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Conserved domains on  [gi|1907068026|ref|XP_036019092|]
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nck-associated protein 5 isoform X9 [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 ...
1431-1733 2.72e-135

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: 423.80  E-value: 2.72e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1431 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1510
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1511 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1582
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1583 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1662
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068026 1663 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1733
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-271 9.56e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 9.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   37 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 116
Cdd:COG1196    222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  117 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 195
Cdd:COG1196    302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068026  196 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQE 271
Cdd:COG1196    376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
PHA03247 super family cl33720
large tegument protein UL36; Provisional
805-1016 1.19e-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: 47.24  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  805 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 880
Cdd:PHA03247  2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  881 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 960
Cdd:PHA03247  2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068026  961 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 1016
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 ...
1431-1733 2.72e-135

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: 423.80  E-value: 2.72e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1431 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1510
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1511 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1582
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1583 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1662
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068026 1663 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1733
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-271 9.56e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 9.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   37 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 116
Cdd:COG1196    222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  117 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 195
Cdd:COG1196    302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068026  196 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQE 271
Cdd:COG1196    376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-254 7.38e-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: 47.74  E-value: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   32 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQmlgLQQQ 111
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE---LEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  112 FSRMEETVRSLlqsqgspeqkkeepakITAYQEglpdeerkEQAALGDLHVVAADEDSRSEhsSVEEGKEDSRLLLKRLK 191
Cdd:TIGR02168  791 IEQLKEELKAL----------------REALDE--------LRAELTLLNEEAANLRERLE--SLERRIAATERRLEDLE 844
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907068026  192 ALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 254
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
PHA03247 PHA03247
large tegument protein UL36; Provisional
805-1016 1.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  805 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 880
Cdd:PHA03247  2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  881 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 960
Cdd:PHA03247  2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068026  961 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 1016
Cdd:PHA03247  2741 -----------PPAVPAGPAT-----PGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
24-262 9.65e-04

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: 43.96  E-value: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   24 EYMDSNKCIEHLLAQLREQHRSLWREKLAVARlQREVAQRTSQGAMHEKLihELEEERHL-RLQSEERLREVtlesERNR 102
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM--AMERERELeRIRQEERKREL----ERIR 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  103 IQMLGLQqqFSRMEETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAADEdsrsehssvEEGKED 182
Cdd:pfam17380  367 QEEIAME--ISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ---------EEARQR 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  183 SRLLLKRLKALEAENsaLALENENQREQYERCLDEVANQVVRALLTQKDLRE--ECVKLKTRVFDLEQQNRALSLLFQQR 260
Cdd:pfam17380  436 EVRRLEEERAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEER 513

                   ..
gi 1907068026  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 6.06e-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: 6.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068026   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 ...
1431-1733 2.72e-135

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: 423.80  E-value: 2.72e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1431 LSPSIEEKVMLCIQENVEKGQVQTKSASVEVKPRAGPSFTSWFGFRKSRLPALSSRRMEASKSKVEKKDTKLKSERKKEK 1510
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1511 KK--------AEVQSKIENELSRGTKKADGqsPDDGLQSSESLKVSQDIYNQMKLEPRNRPSPAVCPTKDAFMTELLNRV 1582
Cdd:pfam15246   81 KSekkkekkkEELQCALEEELAYKNEVGLD--RDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1583 DKRASVQRESGSKGVSCRSVLEGTSQGSCFASGSVSTQGSQKKNIKTKVDMEKPRESLGAEVNEDVQEDEEDRVADTTLQ 1662
Cdd:pfam15246  159 DKKAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQ 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068026 1663 SHMIESNCQMRTLDSGIGTFPLPDSGNRSVGRYICQQDSPEDTDALLPLQPAASMASSARAQTLDREVPSS 1733
Cdd:pfam15246  239 DHFIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-271 9.56e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 9.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   37 AQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSRME 116
Cdd:COG1196    222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  117 ETVRSLLqsqgspEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAAD-EDSRSEHSSVEEGKEDSRLLLKRLKALEA 195
Cdd:COG1196    302 QDIARLE------ERRRELEERLEELEEELAELEEELEELEEELEELEEElEEAEEELEEAEAELAEAEEALLEAEAELA 375
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068026  196 ENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQE 271
Cdd:COG1196    376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
32-253 2.05e-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: 2.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   32 IEHLLAQLREQHRSL------------WREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESE 99
Cdd:COG1196    191 LEDILGELERQLEPLerqaekaeryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  100 RNRIQMLGLQQQFSRMEETVRSLLQSQGSPEQKKEepakitAYQEGLPDEERKEQAALGDLHVVAADEDSRSEH-SSVEE 178
Cdd:COG1196    271 ELRLELEELELELEEAQAEEYELLAELARLEQDIA------RLEERRRELEERLEELEEELAELEEELEELEEElEELEE 344
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907068026  179 GKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRAL 253
Cdd:COG1196    345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
15-273 4.61e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   15 RLSLDSSLVEYMDSNKCIEHLLAQLREQHRslwREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREV 94
Cdd:COG1196    280 ELELEEAQAEEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   95 TLESERNRIQMLGLQQQFSRMEETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLhvvAADEDSRSEHS 174
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAEL 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  175 SVEEGKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREEcvklktrvfdLEQQNRALS 254
Cdd:COG1196    434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL----------LLLEAEADY 503
                          250
                   ....*....|....*....
gi 1907068026  255 LLFQQRVRPASDVLLQEHL 273
Cdd:COG1196    504 EGFLEGVKAALLLAGLRGL 522
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-254 7.38e-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: 47.74  E-value: 7.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   32 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTLESERNRIQmlgLQQQ 111
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE---LEAQ 790
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  112 FSRMEETVRSLlqsqgspeqkkeepakITAYQEglpdeerkEQAALGDLHVVAADEDSRSEhsSVEEGKEDSRLLLKRLK 191
Cdd:TIGR02168  791 IEQLKEELKAL----------------REALDE--------LRAELTLLNEEAANLRERLE--SLERRIAATERRLEDLE 844
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907068026  192 ALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 254
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
PHA03247 PHA03247
large tegument protein UL36; Provisional
805-1016 1.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  805 TPASPMGKLSQCRKAESPGSLcdvQPESHIPKHPAQVP----HIPKISNKKNWVQCPRSQTSGIQSRHLMGRSDSSEMRS 880
Cdd:PHA03247  2597 RPRAPVDDRGDPRGPAPPSPL---PPDTHAPDPPPPSPspaaNEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA 2673
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  881 NGcVSAPQTRMRSPSPPTPPGrSVSLLVRPSyDYPPLPSPAkPETQGPGDAVSPGlksPLLKGSSAPLVSSSPVmseiqk 960
Cdd:PHA03247  2674 AQ-ASSPPQRPRRRAARPTVG-SLTSLADPP-PPPPTPEPA-PHALVSATPLPPG---PAAARQASPALPAAPA------ 2740
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907068026  961 kpsvasrksafPPALPSTQAVvhtryPEHIASSPFAVTTSGPPKVSPKRGIPKPPP 1016
Cdd:PHA03247  2741 -----------PPAVPAGPAT-----PGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
71-277 1.63e-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: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   71 EKLIHELEEE-RHLRLQSE--ERLREVTLESERNRIQMLGLQQQF--SRMEETVRSLLQSQgspEQKKEEPAKITAYQEG 145
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEkaERYKELKAELRELELALLVLRLEElrEELEELQEELKEAE---EELEELTAELQELEEK 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  146 L--------PDEERKE--QAALGDLhvvaadedsRSEHSSVEEGKEDSRLLLKRLKALEAENSALALENENQREQYERCL 215
Cdd:TIGR02168  269 LeelrlevsELEEEIEelQKELYAL---------ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907068026  216 DEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLLFQQRVRPASDVLLQEHLQNAK 277
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-254 1.81e-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: 46.59  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   35 LLAQLREQHRSLWREKLAVARLQREVAQrtsqgamHEKLIHELEEErhlrlQSEERLREVTLESERNRIQ--MLGLQQQF 112
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEE-------LTAELQELEEK-----LEELRLEVSELEEEIEELQkeLYALANEI 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  113 SRMEETVRSLLQSQGSPEQKKEEpakitaYQEGLPDEERKEQAALGDLHVVAADEDS-RSEHSSVEEgkedsrlllkrlk 191
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEE------LEAQLEELESKLDELAEELAELEEKLEElKEELESLEA------------- 358
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907068026  192 alEAENSALALEN-ENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALS 254
Cdd:TIGR02168  359 --ELEELEAELEElESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
24-268 2.13e-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: 46.50  E-value: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   24 EYMDSNKCIEHLLAQLREQHRSLWREKLAVARLQREVA----QRTSQGAMHEKLIHELEEERHLrLQSEERLREVTLESe 99
Cdd:TIGR00618  536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSiltqCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLACE- 613
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  100 rNRIQMLGLQQQFSRMEetvRSLLQSQGSPEQKKEEPAKiTAYQEGLPDEERKEQAALgdlhvVAADEDSRSEHSSVEEG 179
Cdd:TIGR00618  614 -QHALLRKLQPEQDLQD---VRLHLQQCSQELALKLTAL-HALQLTLTQERVREHALS-----IRVLPKELLASRQLALQ 683
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  180 KEDSrlllkrlkalEAENSALALENENQREQYERCLDEVanqvvraLLTQKDLREE-CVKLKTRVFDLEQQNRALSLLFQ 258
Cdd:TIGR00618  684 KMQS----------EKEQLTYWKEMLAQCQTLLRELETH-------IEEYDREFNEiENASSSLGSDLAAREDALNQSLK 746
                          250
                   ....*....|
gi 1907068026  259 QRVRPASDVL 268
Cdd:TIGR00618  747 ELMHQARTVL 756
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
32-289 5.32e-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: 45.05  E-value: 5.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   32 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEERHlRLQSE-----ERLREVTLESERNRIQML 106
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE-ELQKElyalaNEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  107 GLQQQFSRMEEtvrSLLQSQGSPEQKKEEPAKITAYQ-------EGLPDEERKEQAALGDLH--VVAADEDSRSEHSSVE 177
Cdd:TIGR02168  313 NLERQLEELEA---QLEELESKLDELAEELAELEEKLeelkeelESLEAELEELEAELEELEsrLEELEEQLETLRSKVA 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  178 EGKEDSRLLLKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKD-LREECVKLKTRVFDLEQQNRALSLL 256
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeLEEELEELQEELERLEEALEELREE 469
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907068026  257 F---QQRVRPASDVL------------LQEHLQNAKSGTPALKHSGSG 289
Cdd:TIGR02168  470 LeeaEQALDAAERELaqlqarldslerLQENLEGFSEGVKALLKNQSG 517
PHA03378 PHA03378
EBNA-3B; Provisional
768-1069 8.57e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  768 GLTKIPSRGKSSPQKSKLVESMPTMLVPSSALVTPEKTPASPMgklSQCRKAESPGSLCDVQPESHIPKHPAQVPHIPki 847
Cdd:PHA03378   568 GLGPLQIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPT---TQSHIPETSAPRQWPMPLRPIPMRPLRMQPIT-- 642
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  848 snkknwvqcprSQTSGIQSRHLMGRSDSSEMRSNGCVSApqtrmRSPSPPTPPGRSVSLLVRPSydypplPSPAKPETQG 927
Cdd:PHA03378   643 -----------FNVLVFPTPHQPPQVEITPYKPTWTQIG-----HIPYQPSPTGANTMLPIQWA------PGTMQPPPRA 700
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  928 PGDAVSPglkspllkgSSAPLVSSSPVMSEIQKKPSVASRKSAFPPALPSTQAVVHTRYPEHIASSPFAVTTSGPPKVSP 1007
Cdd:PHA03378   701 PTPMRPP---------AAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAP 771
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026 1008 KRGIPKPPPHhaLGTAHMD------TDLQTPKTCPSSCELL--EVTSCKSLSPGRKRQLSDSTVMPHRPS 1069
Cdd:PHA03378   772 GAPTPQPPPQ--APPAPQQrprgapTPQPPPQAGPTSMQLMprAAPGQQGPTKQILRQLLTGGVKRGRPS 839
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
24-262 9.65e-04

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: 43.96  E-value: 9.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   24 EYMDSNKCIEHLLAQLREQHRSLWREKLAVARlQREVAQRTSQGAMHEKLihELEEERHL-RLQSEERLREVtlesERNR 102
Cdd:pfam17380  294 EKMEQERLRQEKEEKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERM--AMERERELeRIRQEERKREL----ERIR 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  103 IQMLGLQqqFSRMEETVRSLLQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAALGDLHVVAADEdsrsehssvEEGKED 182
Cdd:pfam17380  367 QEEIAME--ISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ---------EEARQR 435
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  183 SRLLLKRLKALEAENsaLALENENQREQYERCLDEVANQVVRALLTQKDLRE--ECVKLKTRVFDLEQQNRALSLLFQQR 260
Cdd:pfam17380  436 EVRRLEEERAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEER 513

                   ..
gi 1907068026  261 VR 262
Cdd:pfam17380  514 KR 515
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
885-1023 2.64e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.78  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  885 SAPQTRMRSPSPPTPPGRSvsllvrpsydyPPLPSPAKPETQGPGDAVSPglkspllkgssaPLVSSSPVMSEIQKKPSV 964
Cdd:PRK14951   369 AAEAAAPAEKKTPARPEAA-----------APAAAPVAQAAAAPAPAAAP------------AAAASAPAAPPAAAPPAP 425
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068026  965 ASRKSAFPPALPSTQAVVHTRYPEHIASSPFAVTTSGPPKVSPKRGIPKPPPHHALGTA 1023
Cdd:PRK14951   426 VAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPA 484
PHA03247 PHA03247
large tegument protein UL36; Provisional
773-1016 3.16e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  773 PSRGKSSPQKSKLVESMPTMLVPSSALVTPEKTPASPMGKLSQCRKAESPGSLCDVQPESHIPKHPAQVPHIPKISNKKN 852
Cdd:PHA03247  2679 PPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPA 2758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  853 WVQC---------PRSQTSGIQSRhLMGRSDSSEMRSNGCVSAPQTRMRSPSPPTPPGRSVSLLVRPSydyPPLPSPAKP 923
Cdd:PHA03247  2759 RPPTtagppapapPAAPAAGPPRR-LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPA---GPLPPPTSA 2834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  924 ETQGPGDAVSPGLKSPLLKGSSAP--LVSSSPVMSEIQKKPSVAS----RKSAFPPALPSTQAVVHTRYPEHIASSPFAV 997
Cdd:PHA03247  2835 QPTAPPPPPGPPPPSLPLGGSVAPggDVRRRPPSRSPAAKPAAPArppvRRLARPAVSRSTESFALPPDQPERPPQPQAP 2914
                          250
                   ....*....|....*....
gi 1907068026  998 TTSGPPKVSPKRGIPKPPP 1016
Cdd:PHA03247  2915 PPPQPQPQPPPPPQPQPPP 2933
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
32-278 3.68e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   32 IEHLLAQLREQHRSLWREKLAVARLQREVAQRTSQGAMHEKLIHELEEErhLRLQSEERLREVTLESERnriqmlgLQQQ 111
Cdd:COG4717    137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ--LSLATEEELQDLAEELEE-------LQQR 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  112 FSRMEETVRSLlqsQGSPEQKKEEPAKITAYQEGLPDEERKEQA-----ALGDLHVVAADEDSRSEHSSVEEGKEDSRLL 186
Cdd:COG4717    208 LAELEEELEEA---QEELEELEEELEQLENELEAAALEERLKEArllllIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  187 LKRLKALEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREEcvKLKTRVFDLEQQNRALSLLFQQRVRPASD 266
Cdd:COG4717    285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD--LSPEELLELLDRIEELQELLREAEELEEE 362
                          250
                   ....*....|..
gi 1907068026  267 VLLQEHLQNAKS 278
Cdd:COG4717    363 LQLEELEQEIAA 374
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
35-262 4.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026   35 LLAQLREQHRSLWREKlavarlqrevaQRTSQGAMHEklIHELEEERHLRLQSEERLREVTLESERNRIQMLGLQQQFSR 114
Cdd:COG4717     47 LLERLEKEADELFKPQ-----------GRKPELNLKE--LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907068026  115 MEETVRSL---LQSQGSPEQKKEEPAKITAYQEGLPDEERKEQAalgdlhVVAADEDSRSEHSSVEEGKEDsrlllkrlk 191
Cdd:COG4717    114 LREELEKLeklLQLLPLYQELEALEAELAELPERLEELEERLEE------LRELEEELEELEAELAELQEE--------- 178
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907068026  192 aLEAENSALALENENQREQYERCLDEVANQVVRALLTQKDLREECVKLKTRVFDLEQQNRALSLlfQQRVR 262
Cdd:COG4717    179 -LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL--EERLK 246
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
32-96 6.06e-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: 6.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907068026   32 IEHLLAQLREQHRSLWREKLA----VARLQREVAQRTSQGAMHEKLIHELEEERHLRLQSEERLREVTL 96
Cdd:cd19543    176 IAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
 
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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