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Conserved domains on  [gi|42573439|ref|NP_974816|]
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TMEM192 family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMEM192 super family cl20718
TMEM192 family; The function of this family of transmembrane proteins is unknown. In ...
23-231 1.29e-08

TMEM192 family; The function of this family of transmembrane proteins is unknown. In vertebrates, proteins in this family are located in the lysosomal membrane and late endosome. In Arabidopsis, a member of this family has been found to weakly interact with FRIGIDA, a determinant of flowering time.


The actual alignment was detected with superfamily member pfam14802:

Pssm-ID: 434223  Cd Length: 235  Bit Score: 54.97  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    23 DILHEAPLFGHRESRSLVGSCIYLIILAGYAILAAGAP---WILQSV-DYLIPSLLCSCNVALLMLTGMFQQYFVNQVQK 98
Cdd:pfam14802   7 PALSSEIEPEFRPLPTVPIASLLLLLHVAIVILGIVLAvlcPDDDNKcDKCVYFVLLYLRVILWLLTYLIDRYVKRHHQK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    99 IRLQGYYSFSQKLKHVVRLPFAIMAYGTASMLL--------FMEWRPYVSVLPIFTVQRFIMSV---EAISAASFMIVFV 167
Cdd:pfam14802  87 LRRRGYLDFYRSTKRLKRLPLQIVSLGNAVLLLvlavmhhyYPDDFADHCASGWLSPVVYILIIlalELLVLLPCLIIYI 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573439   168 GYVRQYNSVNSQPDVLNS--LYSPLQPAALEGLRYHEAGRLSDQ---QMALLQYQRENLHYLSEEILRL 231
Cdd:pfam14802 167 VKVRRFNKTRPPPDVLREekLYSYSQSSTSTEVGFRDGSSLEELlekQADLIRYLKQHNALLSRRILAL 235
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
193-348 2.46e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439 193 AALEGLRYHEAGRLSDQQMALLQYQ--RENLHYLSEEILRLQESLSKYETNgsstpQVDLAHLVATRDQELRTLSAEVDQ 270
Cdd:COG1196 211 KAERYRELKEELKELEAELLLLKLRelEAELEELEAELEELEAELEELEAE-----LAELEAELEELRLELEELELELEE 285
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42573439 271 LHSELNLARSLISERDREIQHVRNTNNQYVAENERLRAILGEWSMRAAKLERALEVERISNIELRKKVSALRDQRQVA 348
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
 
Name Accession Description Interval E-value
TMEM192 pfam14802
TMEM192 family; The function of this family of transmembrane proteins is unknown. In ...
23-231 1.29e-08

TMEM192 family; The function of this family of transmembrane proteins is unknown. In vertebrates, proteins in this family are located in the lysosomal membrane and late endosome. In Arabidopsis, a member of this family has been found to weakly interact with FRIGIDA, a determinant of flowering time.


Pssm-ID: 434223  Cd Length: 235  Bit Score: 54.97  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    23 DILHEAPLFGHRESRSLVGSCIYLIILAGYAILAAGAP---WILQSV-DYLIPSLLCSCNVALLMLTGMFQQYFVNQVQK 98
Cdd:pfam14802   7 PALSSEIEPEFRPLPTVPIASLLLLLHVAIVILGIVLAvlcPDDDNKcDKCVYFVLLYLRVILWLLTYLIDRYVKRHHQK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    99 IRLQGYYSFSQKLKHVVRLPFAIMAYGTASMLL--------FMEWRPYVSVLPIFTVQRFIMSV---EAISAASFMIVFV 167
Cdd:pfam14802  87 LRRRGYLDFYRSTKRLKRLPLQIVSLGNAVLLLvlavmhhyYPDDFADHCASGWLSPVVYILIIlalELLVLLPCLIIYI 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573439   168 GYVRQYNSVNSQPDVLNS--LYSPLQPAALEGLRYHEAGRLSDQ---QMALLQYQRENLHYLSEEILRL 231
Cdd:pfam14802 167 VKVRRFNKTRPPPDVLREekLYSYSQSSTSTEVGFRDGSSLEELlekQADLIRYLKQHNALLSRRILAL 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
193-348 2.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439 193 AALEGLRYHEAGRLSDQQMALLQYQ--RENLHYLSEEILRLQESLSKYETNgsstpQVDLAHLVATRDQELRTLSAEVDQ 270
Cdd:COG1196 211 KAERYRELKEELKELEAELLLLKLRelEAELEELEAELEELEAELEELEAE-----LAELEAELEELRLELEELELELEE 285
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42573439 271 LHSELNLARSLISERDREIQHVRNTNNQYVAENERLRAILGEWSMRAAKLERALEVERISNIELRKKVSALRDQRQVA 348
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
228-344 3.53e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    228 ILRLQESLS----KYETNGSSTPQVDLAHLVATRDQELRTLSAEVDQLHSELNLARSLISERDREIQHVRNTNNQYVAEn 303
Cdd:TIGR00606  794 MERFQMELKdverKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE- 872
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 42573439    304 erlRAILGEWSMRAAKLERALEvERISNI-ELRKKVSALRDQ 344
Cdd:TIGR00606  873 ---KLQIGTNLQRRQQFEEQLV-ELSTEVqSLIREIKDAKEQ 910
PRK09039 PRK09039
peptidoglycan -binding protein;
247-344 1.72e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439  247 QVDLAHLVATRDQELRTLSAEVDQLHSELNLARSLISERDREIQHVRNTNNQYVAENERLRAILGEWS-------MRAAK 319
Cdd:PRK09039  41 QFFLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAgagaaaeGRAGE 120
                         90       100       110
                 ....*....|....*....|....*....|..
gi 42573439  320 LERALEVER------ISNIE-LRKKVSALRDQ 344
Cdd:PRK09039 121 LAQELDSEKqvsaraLAQVElLNQQIAALRRQ 152
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
208-347 1.84e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439   208 DQQMALLQYQRENlhyLSEEILRLQESLSKYETNGSSTPQVDLAHLVATRdqELRTLSAEVDQLHSELNLARSLISERDR 287
Cdd:pfam05622  20 DQQVSLLQEEKNS---LQQENKKLQERLDQLESGDDSGTPGGKKYLLLQK--QLEQLQEENFRLETARDDYRIKCEELEK 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573439   288 EIQHVRNTNNQYVAENERLRA------ILGEWSMRAAKLERALEVerisnieLRKKVSALRD-QRQV 347
Cdd:pfam05622  95 EVLELQHRNEELTSLAEEAQAlkdemdILRESSDKVKKLEATVET-------YKKKLEDLGDlRRQV 154
 
Name Accession Description Interval E-value
TMEM192 pfam14802
TMEM192 family; The function of this family of transmembrane proteins is unknown. In ...
23-231 1.29e-08

TMEM192 family; The function of this family of transmembrane proteins is unknown. In vertebrates, proteins in this family are located in the lysosomal membrane and late endosome. In Arabidopsis, a member of this family has been found to weakly interact with FRIGIDA, a determinant of flowering time.


Pssm-ID: 434223  Cd Length: 235  Bit Score: 54.97  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    23 DILHEAPLFGHRESRSLVGSCIYLIILAGYAILAAGAP---WILQSV-DYLIPSLLCSCNVALLMLTGMFQQYFVNQVQK 98
Cdd:pfam14802   7 PALSSEIEPEFRPLPTVPIASLLLLLHVAIVILGIVLAvlcPDDDNKcDKCVYFVLLYLRVILWLLTYLIDRYVKRHHQK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    99 IRLQGYYSFSQKLKHVVRLPFAIMAYGTASMLL--------FMEWRPYVSVLPIFTVQRFIMSV---EAISAASFMIVFV 167
Cdd:pfam14802  87 LRRRGYLDFYRSTKRLKRLPLQIVSLGNAVLLLvlavmhhyYPDDFADHCASGWLSPVVYILIIlalELLVLLPCLIIYI 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42573439   168 GYVRQYNSVNSQPDVLNS--LYSPLQPAALEGLRYHEAGRLSDQ---QMALLQYQRENLHYLSEEILRL 231
Cdd:pfam14802 167 VKVRRFNKTRPPPDVLREekLYSYSQSSTSTEVGFRDGSSLEELlekQADLIRYLKQHNALLSRRILAL 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
193-348 2.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439 193 AALEGLRYHEAGRLSDQQMALLQYQ--RENLHYLSEEILRLQESLSKYETNgsstpQVDLAHLVATRDQELRTLSAEVDQ 270
Cdd:COG1196 211 KAERYRELKEELKELEAELLLLKLRelEAELEELEAELEELEAELEELEAE-----LAELEAELEELRLELEELELELEE 285
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42573439 271 LHSELNLARSLISERDREIQHVRNTNNQYVAENERLRAILGEWSMRAAKLERALEVERISNIELRKKVSALRDQRQVA 348
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
228-344 3.53e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.73  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    228 ILRLQESLS----KYETNGSSTPQVDLAHLVATRDQELRTLSAEVDQLHSELNLARSLISERDREIQHVRNTNNQYVAEn 303
Cdd:TIGR00606  794 MERFQMELKdverKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE- 872
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 42573439    304 erlRAILGEWSMRAAKLERALEvERISNI-ELRKKVSALRDQ 344
Cdd:TIGR00606  873 ---KLQIGTNLQRRQQFEEQLV-ELSTEVqSLIREIKDAKEQ 910
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
181-348 7.23e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    181 DVLNSLYSPLQP------AALEGLRYHEAGRLSDQQMALLQYQ--RENLHYLSEEILRLQESLSKYETNgSSTPQVDLAH 252
Cdd:TIGR02168  193 DILNELERQLKSlerqaeKAERYKELKAELRELELALLVLRLEelREELEELQEELKEAEEELEELTAE-LQELEEKLEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439    253 LVAtrdqELRTLSAEVDQLHSELNLARSLISERDREIQHVRNTNNQYVAENERLRAILGEW-------SMRAAKLERALE 325
Cdd:TIGR02168  272 LRL----EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskldelAEELAELEEKLE 347
                          170       180
                   ....*....|....*....|...
gi 42573439    326 VERISNIELRKKVSALRDQRQVA 348
Cdd:TIGR02168  348 ELKEELESLEAELEELEAELEEL 370
PRK09039 PRK09039
peptidoglycan -binding protein;
247-344 1.72e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439  247 QVDLAHLVATRDQELRTLSAEVDQLHSELNLARSLISERDREIQHVRNTNNQYVAENERLRAILGEWS-------MRAAK 319
Cdd:PRK09039  41 QFFLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAgagaaaeGRAGE 120
                         90       100       110
                 ....*....|....*....|....*....|..
gi 42573439  320 LERALEVER------ISNIE-LRKKVSALRDQ 344
Cdd:PRK09039 121 LAQELDSEKqvsaraLAQVElLNQQIAALRRQ 152
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
208-347 1.84e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.06  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439   208 DQQMALLQYQRENlhyLSEEILRLQESLSKYETNGSSTPQVDLAHLVATRdqELRTLSAEVDQLHSELNLARSLISERDR 287
Cdd:pfam05622  20 DQQVSLLQEEKNS---LQQENKKLQERLDQLESGDDSGTPGGKKYLLLQK--QLEQLQEENFRLETARDDYRIKCEELEK 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42573439   288 EIQHVRNTNNQYVAENERLRA------ILGEWSMRAAKLERALEVerisnieLRKKVSALRD-QRQV 347
Cdd:pfam05622  95 EVLELQHRNEELTSLAEEAQAlkdemdILRESSDKVKKLEATVET-------YKKKLEDLGDlRRQV 154
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
208-344 6.41e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439  208 DQQMALLQYQRENLHYLSE---EILRLQESLSKYETNgsstpQVDLAHLVATrDQELRTLSAEVDQLHSELNLARSLISE 284
Cdd:COG4913  637 EAELDALQERREALQRLAEyswDEIDVASAEREIAEL-----EAELERLDAS-SDDLAALEEQLEELEAELEELEEELDE 710
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439  285 RDREIQHVRNTNNQYVAENERLRAILGEWSMRAAKLERALEVERISNIELRKKVSALRDQ 344
Cdd:COG4913  711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
248-348 6.76e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 38.12  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439   248 VDLAHLVATRDQELRTLSAEVDQLHSELNLARSLISERDREIQHVRNTNNQYVAENERLRAILGEWSMRAAKLERALEVE 327
Cdd:pfam19220  51 LELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAE 130
                          90       100
                  ....*....|....*....|.
gi 42573439   328 RISNIELRKKVSALRDQRQVA 348
Cdd:pfam19220 131 TEQNRALEEENKALREEAQAA 151
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
226-342 8.50e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.92  E-value: 8.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573439 226 EEILRLQESLSKYEtngsstpqvdlaHLVATRDQELRTLSAEVDQLHSELNLARSLISE---RDREIQHVRNtnnqyvaE 302
Cdd:COG2433 413 EEIRRLEEQVERLE------------AEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDR-------E 473
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42573439 303 NERLRAILGEWSMRAAKLERALE-VERISNIELR------KKVSALR 342
Cdd:COG2433 474 IERLERELEEERERIEELKRKLErLKELWKLEHSgelvpvKVVEKFT 520
 
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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