGKTCL---TYRFCAGRFPERTEATIGVDFRErtVEIDGeRIKVQLWDTAGQERFRK----SMVQHYYRNV 76

                        90
                ....*....|...
gi 5729999   86 EVLIYVFDVESRE 98
Cdd:cd04115  77 HAVVFVYDVTNMA 89
Rab36_Rab34 cd04108
Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily ...
 9-156 5.51e-03

Rab GTPase families 34 (Rab34) and 36 (Rab36); Rab34/Rab36 subfamily. Rab34, found primarily in the Golgi, interacts with its effector, Rab-interacting lysosomal protein (RILP). This enables its participation in microtubular dynenin-dynactin-mediated repositioning of lysosomes from the cell periphery to the Golgi. A Rab34 (Rah) isoform that lacks the consensus GTP-binding region has been identified in mice. This isoform is associated with membrane ruffles and promotes macropinosome formation. Rab36 has been mapped to human chromosome 22q11.2, a region that is homozygously deleted in malignant rhabdoid tumors (MRTs). However, experimental assessments do not implicate Rab36 as a tumor suppressor that would enable tumor formation through a loss-of-function mechanism. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206693 [Multi-domain]  Cd Length: 170  Bit Score: 37.16  E-value: 5.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTSMRSIIFANYIARDTRrlgATIDVEHSHVRF--LG-NLVLNLWDCGGQDTfmenyFTSQRDNIFRNV 85
Cdd:cd04108   2 KVIVVGDLSVGKTCLINRFCKDVFDKNYK---ATIGVDFEMERFevLGvPFSLQLWDTAGQER-----FKCIASTYYRGA 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5729999   86 EVLIYVFDVES-RELEkdmHYYQSCLEAILQNSPDAKIFCLV-HKMDLVQEDQRDLIfkerEEDLRRLSRPLE 156
Cdd:cd04108  74 QAIIIVFDLTDvASLE---HTRQWLEDALKENDPSSVLLFLVgTKKDLSSPAQYALM----EQDAIKLAREMK 139
Rho3 cd04134
Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of ...
 8-158 5.87e-03

Ras homology family 3 (Rho3) of small guanosine triphosphatases (GTPases); Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. 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.


Pssm-ID: 206706 [Multi-domain]  Cd Length: 185  Bit Score: 37.15  E-value: 5.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    8 KKVLLMGKSGSGKTSMRSIIFANYIardTRRLGATIDVEHSHVRFL-GNLV-LNLWDCGGQDTfmenyFTSQRDNIFRNV 85
Cdd:cd04134   1 RKVVVLGDGACGKTSLLNVFTRGYF---PQVYEPTVFENYIHDIFVdGLAVeLSLWDTAGQEE-----FDRLRSLSYADT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   86 EVLIYVFDVESRE-LEKDMHYYqscLEAILQNSPDAKIFCLVHKMDL-----VQEDQRDLIfkEREEDL---RRL--SRP 154
Cdd:cd04134  73 HVIMLCFSVDNPDsLENVESKW---LAEIRHHCPGVKLVLVALKCDLreprnERDRGTHTI--SYEEGLavaKRInaCRY 147


                ....
gi 5729999  155 LECA 158
Cdd:cd04134 148 LECS 151
Rab32_Rab38 cd04107
Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are ...
 9-69 5.87e-03

Rab GTPase families 18 (Rab18) and 32 (Rab32); Rab38/Rab32 subfamily. Rab32 and Rab38 are members of the Rab family of small GTPases. Human Rab32 was first identified in platelets but it is expressed in a variety of cell types, where it functions as an A-kinase anchoring protein (AKAP). Rab38 has been shown to be melanocyte-specific. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206692 [Multi-domain]  Cd Length: 201  Bit Score: 37.29  E-value: 5.87e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5729999    9 KVLLMGKSGSGKTsmrSII--FANYIARDTRRlgATIDVEHShVRFL----GNLV-LNLWDCGGQDTF 69
Cdd:cd04107   2 KVLVIGDLGVGKT---SIIkrYVHGVFSQHYK--ATIGVDFA-LKVIewdpNTVVrLQLWDIAGQERF 63
Rab18 cd01863
Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic ...
 9-98 5.90e-03

Rab GTPase family 18 (Rab18); Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206656 [Multi-domain]  Cd Length: 161  Bit Score: 36.91  E-value: 5.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999    9 KVLLMGKSGSGKTS-MRSiiFANYIARDtrRLGATIDVEHShVRFLG----NLVLNLWDCGGQDTFmeNYFTSqrdNIFR 83
Cdd:cd01863   2 KILLIGDSGVGKSSlLLR--FTDDTFDE--DLSSTIGVDFK-VKTVTvdgkKVKLAIWDTAGQERF--RTLTS---SYYR 71

                        90
                ....*....|....*
gi 5729999   84 NVEVLIYVFDVESRE 98
Cdd:cd01863  72 GAQGVILVYDVTRRD 86
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 12-98 9.47e-03

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: 36.14  E-value: 9.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5729999   12 LMGKSGSGKTSMRSIIFANYIARDTRrlgATIDVEHSHVRfLGNLVLNLWDCGGQDTfmenyFTSQRDNIFRNVEVLIYV 91
Cdd:cd04159   4 LVGLQNSGKTTLVNVIASGQFSEDTI---PTVGFNMRKVT-KGNVTIKVWDLGGQPR-----FRSMWERYCRGVNAIVYV 74


                ....*..
gi 5729999   92 FDVESRE 98
Cdd:cd04159  75 VDAADRE 81
 
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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