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Conserved domains on  [gi|755494008|ref|XP_011246260|]
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nck-associated protein 5 isoform X3 [Mus musculus]

Protein Classification

SMC_prok_B and NCKAP5 domain-containing protein( domain architecture ID 10633646)

protein containing domains SMC_prok_B, PHA03247, and NCKAP5

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NCKAP5 pfam15246
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ...
1406-1708 2.72e-134

Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein 5, which is also known as the Peripheral clock protein. NCKAP5 is a protein family, which interacts with the SH3-containing region of the adaptor protein Nck. Nck is a protein that interacts with receptor tyrosine kinases and guanine nucleotide exchange factor Sos. The role of Nck can be thought of as similar to Grb2. The role of NCKAP5 is to assist Nck with its adaptor protein role.


:

Pssm-ID: 464586  Cd Length: 309  Bit Score: 421.49  E-value: 2.72e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1406 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1485
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1486 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1557
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1558 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1637
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494008  1638 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1708
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
12-246 1.25e-05

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: 50.32  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   12 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 91
Cdd:COG1196   222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   92 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 170
Cdd:COG1196   302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494008  171 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQE 246
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PHA03247 super family cl33720
large tegument protein UL36; Provisional
780-991 1.12e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  780 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 855
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  856 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 935
Cdd:PHA03247 2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755494008  936 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 991
Cdd:PHA03247 2741 -----------PPAVPAGPAT-----PGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
 
Name Accession Description Interval E-value
NCKAP5 pfam15246
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ...
1406-1708 2.72e-134

Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein 5, which is also known as the Peripheral clock protein. NCKAP5 is a protein family, which interacts with the SH3-containing region of the adaptor protein Nck. Nck is a protein that interacts with receptor tyrosine kinases and guanine nucleotide exchange factor Sos. The role of Nck can be thought of as similar to Grb2. The role of NCKAP5 is to assist Nck with its adaptor protein role.


Pssm-ID: 464586  Cd Length: 309  Bit Score: 421.49  E-value: 2.72e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1406 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1485
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1486 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1557
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1558 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1637
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494008  1638 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1708
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
12-246 1.25e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   12 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 91
Cdd:COG1196   222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   92 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 170
Cdd:COG1196   302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494008  171 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQE 246
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PHA03247 PHA03247
large tegument protein UL36; Provisional
780-991 1.12e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  780 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 855
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  856 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 935
Cdd:PHA03247 2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755494008  936 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 991
Cdd:PHA03247 2741 -----------PPAVPAGPAT-----PGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-229 1.21e-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: 47.36  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008     7 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQmlgLQQQ 86
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE---LEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    87 FSRMEETVRSLlqsqgspeqkkeepakITAYQEglpdeerkEQAALGDLHVVAADEDSRSEhsSVEEGKEDSRLLLKRLK 166
Cdd:TIGR02168  791 IEQLKEELKAL----------------REALDE--------LRAELTLLNEEAANLRERLE--SLERRIAATERRLEDLE 844
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755494008   167 ALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 229
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
13-237 2.25e-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: 42.80  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    13 QLREQHRSLWREKLAVARlQREVAQRTSQGAMHEKLihELEEERHL-RLQSEERLREVtlesERNRIQMLGLQqqFSRME 91
Cdd:pfam17380  308 KAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM--AMERERELeRIRQEERKREL----ERIRQEEIAME--ISRMR 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    92 ETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAADEdsrsehssvEEGKEDSRLLLKRLKALEAE 171
Cdd:pfam17380  379 ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ---------EEARQREVRRLEEERAREME 449
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755494008   172 NsaLALENENQREQYERCLDEVANQVVRALLTQKDLRE--ECVKLKTRVFDLEQQNRALSLLFQQRVR 237
Cdd:pfam17380  450 R--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR 515
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
7-71 6.26e-03

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 41.03  E-value: 6.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494008    7 IEHLLAQLREQHRSLWREKLA----VARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTL 71
Cdd:cd19543   176 IAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
 
Name Accession Description Interval E-value
NCKAP5 pfam15246
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ...
1406-1708 2.72e-134

Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein 5, which is also known as the Peripheral clock protein. NCKAP5 is a protein family, which interacts with the SH3-containing region of the adaptor protein Nck. Nck is a protein that interacts with receptor tyrosine kinases and guanine nucleotide exchange factor Sos. The role of Nck can be thought of as similar to Grb2. The role of NCKAP5 is to assist Nck with its adaptor protein role.


Pssm-ID: 464586  Cd Length: 309  Bit Score: 421.49  E-value: 2.72e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1406 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1485
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1486 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1557
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  1558 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1637
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494008  1638 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1708
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
12-246 1.25e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   12 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 91
Cdd:COG1196   222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   92 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 170
Cdd:COG1196   302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755494008  171 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQE 246
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
7-228 2.66e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    7 IEHLLAQLREQHRSL------------WREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESE 74
Cdd:COG1196   191 LEDILGELERQLEPLerqaekaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   75 RNRIQMLGLQQQFSRMEETVRSLLQSQGSPEQKKEepakitAYQEGLPDEERKEQAALGDLHVVAADEDSRSEH-SSVEE 153
Cdd:COG1196   271 ELRLELEELELELEEAQAEEYELLAELARLEQDIA------RLEERRRELEERLEELEEELAELEEELEELEEElEELEE 344
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755494008  154 GKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRAL 228
Cdd:COG1196   345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
11-248 6.52e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 6.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   11 LAQLREQHRSLwREKL--AVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFS 88
Cdd:COG1196   297 LARLEQDIARL-EERRreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   89 RMEETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLhvvAADEDSRSEHSSVEEGKEDSRLLLKRLKAL 168
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEALEEAAEEEA 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  169 EAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREEcvklktrvfdLEQQNRALSLLFQQRVRPASDVLLQEHL 248
Cdd:COG1196   453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL----------LLLEAEADYEGFLEGVKAALLLAGLRGL 522
PHA03247 PHA03247
large tegument protein UL36; Provisional
780-991 1.12e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  780 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 855
Cdd:PHA03247 2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  856 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 935
Cdd:PHA03247 2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755494008  936 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 991
Cdd:PHA03247 2741 -----------PPAVPAGPAT-----PGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-229 1.21e-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: 47.36  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008     7 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQmlgLQQQ 86
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE---LEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    87 FSRMEETVRSLlqsqgspeqkkeepakITAYQEglpdeerkEQAALGDLHVVAADEDSRSEhsSVEEGKEDSRLLLKRLK 166
Cdd:TIGR02168  791 IEQLKEELKAL----------------REALDE--------LRAELTLLNEEAANLRERLE--SLERRIAATERRLEDLE 844
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755494008   167 ALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 229
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
46-252 2.68e-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: 46.20  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    46 EKLIHELEEE-RHLRLQSE--ERLREVTLESERNRIQMLGLQQQF--SRMEETVRSLLQSQgspEQKKEEPAKITAYQEG 120
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEkaERYKELKAELRELELALLVLRLEElrEELEELQEELKEAE---EELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   121 L--------PDEERKE--QAALGDLhvvaadedsRSEHSSVEEGKEDSRLLLKRLKALEAENSALALENENQREQYERCL 190
Cdd:TIGR02168  269 LeelrlevsELEEEIEelQKELYAL---------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755494008   191 DEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQEHLQNAK 252
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
10-229 3.34e-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: 45.82  E-value: 3.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    10 LLAQLREQHRSLWREKLAVARLQREVAQrtsqgamHEKLIHELEEErhlrlQSEERLREVTLESERNRIQ--MLGLQQQF 87
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEE-------LTAELQELEEK-----LEELRLEVSELEEEIEELQkeLYALANEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    88 SRMEETVRSLLQSQGSPEQKKEEpakitaYQEGLPDEERKEQAALGDLHVVAADEDS-RSEHSSVEEgkedsrlllkrlk 166
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEE------LEAQLEELESKLDELAEELAELEEKLEElKEELESLEA------------- 358
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755494008   167 alEAENSALALEN-ENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 229
Cdd:TIGR02168  359 --ELEELEAELEElESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
5-243 6.45e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 6.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008     5 KCIEHLLAQLREQHRSLWREKLAVARLQREVA----QRTSQGAMHEKLIHELEEERHLrLQSEERLREVTLESerNRIQM 80
Cdd:TIGR00618  542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLACE--QHALL 618
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    81 LGLQQQFSRMEetvRSLLQSQGSPEQKKEEPAKiTAYQEGLPDEERKEQAALgdlhvVAADEDSRSEHSSVEEGKEDSrl 160
Cdd:TIGR00618  619 RKLQPEQDLQD---VRLHLQQCSQELALKLTAL-HALQLTLTQERVREHALS-----IRVLPKELLASRQLALQKMQS-- 687
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   161 llkrlkalEAENSALALENENQREQYERCLDEVanqvvraLLTQKDLREE-CVKLKTRVFDLEQQNRALSLLFQQRVRPA 239
Cdd:TIGR00618  688 --------EKEQLTYWKEMLAQCQTLLRELETH-------IEEYDREFNEiENASSSLGSDLAAREDALNQSLKELMHQA 752

                   ....
gi 755494008   240 SDVL 243
Cdd:TIGR00618  753 RTVL 756
PHA03378 PHA03378
EBNA-3B; Provisional
743-1044 7.00e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  743 GLTKIPSRGKSSPQKSKLVESMPTMLVPSSALVTPEKTPASPMgklSQCRKAESPGSLCDVQPESHIPKHPAQVPHIPki 822
Cdd:PHA03378  568 GLGPLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPT---TQSHIPETSAPRQWPMPLRPIPMRPLRMQPIT-- 642
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  823 snkknwvqcprSQTSGIQSRHLMGRSDSSEMRSNGCVSApqtrmRSPSPPTPPGRSVSLLVRPSydypplPSPAKPETQG 902
Cdd:PHA03378  643 -----------FNVLVFPTPHQPPQVEITPYKPTWTQIG-----HIPYQPSPTGANTMLPIQWA------PGTMQPPPRA 700
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  903 PGDAVSPglkspllkgSSAPLVSSSPVMSEIQKKPSVASRKSAFPPALPSTQAVVHTRYPEHIASSPFAVTTSGPPKVSP 982
Cdd:PHA03378  701 PTPMRPP---------AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAP 771
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  983 KRGIPKPPPHhaLGTAHMD------TDLQTPKTCPSSCELL--EVTSCKSLSPGRKRQLSDSTVMPHRPS 1044
Cdd:PHA03378  772 GAPTPQPPPQ--APPAPQQrprgapTPQPPPQAGPTSMQLMprAAPGQQGPTKQILRQLLTGGVKRGRPS 839
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-264 9.68e-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: 44.28  E-value: 9.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008     7 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHlRLQSE-----ERLREVTLESERNRIQML 81
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE-ELQKElyalaNEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    82 GLQQQFSRMEETV----RSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLH--VVAADEDSRSEHSSVEEGK 155
Cdd:TIGR02168  313 NLERQLEELEAQLeeleSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrLEELEEQLETLRSKVAQLE 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   156 EDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKD-LREECVKLKTRVFDLEQQNRALSLLF-- 232
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeLEEELEELQEELERLEEALEELREELee 472
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 755494008   233 -QQRVRPASDVL------------LQEHLQNAKSGTPALKHSGSG 264
Cdd:TIGR02168  473 aEQALDAAERELaqlqarldslerLQENLEGFSEGVKALLKNQSG 517
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
13-237 2.25e-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: 42.80  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    13 QLREQHRSLWREKLAVARlQREVAQRTSQGAMHEKLihELEEERHL-RLQSEERLREVtlesERNRIQMLGLQqqFSRME 91
Cdd:pfam17380  308 KAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM--AMERERELeRIRQEERKREL----ERIRQEEIAME--ISRMR 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    92 ETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAADEdsrsehssvEEGKEDSRLLLKRLKALEAE 171
Cdd:pfam17380  379 ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ---------EEARQREVRRLEEERAREME 449
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755494008   172 NsaLALENENQREQYERCLDEVANQVVRALLTQKDLRE--ECVKLKTRVFDLEQQNRALSLLFQQRVR 237
Cdd:pfam17380  450 R--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR 515
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
860-998 2.73e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.78  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  860 SAPQTRMRSPSPPTPPGRSvsllvrpsydyPPLPSPAKPETQGPGDAVSPglkspllkgssaPLVSSSPVMSEIQKKPSV 939
Cdd:PRK14951  369 AAEAAAPAEKKTPARPEAA-----------APAAAPVAQAAAAPAPAAAP------------AAAASAPAAPPAAAPPAP 425
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755494008  940 ASRKSAFPPALPSTQAVVHTRYPEHIASSPFAVTTSGPPKVSPKRGIPKPPPHHALGTA 998
Cdd:PRK14951  426 VAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPA 484
PHA03247 PHA03247
large tegument protein UL36; Provisional
748-991 3.30e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  748 PSRGKSSPQKSKLVESMPTMLVPSSALVTPEKTPASPMGKLSQCRKAESPGSLCDVQPESHIPKHPAQVPHIPKISNKKN 827
Cdd:PHA03247 2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  828 WVQC---------PRSQTSGIQSRhLMGRSDSSEMRSNGCVSAPQTRMRSPSPPTPPGRSVSLLVRPSydyPPLPSPAKP 898
Cdd:PHA03247 2759 RPPTtagppapapPAAPAAGPPRR-LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA---GPLPPPTSA 2834
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  899 ETQGPGDAVSPGLKSPLLKGSSAP--LVSSSPVMSEIQKKPSVAS----RKSAFPPALPSTQAVVHTRYPEHIASSPFAV 972
Cdd:PHA03247 2835 QPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAKPAAPArppvRRLARPAVSRSTESFALPPDQPERPPQPQAP 2914
                         250
                  ....*....|....*....
gi 755494008  973 TTSGPPKVSPKRGIPKPPP 991
Cdd:PHA03247 2915 PPPQPQPQPPPPPQPQPPP 2933
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
7-253 5.82e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008    7 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEErhLRLQSEERLREVTLESERnriqmlgLQQQ 86
Cdd:COG4717   137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ--LSLATEEELQDLAEELEE-------LQQR 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   87 FSRMEETVRSLlqsQGSPEQKKEEPAKITAYQEGLPDEERKEQA-----ALGDLHVVAADEDSRSEHSSVEEGKEDSRLL 161
Cdd:COG4717   208 LAELEEELEEA---QEELEELEEELEQLENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008  162 LKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREEcvKLKTRVFDLEQQNRALSLLFQQRVRPASD 241
Cdd:COG4717   285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD--LSPEELLELLDRIEELQELLREAEELEEE 362
                         250
                  ....*....|..
gi 755494008  242 VLLQEHLQNAKS 253
Cdd:COG4717   363 LQLEELEQEIAA 374
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
7-71 6.26e-03

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 41.03  E-value: 6.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755494008    7 IEHLLAQLREQHRSLWREKLA----VARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTL 71
Cdd:cd19543   176 IAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
10-237 8.04e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   10 LLAQLREQHRSLWREKlavarlqrevaQRTSQGAMHEklIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSR 89
Cdd:COG4717    47 LLERLEKEADELFKPQ-----------GRKPELNLKE--LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755494008   90 MEETVRSL---LQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAalgdlhVVAADEDSRSEHSSVEEGKEDsrlllkrlk 166
Cdd:COG4717   114 LREELEKLeklLQLLPLYQELEALEAELAELPERLEELEERLEE------LRELEEELEELEAELAELQEE--------- 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755494008  167 aLEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLlfQQRVR 237
Cdd:COG4717   179 -LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL--EERLK 246
 
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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