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Conserved domains on  [gi|18399081|ref|NP_564431|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

AIG1 domain-containing protein( domain architecture ID 10518548)

AIG1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 25-239 8.65e-92

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


:

Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 272.56  E-value: 8.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    25 RTLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVQeDGDIINVVDTPGLFDLSTAADFIGKEIVRCISL 104
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTW-DGRIINVIDTPGLFDLSVSNDFISKEIIRCLLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   105 AEDGIHAILLVFSVRRLAEEEQTVLSFLQALFGSKIADYMIVVFTGGDelEENEETLEEYLADYCPEFLKEILgicdnrl 184
Cdd:pfam04548  80 AEPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKD--DLEDDSLDDYLSDGCPEFLKEVL------- 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18399081   185 vlfnnKTTDKVKKAEQVQKLLSLVESVVKQNNGKPYSDELFHELQEEAIKLRDQK 239
Cdd:pfam04548 151 -----RTADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGERLREQQ 200
PTZ00121 super family cl31754
MAEBL; Provisional
 193-335 6.93e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   193 DKVKKAEQVQKLLSLV-----ESVVKQNNGKPYSDELFHELQEEAIKLRDQKKEVELLQgysNNEIDEFKKQIDMSYDRQ 267
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLkkkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK---KAEEDEKKAAEALKKEAE 1699

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   268 LSRITEMVETKLRDTAKRLEQQLGEEQAARLEAE--KRANEVQKRSSDEIKKLRENLERAEKETKELQKK 335
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEeaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
 
Name Accession Description Interval E-value
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 25-239 8.65e-92

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 272.56  E-value: 8.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    25 RTLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVQeDGDIINVVDTPGLFDLSTAADFIGKEIVRCISL 104
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTW-DGRIINVIDTPGLFDLSVSNDFISKEIIRCLLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   105 AEDGIHAILLVFSVRRLAEEEQTVLSFLQALFGSKIADYMIVVFTGGDelEENEETLEEYLADYCPEFLKEILgicdnrl 184
Cdd:pfam04548  80 AEPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKD--DLEDDSLDDYLSDGCPEFLKEVL------- 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18399081   185 vlfnnKTTDKVKKAEQVQKLLSLVESVVKQNNGKPYSDELFHELQEEAIKLRDQK 239
Cdd:pfam04548 151 -----RTADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGERLREQQ 200
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 25-230 9.84e-92

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 272.49  E-value: 9.84e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  25 RTLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVQeDGDIINVVDTPGLFDLSTAADFIGKEIVRCISL 104
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVW-DGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 105 AEDGIHAILLVFSVRRLAEEEQTVLSFLQALFGSKIADYMIVVFTGGDELEENEETleeylaDY---CPEFLKEILGICD 181
Cdd:cd01852  80 SAPGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLE------DYledSCEALKRLLEKCG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18399081 182 NRLVLFNNKTTDKvKKAEQVQKLLSLVESVVKQNNGKPYSDELFHELQE 230
Cdd:cd01852 154 GRYVAFNNKAKGR-EQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
YeeP COG3596
Predicted GTPase [General function prediction only];
26-149 3.70e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 3.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  26 TLVLVGRTGNGKSATGNSILGrkafRSRART-VGVTSTCESQRVV--QEDGDIINVVDTPGLFDlSTAADFIGKEIVRCI 102
Cdd:COG3596  41 VIALVGKTGAGKSSLINALFG----AEVAEVgVGRPCTREIQRYRleSDGLPGLVLLDTPGLGE-VNERDREYRELRELL 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18399081 103 SLAedgiHAILLVFSVRRLAeeEQTVLSFLQALFGSKIADYMIVVFT 149
Cdd:COG3596 116 PEA----DLILWVVKADDRA--LATDEEFLQALRAQYPDPPVLVVLT 156
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 26-92 3.44e-06

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 48.80  E-value: 3.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399081    26 TLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVQedGDIINVVDTPGLfdLSTAAD 92
Cdd:TIGR00993 120 NILVLGKSGVGKSATINSIFGEVKFSTDAFGMGTTSVQEIEGLVQ--GVKIRVIDTPGL--KSSASD 182
PTZ00121 PTZ00121
MAEBL; Provisional
 193-335 6.93e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   193 DKVKKAEQVQKLLSLV-----ESVVKQNNGKPYSDELFHELQEEAIKLRDQKKEVELLQgysNNEIDEFKKQIDMSYDRQ 267
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLkkkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK---KAEEDEKKAAEALKKEAE 1699

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   268 LSRITEMVETKLRDTAKRLEQQLGEEQAARLEAE--KRANEVQKRSSDEIKKLRENLERAEKETKELQKK 335
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEeaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
227-336 8.92e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 8.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 227 ELQEEAIKLRDQKKEVELLQGYsnneIDEFKKQIDmsydrqlsritemvetKLRDTAKRLEQQLGEEQAARLEAEKRANE 306
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAE----VEELEAELE----------------EKDERIERLERELSEARSEERREIRKDRE 466

                        90       100       110
                ....*....|....*....|....*....|
gi 18399081 307 VQKRSSdEIKKLRENLERAEKETKELQKKL 336
Cdd:COG2433 467 ISRLDR-EIERLERELEEERERIEELKRKL 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 227-336 2.83e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    227 ELQEEAIKLRDQKKEVELlqGYSNNEIDEFKKQIDmSYDRQLSRITEMVEtKLRDTAKRLEQQLGEEQAARLEAEKRANE 306
Cdd:TIGR02168  210 EKAERYKELKAELRELEL--ALLVLRLEELREELE-ELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIEE 285

                           90       100       110
                   ....*....|....*....|....*....|...
gi 18399081    307 VQKR---SSDEIKKLRENLERAEKETKELQKKL 336
Cdd:TIGR02168  286 LQKElyaLANEISRLEQQKQILRERLANLERQL 318
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 275-338 7.22e-04

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 40.43  E-value: 7.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18399081 275 VETKLRDTAKRLEQQLGEEQAARLEAEKRA-NEVQKRSSDEIKKLRENLERAEKETKELQKKLGK 338
Cdd:cd07605  80 IEASLEQVAKAFHGELILPLEKKLELDQKViNKFEKDYKKEYKQKREDLDKARSELKKLQKKSQK 144
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 213-335 1.15e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   213 KQNNGKPYSDELFHELQE--EAIKLRDQKKEVELLQgysnNEIDEFKKQIDMSYDRQLSRITEmveTKLRDTAKRLEQQL 290
Cdd:pfam15709 367 QLERAEKMREELELEQQRrfEEIRLRKQRLEEERQR----QEEEERKQRLQLQAAQERARQQQ---EEFRRKLQELQRKK 439

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18399081   291 GEEQAARLEAEK-RANEVQKRSSDEIKKLrenLERAEKETKELQKK 335
Cdd:pfam15709 440 QQEEAERAEAEKqRQKELEMQLAEEQKRL---MEMAEEERLEYQRQ 482
 
Name Accession Description Interval E-value
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 25-239 8.65e-92

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 272.56  E-value: 8.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    25 RTLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVQeDGDIINVVDTPGLFDLSTAADFIGKEIVRCISL 104
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTW-DGRIINVIDTPGLFDLSVSNDFISKEIIRCLLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   105 AEDGIHAILLVFSVRRLAEEEQTVLSFLQALFGSKIADYMIVVFTGGDelEENEETLEEYLADYCPEFLKEILgicdnrl 184
Cdd:pfam04548  80 AEPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKD--DLEDDSLDDYLSDGCPEFLKEVL------- 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18399081   185 vlfnnKTTDKVKKAEQVQKLLSLVESVVKQNNGKPYSDELFHELQEEAIKLRDQK 239
Cdd:pfam04548 151 -----RTADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGERLREQQ 200
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 25-230 9.84e-92

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 272.49  E-value: 9.84e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  25 RTLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVQeDGDIINVVDTPGLFDLSTAADFIGKEIVRCISL 104
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVW-DGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 105 AEDGIHAILLVFSVRRLAEEEQTVLSFLQALFGSKIADYMIVVFTGGDELEENEETleeylaDY---CPEFLKEILGICD 181
Cdd:cd01852  80 SAPGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLE------DYledSCEALKRLLEKCG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 18399081 182 NRLVLFNNKTTDKvKKAEQVQKLLSLVESVVKQNNGKPYSDELFHELQE 230
Cdd:cd01852 154 GRYVAFNNKAKGR-EQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 28-206 3.44e-08

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: 52.07  E-value: 3.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  28 VLVGRTGNGKSATGNSILGRKaFRSRARTVGVTSTCESQRV-VQEDGDIINVVDTPGLFdlstaaDFIGKEIVRCISLAE 106
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGE-VGEVSDVPGTTRDPDVYVKeLDKGKVKLVLVDTPGLD------EFGGLGREELARLLL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 107 DGIHAILLVFSVRRLAEEEQTVLSFLQALFGSKIadYMIVVFTGGDELEENEETLeeyladycPEFLKEILGICDNRLVL 186
Cdd:cd00882  74 RGADLILLVVDSTDRESEEDAKLLILRRLRKEGI--PIILVGNKIDLLEEREVEE--------LLRLEELAKILGVPVFE 143

                       170       180
                ....*....|....*....|
gi 18399081 187 FNNKTTDKVKkaEQVQKLLS 206
Cdd:cd00882 144 VSAKTGEGVD--ELFEKLIE 161
YeeP COG3596
Predicted GTPase [General function prediction only];
26-149 3.70e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 3.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  26 TLVLVGRTGNGKSATGNSILGrkafRSRART-VGVTSTCESQRVV--QEDGDIINVVDTPGLFDlSTAADFIGKEIVRCI 102
Cdd:COG3596  41 VIALVGKTGAGKSSLINALFG----AEVAEVgVGRPCTREIQRYRleSDGLPGLVLLDTPGLGE-VNERDREYRELRELL 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18399081 103 SLAedgiHAILLVFSVRRLAeeEQTVLSFLQALFGSKIADYMIVVFT 149
Cdd:COG3596 116 PEA----DLILWVVKADDRA--LATDEEFLQALRAQYPDPPVLVVLT 156
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 26-149 6.05e-08

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 53.09  E-value: 6.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  26 TLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVqeDGDIINVVDTPGLfdLSTAADFIGKEIVRCIS-- 103
Cdd:cd01853  33 TILVLGKTGVGKSSTINSIFGERKVSVSAFQSETLRPREVSRTV--DGFKLNIIDTPGL--LESQDQRVNRKILSIIKrf 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 18399081 104 LAEDGIHAILLV--FSVRRLAEEEQTVLSFLQALFGSKIADYMIVVFT 149
Cdd:cd01853 109 LKKKTIDVVLYVdrLDMYRVDNLDVPLLRAITDSFGPSIWRNAIVVLT 156
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 26-92 3.44e-06

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 48.80  E-value: 3.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399081    26 TLVLVGRTGNGKSATGNSILGRKAFRSRARTVGVTSTCESQRVVQedGDIINVVDTPGLfdLSTAAD 92
Cdd:TIGR00993 120 NILVLGKSGVGKSATINSIFGEVKFSTDAFGMGTTSVQEIEGLVQ--GVKIRVIDTPGL--KSSASD 182
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 28-149 1.76e-05

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 44.54  E-value: 1.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  28 VLVGRTGNGKSATGNSILGRKAFRSrARTVGVTSTCESQRVVQEDGDIINVVDTPGLFDLSTAADFIGKEIVRcislAED 107
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIV-SPIPGTTRDPVRKEWELLPLGPVVLIDTPGLDEEGGLGRERVEEARQ----VAD 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18399081 108 GIHAILLVFSVRRLAEEEQTVlsfLQALFGSKIAdyMIVVFT 149
Cdd:cd00880  76 RADLVLLVVDSDLTPVEEEAK---LGLLRERGKP--VLLVLN 112
PTZ00121 PTZ00121
MAEBL; Provisional
 193-335 6.93e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   193 DKVKKAEQVQKLLSLV-----ESVVKQNNGKPYSDELFHELQEEAIKLRDQKKEVELLQgysNNEIDEFKKQIDMSYDRQ 267
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLkkkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK---KAEEDEKKAAEALKKEAE 1699

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   268 LSRITEMVETKLRDTAKRLEQQLGEEQAARLEAE--KRANEVQKRSSDEIKKLRENLERAEKETKELQKK 335
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEeaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
227-336 8.92e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 8.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 227 ELQEEAIKLRDQKKEVELLQGYsnneIDEFKKQIDmsydrqlsritemvetKLRDTAKRLEQQLGEEQAARLEAEKRANE 306
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAE----VEELEAELE----------------EKDERIERLERELSEARSEERREIRKDRE 466

                        90       100       110
                ....*....|....*....|....*....|
gi 18399081 307 VQKRSSdEIKKLRENLERAEKETKELQKKL 336
Cdd:COG2433 467 ISRLDR-EIERLERELEEERERIEELKRKL 495
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 26-149 9.48e-05

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: 41.07  E-value: 9.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    26 TLVLVGRTGNGKSATGNSILGRKAFRSraRTVGVTsTCESQRVVQEDGDIINVVDTPGLFDLSTAADFIGKEIVRCISla 105
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVS--DYPGTT-RDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 18399081   106 EDGIhaILLVFSVRRLAEEEQTVLSFLQalfgsKIADYMIVVFT 149
Cdd:pfam01926  76 ADLI--LFVVDSEEGITPLDEELLELLR-----ENKKPIILVLN 112
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 227-336 2.83e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    227 ELQEEAIKLRDQKKEVELlqGYSNNEIDEFKKQIDmSYDRQLSRITEMVEtKLRDTAKRLEQQLGEEQAARLEAEKRANE 306
Cdd:TIGR02168  210 EKAERYKELKAELRELEL--ALLVLRLEELREELE-ELQEELKEAEEELE-ELTAELQELEEKLEELRLEVSELEEEIEE 285

                           90       100       110
                   ....*....|....*....|....*....|...
gi 18399081    307 VQKR---SSDEIKKLRENLERAEKETKELQKKL 336
Cdd:TIGR02168  286 LQKElyaLANEISRLEQQKQILRERLANLERQL 318
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 26-97 3.76e-04

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 41.76  E-value: 3.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  26 TLVLVGRTGNGKSATGNSILGRKAFRSR---ARTVGVTSTCE--SQRVVQEDGDI---INVVDTPGLfdlstaADFIGKE 97
Cdd:cd01850   6 NIMVVGESGLGKSTFINTLFGTKLYPSKyppAPGEHITKTVEikISKAELEENGVklkLTVIDTPGF------GDNINNS 79
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
 275-338 7.22e-04

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 40.43  E-value: 7.22e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18399081 275 VETKLRDTAKRLEQQLGEEQAARLEAEKRA-NEVQKRSSDEIKKLRENLERAEKETKELQKKLGK 338
Cdd:cd07605  80 IEASLEQVAKAFHGELILPLEKKLELDQKViNKFEKDYKKEYKQKREDLDKARSELKKLQKKSQK 144
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
 3-149 8.41e-04

GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding proteins, Nucleosides, purines and pyrimidines]


Pssm-ID: 130064  Cd Length: 313  Bit Score: 40.65  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081     3 LLDMGGDMMEDDwefASSsnpkRTLVLVGRTGNGKSATGNSILGRK-----AFRSRA-RTVGVTSTcesqrvvqEDGDII 76
Cdd:TIGR00991  24 LLELLGKLKEED---VSS----LTILVMGKGGVGKSSTVNSIIGERiatvsAFQSEGlRPMMVSRT--------RAGFTL 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18399081    77 NVVDTPGLFDlstaADFIGKEIVRCIS--LAEDGIHAILLV--FSVRRLAEEEQTVLSFLQALFGSKIADYMIVVFT 149
Cdd:TIGR00991  89 NIIDTPGLIE----GGYINDQAVNIIKrfLLGKTIDVLLYVdrLDAYRVDTLDGQVIRAITDSFGKDIWRKSLVVLT 161
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 213-335 1.15e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   213 KQNNGKPYSDELFHELQE--EAIKLRDQKKEVELLQgysnNEIDEFKKQIDMSYDRQLSRITEmveTKLRDTAKRLEQQL 290
Cdd:pfam15709 367 QLERAEKMREELELEQQRrfEEIRLRKQRLEEERQR----QEEEERKQRLQLQAAQERARQQQ---EEFRRKLQELQRKK 439

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18399081   291 GEEQAARLEAEK-RANEVQKRSSDEIKKLrenLERAEKETKELQKK 335
Cdd:pfam15709 440 QQEEAERAEAEKqRQKELEMQLAEEQKRL---MEMAEEERLEYQRQ 482
PTZ00121 PTZ00121
MAEBL; Provisional
 190-335 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   190 KTTDKVKKAEQVQKLLSLV----------ESVVKQNNGKPYSDELFHELQE-----EAIKLRDQKKEVELLQGYSNNEID 254
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKkkaeeakkadEAKKKAEEAKKKADAAKKKAEEakkaaEAAKAEAEAAADEAEAAEEKAEAA 1369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   255 EFKKQIDMSYDRQLSRITEMVETKLRDTAKRLEQQLGEEQAARLEAEKRANEVQKRSSDEIKKLRENLERAEKETK--EL 332
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKadEA 1449


                  ...
gi 18399081   333 QKK 335
Cdd:PTZ00121 1450 KKK 1452
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
227-336 1.79e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  227 ELQEEAIKLRDQKKEVELLQGYSNNEIDEFKK-------QIDM-SYDRQLSRITEMVEtKLRDTAKRLEQQlgEEQAARL 298
Cdd:COG4913  621 ELEEELAEAEERLEALEAELDALQERREALQRlaeyswdEIDVaSAEREIAELEAELE-RLDASSDDLAAL--EEQLEEL 697

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18399081  299 EAE-KRANEVQKRSSDEIKKLRENLERAEKETKELQKKL 336
Cdd:COG4913  698 EAElEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 194-336 2.10e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    194 KVKKAEQVQKLLSLVESVVKQNNGKPYSDELFHELQEEAIKLRDQKKEVELLQGYSNNEI---DEFKKQIDMSYDRQLSR 270
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerlEARLERLEDRRERLQQE 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18399081    271 ITEMVETKLRDTAKRLEQQLGEEQAARLEAEKRANEVQ---KRSSDEIKKLRENLERAEKETKELQKKL 336
Cdd:TIGR02168  423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLEealEELREELEEAEQALDAAERELAQLQARL 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-342 2.11e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 223 ELFHELQEE---------AIKLRDQKKEVELLQgysnNEIDEFKKQIDmSYDRQLSRITEMVETkLRDTAKRLEQQLGEE 293
Cdd:COG1196 213 ERYRELKEElkeleaellLLKLRELEAELEELE----AELEELEAELE-ELEAELAELEAELEE-LRLELEELELELEEA 286

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 18399081 294 QAARLEAEKRANEVQKRSSDEIKKLRENLERAEKETKELQKKLGKCINL 342
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
PTZ00121 PTZ00121
MAEBL; Provisional
 190-335 4.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   190 KTTDKVKKAEQVQKLLSLvesvvKQNNGKPYSDEL--FHELQE-EAIKLRDQKKEVELLQGYSNNEIDEFKKQIDMSYDR 266
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEA-----KKAEEKKKADELkkAEELKKaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18399081   267 QLSRITEMVETKLRDTAKRLEQQLGEEQAARLEAEKRANEVQKRSSDEIKKLRENLERAEKETK----ELQKK 335
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaEEAKK 1669
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 227-336 4.21e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 38.72  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   227 ELQEEAIKLRDQKKEVELLQGYSNNEIDEFKKQIDMSYDRQLSRITEMveTKLRDTAKRLEQQLGEEQAAR--LEAEKRA 304
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL--ERMKERAKKAGAQRKEEEAERkqLQAKLQQ 182

                          90       100       110
                  ....*....|....*....|....*....|...
gi 18399081   305 NEVQKRS-SDEIKKLRENLERAEKETKELQKKL 336
Cdd:pfam07888 183 TEEELRSlSKEFQELRNSLAQRDTQVLQLQDTI 215
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 28-83 4.52e-03

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: 36.93  E-value: 4.52e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18399081  28 VLVGRTGNGKSATGNSIlgrkaFRSRARTVGVTSTC--ESQRVV-QEDGDIINVVDTPG 83
Cdd:cd11383   1 GLMGKTGAGKSSLCNAL-----FGTEVAAVGDRRPTtrAAQAYVwQTGGDGLVLLDLPG 54
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
227-338 5.45e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 5.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 227 ELQEEAIKLRDQKKEVELLQgySNNEIDEFKKQIDMSYDRQLSRITEMVET--KLRDTAKRLEQQLGEEQAARLEAEKRA 304
Cdd:COG4717 348 ELQELLREAEELEEELQLEE--LEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEAL 425

                        90       100       110
                ....*....|....*....|....*....|....
gi 18399081 305 NEVQKRssDEIKKLRENLERAEKETKELQKKLGK 338
Cdd:COG4717 426 DEEELE--EELEELEEELEELEEELEELREELAE 457
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 27-83 6.95e-03

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: 36.97  E-value: 6.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18399081    27 LVLVGRTGNGKSATGNSILGRKAFRSrARTVGVTSTCESQrVVQEDGDI--INVVDTPG 83
Cdd:TIGR00231   4 IVIVGHPNVGKSTLLNSLLGNKGSIT-EYYPGTTRNYVTT-VIEEDGKTykFNLLDTAG 60
PTZ00121 PTZ00121
MAEBL; Provisional
 190-335 6.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   190 KTTDKVKKAEQVQK----LLSLVESVVKQNNGKPYSDELfHELQEEAIKLRDQKKEVEllqgySNNEIDEFKKQIDMSyd 265
Cdd:PTZ00121 1385 KKAEEKKKADEAKKkaeeDKKKADELKKAAAAKKKADEA-KKKAEEKKKADEAKKKAE-----EAKKADEAKKKAEEA-- 1456

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   266 rqlsRITEMVETKLRDTAKRLEQQLGEEQAARLEAEKRANEVQKRSSDEIKKLRENLERAEKETKELQKK 335
Cdd:PTZ00121 1457 ----KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
PTZ00121 PTZ00121
MAEBL; Provisional
 190-335 8.46e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081   190 KTTDKVKKAEQVQKLLSLvesvvKQNNGKPYSDELfHELQEEAIKLRDQKKEVEllqgYSNNEIDEFKKQIDmsydrqls 269
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEA-----KKAEEKKKADEA-KKKAEEAKKADEAKKKAE----EAKKKADAAKKKAE-------- 1339

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18399081   270 ritemvETKLRDTAKRLEQQLGEEQAARLEAEKRANEVQ----KRSSDEIKKLRENLERAE---KETKELQKK 335
Cdd:PTZ00121 1340 ------EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkeeaKKKADAAKKKAEEKKKADeakKKAEEDKKK 1406
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
222-331 8.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081  222 DELFHELQEEAIKLRDQKKEVELLQGYSNNEIDEFKKQIDMSYDRQLSRITEMVET--KLRDTAKRLEQQLGEEQAARLE 299
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEEleKRREEIKKTLEKLKEELEEREK 708

                         90       100       110
                 ....*....|....*....|....*....|..
gi 18399081  300 AEKRAnEVQKRSSDEIKKLRENLERAEKETKE 331
Cdd:PRK03918 709 AKKEL-EKLEKALERVEELREKVKKYKALLKE 739
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 223-336 9.35e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.13  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    223 ELFHELQEEAIKLRDQKKEVELLQGYSNNEIDEFKKQIDMSYDRQLSRITEmvETKLRDTAKRLEQQLGEEQAARLEAEK 302
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE--LDRLQEELQRLSEELADLNAAIAGIEA 434

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 18399081    303 RANEVQKRSSD---EIKKLRENLERAEKETKELQKKL 336
Cdd:TIGR02169  435 KINELEEEKEDkalEIKKQEWKLEQLAADLSKYEQEL 471
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 187-341 9.38e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 38.11  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    187 FNNKTTDKVKKAEQVQKLLSLVE------------SVVKQNNGKPYSDELFHELQEEAIKLRD-QKKEVELLQGYSN--- 250
Cdd:TIGR01612  968 FDNTLIDKINELDKAFKDASLNDyeaknnelikyfNDLKANLGKNKENMLYHQFDEKEKATNDiEQKIEDANKNIPNiei 1047

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081    251 -------NEIDEFKKQIDMSYDRQLSRITEMVETKLRDTAKRLE--QQLGEEQAARLEAEKRANEVQKrSSDEIKKLREN 321
Cdd:TIGR01612 1048 aihtsiyNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEklKHYNFDDFGKEENIKYADEINK-IKDDIKNLDQK 1126

                          170       180
                   ....*....|....*....|
gi 18399081    322 LERAEKETKELQKKLGKCIN 341
Cdd:TIGR01612 1127 IDHHIKALEEIKKKSENYID 1146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 226-335 9.67e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.21  E-value: 9.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399081 226 HELQEEAIKLRDQKKEVELLQGYSNNEIDEFKKQIDMSYDRQlsritemveTKLRDTAKRLEQQLGEEQAARLEAEKRAN 305
Cdd:COG1579  64 LELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRI---------SDLEDEILELMERIEELEEELAELEAELA 134

                        90       100       110
                ....*....|....*....|....*....|
gi 18399081 306 EVQKRSSDEIKKLRENLERAEKETKELQKK 335
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAE 164
 
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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