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Conserved domains on  [gi|8922873|ref|NP_060796|]
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GTPase IMAP family member 4 isoform 1 [Homo sapiens]

Protein Classification

GTPase IMAP family protein( domain architecture ID 10111261)

GTPase immunity-associated protein (IMAP) family protein may function as regulator of lymphocyte survival and homeostasis

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 ...
31-231 1.94e-109

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: 316.78  E-value: 1.94e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   31 LRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLT 110
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873  111 SPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLREAPEDIQDLMDIFGDRYCALN 190
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 8922873  191 NKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEE 231
Cdd:cd01852 161 NKAKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
PRK00409 super family cl29770
recombination and DNA strand exchange inhibitor protein; Reviewed
203-302 6.37e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


The actual alignment was detected with superfamily member PRK00409:

Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   203 AQLLGLIQRVVRENKEgcytnrMYQRAEEEI--------QKQTQAMQELHRVELEREKA-RIREEYEEKIRKLEDKVEQE 273
Cdd:PRK00409 494 AKRLGLPENIIEEAKK------LIGEDKEKLneliasleELERELEQKAEEAEALLKEAeKLKEELEEKKEKLQEEEDKL 567
                         90       100
                 ....*....|....*....|....*....
gi 8922873   274 KRKkqmekklAEQEAHYAVRQqrARTEVE 302
Cdd:PRK00409 568 LEE-------AEKEAQQAIKE--AKKEAD 587
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
31-231 1.94e-109

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: 316.78  E-value: 1.94e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   31 LRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLT 110
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873  111 SPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLREAPEDIQDLMDIFGDRYCALN 190
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 8922873  191 NKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEE 231
Cdd:cd01852 161 NKAKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
31-235 5.86e-97

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 284.89  E-value: 5.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873     31 LRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLT 110
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    111 SPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLRE-APEDIQDLMDifgdrycal 189
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgCPEFLKEVLR--------- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 8922873    190 nnKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQK 235
Cdd:pfam04548 152 --TADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGER 195
YeeP COG3596
Predicted GTPase [General function prediction only];
23-185 4.08e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 4.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   23 RQEPRNSQLRIVLVGKTGAGKSATGNSILGRKVfhsgtAAKSITKKCEKRSSS--WKETE---LVVVDTPGIFDTEVPNA 97
Cdd:COG3596  32 RLLVELPPPVIALVGKTGAGKSSLINALFGAEV-----AEVGVGRPCTREIQRyrLESDGlpgLVLLDTPGLGEVNERDR 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   98 EtskeiIRCILLTSPGPHALLLVV-PLGRYTEEEHKATEKILKmFGERARsfMILIFTRKDDL--GDTNLHDYLREAPED 174
Cdd:COG3596 107 E-----YRELRELLPEADLILWVVkADDRALATDEEFLQALRA-QYPDPP--VLVVLTQVDRLepEREWDPPYNWPSPPK 178
                       170
                ....*....|.
gi 8922873  175 IQDLMDIFGDR 185
Cdd:COG3596 179 EQNIRRALEAI 189
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
24-89 1.70e-05

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: 46.48  E-value: 1.70e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8922873     24 QEPRNSQLRIVLVGKTGAGKSATGNSILGRKVFhSGTAAKSITKKCEKRSSSWKETELVVVDTPGI 89
Cdd:TIGR00993 112 QDPLDFSLNILVLGKSGVGKSATINSIFGEVKF-STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGL 176
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
203-302 6.37e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   203 AQLLGLIQRVVRENKEgcytnrMYQRAEEEI--------QKQTQAMQELHRVELEREKA-RIREEYEEKIRKLEDKVEQE 273
Cdd:PRK00409 494 AKRLGLPENIIEEAKK------LIGEDKEKLneliasleELERELEQKAEEAEALLKEAeKLKEELEEKKEKLQEEEDKL 567
                         90       100
                 ....*....|....*....|....*....
gi 8922873   274 KRKkqmekklAEQEAHYAVRQqrARTEVE 302
Cdd:PRK00409 568 LEE-------AEKEAQQAIKE--AKKEAD 587
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
196-316 1.34e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873  196 AEQEAQRAQLLGLIQRVVRENKEGcytnrmyQRAEEEIQKQTQAMQELHRvELEREKARIREEYEEKIRKLEDKVEQEKR 275
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDI-------ARLEERRRELEERLEELEE-ELAELEEELEELEEELEELEEELEEAEEE 352
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 8922873  276 KKQMEKKLAEQEAHYAVRQQRARTEVESKDGILELIMTALQ 316
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
227-288 2.43e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 2.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8922873  227 QRAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDKVEQEKRKKQMEK------KLAEQEA 288
Cdd:cd16269 203 ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQeralesKLKEQEA 270
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
193-304 1.14e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.51  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    193 ATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQElhRVELEREKARIREEYEEKIRkLEDKVEQ 272
Cdd:pfam09731 298 QLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQL--RLEFEREREEIRESYEEKLR-TELERQA 374
                          90       100       110
                  ....*....|....*....|....*....|..
gi 8922873    273 EKRKKQMEKKLAEQEAHYAVRQQRartEVESK 304
Cdd:pfam09731 375 EAHEEHLKDVLVEQEIELQREFLQ---DIKEK 403
 
Name Accession Description Interval E-value
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
31-231 1.94e-109

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: 316.78  E-value: 1.94e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   31 LRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLT 110
Cdd:cd01852   1 LRLVLVGKTGNGKSATGNTILGRKVFESKLSASGVTKTCQKESAVWDGRRVNVIDTPGLFDTSVSPEQLSKEIIRCLSLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873  111 SPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLREAPEDIQDLMDIFGDRYCALN 190
Cdd:cd01852  81 APGPHAFLLVVPLGRFTEEEEQAVEELQELFGEKVLDHTIVLFTRGDDLEGGSLEDYLEDSCEALKRLLEKCGGRYVAFN 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 8922873  191 NKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEE 231
Cdd:cd01852 161 NKAKGREQEQQVKELLAKVEEMVRENGGKPYTNEMYEEAEE 201
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
31-235 5.86e-97

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


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 284.89  E-value: 5.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873     31 LRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLT 110
Cdd:pfam04548   1 LRIVLVGKTGNGKSATGNSILGRKAFESKLRAQGVTKTCQLVSRTWDGRIINVIDTPGLFDLSVSNDFISKEIIRCLLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    111 SPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLRE-APEDIQDLMDifgdrycal 189
Cdd:pfam04548  81 EPGPHAVLLVLSLGRFTEEEEQALRTLQELFGSKILDYMIVVFTRKDDLEDDSLDDYLSDgCPEFLKEVLR--------- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 8922873    190 nnKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQK 235
Cdd:pfam04548 152 --TADGEEKEEQVQQLLALVEAIVKENGGKPYTNDLYEKIKEEGER 195
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
19-141 1.11e-12

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: 66.57  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   19 YGPGRQEPRNSqLRIVLVGKTGAGKSATGNSILG-RKVFHSgtAAKSITKKCEKRSSSWKETELVVVDTPGIfdteVPNA 97
Cdd:cd01853  21 EAKLKKELDFS-LTILVLGKTGVGKSSTINSIFGeRKVSVS--AFQSETLRPREVSRTVDGFKLNIIDTPGL----LESQ 93
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 8922873   98 ETSK-----EIIRCILLTSPgPHALLLVVPLGRYTeeEHKATEKILKMF 141
Cdd:cd01853  94 DQRVnrkilSIIKRFLKKKT-IDVVLYVDRLDMYR--VDNLDVPLLRAI 139
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
34-192 7.31e-10

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: 57.08  E-value: 7.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   34 VLVGKTGAGKSATGNSILGRKVF----HSGTAAKSITKKCEKRSsswKETELVVVDTPGIFDTEVPNAEtskeiiRCILL 109
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGevsdVPGTTRDPDVYVKELDK---GKVKLVLVDTPGLDEFGGLGRE------ELARL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873  110 TSPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARsfMILIFTRKDDLGDTNlhdylREAPEDIQDLMDIFGDRYCAL 189
Cdd:cd00882  72 LLRGADLILLVVDSTDRESEEDAKLLILRRLRKEGIP--IILVGNKIDLLEERE-----VEELLRLEELAKILGVPVFEV 144

                ...
gi 8922873  190 NNK 192
Cdd:cd00882 145 SAK 147
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
32-155 2.82e-09

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 54.16  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873     32 RIVLVGKTGAGKSATGNSILGRKVF---HSGTaaksiTKKCEKRSSSWKETELVVVDTPGIFDTEVPN---AETSKEIIR 105
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIvsdYPGT-----TRDPNEGRLELKGKQIILVDTPGLIEGASEGeglGRAFLAIIE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 8922873    106 CilltspgpHALLLVVPlgryTEEEHKATEKILKMFGERARSFMILIFTR 155
Cdd:pfam01926  76 A--------DLILFVVD----SEEGITPLDEELLELLRENKKPIILVLNK 113
YeeP COG3596
Predicted GTPase [General function prediction only];
23-185 4.08e-08

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 54.00  E-value: 4.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   23 RQEPRNSQLRIVLVGKTGAGKSATGNSILGRKVfhsgtAAKSITKKCEKRSSS--WKETE---LVVVDTPGIFDTEVPNA 97
Cdd:COG3596  32 RLLVELPPPVIALVGKTGAGKSSLINALFGAEV-----AEVGVGRPCTREIQRyrLESDGlpgLVLLDTPGLGEVNERDR 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   98 EtskeiIRCILLTSPGPHALLLVV-PLGRYTEEEHKATEKILKmFGERARsfMILIFTRKDDL--GDTNLHDYLREAPED 174
Cdd:COG3596 107 E-----YRELRELLPEADLILWVVkADDRALATDEEFLQALRA-QYPDPP--VLVVLTQVDRLepEREWDPPYNWPSPPK 178
                       170
                ....*....|.
gi 8922873  175 IQDLMDIFGDR 185
Cdd:COG3596 179 EQNIRRALEAI 189
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
34-157 2.92e-07

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: 49.55  E-value: 2.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   34 VLVGKTGAGKSATGNSILGRKVFH----SGTAAKSITKKCEKRssswKETELVVVDTPGIFDTEVPNAETSKEIIRCILL 109
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLGQNVGIvspiPGTTRDPVRKEWELL----PLGPVVLIDTPGLDEEGGLGRERVEEARQVADR 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 8922873  110 TspgpHALLLVVPLGRYTEEEhkaTEKILKMFGERARSfmILIFTRKD 157
Cdd:cd00880  77 A----DLVLLVVDSDLTPVEE---EAKLGLLRERGKPV--LLVLNKID 115
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
24-89 1.70e-05

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: 46.48  E-value: 1.70e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8922873     24 QEPRNSQLRIVLVGKTGAGKSATGNSILGRKVFhSGTAAKSITKKCEKRSSSWKETELVVVDTPGI 89
Cdd:TIGR00993 112 QDPLDFSLNILVLGKSGVGKSATINSIFGEVKF-STDAFGMGTTSVQEIEGLVQGVKIRVIDTPGL 176
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
203-302 6.37e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.82  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   203 AQLLGLIQRVVRENKEgcytnrMYQRAEEEI--------QKQTQAMQELHRVELEREKA-RIREEYEEKIRKLEDKVEQE 273
Cdd:PRK00409 494 AKRLGLPENIIEEAKK------LIGEDKEKLneliasleELERELEQKAEEAEALLKEAeKLKEELEEKKEKLQEEEDKL 567
                         90       100
                 ....*....|....*....|....*....
gi 8922873   274 KRKkqmekklAEQEAHYAVRQqrARTEVE 302
Cdd:PRK00409 568 LEE-------AEKEAQQAIKE--AKKEAD 587
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
196-316 1.34e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873  196 AEQEAQRAQLLGLIQRVVRENKEGcytnrmyQRAEEEIQKQTQAMQELHRvELEREKARIREEYEEKIRKLEDKVEQEKR 275
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDI-------ARLEERRRELEERLEELEE-ELAELEEELEELEEELEELEEELEEAEEE 352
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 8922873  276 KKQMEKKLAEQEAHYAVRQQRARTEVESKDGILELIMTALQ 316
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
3a0901s02IAP34 TIGR00991
GTP-binding protein (Chloroplast Envelope Protein Translocase); [Transport and binding ...
1-109 2.01e-04

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


Pssm-ID: 130064  Cd Length: 313  Bit Score: 42.58  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873      1 MAAQY------GSMSFNPSTPGASY---GPGRQEPRNSqLRIVLVGKTGAGKSATGNSILGRKVfhsgtAAKSITKKCEK 71
Cdd:TIGR00991   1 MASPQtprewvGIQQFPPATQTKLLellGKLKEEDVSS-LTILVMGKGGVGKSSTVNSIIGERI-----ATVSAFQSEGL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 8922873     72 RSSSWKETE----LVVVDTPGIFDTEVPNaETSKEIIRCILL 109
Cdd:TIGR00991  75 RPMMVSRTRagftLNIIDTPGLIEGGYIN-DQAVNIIKRFLL 115
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
227-288 2.43e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 2.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8922873  227 QRAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDKVEQEKRKKQMEK------KLAEQEA 288
Cdd:cd16269 203 ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQeralesKLKEQEA 270
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
32-164 2.45e-04

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: 40.82  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873     32 RIVLVGKTGAGKSATGNSILGRKVF----HSGTAAKSITKKCEKRSsswKETELVVVDTPGIFDTEVPNAETSKEIIRCI 107
Cdd:TIGR00231   3 KIVIVGHPNVGKSTLLNSLLGNKGSiteyYPGTTRNYVTTVIEEDG---KTYKFNLLDTAGQEDYDAIRRLYYPQVERSL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 8922873    108 LLTSpgphallLVVPLGRYTEEEHKATEKIlkmFGERARSFMILIFTRKDDLGDTNL 164
Cdd:TIGR00231  80 RVFD-------IVILVLDVEEILEKQTKEI---IHHADSGVPIILVGNKIDLKDADL 126
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
31-157 3.56e-04

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: 40.61  E-value: 3.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   31 LRIVLVGKTGAGKSATGNSILGRKVFHSG----TAAKSITK-KCEKrssswketELVVVDTPGIFDTEVPNAETSKEII- 104
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGvtptTAVITVLRyGLLK--------GVVLVDTPGLNSTIEHHTEITESFLp 72
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 8922873  105 RCilltspgpHALLLVVPLGR-YTEEEHKATEKILKMFGERarsfMILIFTRKD 157
Cdd:cd09912  73 RA--------DAVIFVLSADQpLTESEREFLKEILKWSGKK----IFFVLNKID 114
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
227-304 4.38e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   227 QRAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDK--VEQEKRKKQMEKKLAEQEAHYAVRQQRARTEVESK 304
Cdd:PRK09510  75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKkqAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAK 154
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
30-169 6.20e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 39.96  E-value: 6.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873   30 QLRIVLVGKTGAGKSATGNSILGRKVFHS---GTAAKSITKKCEKRSSswKETELVVVDTPGIfdTEVpnAETSKEIIRC 106
Cdd:COG1100   3 EKKIVVVGTGGVGKTSLVNRLVGDIFSLEkylSTNGVTIDKKELKLDG--LDVDLVIWDTPGQ--DEF--RETRQFYARQ 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8922873  107 ILltspGPHALLLVV----PLGRYTEEEHkatEKILKMFGERARsfMILIFTRKDDLGDTNLHDYLR 169
Cdd:COG1100  77 LT----GASLYLFVVdgtrEETLQSLYEL---LESLRRLGKKSP--IILVLNKIDLYDEEEIEDEER 134
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
193-304 1.14e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.51  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    193 ATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQElhRVELEREKARIREEYEEKIRkLEDKVEQ 272
Cdd:pfam09731 298 QLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQL--RLEFEREREEIRESYEEKLR-TELERQA 374
                          90       100       110
                  ....*....|....*....|....*....|..
gi 8922873    273 EKRKKQMEKKLAEQEAHYAVRQQRartEVESK 304
Cdd:pfam09731 375 EAHEEHLKDVLVEQEIELQREFLQ---DIKEK 403
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
227-304 1.23e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.96  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    227 QRAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDKVEQEKRKKQ------MEKKLAEQEahyAVRQQRARTE 300
Cdd:pfam02841 209 ERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLaeqermLEHKLQEQE---ELLKEGFKTE 285

                  ....
gi 8922873    301 VESK 304
Cdd:pfam02841 286 AESL 289
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
196-304 1.51e-03

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: 40.49  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    196 AEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQELHRVELEREKaRIREEYEEKIRKLEDK------ 269
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK-RDRKRAEEQRRKILEKeleerk 505
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 8922873    270 ---VEQEKRKKQMEKKLAEQEAHYAVRQQRARTEVESK 304
Cdd:pfam17380 506 qamIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR 543
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
191-318 3.10e-03

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: 39.34  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    191 NKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQElhrvELEREKARIREEYEEKIRKLE--- 267
Cdd:pfam17380 391 NERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE----ERAREMERVRLEEQERQQQVErlr 466
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8922873    268 -DKVEQEKRKKQMEK-----KLAEQEAHYAVRQQ-----RARTEVESKDGILELIMTALQIA 318
Cdd:pfam17380 467 qQEEERKRKKLELEKekrdrKRAEEQRRKILEKEleerkQAMIEEERKRKLLEKEMEERQKA 528
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
185-302 3.29e-03

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: 39.34  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    185 RYCALNNKAT-GAEQEAQRAQLLGLIQRVVRENKEgcytNRMYQRAEEEIQKQTQAMQELHRVELEREKA--RIREEYE- 260
Cdd:pfam17380 325 RQAEMDRQAAiYAEQERMAMERERELERIRQEERK----RELERIRQEEIAMEISRMRELERLQMERQQKneRVRQELEa 400
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 8922873    261 ---EKIRKLEDKVEQEKRKKQMEKKLAEQEAHYAVRQQRARTEVE 302
Cdd:pfam17380 401 arkVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
231-323 5.36e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.78  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    231 EEIQKQTQAMQELHRVELErEKARIREEYEEKIRKL-EDKVEQEKRKKQMEKKLAEQEAHYA-VRQQRARTEVESKdgiL 308
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLE-LQAREKAQSQALAEAQqQELVALEGLAAELEEKQQELEAQLEqLQEKAAETSQERK---Q 216
                          90
                  ....*....|....*
gi 8922873    309 ELIMTALQIASFILL 323
Cdd:PRK11448  217 KRKEITDQAAKRLEL 231
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
197-305 5.62e-03

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: 38.57  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    197 EQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQELHRVELERE-KARIREEYEEKIRKledKVEQEKR 275
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmEERQKAIYEEERRR---EAEEERR 543
                          90       100       110
                  ....*....|....*....|....*....|.
gi 8922873    276 KKQ-MEKKLAEQEAHYAVRQQRARTEVESKD 305
Cdd:pfam17380 544 KQQeMEERRRIQEQMRKATEERSRLEAMERE 574
PTZ00121 PTZ00121
MAEBL; Provisional
228-304 6.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 6.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8922873    228 RAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDKVEQEKRKKQMEKKLAEQEAHYAVRQQRARTEVESK 304
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
230-304 6.47e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 36.70  E-value: 6.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8922873    230 EEEIQKQTQAMQELhrvELEREKARIREEYEEKIRKLEDKVEQEKRKKQ--MEKKLAEQEAHYAVRQQRARTEVESK 304
Cdd:pfam15236  75 EEERRRQEEQEEEE---RLRREREEEQKQFEEERRKQKEKEEAMTRKTQalLQAMQKAQELAQRLKQEQRIRELAEK 148
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
201-312 7.14e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 38.10  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    201 QRAQLLGLIQRVVRENKEgcYTNRMYQRAE--EEIQ-KQTQAMQELHRV------------ELEREKARIREEYEEKIRK 265
Cdd:pfam10168 569 QKEQQLQELQSLEEERKS--LSERAEKLAEkyEEIKdKQEKLMRRCKKVlqrlnsqlpvlsDAEREMKKELETINEQLKH 646
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 8922873    266 LEDKVEQEKRK-----KQMEK-KLAEQEAHYAV--RQQRARTEVESKDG--ILELIM 312
Cdd:pfam10168 647 LANAIKQAKKKmnyqrYQIAKsQSIRKKSSLSLseKQRKTIKEILKQLGseIDELIK 703
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
235-300 8.02e-03

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 37.27  E-value: 8.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8922873    235 KQTQAMQELHRVElerekaRIREEYEEKIRKLEDKVEQEKRKKQMEKKLAEQEAHYAVRQQRARTE 300
Cdd:pfam12037  67 KEYEAAQEQLKIE------RQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNE 126
PTZ00121 PTZ00121
MAEBL; Provisional
168-304 8.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 8.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8922873    168 LREAPED-IQDLMDIFGDRYCALNNKATGAEQEAQRAQllgliqRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQELHRV 246
Cdd:PTZ00121 1586 AKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE------ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 8922873    247 ELEREKARIREEYEEKIRKLEDKVEQEKRKKQMEKKLAEQEAHyAVRQQRARTEVESK 304
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKK 1716
 
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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