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Conserved domains on  [gi|1678779887|ref|XP_029295984|]
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GTPase IMAP family member 8-like [Cottoperca gobio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
451-648 1.73e-88

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: 280.19  E-value: 1.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISML 530
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 531 SPGPHGILLVLQIGRFTQEERNSVELIKKVFGKKSGNFIIIIFTRGEELKDTTIESYIDDCDDFLKKLINDCGGRYQVFN 610
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1678779887 611 N--NNQTDRTQVRELIKKSNNMLKENGGSCYTSEMFEEAE 648
Cdd:cd01852   161 NkaKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAE 200
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
227-413 4.00e-41

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd01852:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 201  Bit Score: 149.99  E-value: 4.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 227 LNLVLCGRRGARKTSAAKAILGETEFHSASNSS----ECVKHQGEVCGRWLSLVELPALF--EKPQEEVMEESFRCISLC 300
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASgvtkTCQKESAVWDGRRVNVIDTPGLFdtSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 301 DPeGVHAFILVLPVGPLTDEDKGELETIQNTFSSRVNDFTMILFTVESDPTAPDVDNFVKEN-KDIQELRQSCGGRYVVL 379
Cdd:cd01852    81 AP-GPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDScEALKRLLEKCGGRYVAF 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1678779887 380 NIK-----DQQQIPQLLDAVEEMRVEES---FTLKMFTKAQM 413
Cdd:cd01852   160 NNKakgreQEQQVKELLAKVEEMVRENGgkpYTNEMYEEAEE 201
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
28-211 3.06e-27

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd01852:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 201  Bit Score: 109.93  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  28 LRVVLLGNSWSERSSVGNWILGETVFNTEEEP----DRCVRVRGQVKRKEIVLINTPDLMHANISEDKLTEHVNSCVRLS 103
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSAsgvtKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 104 APGPHVFLLLLQSEDFTEEKNTKLCRTLEKFSDRWFDHSLILISapREE--SSGVMEEYMEH--PPLQEVIRRCSFRYL- 178
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFT--RGDdlEGGSLEDYLEDscEALKRLLEKCGGRYVa 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1678779887 179 -------KRKNLQRPELLTRLGQTAKEHNREPVSCDAFED 211
Cdd:cd01852   159 fnnkakgREQEQQVKELLAKVEEMVRENGGKPYTNEMYEE 198
PTZ00121 super family cl31754
MAEBL; Provisional
616-924 2.39e-07

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  616 DRTQVRELIKKSNNMLKENGGSCYTSEMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEE-IEAVKRRMEQQKTE 694
Cdd:PTZ00121  1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEkAEAAEKKKEEAKKK 1379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  695 IE--QKRTKQLKEMEENIIKEREEKRKEWEMREKEFMKKKSkEENKIKDWEQKVDKEMEQSKEDMRKQKEdwekERKDWW 772
Cdd:PTZ00121  1380 ADaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEAKKADE----AKKKAE 1454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  773 EKQYQENKQRRHEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARK--QAE 850
Cdd:PTZ00121  1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAK 1534
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678779887  851 ELNEFRKKYNKDFTALVEKHMEEIKENKLKHVREIKETEESLSQNLSSLKEKEQTENMEKRHEIEINELNQKYK 924
Cdd:PTZ00121  1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
451-648 1.73e-88

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: 280.19  E-value: 1.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISML 530
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 531 SPGPHGILLVLQIGRFTQEERNSVELIKKVFGKKSGNFIIIIFTRGEELKDTTIESYIDDCDDFLKKLINDCGGRYQVFN 610
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1678779887 611 N--NNQTDRTQVRELIKKSNNMLKENGGSCYTSEMFEEAE 648
Cdd:cd01852   161 NkaKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAE 200
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
451-648 4.99e-65

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 217.09  E-value: 4.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISML 530
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 531 SPGPHGILLVLQIGRFTQEERNSVELIKKVFGKKSGNFIIIIFTRGEELKDTTIESYI-DDCDDFLKKLINDCGGRYQVf 609
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLsDGCPEFLKEVLRTADGEEKE- 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1678779887 610 nnnnqtdrTQVRELIKKSNNMLKENGGSCYTSEMFEEAE 648
Cdd:pfam04548 160 --------EQVQQLLALVEAIVKENGGKPYTNDLYEKIK 190
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
227-413 4.00e-41

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: 149.99  E-value: 4.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 227 LNLVLCGRRGARKTSAAKAILGETEFHSASNSS----ECVKHQGEVCGRWLSLVELPALF--EKPQEEVMEESFRCISLC 300
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASgvtkTCQKESAVWDGRRVNVIDTPGLFdtSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 301 DPeGVHAFILVLPVGPLTDEDKGELETIQNTFSSRVNDFTMILFTVESDPTAPDVDNFVKEN-KDIQELRQSCGGRYVVL 379
Cdd:cd01852    81 AP-GPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDScEALKRLLEKCGGRYVAF 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1678779887 380 NIK-----DQQQIPQLLDAVEEMRVEES---FTLKMFTKAQM 413
Cdd:cd01852   160 NNKakgreQEQQVKELLAKVEEMVRENGgkpYTNEMYEEAEE 201
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
28-211 3.06e-27

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: 109.93  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  28 LRVVLLGNSWSERSSVGNWILGETVFNTEEEP----DRCVRVRGQVKRKEIVLINTPDLMHANISEDKLTEHVNSCVRLS 103
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSAsgvtKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 104 APGPHVFLLLLQSEDFTEEKNTKLCRTLEKFSDRWFDHSLILISapREE--SSGVMEEYMEH--PPLQEVIRRCSFRYL- 178
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFT--RGDdlEGGSLEDYLEDscEALKRLLEKCGGRYVa 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1678779887 179 -------KRKNLQRPELLTRLGQTAKEHNREPVSCDAFED 211
Cdd:cd01852   159 fnnkakgREQEQQVKELLAKVEEMVRENGGKPYTNEMYEE 198
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
227-412 5.11e-25

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 103.46  E-value: 5.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 227 LNLVLCGRRGARKTSAAKAILGETEFHS----ASNSSECVKHQGEVCGRWLSLVELPALFE--KPQEEVMEESFRCISLC 300
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESklraQGVTKTCQLVSRTWDGRIINVIDTPGLFDlsVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 301 DPeGVHAFILVLPVGPLTDEDKGELETIQNTFSSRVNDFTMILFTVESDPTAPDVDNFVKE--NKDIQELRQSCGGRyvv 378
Cdd:pfam04548  81 EP-GPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgcPEFLKEVLRTADGE--- 156
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1678779887 379 lniKDQQQIPQLLDAVEEMRVEES---FTLKMFTKAQ 412
Cdd:pfam04548 157 ---EKEEQVQQLLALVEAIVKENGgkpYTNDLYEKIK 190
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
28-211 4.44e-19

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 86.51  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  28 LRVVLLGNSWSERSSVGNWILGETVFNTEEEPD----RCVRVRGQVKRKEIVLINTPDLMHANISEDKLTEHVNSCVRLS 103
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQgvtkTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 104 APGPHVFLLLLQSEDFTEEKNTKLCRTLEKFSDRWFDHSLILISapREESSG--VMEEYMEHP---PLQEVIRRCSfrYL 178
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFT--RKDDLEddSLDDYLSDGcpeFLKEVLRTAD--GE 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1678779887 179 KrKNLQRPELLTRLGQTAKEHNREPVSCDAFED 211
Cdd:pfam04548 157 E-KEEQVQQLLALVEAIVKENGGKPYTNDLYEK 188
PTZ00121 PTZ00121
MAEBL; Provisional
616-924 2.39e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  616 DRTQVRELIKKSNNMLKENGGSCYTSEMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEE-IEAVKRRMEQQKTE 694
Cdd:PTZ00121  1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEkAEAAEKKKEEAKKK 1379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  695 IE--QKRTKQLKEMEENIIKEREEKRKEWEMREKEFMKKKSkEENKIKDWEQKVDKEMEQSKEDMRKQKEdwekERKDWW 772
Cdd:PTZ00121  1380 ADaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEAKKADE----AKKKAE 1454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  773 EKQYQENKQRRHEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARK--QAE 850
Cdd:PTZ00121  1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAK 1534
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678779887  851 ELNEFRKKYNKDFTALVEKHMEEIKENKLKHVREIKETEESLSQNLSSLKEKEQTENMEKRHEIEINELNQKYK 924
Cdd:PTZ00121  1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
451-562 4.98e-07

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: 53.80  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSvTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISML 530
Cdd:TIGR00993 119 LNILVLGKSGVGKSATINSIFGEVKFSTDAFGMG-TTSVQEIEGLVQGVKIRVIDTPGLKSSASDQSKNEKILSSVKKFI 197
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1678779887 531 SPGPHGIllVLQIGRFTQEERNSVEL-----IKKVFG 562
Cdd:TIGR00993 198 KKNPPDI--VLYVDRLDMQTRDSNDLpllrtITDVLG 232
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
644-914 5.69e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.59  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 644 FEEAEAAIQKEVER---ILKEKEEEMKRRMEELQRQHNEEIEAVKRRMEQQKTEIEQKRTKQLKEMEeniikereekrkE 720
Cdd:pfam17380 318 LEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQ------------M 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 721 WEMREKEFMKKKSKEENKIKDWEQKVDKEMEQSKEDMRK----QKEDWEKERKDWWEKQYQENKQRRHEEQTRLTKLQEE 796
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQiraeQEEARQREVRRLEEERAREMERVRLEEQERQQQVERL 465
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 797 YDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKynkdftALVEKHMEEIKE 876
Cdd:pfam17380 466 RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQK------AIYEEERRREAE 539
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1678779887 877 NKLKHVREIKETEESLSQNLSSLKEKEQTENMEKRHEI 914
Cdd:pfam17380 540 EERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
YeeP COG3596
Predicted GTPase [General function prediction only];
420-574 2.76e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.07  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 420 DNTNTRIKAELRDLKQKSEKRTDDNIQNRECLRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFCQKATGEIDGR 499
Cdd:COG3596     9 TERLEALKRLPQVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLP 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678779887 500 PVAVVDTPGLfDTTLSNDDVQQELVKcismLSPGPHGILLVLQIG-RFTQEERnsvELIKKVFGKKSGNFIIIIFT 574
Cdd:COG3596    89 GLVLLDTPGL-GEVNERDREYRELRE----LLPEADLILWVVKADdRALATDE---EFLQALRAQYPDPPVLVVLT 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
645-925 2.61e-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: 41.59  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  645 EEAEAAIQKEVERIlKEKEEEMKRRMEELQRQHNE---EIEAVKRRMEQQKTEIEQKRTKQ------------------- 702
Cdd:TIGR02169  687 KRELSSLQSELRRI-ENRLDELSQELSDASRKIGEiekEIEQLEQEEEKLKERLEELEEDLssleqeienvkselkelea 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  703 -LKEMEENIIKEREEKRKEWEMREKEFMKKKSKEENKIKDWEQKVDK---EMEQSKEDMRKQKEDWEKERKD------WW 772
Cdd:TIGR02169  766 rIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlrEIEQKLNRLTLEKEYLEKEIQElqeqriDL 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  773 EKQYQENKQRRHEEQTRLTKLQEE--------YDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEE 844
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEEleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  845 ARKQAEELNEfrkkYNKDFTALVEKHMEEIKENKLKHVRE----------------IKETEESLSQnLSSLKEKEQTENM 908
Cdd:TIGR02169  926 LEALEEELSE----IEDPKGEDEEIPEEELSLEDVQAELQrveeeiralepvnmlaIQEYEEVLKR-LDELKEKRAKLEE 1000
                          330
                   ....*....|....*...
gi 1678779887  909 EKRHEIE-INELNQKYKD 925
Cdd:TIGR02169 1001 ERKAILErIEEYEKKKRE 1018
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
451-648 1.73e-88

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: 280.19  E-value: 1.73e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISML 530
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 531 SPGPHGILLVLQIGRFTQEERNSVELIKKVFGKKSGNFIIIIFTRGEELKDTTIESYIDDCDDFLKKLINDCGGRYQVFN 610
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1678779887 611 N--NNQTDRTQVRELIKKSNNMLKENGGSCYTSEMFEEAE 648
Cdd:cd01852   161 NkaKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAE 200
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
451-648 4.99e-65

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 217.09  E-value: 4.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISML 530
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 531 SPGPHGILLVLQIGRFTQEERNSVELIKKVFGKKSGNFIIIIFTRGEELKDTTIESYI-DDCDDFLKKLINDCGGRYQVf 609
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLsDGCPEFLKEVLRTADGEEKE- 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1678779887 610 nnnnqtdrTQVRELIKKSNNMLKENGGSCYTSEMFEEAE 648
Cdd:pfam04548 160 --------EQVQQLLALVEAIVKENGGKPYTNDLYEKIK 190
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
227-413 4.00e-41

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: 149.99  E-value: 4.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 227 LNLVLCGRRGARKTSAAKAILGETEFHSASNSS----ECVKHQGEVCGRWLSLVELPALF--EKPQEEVMEESFRCISLC 300
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASgvtkTCQKESAVWDGRRVNVIDTPGLFdtSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 301 DPeGVHAFILVLPVGPLTDEDKGELETIQNTFSSRVNDFTMILFTVESDPTAPDVDNFVKEN-KDIQELRQSCGGRYVVL 379
Cdd:cd01852    81 AP-GPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDScEALKRLLEKCGGRYVAF 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1678779887 380 NIK-----DQQQIPQLLDAVEEMRVEES---FTLKMFTKAQM 413
Cdd:cd01852   160 NNKakgreQEQQVKELLAKVEEMVRENGgkpYTNEMYEEAEE 201
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
28-211 3.06e-27

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: 109.93  E-value: 3.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  28 LRVVLLGNSWSERSSVGNWILGETVFNTEEEP----DRCVRVRGQVKRKEIVLINTPDLMHANISEDKLTEHVNSCVRLS 103
Cdd:cd01852     1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSAsgvtKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 104 APGPHVFLLLLQSEDFTEEKNTKLCRTLEKFSDRWFDHSLILISapREE--SSGVMEEYMEH--PPLQEVIRRCSFRYL- 178
Cdd:cd01852    81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFT--RGDdlEGGSLEDYLEDscEALKRLLEKCGGRYVa 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1678779887 179 -------KRKNLQRPELLTRLGQTAKEHNREPVSCDAFED 211
Cdd:cd01852   159 fnnkakgREQEQQVKELLAKVEEMVRENGGKPYTNEMYEE 198
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
227-412 5.11e-25

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 103.46  E-value: 5.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 227 LNLVLCGRRGARKTSAAKAILGETEFHS----ASNSSECVKHQGEVCGRWLSLVELPALFE--KPQEEVMEESFRCISLC 300
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESklraQGVTKTCQLVSRTWDGRIINVIDTPGLFDlsVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 301 DPeGVHAFILVLPVGPLTDEDKGELETIQNTFSSRVNDFTMILFTVESDPTAPDVDNFVKE--NKDIQELRQSCGGRyvv 378
Cdd:pfam04548  81 EP-GPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgcPEFLKEVLRTADGE--- 156
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1678779887 379 lniKDQQQIPQLLDAVEEMRVEES---FTLKMFTKAQ 412
Cdd:pfam04548 157 ---EKEEQVQQLLALVEAIVKENGgkpYTNDLYEKIK 190
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
28-211 4.44e-19

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 86.51  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  28 LRVVLLGNSWSERSSVGNWILGETVFNTEEEPD----RCVRVRGQVKRKEIVLINTPDLMHANISEDKLTEHVNSCVRLS 103
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQgvtkTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 104 APGPHVFLLLLQSEDFTEEKNTKLCRTLEKFSDRWFDHSLILISapREESSG--VMEEYMEHP---PLQEVIRRCSfrYL 178
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFT--RKDDLEddSLDDYLSDGcpeFLKEVLRTAD--GE 156
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1678779887 179 KrKNLQRPELLTRLGQTAKEHNREPVSCDAFED 211
Cdd:pfam04548 157 E-KEEQVQQLLALVEAIVKENGGKPYTNDLYEK 188
PTZ00121 PTZ00121
MAEBL; Provisional
616-924 2.39e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  616 DRTQVRELIKKSNNMLKENGGSCYTSEMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEE-IEAVKRRMEQQKTE 694
Cdd:PTZ00121  1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEkAEAAEKKKEEAKKK 1379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  695 IE--QKRTKQLKEMEENIIKEREEKRKEWEMREKEFMKKKSkEENKIKDWEQKVDKEMEQSKEDMRKQKEdwekERKDWW 772
Cdd:PTZ00121  1380 ADaaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEAKKADE----AKKKAE 1454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  773 EKQYQENKQRRHEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARK--QAE 850
Cdd:PTZ00121  1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeEAK 1534
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678779887  851 ELNEFRKKYNKDFTALVEKHMEEIKENKLKHVREIKETEESLSQNLSSLKEKEQTENMEKRHEIEINELNQKYK 924
Cdd:PTZ00121  1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
PTZ00121 PTZ00121
MAEBL; Provisional
622-926 2.47e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  622 ELIKKSNNMLKENGGSCYTSEMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEEIEAvkrrMEQQKTEIEQKRTK 701
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA----EELKKAEEEKKKVE 1636
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  702 QLKEMEENIIKEREEKRKEWEMRE--KEFMKKKSKEENKIKDWEQKVDKEMEQSKEDMRKQKEDWEK--ERKDWWEKQYQ 777
Cdd:PTZ00121  1637 QLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKK 1716
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  778 ENKQRRHEEQTRLTKLQEeydQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRK 857
Cdd:PTZ00121  1717 KAEELKKAEEENKIKAEE---AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678779887  858 ----KYNKDFTALVEKHMEEIKENKLkHVREIKETEESLSQNLSSLKEKEQTENME-KRHEIEINELNQKYKDK 926
Cdd:PTZ00121  1794 mevdKKIKDIFDNFANIIEGGKEGNL-VINDSKEMEDSAIKEVADSKNMQLEEADAfEKHKFNKNNENGEDGNK 1866
PTZ00121 PTZ00121
MAEBL; Provisional
675-925 3.90e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  675 RQHNEEIEAVKRRMEQQKTEIEQKRTKQLKEMEENIIKEREEKRKEWEMREKEFMKKKskEENKIKDwEQKVDKEMEQSK 754
Cdd:PTZ00121  1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKA-EELKKAEEEKKK 1634
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  755 EDMRKQKEDWEKERKDWWEKQYQENKQRRHEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKK 834
Cdd:PTZ00121  1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  835 EEMKKN---YEEEARKQAEELnefRKKYNKDFTALVEKHMEEIKENKLKHvreIKETEESLSQNLSSLKEKEQTENMEKR 911
Cdd:PTZ00121  1715 KKKAEElkkAEEENKIKAEEA---KKEAEEDKKKAEEAKKDEEEKKKIAH---LKKEEEKKAEEIRKEKEAVIEEELDEE 1788
                          250
                   ....*....|....
gi 1678779887  912 HEIEINELNQKYKD 925
Cdd:PTZ00121  1789 DEKRRMEVDKKIKD 1802
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
451-562 4.98e-07

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: 53.80  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSvTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISML 530
Cdd:TIGR00993 119 LNILVLGKSGVGKSATINSIFGEVKFSTDAFGMG-TTSVQEIEGLVQGVKIRVIDTPGLKSSASDQSKNEKILSSVKKFI 197
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1678779887 531 SPGPHGIllVLQIGRFTQEERNSVEL-----IKKVFG 562
Cdd:TIGR00993 198 KKNPPDI--VLYVDRLDMQTRDSNDLpllrtITDVLG 232
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
644-914 5.69e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.59  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 644 FEEAEAAIQKEVER---ILKEKEEEMKRRMEELQRQHNEEIEAVKRRMEQQKTEIEQKRTKQLKEMEeniikereekrkE 720
Cdd:pfam17380 318 LEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQ------------M 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 721 WEMREKEFMKKKSKEENKIKDWEQKVDKEMEQSKEDMRK----QKEDWEKERKDWWEKQYQENKQRRHEEQTRLTKLQEE 796
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQiraeQEEARQREVRRLEEERAREMERVRLEEQERQQQVERL 465
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 797 YDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKynkdftALVEKHMEEIKE 876
Cdd:pfam17380 466 RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQK------AIYEEERRREAE 539
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1678779887 877 NKLKHVREIKETEESLSQNLSSLKEKEQTENMEKRHEI 914
Cdd:pfam17380 540 EERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
454-592 1.60e-06

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: 48.78  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 454 VLIGKTGNGKSATANTILGQKRFKsTASSKSVTKFCQKATGEIDG-RPVAVVDTPGLFDTtlsnDDVQQELVKCISMLSP 532
Cdd:cd00880     1 AIFGRPNVGKSSLLNALLGQNVGI-VSPIPGTTRDPVRKEWELLPlGPVVLIDTPGLDEE----GGLGRERVEEARQVAD 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678779887 533 GPHGILLVLQIGRFTQEERNSVELIKKVfGKKsgnfIIIIFTR--------GEELKDTTIESYIDDCD 592
Cdd:cd00880    76 RADLVLLVVDSDLTPVEEEAKLGLLRER-GKP----VLLVLNKidlvpeseEEELLRERKLELLPDLP 138
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
452-575 2.34e-06

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: 47.23  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 452 RMVLIGKTGNGKSATANTILGQKrfkSTASSKS-VTKFCQKATGEIDGRPVAVVDTPGLFDTTLSNDDVQQELVKCISml 530
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAK---AIVSDYPgTTRDPNEGRLELKGKQIILVDTPGLIEGASEGEGLGRAFLAIIE-- 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1678779887 531 spgPHGILLVLQ-IGRFTQEERnsvELIKkvFGKKSGNFIIIIFTR 575
Cdd:pfam01926  76 ---ADLILFVVDsEEGITPLDE---ELLE--LLRENKKPIILVLNK 113
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
451-509 3.03e-06

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: 49.62  E-value: 3.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFcQKATGEIDGRPVAVVDTPGL 509
Cdd:cd01853    32 LTILVLGKTGVGKSSTINSIFGERKVSVSAFQSETLRP-REVSRTVDGFKLNIIDTPGL 89
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
454-626 7.80e-06

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: 47.07  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 454 VLIGKTGNGKSATANTILGQKrFKSTASSKSVTKFCQKATGEID--GRPVAVVDTPGLFDTtlsnddVQQELVKCISMLS 531
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGE-VGEVSDVPGTTRDPDVYVKELDkgKVKLVLVDTPGLDEF------GGLGREELARLLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 532 PGPHGILLV--LQIGRFTQEERNSVELIKKVFGKKsgnfIIIIFTRGeELKDTTIESYIDDCDDFLKKLINDCggryqVF 609
Cdd:cd00882    74 RGADLILLVvdSTDRESEEDAKLLILRRLRKEGIP----IILVGNKI-DLLEEREVEELLRLEELAKILGVPV-----FE 143
                         170
                  ....*....|....*..
gi 1678779887 610 NNNnqTDRTQVRELIKK 626
Cdd:cd00882   144 VSA--KTGEGVDELFEK 158
PTZ00121 PTZ00121
MAEBL; Provisional
640-926 1.17e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  640 TSEMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEEIEAVKRRMEQQKTEIEQKRTKQLKEMEENIIKEREEKRK 719
Cdd:PTZ00121  1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK 1452
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  720 EWEMREKEFMKKKSKEENKIKDWEQKVDkemEQSKEDMRKQKEDWEKERKDWWEKQYQENKQ----RRHEEQTRLTKLQE 795
Cdd:PTZ00121  1453 AEEAKKAEEAKKKAEEAKKADEAKKKAE---EAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKK 1529
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  796 EYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKYNKDftalVEKHMEEIK 875
Cdd:PTZ00121  1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE----VMKLYEEEK 1605
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1678779887  876 ENKLKHVREIKETEESLSQNLSSLKEKEQTENMEKRHEIEINELNQKYKDK 926
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
PTZ00121 PTZ00121
MAEBL; Provisional
642-924 1.37e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  642 EMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEEIEAVKRRMEQQKTEIEQKRTKQLKEMEENIIKEREEKRKEW 721
Cdd:PTZ00121  1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  722 EMREKEFMKK-----KSKEENKIKDWEQKVDKEMEQSKEDMRKQKEDWEKERKDWWEKQYQENKQR------RHEEQTRL 790
Cdd:PTZ00121  1314 AKKADEAKKKaeeakKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkKAEEKKKA 1393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  791 TKLQEEYDQEREKHDR-KRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELnefRKKYNKDFTALVEK 869
Cdd:PTZ00121  1394 DEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA---KKAEEAKKKAEEAK 1470
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678779887  870 HMEEIKEN--KLKHVREIKETEESLSQNLSSLKEKEQtenmEKRHEIEINELNQKYK 924
Cdd:PTZ00121  1471 KADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAE----AKKKADEAKKAEEAKK 1523
YeeP COG3596
Predicted GTPase [General function prediction only];
420-574 2.76e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.07  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 420 DNTNTRIKAELRDLKQKSEKRTDDNIQNRECLRMVLIGKTGNGKSATANTILGQKRFKSTASSKSVTKFCQKATGEIDGR 499
Cdd:COG3596     9 TERLEALKRLPQVLRELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRPCTREIQRYRLESDGLP 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678779887 500 PVAVVDTPGLfDTTLSNDDVQQELVKcismLSPGPHGILLVLQIG-RFTQEERnsvELIKKVFGKKSGNFIIIIFT 574
Cdd:COG3596    89 GLVLLDTPGL-GEVNERDREYRELRE----LLPEADLILWVVKADdRALATDE---EFLQALRAQYPDPPVLVVLT 156
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
451-581 2.99e-05

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 45.62  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 451 LRMVLIGKTGNGKSATANTILGQKRFKStasskSVTKfcqkATGEI--------DGrpVAVVDTPGLFDTTLSNDDV-QQ 521
Cdd:cd09912     1 FLLAVVGEFSAGKSTLLNALLGEEVLPT-----GVTP----TTAVItvlrygllKG--VVLVDTPGLNSTIEHHTEItES 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678779887 522 ELVKCismlspgpHGILLVLQIGR-FTQEERNSVELIKKVFGKKsgnfIIIIFTRGEELKD 581
Cdd:cd09912    70 FLPRA--------DAVIFVLSADQpLTESEREFLKEILKWSGKK----IFFVLNKIDLLSE 118
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
638-915 1.43e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.73  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  638 CYTSEMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEEIEAVKRRMEQQKTEIE-QKRTKQLKEMEENIIKEREE 716
Cdd:pfam02463  153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyYQLKEKLELEEEYLLYLDYL 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  717 KRKEWEMREKEfmKKKSKEENKIKDWEQKVDKEMEQSKEDMRKQKEDWEKERKDWWEKQYQENKQRRHEEQTRLTKLQEE 796
Cdd:pfam02463  233 KLNEERIDLLQ--ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  797 YDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKYNKDFTALVEKHMEEIKE 876
Cdd:pfam02463  311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1678779887  877 NKLKHVREIKETEESLSQNLSSLKEKEQTENMEKRHEIE 915
Cdd:pfam02463  391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL 429
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
735-925 1.91e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.55  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  735 EENKIKDWEQKVDKEMEQSKEDmrKQKEDWEKERKDWWEKQYQENKQRRHEEQTrltklqEEYDQEREKHDRKRKKEDRN 814
Cdd:PTZ00341   952 EENVEEDAEENVEENVEENVEE--NVEENVEENVEENVEENVEENVEENVEENI------EENVEENVEENIEENVEEYD 1023
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  815 RREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKYNKDFTALVEKHMEE-IKENKLKHVREIKET-EESL 892
Cdd:PTZ00341  1024 EENVEEVEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEEnVEENVEENVEEIEENvEENV 1103
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1678779887  893 SQNLSSLKEKEQTENMEKRHEIEINELNQKYKD 925
Cdd:PTZ00341  1104 EENAEENAEENAEENAEEYDDENPEEHNEEYDE 1136
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
645-883 4.19e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 4.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  645 EEAEAAIQKEVERILKEKEEEM-KRRMEELQRQHNEEIEAVKRRMEQQKTEIEQKRTKQLKEMEENIIKEREEKRKEWEM 723
Cdd:pfam02463  260 IEKEEEKLAQVLKENKEEEKEKkLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  724 REKE---FMKKKSKEENKIKDWEQKVDKEMEQSKEDMRKQKEDWEKERKDwwEKQYQENKQRRHEEQTRLTKLQEEYDQE 800
Cdd:pfam02463  340 LEKElkeLEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA--AKLKEEELELKSEEEKEAQLLLELARQL 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  801 rEKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKYNKDFTALVEKHMEEIKENKLK 880
Cdd:pfam02463  418 -EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496

                   ...
gi 1678779887  881 HVR 883
Cdd:pfam02463  497 ERS 499
PTZ00121 PTZ00121
MAEBL; Provisional
625-922 4.99e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  625 KKSNNMLKENGGSCYTSEMFEEAEAAIQKEVERILKEKEEEMKRRMEELQRQHNEEIEAVKRRMEQQKTEIEQKRTKQLK 704
Cdd:PTZ00121  1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  705 EMEENIIKEREEKrkewemREKEFMKKKSKEENKIKDWEQKVDKEMEQSKEDMRKQKEDWEKERKDWWEKQYQENKQRRH 784
Cdd:PTZ00121  1457 KKAEEAKKKAEEA------KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  785 EEQTRLTKLQEEydQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKYNKDFT 864
Cdd:PTZ00121  1531 EEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1678779887  865 ALVEKHMEE--IKENKLKHVREIKETEESLSQNLSSLKEK-EQTENMEKRHEIEINELNQK 922
Cdd:PTZ00121  1609 AEEAKKAEEakIKAEELKKAEEEKKKVEQLKKKEAEEKKKaEELKKAEEENKIKAAEEAKK 1669
PTZ00121 PTZ00121
MAEBL; Provisional
653-913 5.57e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 5.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  653 KEVERILKEKEEEMKRRMEELQRQHNE-EIEAVKRRMEQQKTEIEQKRTKQLKEMEEnIIKEREEKRKEWEMREKEFMKK 731
Cdd:PTZ00121  1197 EDARKAEAARKAEEERKAEEARKAEDAkKAEAVKKAEEAKKDAEEAKKAEEERNNEE-IRKFEEARMAHFARRQAAIKAE 1275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  732 KSKEENKIKDWEQKVDKEMEQSKEDMRK----QKEDWEKERKDWWEKQYQENKQRRHEeqtrLTKLQEEYDQEREKHDRK 807
Cdd:PTZ00121  1276 EARKADELKKAEEKKKADEAKKAEEKKKadeaKKKAEEAKKADEAKKKAEEAKKKADA----AKKKAEEAKKAAEAAKAE 1351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  808 RKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEFRKKYNKDFTALVEKHMEEIKENKLKHVREIKE 887
Cdd:PTZ00121  1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
                          250       260
                   ....*....|....*....|....*.
gi 1678779887  888 TEESLSQNlssLKEKEQTENMEKRHE 913
Cdd:PTZ00121  1432 KADEAKKK---AEEAKKADEAKKKAE 1454
PTZ00121 PTZ00121
MAEBL; Provisional
682-926 1.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  682 EAVKRRMEQQKTEIEQKRTKQLKEMEEniikereekrKEWEMREKEFMKKKSKEENKIKDWEQKVDKEMEQSKEDMRKQK 761
Cdd:PTZ00121  1332 DAAKKKAEEAKKAAEAAKAEAEAAADE----------AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  762 EDWEKE---RKDWWEKQYQENKQRRHEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEE--NYEKKKEE 836
Cdd:PTZ00121  1402 EDKKKAdelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEE 1481
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  837 MkkNYEEEARKQAEEL----NEFRKKYNKDFTALVEKHMEEIKE-NKLKHVREIKETEEslsqnLSSLKEKEQTENMEKR 911
Cdd:PTZ00121  1482 A--KKADEAKKKAEEAkkkaDEAKKAAEAKKKADEAKKAEEAKKaDEAKKAEEAKKADE-----AKKAEEKKKADELKKA 1554
                          250
                   ....*....|....*
gi 1678779887  912 HEIEINELNQKYKDK 926
Cdd:PTZ00121  1555 EELKKAEEKKKAEEA 1569
PTZ00121 PTZ00121
MAEBL; Provisional
682-922 1.57e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  682 EAVKRRMEQQKTEIEQKRTKQLKEMEENIIKEREEKRKEWEMREKEFMK----KKSKE----ENKIKDWEQKVDKEMEQS 753
Cdd:PTZ00121  1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaeeaKKADEakkaEEKKKADELKKAEELKKA 1560
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  754 KEDMRKQKEDWEKERKDWWEKQYQENKQRRHEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKK 833
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  834 KEEMKKNYEEEARKqAEELNEFRKKYNKDFTALVEKHMEEIK----------ENKLKHVREIKETEESLSQNLSSLKEKE 903
Cdd:PTZ00121  1641 KEAEEKKKAEELKK-AEEENKIKAAEEAKKAEEDKKKAEEAKkaeedekkaaEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
                          250
                   ....*....|....*....
gi 1678779887  904 QTENMEKRHEIEINELNQK 922
Cdd:PTZ00121  1720 ELKKAEEENKIKAEEAKKE 1738
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
645-925 2.61e-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: 41.59  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  645 EEAEAAIQKEVERIlKEKEEEMKRRMEELQRQHNE---EIEAVKRRMEQQKTEIEQKRTKQ------------------- 702
Cdd:TIGR02169  687 KRELSSLQSELRRI-ENRLDELSQELSDASRKIGEiekEIEQLEQEEEKLKERLEELEEDLssleqeienvkselkelea 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  703 -LKEMEENIIKEREEKRKEWEMREKEFMKKKSKEENKIKDWEQKVDK---EMEQSKEDMRKQKEDWEKERKD------WW 772
Cdd:TIGR02169  766 rIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlrEIEQKLNRLTLEKEYLEKEIQElqeqriDL 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  773 EKQYQENKQRRHEEQTRLTKLQEE--------YDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEE 844
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEEleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  845 ARKQAEELNEfrkkYNKDFTALVEKHMEEIKENKLKHVRE----------------IKETEESLSQnLSSLKEKEQTENM 908
Cdd:TIGR02169  926 LEALEEELSE----IEDPKGEDEEIPEEELSLEDVQAELQrveeeiralepvnmlaIQEYEEVLKR-LDELKEKRAKLEE 1000
                          330
                   ....*....|....*...
gi 1678779887  909 EKRHEIE-INELNQKYKD 925
Cdd:TIGR02169 1001 ERKAILErIEEYEKKKRE 1018
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
696-927 2.75e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  696 EQKRTKQLKEMEENIIKEREEKRKEWEMREKEfmkKKSKEENKIKDWEQKVDKEMEQSKEDMRKQKEDWEKERKDWWEKQ 775
Cdd:pfam02463  152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETE---NLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  776 YQENKQRRhEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEARKQAEELNEF 855
Cdd:pfam02463  229 LDYLKLNE-ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678779887  856 RKKYNKDFTALVEKHME--EIKENKLKHVREIKETEESlSQNLSSLKEKEQTENMEKRHEIEINELNQKYKDKC 927
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKkaEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
679-918 4.97e-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: 40.82  E-value: 4.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  679 EEIEAVKRRMEQQKTEIEQKRtKQLKEMEENIIKEREEKRKEWEMREKEFMKKKSKEENKIKDWEQKV---DKEMEQSKE 755
Cdd:TIGR02169  251 EELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELedaEERLAKLEA 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  756 DMRKQKEDWE---------KERKDWWEKQYQENKQRRHEEQTRLTKLQEEYDQEREKH-DRKRKKEDRNRREQEEQERKE 825
Cdd:TIGR02169  330 EIDKLLAEIEelereieeeRKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkDYREKLEKLKREINELKRELD 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  826 LEENYEKKKEEMKKNYEEEARKQAEELNEFRkkynkdftALVEKHMEEIK--ENKLKHVREIKETEESLSQNLSSLKEKE 903
Cdd:TIGR02169  410 RLQEELQRLSEELADLNAAIAGIEAKINELE--------EEKEDKALEIKkqEWKLEQLAADLSKYEQELYDLKEEYDRV 481
                          250
                   ....*....|....*
gi 1678779887  904 QTENMEKRHEIEINE 918
Cdd:TIGR02169  482 EKELSKLQRELAEAE 496
PRK12704 PRK12704
phosphodiesterase; Provisional
732-915 5.88e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 732 KSKEENKIKDWEQKVDKEMEQSKEDMRKQKEDWEKERKDWWEKQ----YQENKQRRHEEQTRLTKLQEEYDQEREKHDRK 807
Cdd:PRK12704   26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLrnefEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 808 RKKEdrnrreqeeqerkeleenyekkkeemkknyeeearkqaEELNEFRKKYNKDFTALVEKHmEEIKENKLKHVREIKE 887
Cdd:PRK12704  106 EKRE--------------------------------------EELEKKEKELEQKQQELEKKE-EELEELIEEQLQELER 146
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1678779887 888 -----TEESLSQNLSSLKEKEQTENMEKRHEIE 915
Cdd:PRK12704  147 isgltAEEAKEILLEKVEEEARHEAAVLIKEIE 179
PTZ00121 PTZ00121
MAEBL; Provisional
682-922 7.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  682 EAVKRRMEQQKTEIEQKRTKQLKEMEE----NIIKEREEKRKEWEMREKEFMKK----KSKEENKIKDWEQKVD---KEM 750
Cdd:PTZ00121  1494 EAKKKADEAKKAAEAKKKADEAKKAEEakkaDEAKKAEEAKKADEAKKAEEKKKadelKKAEELKKAEEKKKAEeakKAE 1573
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  751 EQSKEDMRKQKE--DWEKERKDWWEKQYQENK-----QRRHEEQTRLTKLQEEYDQEREKHDRKRKKEDRNRREQEEQER 823
Cdd:PTZ00121  1574 EDKNMALRKAEEakKAEEARIEEVMKLYEEEKkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887  824 KELEENYEKKKEEMKKNYEEeaRKQAEELNEFRKKYNKDFTALVEKHMEEIK--------ENKLKHVREIKETEESLSQN 895
Cdd:PTZ00121  1654 KAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeelkkkeAEEKKKAEELKKAEEENKIK 1731
                          250       260
                   ....*....|....*....|....*..
gi 1678779887  896 LSSLKEKEQtENMEKRHEIEINELNQK 922
Cdd:PTZ00121  1732 AEEAKKEAE-EDKKKAEEAKKDEEEKK 1757
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
687-852 7.46e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.79  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 687 RMEQQKTEieQKRTKQLKEMEEniikereekrkewEMREKEFMKKKSKEENKIKDWEQKVDKEMEQskedmRKQKEDWEK 766
Cdd:PRK09510   66 RQQQQQKS--AKRAEEQRKKKE-------------QQQAEELQQKQAAEQERLKQLEKERLAAQEQ-----KKQAEEAAK 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678779887 767 ERKDWwEKQYQENKQRRHEEqtrlTKLQEEYDQEREKHDRKRKKEDRNRREQEEQERKELEENYEKKKEEMKKNYEEEAR 846
Cdd:PRK09510  126 QAALK-QKQAEEAAAKAAAA----AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK 200

                  ....*.
gi 1678779887 847 KQAEEL 852
Cdd:PRK09510  201 KKAEAE 206
 
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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