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Conserved domains on  [gi|1907068028|ref|XP_036019094|]
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nck-associated protein 5 isoform X10 [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 ...
1367-1669 3.44e-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: 420.33  E-value: 3.44e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1367 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1446
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1447 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1518
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1519 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1598
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068028 1599 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1669
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
57-254 9.36e-06

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 9.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   57 QREVAQRTSQGAMHEKLIHELEEE----RHLRLQSEERLREVTLESERNRIQMLGLQQQFSRMEETVRSLLQSQgspEQK 132
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI---AQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  133 KEEPAKITAYQEGLPDEERKEQAALgdlhvVAADEDSRSEHSSVEEGKEDSRLLLKRLKALEAENSAL---ALENENQRE 209
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEEL-----AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLE 827
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907068028  210 QYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 254
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
PHA03247 super family cl33720
large tegument protein UL36; Provisional
741-952 1.16e-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: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  741 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 816
Cdd:PHA03247  2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  817 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 896
Cdd:PHA03247  2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068028  897 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 952
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 ...
1367-1669 3.44e-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: 420.33  E-value: 3.44e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1367 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1446
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1447 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1518
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1519 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1598
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068028 1599 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1669
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
57-254 9.36e-06

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: 50.83  E-value: 9.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   57 QREVAQRTSQGAMHEKLIHELEEE----RHLRLQSEERLREVTLESERNRIQMLGLQQQFSRMEETVRSLLQSQgspEQK 132
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI---AQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  133 KEEPAKITAYQEGLPDEERKEQAALgdlhvVAADEDSRSEHSSVEEGKEDSRLLLKRLKALEAENSAL---ALENENQRE 209
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEEL-----AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLE 827
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907068028  210 QYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 254
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-271 1.46e-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: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   37 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 116
Cdd:COG1196    222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  117 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 195
Cdd:COG1196    302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068028  196 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQQ 271
Cdd:COG1196    376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PHA03247 PHA03247
large tegument protein UL36; Provisional
741-952 1.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  741 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 816
Cdd:PHA03247  2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  817 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 896
Cdd:PHA03247  2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068028  897 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 952
Cdd:PHA03247  2741 -----------PPAVPAGPAT-----PGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
24-262 1.78e-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: 43.19  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   24 EYMDSNKCIEHLLAQLREQHRSLWREKLAVARlQREVAQRTSQGAMHEKLihELEEERHL-RLQSEERLREVtlesERNR 102
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM--AMERERELeRIRQEERKREL----ERIR 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  103 IQMLGLQqqFSRMEETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAADEdsrsehssvEEGKED 182
Cdd:pfam17380  367 QEEIAME--ISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ---------EEARQR 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  183 SRLLLKRLKALEAENsaLALENENQREQYERCLDEVANQVVRALLTQKDLRE--ECVKLKTRVFDLEQQNRALSLLFQQR 260
Cdd:pfam17380  436 EVRRLEEERAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEER 513

                   ..
gi 1907068028  261 VR 262
Cdd:pfam17380  514 KR 515
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
32-96 6.02e-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: 6.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068028   32 IEHLLAQLREQHRSLWREKLA----VARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTL 96
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 ...
1367-1669 3.44e-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: 420.33  E-value: 3.44e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1367 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1446
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1447 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1518
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028 1519 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1598
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068028 1599 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1669
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
57-254 9.36e-06

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: 50.83  E-value: 9.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   57 QREVAQRTSQGAMHEKLIHELEEE----RHLRLQSEERLREVTLESERNRIQMLGLQQQFSRMEETVRSLLQSQgspEQK 132
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKAlaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI---AQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  133 KEEPAKITAYQEGLPDEERKEQAALgdlhvVAADEDSRSEHSSVEEGKEDSRLLLKRLKALEAENSAL---ALENENQRE 209
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEEL-----AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLE 827
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907068028  210 QYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 254
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-271 1.46e-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: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   37 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 116
Cdd:COG1196    222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  117 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 195
Cdd:COG1196    302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068028  196 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQQ 271
Cdd:COG1196    376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
32-253 3.05e-05

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: 3.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   32 IEHLLAQLREQHRSL------------WREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESE 99
Cdd:COG1196    191 LEDILGELERQLEPLerqaekaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  100 RNRIQMLGLQQQFSRMEETVRSLLQSQGSPEQKKEepakitAYQEGLPDEERKEQAALGDLHVVAADEDSRSEH-SSVEE 178
Cdd:COG1196    271 ELRLELEELELELEEAQAEEYELLAELARLEQDIA------RLEERRRELEERLEELEEELAELEEELEELEEElEELEE 344
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907068028  179 GKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRAL 253
Cdd:COG1196    345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-275 7.09e-05

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: 48.13  E-value: 7.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   35 LLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHlRLQSEERLREVTLESERNRIQMLGLQQQF-- 112
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-ELEEEIEELQKELYALANEISRLEQQKQIlr 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  113 SRMEETVRSLLQSQGSPE---QKKEEPAKITAYQE-----------GLPDEERKEQAALGDLH--VVAADEDSRSEHSSV 176
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEeleSKLDELAEELAELEekleelkeeleSLEAELEELEAELEELEsrLEELEEQLETLRSKV 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  177 EEGKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKD-LREECVKLKTRVFDLEQQNRALSL 255
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeLEEELEELQEELERLEEALEELRE 468
                          250       260
                   ....*....|....*....|...
gi 1907068028  256 LF---QQRVRPASDVLLQQSSRI 275
Cdd:TIGR02168  469 ELeeaEQALDAAERELAQLQARL 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-271 7.48e-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: 7.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   15 RLSLDSSLVEYMDSNKCIEHLLAQLREQHRslwREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREV 94
Cdd:COG1196    280 ELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   95 TLESERNRIQMLGLQQQFSRMEETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLhvvAADEDSRSEHS 174
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAEL 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  175 SVEEGKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREEcvklktrvfdLEQQNRALS 254
Cdd:COG1196    434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL----------LLLEAEADY 503
                          250
                   ....*....|....*..
gi 1907068028  255 LLFQQRVRPASDVLLQQ 271
Cdd:COG1196    504 EGFLEGVKAALLLAGLR 520
PHA03247 PHA03247
large tegument protein UL36; Provisional
741-952 1.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  741 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 816
Cdd:PHA03247  2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  817 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 896
Cdd:PHA03247  2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068028  897 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 952
Cdd:PHA03247  2741 -----------PPAVPAGPAT-----PGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-254 1.36e-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: 46.97  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   32 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQmlgLQQQ 111
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE---LEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  112 FSRMEETVRSLlqsqgspeqkkeepakITAYQEglpdeerkEQAALGDLHVVAADEDSRSEhsSVEEGKEDSRLLLKRLK 191
Cdd:TIGR02168  791 IEQLKEELKAL----------------REALDE--------LRAELTLLNEEAANLRERLE--SLERRIAATERRLEDLE 844
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907068028  192 ALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 254
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
24-271 3.86e-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: 45.34  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   24 EYMDSNKCIEHLLAQLREQHRSLWREKLAVARLQREVA----QRTSQGAMHEKLIHELEEERHLrLQSEERLREVTLESe 99
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLACE- 613
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  100 rNRIQMLGLQQQFSRMEetvRSLLQSQGSPEQKKEEPAKiTAYQEGLPDEERKEQAALgdlhvVAADEDSRSEHSSVEEG 179
Cdd:TIGR00618  614 -QHALLRKLQPEQDLQD---VRLHLQQCSQELALKLTAL-HALQLTLTQERVREHALS-----IRVLPKELLASRQLALQ 683
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  180 KEDSrlllkrlkalEAENSALALENENQREQYERCLDEVanqvvraLLTQKDLREE-CVKLKTRVFDLEQQNRALSLLFQ 258
Cdd:TIGR00618  684 KMQS----------EKEQLTYWKEMLAQCQTLLRELETH-------IEEYDREFNEiENASSSLGSDLAAREDALNQSLK 746
                          250
                   ....*....|...
gi 1907068028  259 QRVRPASDVLLQQ 271
Cdd:TIGR00618  747 ELMHQARTVLKAR 759
PHA03378 PHA03378
EBNA-3B; Provisional
704-1005 8.03e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  704 GLTKIPSRGKSSPQKSKLVESMPTMLVPSSALVTPEKTPASPMgklSQCRKAESPGSLCDVQPESHIPKHPAQVPHIPki 783
Cdd:PHA03378   568 GLGPLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPT---TQSHIPETSAPRQWPMPLRPIPMRPLRMQPIT-- 642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  784 snkknwvqcprSQTSGIQSRHLMGRSDSSEMRSNGCVSApqtrmRSPSPPTPPGRSVSLLVRPSydypplPSPAKPETQG 863
Cdd:PHA03378   643 -----------FNVLVFPTPHQPPQVEITPYKPTWTQIG-----HIPYQPSPTGANTMLPIQWA------PGTMQPPPRA 700
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  864 PGDAVSPglkspllkgSSAPLVSSSPVMSEIQKKPSVASRKSAFPPALPSTQAVVHTRYPEHIASSPFAVTTSGPPKVSP 943
Cdd:PHA03378   701 PTPMRPP---------AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAP 771
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  944 KRGIPKPPPHhaLGTAHMD------TDLQTPKTCPSSCELL--EVTSCKSLSPGRKRQLSDSTVMPHRPS 1005
Cdd:PHA03378   772 GAPTPQPPPQ--APPAPQQrprgapTPQPPPQAGPTSMQLMprAAPGQQGPTKQILRQLLTGGVKRGRPS 839
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
24-262 1.78e-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: 43.19  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   24 EYMDSNKCIEHLLAQLREQHRSLWREKLAVARlQREVAQRTSQGAMHEKLihELEEERHL-RLQSEERLREVtlesERNR 102
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM--AMERERELeRIRQEERKREL----ERIR 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  103 IQMLGLQqqFSRMEETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAADEdsrsehssvEEGKED 182
Cdd:pfam17380  367 QEEIAME--ISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ---------EEARQR 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  183 SRLLLKRLKALEAENsaLALENENQREQYERCLDEVANQVVRALLTQKDLRE--ECVKLKTRVFDLEQQNRALSLLFQQR 260
Cdd:pfam17380  436 EVRRLEEERAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEER 513

                   ..
gi 1907068028  261 VR 262
Cdd:pfam17380  514 KR 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
71-273 2.02e-03

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: 43.12  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   71 EKLIHELEEE-RHLRLQSE--ERLREVTLESERNRIQMLGLQQQF--SRMEETVRSLLQSQgspEQKKEEPAKITAYQEG 145
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEkaERYKELKAELRELELALLVLRLEElrEELEELQEELKEAE---EELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  146 L--------PDEERKE--QAALGDLhvvaadedsRSEHSSVEEGKEDSRLLLKRLKALEAENSALALENENQREQYERCL 215
Cdd:TIGR02168  269 LeelrlevsELEEEIEelQKELYAL---------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907068028  216 DEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQQSS 273
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
821-959 2.78e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  821 SAPQTRMRSPSPPTPPGRSvsllvrpsydyPPLPSPAKPETQGPGDAVSPglkspllkgssaPLVSSSPVMSEIQKKPSV 900
Cdd:PRK14951   369 AAEAAAPAEKKTPARPEAA-----------APAAAPVAQAAAAPAPAAAP------------AAAASAPAAPPAAAPPAP 425
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068028  901 ASRKSAFPPALPSTQAVVHTRYPEHIASSPFAVTTSGPPKVSPKRGIPKPPPHHALGTA 959
Cdd:PRK14951   426 VAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPA 484
PHA03247 PHA03247
large tegument protein UL36; Provisional
709-952 3.33e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  709 PSRGKSSPQKSKLVESMPTMLVPSSALVTPEKTPASPMGKLSQCRKAESPGSLCDVQPESHIPKHPAQVPHIPKISNKKN 788
Cdd:PHA03247  2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  789 WVQC---------PRSQTSGIQSRhLMGRSDSSEMRSNGCVSAPQTRMRSPSPPTPPGRSVSLLVRPSydyPPLPSPAKP 859
Cdd:PHA03247  2759 RPPTtagppapapPAAPAAGPPRR-LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA---GPLPPPTSA 2834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  860 ETQGPGDAVSPGLKSPLLKGSSAP--LVSSSPVMSEIQKKPSVAS----RKSAFPPALPSTQAVVHTRYPEHIASSPFAV 933
Cdd:PHA03247  2835 QPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAKPAAPArppvRRLARPAVSRSTESFALPPDQPERPPQPQAP 2914
                          250
                   ....*....|....*....
gi 1907068028  934 TTSGPPKVSPKRGIPKPPP 952
Cdd:PHA03247  2915 PPPQPQPQPPPPPQPQPPP 2933
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
32-96 6.02e-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: 6.02e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068028   32 IEHLLAQLREQHRSLWREKLA----VARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTL 96
Cdd:cd19543    176 IAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
32-318 6.10e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   32 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHL-------------RLQSEERLREVTLES 98
Cdd:COG4372     75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDleqqrkqleaqiaELQSEIAEREEELKE 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   99 ERNRIQMlgLQQQFSRMEETVRSLLQSQGSPE-QKKEEPAKITAYQEGLPDEERKEQAALGDlhvVAADEDSRSEHSSVE 177
Cdd:COG4372    155 LEEQLES--LQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESLPR---ELAEELLEAKDSLEA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  178 EGKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLF 257
Cdd:COG4372    230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068028  258 QQRVRPASDVLLQQSSRIWDKRLSIDSSLPSGFASPADELPPTRIKESHILEGLRKLQKRK 318
Cdd:COG4372    310 IGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
35-262 8.71e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 8.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028   35 LLAQLREQHRSLWREKlavarlqrevaQRTSQGAMHEklIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSR 114
Cdd:COG4717     47 LLERLEKEADELFKPQ-----------GRKPELNLKE--LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068028  115 MEETVRSL---LQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAalgdlhVVAADEDSRSEHSSVEEGKEDsrlllkrlk 191
Cdd:COG4717    114 LREELEKLeklLQLLPLYQELEALEAELAELPERLEELEERLEE------LRELEEELEELEAELAELQEE--------- 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068028  192 aLEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLlfQQRVR 262
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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