NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034613615|ref|XP_016859466|]
View 

nck-associated protein 5 isoform X2 [Homo sapiens]

Protein Classification

C_NRPS-like and NCKAP5 domain-containing protein( domain architecture ID 13315136)

protein containing domains C_NRPS-like, PTZ00449, and NCKAP5

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1443-1751 2.10e-149

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: 463.09  E-value: 2.10e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1443 LSPTIEEKVMLCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1522
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1523 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1602
Cdd:pfam15246   81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1603 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1682
Cdd:pfam15246  161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613615 1683 IIESNCQMRTLDSGIGTFPLPDSGNRSTGRYLCQPDSPEDAEPLLPLQSALSAVSSMRAQTLEREVPSS 1751
Cdd:pfam15246  241 FIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-223 4.36e-08

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: 58.53  E-value: 4.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    4 NKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSL 83
Cdd:TIGR02168  213 ERYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   84 QQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLhmvvdedsrsessstDEGKEKTKLLLER 163
Cdd:TIGR02168  280 EEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL---------------EELESKLDELAEE 338
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  164 LKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQ 223
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
779-1050 3.15e-03

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  779 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 856
Cdd:PTZ00449   536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  857 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 929
Cdd:PTZ00449   609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  930 KsETRVP---------------SETARTPFKSPllkGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 994
Cdd:PTZ00449   687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613615  995 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1050
Cdd:PTZ00449   763 TPADTPLPDILAEEFKEEDIHAETGEP-------------DEAMKRPD-SPSEHED 804
 
Name Accession Description Interval E-value
NCKAP5 pfam15246
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ...
1443-1751 2.10e-149

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: 463.09  E-value: 2.10e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1443 LSPTIEEKVMLCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1522
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1523 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1602
Cdd:pfam15246   81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1603 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1682
Cdd:pfam15246  161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613615 1683 IIESNCQMRTLDSGIGTFPLPDSGNRSTGRYLCQPDSPEDAEPLLPLQSALSAVSSMRAQTLEREVPSS 1751
Cdd:pfam15246  241 FIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-223 4.36e-08

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: 58.53  E-value: 4.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    4 NKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSL 83
Cdd:TIGR02168  213 ERYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   84 QQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLhmvvdedsrsessstDEGKEKTKLLLER 163
Cdd:TIGR02168  280 EEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL---------------EELESKLDELAEE 338
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  164 LKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQ 223
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
7-246 3.79e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    7 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEgamHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQ 86
Cdd:COG1196    262 LAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   87 FSRMEETVRNLLQSQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKL------L 160
Cdd:COG1196    339 LEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeaL 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  161 LERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSD 240
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488

                   ....*.
gi 1034613615  241 LLLQKL 246
Cdd:COG1196    489 AAARLL 494
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
8-281 4.21e-05

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: 48.58  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    8 EHLLTQLEEQHRSLWReklavaRLQREVAQRTSEGAMHEKLIHELEEERhLRLQSEKRLQEVTLES---ERNRIQMRSLQ 84
Cdd:pfam17380  299 ERLRQEKEEKAREVER------RRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERELERIRQEErkrELERIRQEEIA 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   85 QQFSRMEETVRNLLQSQGSPEQKKEETVniMVYQEKLSEEERKHKEALEDLHMvvdedsRSESSSTDEGKEKTKLLLERL 164
Cdd:pfam17380  372 MEISRMRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEE 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  165 KALEAENsaLALENENQREQYERCLDEVANQVVQALLTQKDLRE--ECVKLKTRVFDLEQQNRTLSILFQQRVRptsdll 242
Cdd:pfam17380  444 RAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR------ 515
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034613615  243 lqKLHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHEHQ 281
Cdd:pfam17380  516 --KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
779-1050 3.15e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  779 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 856
Cdd:PTZ00449   536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  857 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 929
Cdd:PTZ00449   609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  930 KsETRVP---------------SETARTPFKSPllkGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 994
Cdd:PTZ00449   687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613615  995 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1050
Cdd:PTZ00449   763 TPADTPLPDILAEEFKEEDIHAETGEP-------------DEAMKRPD-SPSEHED 804
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
697-1171 5.99e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  697 PRAAARDYTFFKR----SEEDTEKNIPKDNVD----------NVPRVSTESFSSRTVTQNPQQQKLVKPTHNISCQSNSR 762
Cdd:pfam05109  290 PKASGGDYCIQSNivfsDEIPASQDMPTNTTDityvgdnatySVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLT 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  763 SSAPMGI------YQKQNLTKIPPRGKSSPQKSKLMEPEATTLLPSSGLVTLEKSPalapgklsrfmKTESSGPLFElRS 836
Cdd:pfam05109  370 SGTPSGCenisgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAP-----------ESTTTSPTLN-TT 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  837 DPHIPKHSAQLPHSSRMPSrrdwvqcpkSQTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAGVKSPSPPPPPGRSVSLLA 916
Cdd:pfam05109  438 GFAAPNTTTGLPSSTHVPT---------NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTS 508
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  917 RPSYDYSPAPSSTkseTRVPSETARTPFKSPLLKGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPM---PSPEAVIQT 993
Cdd:pfam05109  509 PTSAVTTPTPNAT---SPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTlgkTSPTSAVTT 585
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  994 RCP--------AHAPSSSFTVMALGPPKVSPKRGVPKTSPRQTLGTPQRDIGLQTPR------------ISPST------ 1047
Cdd:pfam05109  586 PTPnatsptvgETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSsmslrpssisetLSPSTsdnsts 665
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1048 HEPLEMTSSKS-------VSPGRKGQLNDSASTP-PKP------SFLGVNESPSSQVSSSSSSSSPAKSHNSPHGcqsah 1113
Cdd:pfam05109  666 HMPLLTSAHPTggenitqVTPASTSTHHVSTSSPaPRPgttsqaSGPGNSSTSTKPGEVNVTKGTPPKNATSPQA----- 740
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613615 1114 EKGLKTRLPVGLKVLMKSpqllrkSSTVPGKHekdSLNEASKSSVAVNKSKPEDSKNP 1171
Cdd:pfam05109  741 PSGQKTAVPTVTSTGGKA------NSTTGGKH---TTGHGARTSTEPTTDYGGDSTTP 789
PRK12704 PRK12704
phosphodiesterase; Provisional
18-135 7.86e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 7.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   18 HRSLWREKLAVARLQREV----AQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESER--NRIQMR--SLQQQFSR 89
Cdd:PRK12704    25 RKKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQKeeNLDRKLEL 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034613615   90 MEETVRNLLQSQGSPEQKKEEtvnimvYQEKLSEEERKHKEALEDL 135
Cdd:PRK12704   105 LEKREEELEKKEKELEQKQQE------LEKKEEELEELIEEQLQEL 144
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
6-71 7.90e-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: 7.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    6 YIEHLLTQLEEQHRSLWREKLA----VARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTL 71
Cdd:cd19543    175 YIAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
 
Name Accession Description Interval E-value
NCKAP5 pfam15246
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ...
1443-1751 2.10e-149

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: 463.09  E-value: 2.10e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1443 LSPTIEEKVMLCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1522
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1523 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1602
Cdd:pfam15246   81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1603 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1682
Cdd:pfam15246  161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613615 1683 IIESNCQMRTLDSGIGTFPLPDSGNRSTGRYLCQPDSPEDAEPLLPLQSALSAVSSMRAQTLEREVPSS 1751
Cdd:pfam15246  241 FIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-223 4.36e-08

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: 58.53  E-value: 4.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    4 NKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSL 83
Cdd:TIGR02168  213 ERYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   84 QQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLhmvvdedsrsessstDEGKEKTKLLLER 163
Cdd:TIGR02168  280 EEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL---------------EELESKLDELAEE 338
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  164 LKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQ 223
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
7-246 3.79e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    7 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEgamHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQ 86
Cdd:COG1196    262 LAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   87 FSRMEETVRNLLQSQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKL------L 160
Cdd:COG1196    339 LEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeaL 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  161 LERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSD 240
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488

                   ....*.
gi 1034613615  241 LLLQKL 246
Cdd:COG1196    489 AAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
46-289 9.57e-07

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: 54.29  E-value: 9.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   46 EKLIHELEEE-RHLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQGSPEQKKEE-TVNIMVYQEKLSE 123
Cdd:TIGR02168  192 EDILNELERQlKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEElTAELQELEEKLEE 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  124 EERKHKEALEDLHmvVDEDSRSESSSTDEGKEKTKLLL-ERLKALEAENSALA---LENENQREQYERCLDEVANQVVQA 199
Cdd:TIGR02168  272 LRLEVSELEEEIE--ELQKELYALANEISRLEQQKQILrERLANLERQLEELEaqlEELESKLDELAEELAELEEKLEEL 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  200 LLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQKLHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHE 279
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
                          250
                   ....*....|
gi 1034613615  280 HQLNTKSALK 289
Cdd:TIGR02168  430 LEEAELKELQ 439
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
7-279 3.56e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 3.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    7 IEHLLTQLEEQHRSLwreklavaRLQREVAQRtsegamHEKLIHELEE-ERHLRLqseKRLQEVTLESERNRIQMRSLQQ 85
Cdd:COG1196    191 LEDILGELERQLEPL--------ERQAEKAER------YRELKEELKElEAELLL---LKLRELEAELEELEAELEELEA 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   86 QFSRMEETVRNLlqsqgspEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEgKEKTKLLLERLK 165
Cdd:COG1196    254 ELEELEAELAEL-------EAELEEL------RLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLE 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  166 ALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQK 245
Cdd:COG1196    320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034613615  246 LHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHE 279
Cdd:COG1196    400 AQLEELEEAEEALLERLERLEEELEELEEALAEL 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
6-236 9.33e-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: 9.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    6 YIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSE----KRLQEVTLESERNRIQMR 81
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRR 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   82 SLQQQFSRMEETVRNLL-QSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKLL 160
Cdd:COG1196    313 ELEERLEELEEELAELEeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613615  161 LERLKALEAENSALALE--NENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVR 236
Cdd:COG1196    393 RAAAELAAQLEELEEAEeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
7-236 2.34e-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: 49.67  E-value: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    7 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNR--------- 77
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqieq 793
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   78 --IQMRSLQQQFSRMEETVRNLLQSQGSPEQKKEETVNIMVYQEKLSEE-ERKHKEALEDLHMVVDEDSRSESSSTDEgK 154
Cdd:TIGR02168  794 lkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEELEELIEEL-E 872
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  155 EKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLsilfQQR 234
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL----QER 944

                   ..
gi 1034613615  235 VR 236
Cdd:TIGR02168  945 LS 946
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
8-281 4.21e-05

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: 48.58  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    8 EHLLTQLEEQHRSLWReklavaRLQREVAQRTSEGAMHEKLIHELEEERhLRLQSEKRLQEVTLES---ERNRIQMRSLQ 84
Cdd:pfam17380  299 ERLRQEKEEKAREVER------RRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERELERIRQEErkrELERIRQEEIA 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   85 QQFSRMEETVRNLLQSQGSPEQKKEETVniMVYQEKLSEEERKHKEALEDLHMvvdedsRSESSSTDEGKEKTKLLLERL 164
Cdd:pfam17380  372 MEISRMRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEE 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  165 KALEAENsaLALENENQREQYERCLDEVANQVVQALLTQKDLRE--ECVKLKTRVFDLEQQNRTLSILFQQRVRptsdll 242
Cdd:pfam17380  444 RAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR------ 515
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034613615  243 lqKLHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHEHQ 281
Cdd:pfam17380  516 --KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
28-263 4.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 4.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   28 VARLQREVAQRTSEgamHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQgspEQK 107
Cdd:COG4372     47 LEQLREELEQAREE---LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL---EEL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  108 KEETVNIMVYQEKLSEEERKHKEALEDlhmvvdedsrsessstdegKEktklllERLKALEAENSALALENENQREQYER 187
Cdd:COG4372    121 QKERQDLEQQRKQLEAQIAELQSEIAE-------------------RE------EELKELEEQLESLQEELAALEQELQA 175
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613615  188 CLDEVANQVVQALLTQKDLREECVKLKTRVFDL-EQQNRTLSILFQQRVRPTSDLLLQKLHSRLLDLSSGDLLSEVE 263
Cdd:COG4372    176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLiESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2-214 5.01e-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: 45.43  E-value: 5.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    2 DSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEErHLRLQSEKRLQEVTLESERNRI--- 78
Cdd:TIGR02168  758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIaat 836
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   79 --QMRSLQQQFSRMEETV----RNLLQSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDE 152
Cdd:TIGR02168  837 erRLEDLEEQIEELSEDIeslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613615  153 GKEKTKLL------LERLKALEAENsalaleNENQREQYERCLDEVANQVVQALLTQKDLREECVKLK 214
Cdd:TIGR02168  917 LEELREKLaqlelrLEGLEVRIDNL------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
28-236 1.28e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   28 VARLQREVAQ------RTSEGAMHEklIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNL--LQ 99
Cdd:COG4717     48 LERLEKEADElfkpqgRKPELNLKE--LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  100 SQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSessstdegKEKTKLLLERLKALEAENSALALENE 179
Cdd:COG4717    126 QLLPLYQELEAL------EAELAELPERLEELEERLEELRELEEEL--------EELEAELAELQEELEELLEQLSLATE 191
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613615  180 NQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSIlfQQRVR 236
Cdd:COG4717    192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL--EERLK 246
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
5-233 1.90e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    5 KYIEHLLTQLEEQHRSLWREklaVARLQREVAQRtsegamhEKLIHELEEERHlrlQSEKRLQEVTLESERNRIQMRSLQ 84
Cdd:COG4942     37 AELEKELAALKKEEKALLKQ---LAALERRIAAL-------ARRIRALEQELA---ALEAELAELEKEIAELRAELEAQK 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   85 QQFSRM--------EETVRNLLQSQGSPEQkkeeTVNIMVYQEKLSEEERKHKEALedlhmvvdedsrsessstdegKEK 156
Cdd:COG4942    104 EELAELlralyrlgRQPPLALLLSPEDFLD----AVRRLQYLKYLAPARREQAEEL---------------------RAD 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613615  157 TKLLLERLKALEAENSALALENENQREQYERCLDEVANQvvQALLTQkdLREECVKLKTRVFDLEQQNRTLSILFQQ 233
Cdd:COG4942    159 LAELAALRAELEAERAELEALLAELEEERAALEALKAER--QKLLAR--LEKELAELAAELAELQQEAEELEALIAR 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-223 2.18e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   23 REKLAvaRLQREVAQRTSEGAMHEKLIHELEEERHlRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQG 102
Cdd:COG4913    609 RAKLA--ALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSD 685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  103 SPEQKKEEtvnimvyQEKLSEEERKHKEALEDLhmvvdedsrsESSSTDEGKEKTKLLLERLKALEAENSALALENENQR 182
Cdd:COG4913    686 DLAALEEQ-------LEELEAELEELEEELDEL----------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034613615  183 EQYERCLDEVANQVVQALLtQKDLREECVKLKTRVFDLEQQ 223
Cdd:COG4913    749 ALLEERFAAALGDAVEREL-RENLEERIDALRARLNRAEEE 788
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
7-227 2.43e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    7 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRI----QMRS 82
Cdd:COG4372     75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAereeELKE 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   83 LQQQFSRMEETVRNLLQS-QGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKLLL 161
Cdd:COG4372    155 LEEQLESLQEELAALEQElQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613615  162 ERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTL 227
Cdd:COG4372    235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
779-1050 3.15e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 3.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  779 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 856
Cdd:PTZ00449   536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  857 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 929
Cdd:PTZ00449   609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  930 KsETRVP---------------SETARTPFKSPllkGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 994
Cdd:PTZ00449   687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613615  995 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1050
Cdd:PTZ00449   763 TPADTPLPDILAEEFKEEDIHAETGEP-------------DEAMKRPD-SPSEHED 804
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
6-174 3.48e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 3.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    6 YIEHLLTQLEEQHRSLWREKLAVA-RLQRE-------------VAQRTSEgamHEKLIHELE------EERHLRLQSE-K 64
Cdd:pfam01576   23 KAESELKELEKKHQQLCEEKNALQeQLQAEtelcaeaeemrarLAARKQE---LEEILHELEsrleeeEERSQQLQNEkK 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   65 RLQ------EVTLESE---RNRIQMR--SLQQQFSRMEETVrNLLQSQGSPEQKK----EETVNIMVYQekLSEEERKHK 129
Cdd:pfam01576  100 KMQqhiqdlEEQLDEEeaaRQKLQLEkvTTEAKIKKLEEDI-LLLEDQNSKLSKErkllEERISEFTSN--LAEEEEKAK 176
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034613615  130 --EALEDLHMVVDEDSRSESSStdegKEKTKLLLERLK-ALEAENSAL 174
Cdd:pfam01576  177 slSKLKNKHEAMISDLEERLKK----EEKGRQELEKAKrKLEGESTDL 220
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
8-238 4.13e-03

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: 42.26  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    8 EHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELE---------EERHLRLQSEKRLQEVTLESERNRI 78
Cdd:TIGR00618  479 EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQR 558
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   79 -----QMRSLQQQFSRM-----------------EETVRNLLQSQGSPEQ-----------KKEETVN---IMVYQEKLS 122
Cdd:TIGR00618  559 aslkeQMQEIQQSFSILtqcdnrskedipnlqniTVRLQDLTEKLSEAEDmlaceqhallrKLQPEQDlqdVRLHLQQCS 638
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  123 EEERKHKEALEDLHMVVDEDSRSESSSTDegKEKTKLLLERLKALEAENSALALENENQREQYERClDEVANQVVQALLT 202
Cdd:TIGR00618  639 QELALKLTALHALQLTLTQERVREHALSI--RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEE 715
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034613615  203 QKDLREE-CVKLKTRVFDLEQQNRTLSILFQ--QRVRPT 238
Cdd:TIGR00618  716 YDREFNEiENASSSLGSDLAAREDALNQSLKelMHQART 754
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
2-244 5.73e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 41.63  E-value: 5.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    2 DSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTsegamheKLIHELEEERHLRLQsekrlqevtlESERNRIQMR 81
Cdd:pfam05483  286 ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT-------KTICQLTEEKEAQME----------ELNKAKAAHS 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   82 SLQQQFSRMEETVRNLLQSQGSPEQKKEETVNI--MVYQEKLSEEE-----RKHKEA-LEDLHMVVDEDSRSESSstdeg 153
Cdd:pfam05483  349 FVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIitMELQKKSSELEemtkfKNNKEVeLEELKKILAEDEKLLDE----- 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  154 KEKTKLLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQ 233
Cdd:pfam05483  424 KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKE 503
                          250
                   ....*....|.
gi 1034613615  234 RVRPTSDLLLQ 244
Cdd:pfam05483  504 LTQEASDMTLE 514
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
697-1171 5.99e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 41.83  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  697 PRAAARDYTFFKR----SEEDTEKNIPKDNVD----------NVPRVSTESFSSRTVTQNPQQQKLVKPTHNISCQSNSR 762
Cdd:pfam05109  290 PKASGGDYCIQSNivfsDEIPASQDMPTNTTDityvgdnatySVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLT 369
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  763 SSAPMGI------YQKQNLTKIPPRGKSSPQKSKLMEPEATTLLPSSGLVTLEKSPalapgklsrfmKTESSGPLFElRS 836
Cdd:pfam05109  370 SGTPSGCenisgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAP-----------ESTTTSPTLN-TT 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  837 DPHIPKHSAQLPHSSRMPSrrdwvqcpkSQTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAGVKSPSPPPPPGRSVSLLA 916
Cdd:pfam05109  438 GFAAPNTTTGLPSSTHVPT---------NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTS 508
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  917 RPSYDYSPAPSSTkseTRVPSETARTPFKSPLLKGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPM---PSPEAVIQT 993
Cdd:pfam05109  509 PTSAVTTPTPNAT---SPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTlgkTSPTSAVTT 585
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  994 RCP--------AHAPSSSFTVMALGPPKVSPKRGVPKTSPRQTLGTPQRDIGLQTPR------------ISPST------ 1047
Cdd:pfam05109  586 PTPnatsptvgETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSsmslrpssisetLSPSTsdnsts 665
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615 1048 HEPLEMTSSKS-------VSPGRKGQLNDSASTP-PKP------SFLGVNESPSSQVSSSSSSSSPAKSHNSPHGcqsah 1113
Cdd:pfam05109  666 HMPLLTSAHPTggenitqVTPASTSTHHVSTSSPaPRPgttsqaSGPGNSSTSTKPGEVNVTKGTPPKNATSPQA----- 740
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613615 1114 EKGLKTRLPVGLKVLMKSpqllrkSSTVPGKHekdSLNEASKSSVAVNKSKPEDSKNP 1171
Cdd:pfam05109  741 PSGQKTAVPTVTSTGGKA------NSTTGGKH---TTGHGARTSTEPTTDYGGDSTTP 789
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
10-203 6.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   10 LLTQLEEQHRSLWRE-----KLAVARLQrEVAQRTSEGAMHEKLIHELEEERHlrlQSEKRLQEV-----TLESERNRI- 78
Cdd:COG4717     47 LLERLEKEADELFKPqgrkpELNLKELK-ELEEELKEAEEKEEEYAELQEELE---ELEEELEELeaeleELREELEKLe 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   79 QMRSLQQQFSRMEETVRNLLQSQGSPE---QKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKE 155
Cdd:COG4717    123 KLLQLLPLYQELEALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034613615  156 KtklLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQ 203
Cdd:COG4717    203 E---LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
46-293 6.86e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   46 EKLIHELEEERHLRLQSEKRLQEV-TLESERNRIQmRSLQQQFSRMEETVRNLlqsqgspEQKKEETvnimvyqEKLSEE 124
Cdd:COG4372     31 EQLRKALFELDKLQEELEQLREELeQAREELEQLE-EELEQARSELEQLEEEL-------EELNEQL-------QAAQAE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  125 ERKHKEALEDLhmvvdedsrsessstdegKEKTKLLLERLKALEAENSALALENENQREQYERCLDEVANQVVQAlltqK 204
Cdd:COG4372     96 LAQAQEELESL------------------QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL----K 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  205 DLREECVKLKTRVFDLEQQNRTLSILFQQRVrptsdllLQKLHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHEHQLNT 284
Cdd:COG4372    154 ELEEQLESLQEELAALEQELQALSEAEAEQA-------LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDS 226

                   ....*....
gi 1034613615  285 KSALKCPGL 293
Cdd:COG4372    227 LEAKLGLAL 235
PRK12704 PRK12704
phosphodiesterase; Provisional
18-135 7.86e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 7.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   18 HRSLWREKLAVARLQREV----AQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESER--NRIQMR--SLQQQFSR 89
Cdd:PRK12704    25 RKKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQKeeNLDRKLEL 104
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034613615   90 MEETVRNLLQSQGSPEQKKEEtvnimvYQEKLSEEERKHKEALEDL 135
Cdd:PRK12704   105 LEKREEELEKKEKELEQKQQE------LEKKEEELEELIEEQLQEL 144
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
6-71 7.90e-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: 7.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615    6 YIEHLLTQLEEQHRSLWREKLA----VARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTL 71
Cdd:cd19543    175 YIAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
10-229 7.91e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   10 LLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQ--- 86
Cdd:pfam02463  715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEkee 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615   87 -FSRMEETVRNLLQSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEdlhmvvdedsrsessstDEGKEKTKLLLERLK 165
Cdd:pfam02463  795 kLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL-----------------KEEQKLEKLAEEELE 857
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034613615  166 ALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSI 229
Cdd:pfam02463  858 RLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
655-1080 9.20e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 40.71  E-value: 9.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  655 EFSSHQTGVVTVTRNEISINSTPAGPKAEHTELLPQGIACLQPRAAArDYTFFKRSEEDTEknIPKDNVDNVPRVSTESF 734
Cdd:pfam17823   89 EHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIA-ALPSEAFSAPRAA--ACRANASAAPRAAIAAA 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  735 SSrTVTQNPQQQKLVKPTHNIScQSNSRSSAPMGIYQKQNLTKIPPRGKSSPQKSKlMEPEATTLLPSSGLVTLekspal 814
Cdd:pfam17823  166 SA-PHAASPAPRTAASSTTAAS-STTAASSAPTTAASSAPATLTPARGISTAATAT-GHPAAGTALAAVGNSSP------ 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  815 APGKLSRFMKTESSGPLFELRSDPHIPKHSAQLPHSSRmpsrrdwvqcPKSQTPG-SRSRPAIESSDSGEPPTRDEHCGS 893
Cdd:pfam17823  237 AAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGD----------PHARRLSpAKHMPSDTMARNPAAPMGAQAQGP 306
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  894 GPEAGVKSPSpppppgrsVSLLARPSydysPAPSSTKSETRVPSETARTpfkspllkgiSAPVISsnpaTTEVQRKKPSV 973
Cdd:pfam17823  307 IIQVSTDQPV--------HNTAGEPT----PSPSNTTLEPNTPKSVAST----------NLAVVT----TTKAQAKEPSA 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613615  974 AFKKPIFTHPMPSPEAVIQTRCPAHAPsssFTVMALGPpkvspkrGVPKTsPRQ--TLGTPQRDIGLQTPRISPSTHEPl 1051
Cdd:pfam17823  361 SPVPVLHTSMIPEVEATSPTTQPSPLL---PTQGAAGP-------GILLA-PEQvaTEATAGTASAGPTPRSSGDPKTL- 428
                          410       420
                   ....*....|....*....|....*....
gi 1034613615 1052 emtSSKSVSPGRKGQLNDSASTPPKPSFL 1080
Cdd:pfam17823  429 ---AMASCQLSTQGQYLVVTTDPLTPALV 454
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH