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Conserved domains on  [gi|1034613609|ref|XP_016859464|]
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nck-associated protein 5 isoform X1 [Homo sapiens]

Protein Classification

LCP family protein; protein kinase family protein( domain architecture ID 13315136)

LytR-CpsA-Psr (LCP) family protein is implicated in the attachment of anionic polymers to cell wall peptidoglycan in bacteria| fungal protein kinase family protein containing a variant of the protein kinase domain

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 ...
 1468-1776 2.26e-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: 463.47  E-value: 2.26e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1468 LSPTIEEKVMLCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1547
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1548 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1627
Cdd:pfam15246   81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1628 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1707
Cdd:pfam15246  161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613609 1708 IIESNCQMRTLDSGIGTFPLPDSGNRSTGRYLCQPDSPEDAEPLLPLQSALSAVSSMRAQTLEREVPSS 1776
Cdd:pfam15246  241 FIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-248 1.82e-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: 59.69  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609    2 EGKRQLEKrdfgkrLSLDSSLVEymdsnKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEER 81
Cdd:TIGR02168  197 ELERQLKS------LERQAEKAE-----RYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   82 HLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLh 161
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL- 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  162 mvvdedsrsessstDEGKEKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTR 241
Cdd:TIGR02168  326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSK 387


                   ....*..
gi 1034613609  242 VFDLEQQ 248
Cdd:TIGR02168  388 VAQLELQ 394
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 804-1075 3.25e-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: 42.37  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  804 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 881
Cdd:PTZ00449   536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  882 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 954
Cdd:PTZ00449   609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  955 KsETRVP---------------SETARTPFKSPllkGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 1019
Cdd:PTZ00449   687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613609 1020 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1075
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 ...
 1468-1776 2.26e-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: 463.47  E-value: 2.26e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1468 LSPTIEEKVMLCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1547
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1548 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1627
Cdd:pfam15246   81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1628 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1707
Cdd:pfam15246  161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613609 1708 IIESNCQMRTLDSGIGTFPLPDSGNRSTGRYLCQPDSPEDAEPLLPLQSALSAVSSMRAQTLEREVPSS 1776
Cdd:pfam15246  241 FIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-248 1.82e-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: 59.69  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609    2 EGKRQLEKrdfgkrLSLDSSLVEymdsnKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEER 81
Cdd:TIGR02168  197 ELERQLKS------LERQAEKAE-----RYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   82 HLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLh 161
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL- 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  162 mvvdedsrsessstDEGKEKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTR 241
Cdd:TIGR02168  326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSK 387


                   ....*..
gi 1034613609  242 VFDLEQQ 248
Cdd:TIGR02168  388 VAQLELQ 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 32-271 4.18e-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: 4.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEgamHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQ 111
Cdd:COG1196    262 LAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  112 FSRMEETVRNLLQSQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKL------L 185
Cdd:COG1196    339 LEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeaL 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  186 LERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSD 265
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488


                   ....*.
gi 1034613609  266 LLLQKL 271
Cdd:COG1196    489 AAARLL 494
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-306 4.39e-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: 4.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   33 EHLLTQLEEQHRSLWReklavaRLQREVAQRTSEGAMHEKLIHELEEERhLRLQSEKRLQEVTLES---ERNRIQMRSLQ 109
Cdd:pfam17380  299 ERLRQEKEEKAREVER------RRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERELERIRQEErkrELERIRQEEIA 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  110 QQFSRMEETVRNLLQSQGSPEQKKEETVniMVYQEKLSEEERKHKEALEDLHMvvdedsRSESSSTDEGKEKTKLLLERL 189
Cdd:pfam17380  372 MEISRMRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEE 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  190 KALEAENsaLALENENQREQYERCLDEVANQVVQALLTQKDLRE--ECVKLKTRVFDLEQQNRTLSILFQQRVRptsdll 267
Cdd:pfam17380  444 RAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR------ 515

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034613609  268 lqKLHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHEHQ 306
Cdd:pfam17380  516 --KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 804-1075 3.25e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  804 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 881
Cdd:PTZ00449   536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  882 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 954
Cdd:PTZ00449   609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  955 KsETRVP---------------SETARTPFKSPllkGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 1019
Cdd:PTZ00449   687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613609 1020 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1075
Cdd:PTZ00449   763 TPADTPLPDILAEEFKEEDIHAETGEP-------------DEAMKRPD-SPSEHED 804
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 722-1196 4.80e-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: 4.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  722 PRAAARDYTFFKR----SEEDTEKNIPKDNVD----------NVPRVSTESFSSRTVTQNPQQQKLVKPTHNISCQSNSR 787
Cdd:pfam05109  290 PKASGGDYCIQSNivfsDEIPASQDMPTNTTDityvgdnatySVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLT 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  788 SSAPMGI------YQKQNLTKIPPRGKSSPQKSKLMEPEATTLLPSSGLVTLEKSPalapgklsrfmKTESSGPLFElRS 861
Cdd:pfam05109  370 SGTPSGCenisgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAP-----------ESTTTSPTLN-TT 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  862 DPHIPKHSAQLPHSSRMPSrrdwvqcpkSQTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAGVKSPSPPPPPGRSVSLLA 941
Cdd:pfam05109  438 GFAAPNTTTGLPSSTHVPT---------NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTS 508

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  942 RPSYDYSPAPSSTkseTRVPSETARTPFKSPLLKGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPM---PSPEAVIQT 1018
Cdd:pfam05109  509 PTSAVTTPTPNAT---SPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTlgkTSPTSAVTT 585

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1019 RCP--------AHAPSSSFTVMALGPPKVSPKRGVPKTSPRQTLGTPQRDIGLQTPR------------ISPST------ 1072
Cdd:pfam05109  586 PTPnatsptvgETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSsmslrpssisetLSPSTsdnsts 665

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1073 HEPLEMTSSKS-------VSPGRKGQLNDSASTP-PKP------SFLGVNESPSSQVSSSSSSSSPAKSHNSPHGcqsah 1138
Cdd:pfam05109  666 HMPLLTSAHPTggenitqVTPASTSTHHVSTSSPaPRPgttsqaSGPGNSSTSTKPGEVNVTKGTPPKNATSPQA----- 740

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613609 1139 EKGLKTRLPVGLKVLMKSpqllrkSSTVPGKHekdSLNEASKSSVAVNKSKPEDSKNP 1196
Cdd:pfam05109  741 PSGQKTAVPTVTSTGGKA------NSTTGGKH---TTGHGARTSTEPTTDYGGDSTTP 789
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 31-96 8.01e-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: 8.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   31 YIEHLLTQLEEQHRSLWREKLA----VARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTL 96
Cdd:cd19543    175 YIAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
PRK12704 PRK12704
phosphodiesterase; Provisional
 43-160 8.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   43 HRSLWREKLAVARLQREV----AQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESER--NRIQMR--SLQQQFSR 114
Cdd:PRK12704    25 RKKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQKeeNLDRKLEL 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034613609  115 MEETVRNLLQSQGSPEQKKEEtvnimvYQEKLSEEERKHKEALEDL 160
Cdd:PRK12704   105 LEKREEELEKKEKELEQKQQE------LEKKEEELEELIEEQLQEL 144
 
Name Accession Description Interval E-value
NCKAP5 pfam15246
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ...
 1468-1776 2.26e-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: 463.47  E-value: 2.26e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1468 LSPTIEEKVMLCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1547
Cdd:pfam15246    1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1548 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1627
Cdd:pfam15246   81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1628 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1707
Cdd:pfam15246  161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034613609 1708 IIESNCQMRTLDSGIGTFPLPDSGNRSTGRYLCQPDSPEDAEPLLPLQSALSAVSSMRAQTLEREVPSS 1776
Cdd:pfam15246  241 FIGSGCQMRTLDSGIGTFPLPDSGNRSTGRHIPKPESSEETEPLLSLQPALPTAVPRRARTLEREVPSS 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-248 1.82e-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: 59.69  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609    2 EGKRQLEKrdfgkrLSLDSSLVEymdsnKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEER 81
Cdd:TIGR02168  197 ELERQLKS------LERQAEKAE-----RYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   82 HLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLh 161
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL- 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  162 mvvdedsrsessstDEGKEKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTR 241
Cdd:TIGR02168  326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSK 387


                   ....*..
gi 1034613609  242 VFDLEQQ 248
Cdd:TIGR02168  388 VAQLELQ 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 32-271 4.18e-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: 4.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEgamHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQ 111
Cdd:COG1196    262 LAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  112 FSRMEETVRNLLQSQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKL------L 185
Cdd:COG1196    339 LEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeaL 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  186 LERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSD 265
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488


                   ....*.
gi 1034613609  266 LLLQKL 271
Cdd:COG1196    489 AAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 32-304 3.93e-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: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   32 IEHLLTQLEEQHRSLwreklavaRLQREVAQRtsegamHEKLIHELEE-ERHLRLqseKRLQEVTLESERNRIQMRSLQQ 110
Cdd:COG1196    191 LEDILGELERQLEPL--------ERQAEKAER------YRELKEELKElEAELLL---LKLRELEAELEELEAELEELEA 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  111 QFSRMEETVRNLlqsqgspEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEgKEKTKLLLERLK 190
Cdd:COG1196    254 ELEELEAELAEL-------EAELEEL------RLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLE 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  191 ALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQK 270
Cdd:COG1196    320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034613609  271 LHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHE 304
Cdd:COG1196    400 AQLEELEEAEEALLERLERLEEELEELEEALAEL 433
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-261 9.87e-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: 9.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   31 YIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSE----KRLQEVTLESERNRIQMR 106
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRR 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  107 SLQQQFSRMEETVRNLL-QSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKLL 185
Cdd:COG1196    313 ELEERLEELEEELAELEeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613609  186 LERLKALEAENSALALE--NENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVR 261
Cdd:COG1196    393 RAAAELAAQLEELEEAEeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-261 2.61e-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: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNR--------- 102
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqieq 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  103 --IQMRSLQQQFSRMEETVRNLLQSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKE 180
Cdd:TIGR02168  794 lkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  181 KTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLsilfQQRV 260
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL----QERL 945


                   .
gi 1034613609  261 R 261
Cdd:TIGR02168  946 S 946
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 33-306 4.39e-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: 4.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   33 EHLLTQLEEQHRSLWReklavaRLQREVAQRTSEGAMHEKLIHELEEERhLRLQSEKRLQEVTLES---ERNRIQMRSLQ 109
Cdd:pfam17380  299 ERLRQEKEEKAREVER------RRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERELERIRQEErkrELERIRQEEIA 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  110 QQFSRMEETVRNLLQSQGSPEQKKEETVniMVYQEKLSEEERKHKEALEDLHMvvdedsRSESSSTDEGKEKTKLLLERL 189
Cdd:pfam17380  372 MEISRMRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEE 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  190 KALEAENsaLALENENQREQYERCLDEVANQVVQALLTQKDLRE--ECVKLKTRVFDLEQQNRTLSILFQQRVRptsdll 267
Cdd:pfam17380  444 RAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR------ 515

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034613609  268 lqKLHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHEHQ 306
Cdd:pfam17380  516 --KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 18-239 4.92e-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: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   18 LDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEErHLRLQSEKRLQEVTLE 97
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLRERLE 827

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   98 SERNRI-----QMRSLQQQFSRMEETV----RNLLQSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDS 168
Cdd:TIGR02168  828 SLERRIaaterRLEDLEEQIEELSEDIeslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613609  169 RSESSSTDEGKEKTKLL------LERLKALEAENsalaleNENQREQYERCLDEVANQVVQALLTQKDLREECVKLK 239
Cdd:TIGR02168  908 SKRSELRRELEELREKLaqlelrLEGLEVRIDNL------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-271 8.57e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609    7 LEKRDFGKRLSldsSLVEYMDSNKYIEHLLTQLEEQHRSLwrekLAVARLQREVAQRTSEGAMHEKLIHELE-EERHLRL 85
Cdd:COG4913    218 LEEPDTFEAAD---ALVEHFDDLERAHEALEDAREQIELL----EPIRELAERYAAARERLAELEYLRAALRlWFAQRRL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   86 QS-EKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQS-QGSPEQKKEEtvnimvYQEKLSEEERKHKEALEDLhmv 163
Cdd:COG4913    291 ELlEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQ------LEREIERLERELEERERRR--- 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  164 vdedsrsessstdegkEKTKLLLERLKaLEAENSALALEN-----ENQREQYERCLDEVANQVVQALLTQKDLREECVKL 238
Cdd:COG4913    362 ----------------ARLEALLAALG-LPLPASAEEFAAlraeaAALLEALEEELEALEEALAEAEAALRDLRRELREL 424

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1034613609  239 KTRVFDLEQQNRTLSiLFQQRVRptsDLLLQKL 271
Cdd:COG4913    425 EAEIASLERRKSNIP-ARLLALR---DALAEAL 453
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-261 1.50e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   53 VARLQREVAQ------RTSEGAMHEklIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNL--LQ 124
Cdd:COG4717     48 LERLEKEADElfkpqgRKPELNLKE--LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLL 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  125 SQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSessstdegKEKTKLLLERLKALEAENSALALENE 204
Cdd:COG4717    126 QLLPLYQELEAL------EAELAELPERLEELEERLEELRELEEEL--------EELEAELAELQEELEELLEQLSLATE 191

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613609  205 NQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSIlfQQRVR 261
Cdd:COG4717    192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL--EERLK 246
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 19-199 1.55e-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: 43.63  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   19 DSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVA-RLQRE-------------VAQRTSEgamHEKLIHELE------ 78
Cdd:pfam01576   11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQeQLQAEtelcaeaeemrarLAARKQE---LEEILHELEsrleee 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   79 EERHLRLQSE-KRLQ------EVTLESE---RNRIQMR--SLQQQFSRMEETVrNLLQSQGSPEQKK----EETVNIMVY 142
Cdd:pfam01576   88 EERSQQLQNEkKKMQqhiqdlEEQLDEEeaaRQKLQLEkvTTEAKIKKLEEDI-LLLEDQNSKLSKErkllEERISEFTS 166

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  143 QekLSEEERKHK--EALEDLHMVVDEDSRSESSStdegKEKTKLLLERLK-ALEAENSAL 199
Cdd:pfam01576  167 N--LAEEEEKAKslSKLKNKHEAMISDLEERLKK----EEKGRQELEKAKrKLEGESTDL 220
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 11-254 1.62e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 43.67  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   11 DFGKRLSLDSSL----VEYMDSNKYIEhllTQLEEQHRSLWREKLAVARLQREVAQRTSE-----GAMHEKLI---HELE 78
Cdd:pfam12128  249 EFNTLESAELRLshlhFGYKSDETLIA---SRQEERQETSAELNQLLRTLDDQWKEKRDElngelSAADAAVAkdrSELE 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   79 --EERHLRLQSEkRLQEVTLESErnriQMRSLQQQFSRMEETVRNLLQSQGSPEQK-------------------KEETV 137
Cdd:pfam12128  326 alEDQHGAFLDA-DIETAAADQE----QLPSWQSELENLEERLKALTGKHQDVTAKynrrrskikeqnnrdiagiKDKLA 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  138 NIMVYQEKLSEEERKHKEALEDlhmVVDEDSRSESSSTDEGKEKTKLLLERLKALEAENSALALENENQREQYERClDEV 217
Cdd:pfam12128  401 KIREARDRQLAVAEDDLQALES---ELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERI-ERA 476

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1034613609  218 ANQVVQALLTQKDLREECVKLKTRvfdLEQQNRTLSI 254
Cdd:pfam12128  477 REEQEAANAEVERLQSELRQARKR---RDQASEALRQ 510
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 30-258 2.14e-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: 42.44  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   30 KYIEHLLTQLEEQHRSLWREklaVARLQREVAQRtsegamhEKLIHELEEERHlrlQSEKRLQEVTLESERNRIQMRSLQ 109
Cdd:COG4942     37 AELEKELAALKKEEKALLKQ---LAALERRIAAL-------ARRIRALEQELA---ALEAELAELEKEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  110 QQFSRM--------EETVRNLLQSQGSPEQkkeeTVNIMVYQEKLSEEERKHKEALedlhmvvdedsrsessstdegKEK 181
Cdd:COG4942    104 EELAELlralyrlgRQPPLALLLSPEDFLD----AVRRLQYLKYLAPARREQAEEL---------------------RAD 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034613609  182 TKLLLERLKALEAENSALALENENQREQYERCLDEVANQvvQALLTQkdLREECVKLKTRVFDLEQQNRTLSILFQQ 258
Cdd:COG4942    159 LAELAALRAELEAERAELEALLAELEEERAALEALKAER--QKLLAR--LEKELAELAAELAELQQEAEELEALIAR 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-248 2.19e-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: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   48 REKLAvaRLQREVAQRTSEGAMHEKLIHELEEERHlRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQG 127
Cdd:COG4913    609 RAKLA--ALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  128 SPEQKKEEtvnimvyQEKLSEEERKHKEALEDLhmvvdedsrsESSSTDEGKEKTKLLLERLKALEAENSALALENENQR 207
Cdd:COG4913    686 DLAALEEQ-------LEELEAELEELEEELDEL----------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034613609  208 EQYERCLDEVANQVVQALLtQKDLREECVKLKTRVFDLEQQ 248
Cdd:COG4913    749 ALLEERFAAALGDAVEREL-RENLEERIDALRARLNRAEEE 788
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
32-252 2.73e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRI----QMRS 107
Cdd:COG4372     75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAereeELKE 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  108 LQQQFSRMEETVRNLLQS-QGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKLLL 186
Cdd:COG4372    155 LEEQLESLQEELAALEQElQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613609  187 ERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTL 252
Cdd:COG4372    235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 7-254 3.20e-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: 42.65  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609    7 LEKRDFGKRLSLDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQ 86
Cdd:pfam02463  692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   87 SEKRLQEVTLESERNRIQmRSLQQQFSRMEETVRNLLQSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEdlhmvvde 166
Cdd:pfam02463  772 KEKELAEEREKTEKLKVE-EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL-------- 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  167 dsrsessstDEGKEKTKLLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLE 246
Cdd:pfam02463  843 ---------KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913


                   ....*...
gi 1034613609  247 QQNRTLSI 254
Cdd:pfam02463  914 EKENEIEE 921
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 804-1075 3.25e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  804 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 881
Cdd:PTZ00449   536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  882 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 954
Cdd:PTZ00449   609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  955 KsETRVP---------------SETARTPFKSPllkGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 1019
Cdd:PTZ00449   687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034613609 1020 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1075
Cdd:PTZ00449   763 TPADTPLPDILAEEFKEEDIHAETGEP-------------DEAMKRPD-SPSEHED 804
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 8-269 4.11e-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: 42.02  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609    8 EKRDFGKRLSLDSSLVE--YMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTsegamheKLIHELEEERHLRL 85
Cdd:pfam05483  265 ESRDKANQLEEKTKLQDenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT-------KTICQLTEEKEAQM 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   86 QsekrlqevtlESERNRIQMRSLQQQFSRMEETVRNLLQSQGSPEQKKEETVNI--MVYQEKLSEEE-----RKHKEA-L 157
Cdd:pfam05483  338 E----------ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIitMELQKKSSELEemtkfKNNKEVeL 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  158 EDLHMVVDEDSRSESSstdegKEKTKLLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVK 237
Cdd:pfam05483  408 EELKKILAEDEKLLDE-----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034613609  238 LKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQ 269
Cdd:pfam05483  483 EKLKNIELTAHCDKLLLENKELTQEASDMTLE 514
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 722-1196 4.80e-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: 4.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  722 PRAAARDYTFFKR----SEEDTEKNIPKDNVD----------NVPRVSTESFSSRTVTQNPQQQKLVKPTHNISCQSNSR 787
Cdd:pfam05109  290 PKASGGDYCIQSNivfsDEIPASQDMPTNTTDityvgdnatySVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLT 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  788 SSAPMGI------YQKQNLTKIPPRGKSSPQKSKLMEPEATTLLPSSGLVTLEKSPalapgklsrfmKTESSGPLFElRS 861
Cdd:pfam05109  370 SGTPSGCenisgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAP-----------ESTTTSPTLN-TT 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  862 DPHIPKHSAQLPHSSRMPSrrdwvqcpkSQTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAGVKSPSPPPPPGRSVSLLA 941
Cdd:pfam05109  438 GFAAPNTTTGLPSSTHVPT---------NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTS 508

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  942 RPSYDYSPAPSSTkseTRVPSETARTPFKSPLLKGISAPVISSNPATTEVQRKKPSVAFKKPIFTHPM---PSPEAVIQT 1018
Cdd:pfam05109  509 PTSAVTTPTPNAT---SPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTlgkTSPTSAVTT 585

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1019 RCP--------AHAPSSSFTVMALGPPKVSPKRGVPKTSPRQTLGTPQRDIGLQTPR------------ISPST------ 1072
Cdd:pfam05109  586 PTPnatsptvgETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSsmslrpssisetLSPSTsdnsts 665

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609 1073 HEPLEMTSSKS-------VSPGRKGQLNDSASTP-PKP------SFLGVNESPSSQVSSSSSSSSPAKSHNSPHGcqsah 1138
Cdd:pfam05109  666 HMPLLTSAHPTggenitqVTPASTSTHHVSTSSPaPRPgttsqaSGPGNSSTSTKPGEVNVTKGTPPKNATSPQA----- 740

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034613609 1139 EKGLKTRLPVGLKVLMKSpqllrkSSTVPGKHekdSLNEASKSSVAVNKSKPEDSKNP 1196
Cdd:pfam05109  741 PSGQKTAVPTVTSTGGKA------NSTTGGKH---TTGHGARTSTEPTTDYGGDSTTP 789
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 680-1105 4.96e-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: 41.87  E-value: 4.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  680 EFSSHQTGVVTVTRNEISINSTPAGPKAEHTELLPQGIACLQPRAAArDYTFFKRSEEDTEknIPKDNVDNVPRVSTESF 759
Cdd:pfam17823   89 EHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIA-ALPSEAFSAPRAA--ACRANASAAPRAAIAAA 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  760 SSrTVTQNPQQQKLVKPTHNIScQSNSRSSAPMGIYQKQNLTKIPPRGKSSPQKSKlMEPEATTLLPSSGLVTLekspal 839
Cdd:pfam17823  166 SA-PHAASPAPRTAASSTTAAS-STTAASSAPTTAASSAPATLTPARGISTAATAT-GHPAAGTALAAVGNSSP------ 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  840 APGKLSRFMKTESSGPLFELRSDPHIPKHSAQLPHSSRmpsrrdwvqcPKSQTPG-SRSRPAIESSDSGEPPTRDEHCGS 918
Cdd:pfam17823  237 AAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGD----------PHARRLSpAKHMPSDTMARNPAAPMGAQAQGP 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  919 GPEAGVKSPSpppppgrsVSLLARPSydysPAPSSTKSETRVPSETARTpfkspllkgiSAPVISsnpaTTEVQRKKPSV 998
Cdd:pfam17823  307 IIQVSTDQPV--------HNTAGEPT----PSPSNTTLEPNTPKSVAST----------NLAVVT----TTKAQAKEPSA 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  999 AFKKPIFTHPMPSPEAVIQTRCPAHAPsssFTVMALGPpkvspkrGVPKTsPRQ--TLGTPQRDIGLQTPRISPSTHEPl 1076
Cdd:pfam17823  361 SPVPVLHTSMIPEVEATSPTTQPSPLL---PTQGAAGP-------GILLA-PEQvaTEATAGTASAGPTPRSSGDPKTL- 428

                          410       420
                   ....*....|....*....|....*....
gi 1034613609 1077 emtSSKSVSPGRKGQLNDSASTPPKPSFL 1105
Cdd:pfam17823  429 ---AMASCQLSTQGQYLVVTTDPLTPALV 454
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 33-263 5.05e-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: 41.88  E-value: 5.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   33 EHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELE---------EERHLRLQSEKRLQEVTLESERNRI 103
Cdd:TIGR00618  479 EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQR 558

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  104 -----QMRSLQQQFSRM-----------------EETVRNLLQSQGSPEQ-----------KKEETVN---IMVYQEKLS 147
Cdd:TIGR00618  559 aslkeQMQEIQQSFSILtqcdnrskedipnlqniTVRLQDLTEKLSEAEDmlaceqhallrKLQPEQDlqdVRLHLQQCS 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  148 EEERKHKEALEDLHMVVDEDSRSESSSTDegKEKTKLLLERLKALEAENSALALENENQREQYERClDEVANQVVQALLT 227
Cdd:TIGR00618  639 QELALKLTALHALQLTLTQERVREHALSI--RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEE 715

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034613609  228 QKDLREE-CVKLKTRVFDLEQQNRTLSILFQ--QRVRPT 263
Cdd:TIGR00618  716 YDREFNEiENASSSLGSDLAAREDALNQSLKelMHQART 754
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
5-234 6.94e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609    5 RQLEKRDFGKRLSLDSSLveymdSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLR 84
Cdd:COG4717    317 EEEELEELLAALGLPPDL-----SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   85 LQSEKRlqevtlesERNRIQMRSLQQQFSRMEETVRNLLQsQGSPEQKKEETVNImvyQEKLSEEERKHKEaledlhmvv 164
Cdd:COG4717    392 EQAEEY--------QELKEELEELEEQLEELLGELEELLE-ALDEEELEEELEEL---EEELEELEEELEE--------- 450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  165 dedsrsessstdegkektklLLERLKALEAENSALALENE--NQREQYERCLDEV--------ANQVVQALL--TQKDLR 232
Cdd:COG4717    451 --------------------LREELAELEAELEQLEEDGElaELLQELEELKAELrelaeewaALKLALELLeeAREEYR 510


                   ..
gi 1034613609  233 EE 234
Cdd:COG4717    511 EE 512
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
35-228 7.62e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 7.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   35 LLTQLEEQHRSLWRE-----KLAVARLQrEVAQRTSEGAMHEKLIHELEEERHlrlQSEKRLQEV-----TLESERNRI- 103
Cdd:COG4717     47 LLERLEKEADELFKPqgrkpELNLKELK-ELEEELKEAEEKEEEYAELQEELE---ELEEELEELeaeleELREELEKLe 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609  104 QMRSLQQQFSRMEETVRNLLQSQGSPE---QKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKE 180
Cdd:COG4717    123 KLLQLLPLYQELEALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034613609  181 KtklLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQ 228
Cdd:COG4717    203 E---LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 31-96 8.01e-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: 8.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   31 YIEHLLTQLEEQHRSLWREKLA----VARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTL 96
Cdd:cd19543    175 YIAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
PRK12704 PRK12704
phosphodiesterase; Provisional
 43-160 8.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034613609   43 HRSLWREKLAVARLQREV----AQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESER--NRIQMR--SLQQQFSR 114
Cdd:PRK12704    25 RKKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQKeeNLDRKLEL 104

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1034613609  115 MEETVRNLLQSQGSPEQKKEEtvnimvYQEKLSEEERKHKEALEDL 160
Cdd:PRK12704   105 LEKREEELEKKEKELEQKQQE------LEKKEEELEELIEEQLQEL 144
 
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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