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Conserved domains on  [gi|1487353607|ref|XP_026541265|]
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adenosine monophosphate-protein transferase FICD [Notechis scutatus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
251-483 1.92e-61

Fic family protein [Transcription];


:

Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 204.15  E-value: 1.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 251 IDSKVQKVLSIPKGNSALRR--VMEEsyyhhIYHTVAIEGNTLTLAEIRHIIETRYaVPGKSLEEQNEVIGMHAAMKYVN 328
Cdd:COG3177    11 ADEALGRLDGLPEELRELLRklLIEE-----AYASSAIEGNTLTLDEVRSLLEGGL-TGGPPLRDEREVLNYVEALEYLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 329 TTLLSRigSVSLPDILEIHRRVLGFV--DPVEGGRFRTTQVFVG-HHVPPHPRDVEKQMLEFVQWINSEDamGLHPVEFA 405
Cdd:COG3177    85 ELLRGE--PLTEELILELHRILLKGLrgEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEED--ELHPLIKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 406 ALVHYKLVYIHPFVDGNGRTSRLLMNLILMQAG------YPPITIRKEQRAEYYHALEVANE-GDVRPFIRLIAKCTETT 478
Cdd:COG3177   161 AIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVREtGDLTPWIEFFLEAILEA 240

                  ....*
gi 1487353607 479 LDMLL 483
Cdd:COG3177   241 AEEAL 245
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
158-245 1.09e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.01  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG0457    60 EALADYEQALELDpddaealnnlglalqALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL 139
                          90       100
                  ....*....|....*....|...
gi 1487353607 223 SPHNKKALVSRDRTLPLVEEIDQ 245
Cdd:COG0457   140 DPDDADALYNLGIALEKLGRYEE 162
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
251-483 1.92e-61

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 204.15  E-value: 1.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 251 IDSKVQKVLSIPKGNSALRR--VMEEsyyhhIYHTVAIEGNTLTLAEIRHIIETRYaVPGKSLEEQNEVIGMHAAMKYVN 328
Cdd:COG3177    11 ADEALGRLDGLPEELRELLRklLIEE-----AYASSAIEGNTLTLDEVRSLLEGGL-TGGPPLRDEREVLNYVEALEYLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 329 TTLLSRigSVSLPDILEIHRRVLGFV--DPVEGGRFRTTQVFVG-HHVPPHPRDVEKQMLEFVQWINSEDamGLHPVEFA 405
Cdd:COG3177    85 ELLRGE--PLTEELILELHRILLKGLrgEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEED--ELHPLIKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 406 ALVHYKLVYIHPFVDGNGRTSRLLMNLILMQAG------YPPITIRKEQRAEYYHALEVANE-GDVRPFIRLIAKCTETT 478
Cdd:COG3177   161 AIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVREtGDLTPWIEFFLEAILEA 240

                  ....*
gi 1487353607 479 LDMLL 483
Cdd:COG3177   241 AEEAL 245
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
338-434 8.15e-25

Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc.This domain forms complexes with Phd antitoxins containing pfam02604.


Pssm-ID: 426907  Cd Length: 94  Bit Score: 98.31  E-value: 8.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 338 VSLPDILEIHRRVLGFVDPVEGgrFRTTQVF-VGHHVPPHPRDVEKQMLEFVQWINSEDAmglHPVEFAALVHYKLVYIH 416
Cdd:pfam02661   2 LDLEDLLALHRLLIERHGGAGG--ARDVNVSgLLESALARPEQIPFGLEELLLYPDLDRE---HPLEKAAALHFGFAKIH 76
                          90
                  ....*....|....*...
gi 1487353607 417 PFVDGNGRTSRLLMNLIL 434
Cdd:pfam02661  77 PFRDGNGRTARLLANLFL 94
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
338-468 8.66e-16

mobile mystery protein B; Members of this protein family, which we designate mobile mystery protein B, are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein A (TIGR02612), a member of the family of helix-turn-helix DNA binding proteins (pfam01381). This protein is encoded by the downstream member of the gene pair and belongs to the Fic protein family (pfam02661), where Fic (filamentation induced by cAMP) is a regulator of cell division. The characteristics of having a two-gene operon in a varied context and often on plasmids, with one member affecting cell division and the other able to bind DNA, suggests similarity to addiction modules.


Pssm-ID: 131662  Cd Length: 186  Bit Score: 75.64  E-value: 8.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 338 VSLPDILEIHRRVLGFVDPVeGGRFRTTQVFVGHHVPPHPRDVEKQMLEFVQWINSEDAMglhPVEFAALVHYKLVYIHP 417
Cdd:TIGR02613  49 LSETFLRRLHRRMFGDVWRW-AGDFRTTQKNIGVSPLQIPSELAILLDDVRYWLQNGTFS---PDEIAIRFHHRLVAIHP 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487353607 418 FVDGNGRTSRLLMNLILMQAGYPPIT-------IRKEQRAEYYHALEVANEGDVRPFI 468
Cdd:TIGR02613 125 FPNGNGRHARLATDLLLEQQGYSPFTwgsgslaLVGDLRKEYIAALKAADRHDYGPLL 182
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
158-245 1.09e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.01  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG0457    60 EALADYEQALELDpddaealnnlglalqALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL 139
                          90       100
                  ....*....|....*....|...
gi 1487353607 223 SPHNKKALVSRDRTLPLVEEIDQ 245
Cdd:COG0457   140 DPDDADALYNLGIALEKLGRYEE 162
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
173-230 7.11e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 7.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487353607 173 GKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKAL 230
Cdd:TIGR02917 479 GDLAKAREAFEKALSIEPDFFPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAI 536
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
340-473 4.23e-05

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 44.80  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 340 LPDILEIHRRVlgFVDPVE-GGRFRTTQVFVGHHVPPHPRDVEKQMLEFVQWINSEDAM-GLHPVEFAA-LVHY--KLVY 414
Cdd:PRK10347   56 LPHLCAIHRQL--YQDIFDwAGQLREVDIYQGDTPFCHFAYIEKEGNALMQDLEEEGYLvGLEKAKFVErLAHYycEINV 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1487353607 415 IHPFVDGNGRTSRLLMNLILMQAGYpPITIRKEQRAEYYHALEVANEGDVRPFIRLIAK 473
Cdd:PRK10347  134 LHPFRVGSGLAQRIFFEQLAIHAGY-QLSWQGIEKEAWNQANQSGAMGDLTALQMIFSK 191
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
163-226 2.58e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 39.92  E-value: 2.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487353607 163 LHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHN 226
Cdd:cd24142     4 LEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDG 67
 
Name Accession Description Interval E-value
COG3177 COG3177
Fic family protein [Transcription];
251-483 1.92e-61

Fic family protein [Transcription];


Pssm-ID: 442410 [Multi-domain]  Cd Length: 316  Bit Score: 204.15  E-value: 1.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 251 IDSKVQKVLSIPKGNSALRR--VMEEsyyhhIYHTVAIEGNTLTLAEIRHIIETRYaVPGKSLEEQNEVIGMHAAMKYVN 328
Cdd:COG3177    11 ADEALGRLDGLPEELRELLRklLIEE-----AYASSAIEGNTLTLDEVRSLLEGGL-TGGPPLRDEREVLNYVEALEYLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 329 TTLLSRigSVSLPDILEIHRRVLGFV--DPVEGGRFRTTQVFVG-HHVPPHPRDVEKQMLEFVQWINSEDamGLHPVEFA 405
Cdd:COG3177    85 ELLRGE--PLTEELILELHRILLKGLrgEDKEPGEYRTGQVGIGaVYVPPPPEEVPELMEELLDWLNEED--ELHPLIKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 406 ALVHYKLVYIHPFVDGNGRTSRLLMNLILMQAG------YPPITIRKEQRAEYYHALEVANE-GDVRPFIRLIAKCTETT 478
Cdd:COG3177   161 AIAHYQFETIHPFADGNGRTGRLLMNLLLLRAGllsqplLPLSRIIEEDRDEYYDALEAVREtGDLTPWIEFFLEAILEA 240

                  ....*
gi 1487353607 479 LDMLL 483
Cdd:COG3177   241 AEEAL 245
Fic pfam02661
Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and ...
338-434 8.15e-25

Fic/DOC family; This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc.This domain forms complexes with Phd antitoxins containing pfam02604.


Pssm-ID: 426907  Cd Length: 94  Bit Score: 98.31  E-value: 8.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 338 VSLPDILEIHRRVLGFVDPVEGgrFRTTQVF-VGHHVPPHPRDVEKQMLEFVQWINSEDAmglHPVEFAALVHYKLVYIH 416
Cdd:pfam02661   2 LDLEDLLALHRLLIERHGGAGG--ARDVNVSgLLESALARPEQIPFGLEELLLYPDLDRE---HPLEKAAALHFGFAKIH 76
                          90
                  ....*....|....*...
gi 1487353607 417 PFVDGNGRTSRLLMNLIL 434
Cdd:pfam02661  77 PFRDGNGRTARLLANLFL 94
FIDO COG2184
Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];
309-475 5.32e-22

Fido, protein-threonine AMPylation domain [Signal transduction mechanisms];


Pssm-ID: 441787 [Multi-domain]  Cd Length: 196  Bit Score: 93.84  E-value: 5.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 309 KSLEEQNEVIGMHAAMKYVNTTLLSRIGSVSLPDILEIHRRVLGFVDPVeGGRFRTTQVFVGHHVPPHPRDVEKQMLEFV 388
Cdd:COG2184    22 TDAAELDEAEAELTALRAAELFERPPPGVFDLAHLKAIHRRLFGDVYDW-AGQIRTVNISKGGTRFAPPSFIERELEALF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 389 QWINSEDAM-GLHPVEFA-ALVHYK--LVYIHPFVDGNGRTSRLLMNLILMQAGYpPITIRKEQRAEYYHALEVANEGDV 464
Cdd:COG2184   101 DDLREENYLrGLDREEFAeRLARFHgeLNVIHPFREGNGRTQRLFFDQLARQAGY-PLDWSRVDKEEYLEALIAADNGDY 179
                         170
                  ....*....|.
gi 1487353607 465 RPFIRLIAKCT 475
Cdd:COG2184   180 SPLKALFRDAL 190
mob_myst_B TIGR02613
mobile mystery protein B; Members of this protein family, which we designate mobile mystery ...
338-468 8.66e-16

mobile mystery protein B; Members of this protein family, which we designate mobile mystery protein B, are found in mobization-related contexts more often than not, including within a CRISPR-associated gene region in Geobacter sulfurreducens PCA, and on plasmids in Agrobacterium tumefaciens and Coxiella burnetii, always together with mobile mystery protein A (TIGR02612), a member of the family of helix-turn-helix DNA binding proteins (pfam01381). This protein is encoded by the downstream member of the gene pair and belongs to the Fic protein family (pfam02661), where Fic (filamentation induced by cAMP) is a regulator of cell division. The characteristics of having a two-gene operon in a varied context and often on plasmids, with one member affecting cell division and the other able to bind DNA, suggests similarity to addiction modules.


Pssm-ID: 131662  Cd Length: 186  Bit Score: 75.64  E-value: 8.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 338 VSLPDILEIHRRVLGFVDPVeGGRFRTTQVFVGHHVPPHPRDVEKQMLEFVQWINSEDAMglhPVEFAALVHYKLVYIHP 417
Cdd:TIGR02613  49 LSETFLRRLHRRMFGDVWRW-AGDFRTTQKNIGVSPLQIPSELAILLDDVRYWLQNGTFS---PDEIAIRFHHRLVAIHP 124
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487353607 418 FVDGNGRTSRLLMNLILMQAGYPPIT-------IRKEQRAEYYHALEVANEGDVRPFI 468
Cdd:TIGR02613 125 FPNGNGRHARLATDLLLEQQGYSPFTwgsgslaLVGDLRKEYIAALKAADRHDYGPLL 182
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
158-245 1.09e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.01  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG0457    60 EALADYEQALELDpddaealnnlglalqALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALEL 139
                          90       100
                  ....*....|....*....|...
gi 1487353607 223 SPHNKKALVSRDRTLPLVEEIDQ 245
Cdd:COG0457   140 DPDDADALYNLGIALEKLGRYEE 162
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
171-230 2.85e-06

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.55  E-value: 2.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 171 RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQAdYLYSKALTISPHNKKAL 230
Cdd:COG3063     4 KLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEAL 62
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
158-235 4.47e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 46.15  E-value: 4.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG4235    35 EALAAYEKALRLDpdnadalldlaeallAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLAL 114
                          90
                  ....*....|...
gi 1487353607 223 SPHNKKALVSRDR 235
Cdd:COG4235   115 LPADAPARLLEAS 127
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
155-230 4.61e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.22  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 155 GRL-EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSK 218
Cdd:COG3914   126 GRLeEALAALRRALALNpdfaeaylnlgealrRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRR 205
                          90
                  ....*....|..
gi 1487353607 219 ALTISPHNKKAL 230
Cdd:COG3914   206 ALELDPDNADAH 217
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
158-233 4.96e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.08  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG0457    26 EAIEDYEKALELDpddaealynlglaylRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALEL 105
                          90
                  ....*....|.
gi 1487353607 223 SPHNKKALVSR 233
Cdd:COG0457   106 DPDDAEALYNL 116
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
173-230 7.11e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 7.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1487353607 173 GKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKAL 230
Cdd:TIGR02917 479 GDLAKAREAFEKALSIEPDFFPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAI 536
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
171-230 1.67e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 44.95  E-value: 1.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 171 RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKAL 230
Cdd:COG5010    66 KLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAY 125
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
158-237 2.20e-05

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 45.68  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKALVSRDRTL 237
Cdd:COG4785    72 LAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIAL 151
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
158-226 2.28e-05

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 44.41  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALE---------------MKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG4783    56 EAIVLLHEALEldpdepearlnlglaLLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135

                  ....
gi 1487353607 223 SPHN 226
Cdd:COG4783   136 DPDD 139
PRK10347 PRK10347
putative adenosine monophosphate-protein transferase Fic;
340-473 4.23e-05

putative adenosine monophosphate-protein transferase Fic;


Pssm-ID: 182396 [Multi-domain]  Cd Length: 200  Bit Score: 44.80  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 340 LPDILEIHRRVlgFVDPVE-GGRFRTTQVFVGHHVPPHPRDVEKQMLEFVQWINSEDAM-GLHPVEFAA-LVHY--KLVY 414
Cdd:PRK10347   56 LPHLCAIHRQL--YQDIFDwAGQLREVDIYQGDTPFCHFAYIEKEGNALMQDLEEEGYLvGLEKAKFVErLAHYycEINV 133
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1487353607 415 IHPFVDGNGRTSRLLMNLILMQAGYpPITIRKEQRAEYYHALEVANEGDVRPFIRLIAK 473
Cdd:PRK10347  134 LHPFRVGSGLAQRIFFEQLAIHAGY-QLSWQGIEKEAWNQANQSGAMGDLTALQMIFSK 191
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
158-233 5.96e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.61  E-value: 5.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1487353607 158 EAKAALHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKALVSR 233
Cdd:COG0457     7 DAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNL 82
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
158-224 6.29e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 41.69  E-value: 6.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKlFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG3063    10 EAEEYYEKALELDpdnadalnnlgllllEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALEL 88

                  ..
gi 1487353607 223 SP 224
Cdd:COG3063    89 DP 90
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
142-230 8.90e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.46  E-value: 8.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 142 LELMVLKPKVSPEGRLEAKAAL-HQALemkRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKAL 220
Cdd:TIGR02917 110 LDELPGKTLLDDEGAAELLALRgLAYL---GLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVL 186
                          90
                  ....*....|
gi 1487353607 221 TISPHNKKAL 230
Cdd:TIGR02917 187 TADPGNVDAL 196
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
171-230 1.49e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.92  E-value: 1.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 171 RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKAL 230
Cdd:COG4235    29 RLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEAL 88
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
158-224 1.73e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 42.25  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG5010    72 ESLALLEQALQLDpnnpelyynlallysRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151

                  ..
gi 1487353607 223 SP 224
Cdd:COG5010   152 SP 153
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
158-230 1.85e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 44.21  E-value: 1.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487353607 158 EAKAALHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKAL 230
Cdd:COG3914   111 NAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEAL 183
DOC_P1 TIGR01550
death-on-curing family protein; The characterized member of this family is the death-on-curing ...
337-439 2.41e-04

death-on-curing family protein; The characterized member of this family is the death-on-curing (DOC) protein of phage P1. It is part of a two protein operon with prevents-host-death (phd) that forms an addiction module. DOC lacks homology to analogous addiction module post-segregational killing proteins involved in plasmid maintenance. These modules work as a combination of a long lived poison (e.g. this protein) and a more abundant but shorter lived antidote. Members of this family have a well-conserved central motif HxFx[ND][AG]NKR. A similar region, with K replaced by G, is found in the huntingtin interacting protein (HYPE) family. [Unknown function, General]


Pssm-ID: 273687  Cd Length: 121  Bit Score: 40.92  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 337 SVSLPDILEIHRRVLGFVDPVEGGrfrttqvfvghhVPPHPRDVEKQ--MLEFVQWINSEDAMglhpvEFAALVHYKLVY 414
Cdd:TIGR01550   1 HISVEEIIAIHDANIERDGGLEFG------------MSNPGRAEATIerVSERLSYEESTDIF-----EVSAVLLYALIR 63
                          90       100
                  ....*....|....*....|....*
gi 1487353607 415 IHPFVDGNGRTSRLLMNLILMQAGY 439
Cdd:TIGR01550  64 SHPFNNANKRTALNALLLFLELNGY 88
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
156-237 5.22e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 156 RLEAKAALHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKALVSRDR 235
Cdd:COG3914    75 LLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGE 154

                  ..
gi 1487353607 236 TL 237
Cdd:COG3914   155 AL 156
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
158-230 6.23e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.64  E-value: 6.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1487353607 158 EAKAALHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKAL 230
Cdd:COG2956   143 NAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPAL 215
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
159-233 6.88e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.18  E-value: 6.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487353607 159 AKAALHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKALVSR 233
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNL 78
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
156-230 8.28e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 41.25  E-value: 8.28e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1487353607 156 RLEAKAALhqALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKAL 230
Cdd:COG2956    75 RAEALLEL--AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAY 147
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
158-220 1.36e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.38  E-value: 1.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKAL 220
Cdd:COG0457    94 EALEDYDKALELDpddaealynlglallELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLE 171
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
163-226 2.58e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 39.92  E-value: 2.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1487353607 163 LHQALEMKRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHN 226
Cdd:cd24142     4 LEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDPDG 67
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
157-233 9.18e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 38.17  E-value: 9.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487353607 157 LEAKAALHQalemkRQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTISPHNKKALVSR 233
Cdd:COG2956   113 LRLLAEIYE-----QEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLL 184
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
158-226 9.76e-03

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 36.71  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487353607 158 EAKAALHQALEMK---------------RQGKREKAQKLFLHALKMDPDYVDALTEFGLFSEEEKDIIQADYLYSKALTI 222
Cdd:COG4783    22 EAEALLEKALELDpdnpeafallgeillQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKL 101

                  ....
gi 1487353607 223 SPHN 226
Cdd:COG4783   102 DPEH 105
 
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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