|
Name |
Accession |
Description |
Interval |
E-value |
| NCKAP5 |
pfam15246 |
Nck-associated protein 5, Peripheral clock protein; NCKAP5 is short for Nck-associated protein ... |
1468-1776 |
3.33e-148 |
|
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: 460.01 E-value: 3.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1468 LSPTIEEKVILCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1547
Cdd:pfam15246 1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1548 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1627
Cdd:pfam15246 81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1628 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1707
Cdd:pfam15246 161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462572620 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 |
1.75e-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: 60.07 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 2 EGKRQLEKrdfgkrLSLDSSLVEymdsnKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEER 81
Cdd:TIGR02168 197 ELERQLKS------LERQAEKAE-----RYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 82 HLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLh 161
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 162 mvvdedsrsessstDEGKEKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTR 241
Cdd:TIGR02168 326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSK 387
|
....*..
gi 2462572620 242 VFDLEQQ 248
Cdd:TIGR02168 388 VAQLELQ 394
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-271 |
4.22e-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: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEgamHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQ 111
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 112 FSRMEETVRNLLQSQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKL------L 185
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeaL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 186 LERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSD 265
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
....*.
gi 2462572620 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 |
4.42e-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: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 33 EHLLTQLEEQHRSLWReklavaRLQREVAQRTSEGAMHEKLIHELEEERhLRLQSEKRLQEVTLES---ERNRIQMRSLQ 109
Cdd:pfam17380 299 ERLRQEKEEKAREVER------RRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERELERIRQEErkrELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 110 QQFSRMEETVRNLLQSQGSPEQKKEETVniMVYQEKLSEEERKHKEALEDLHMvvdedsRSESSSTDEGKEKTKLLLERL 189
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 190 KALEAENsaLALENENQREQYERCLDEVANQVVQALLTQKDLRE--ECVKLKTRVFDLEQQNRTLSILFQQRVRptsdll 267
Cdd:pfam17380 444 RAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR------ 515
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462572620 268 lqKLHSRLLDLSSGDLLSEVERNRSLTQSRTDAEVHEHQ 306
Cdd:pfam17380 516 --KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
680-1105 |
1.79e-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: 43.02 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 680 EFSSHQTGVVTVTRNEISINSTPAGPKAEHTELLPQGIACLQPRAAArDYTFFKRSEEDTEknIPKDNVDNVPRVSTESF 759
Cdd:pfam17823 89 EHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIA-ALPSEAFSAPRAA--ACRANASAAPRAAIAAA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 760 SSrTVTQNPQQQKLVKPTHNIScQSNSRSSAPMGIYQKQNLTKIPPRGKSSPQKSKlMEPEATTLLPSSGLVTLekspal 839
Cdd:pfam17823 166 SA-PHAASPAPRTAASSTTAAS-STTAASSAPTTAASSAPATLTPARGISTAATAT-GHPAAGTALAAVGNSSP------ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 840 APGKLSRFMKTESSGPLFELRSDPHIPKHSAQLPHSSRmpsrrdwvqcPKSQTPG-SRSRPAIESSDSGEPPTRDEHCGS 918
Cdd:pfam17823 237 AAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGD----------PHARRLSpAKHMPSDTMARNPAAPMGAQAQGP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 919 GPEAGVKspspppppgrsvsllarpsydySPAPSSTKSETRVPSETARTPFKSPLLKGTSAPVISsnpaTTEVQRKKPSV 998
Cdd:pfam17823 307 IIQVSTD----------------------QPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVT----TTKAQAKEPSA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 999 AFKKPIFTHPMPSPEAVIQTRCPAHAPsssFTVMALGPpkvspkrGVPKTsPRQ--TLGTPQRDIGLQTPRISPSTHEPl 1076
Cdd:pfam17823 361 SPVPVLHTSMIPEVEATSPTTQPSPLL---PTQGAAGP-------GILLA-PEQvaTEATAGTASAGPTPRSSGDPKTL- 428
|
410 420
....*....|....*....|....*....
gi 2462572620 1077 emtSSKSVSPGRKGQLYDSASTPPKPSFL 1105
Cdd:pfam17823 429 ---AMASCQLSTQGQYLVVTTDPLTPALV 454
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
804-1075 |
2.59e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 804 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 881
Cdd:PTZ00449 536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 882 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 954
Cdd:PTZ00449 609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 955 KsETRVP---------------SETARTPFKSPllkGTSAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 1019
Cdd:PTZ00449 687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572620 1020 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1075
Cdd:PTZ00449 763 TPADTPLPDILAEEFKEEDIHAETGEP-------------DEAMKRPD-SPSEHED 804
|
|
| 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 2462572620 31 YIEHLLTQLEEQHRSLWREKLA----VARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTL 96
Cdd:cd19543 175 YIAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
43-160 |
8.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 43 HRSLWREKLAVARLQREV----AQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESER--NRIQMR--SLQQQFSR 114
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQKeeNLDRKLEL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462572620 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 |
3.33e-148 |
|
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: 460.01 E-value: 3.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1468 LSPTIEEKVILCIQENVEKGQVQTKPTSVEAKQKPGPSFASWFGFRKSRLPALSSRKMDISKTKVEKKDAKVLGFGNRQL 1547
Cdd:pfam15246 1 LQSTIEEKVMLGIQENVLKGQVQDKSQSVETKQKTGPSIASWFGFRKSKLPALSSRKMDVSKGKEEKKEWKGSGFGGKQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1548 KSERKKEKKKPELQCETENELIKDTKSADNPDGGLQSKNNRRTPQDIYNQLKIEPRNRHSPVACSTKDTFMTELLNRVDK 1627
Cdd:pfam15246 81 KSEKKKEKKKEELQCALEEELAYKNEVGLDRDGRGHSKKLLKIPQDCEVQMGQEQSQLSSPYTCMTKDTFMQELLNRVDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1628 KAAPQTESGSSNASCRNVLKGSSQGSCLIGSSISTQGNHKKNMKIKADMEVPKDSLVKEANENLQEDEDDAVADSVFQSH 1707
Cdd:pfam15246 161 KAAQQTESGSNNVSCRSVSKGSSQGSCLPSNSISTQGNHKKNSKTKADMEIPRESLIKEVAENVQEDEEDTLADSACQDH 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462572620 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 |
1.75e-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: 60.07 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 2 EGKRQLEKrdfgkrLSLDSSLVEymdsnKYIEhLLTQLEEQHRSLWreklaVARLQREVAQRtsegamhEKLIHELEEER 81
Cdd:TIGR02168 197 ELERQLKS------LERQAEKAE-----RYKE-LKAELRELELALL-----VLRLEELREEL-------EELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 82 HLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQgspeQKKEEtvNIMVYQEKLSEEERKHKEALEDLh 161
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----SRLEQ--QKQILRERLANLERQLEELEAQL- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 162 mvvdedsrsessstDEGKEKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTR 241
Cdd:TIGR02168 326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAE----LEELEAELEELESRLEELEEQLETLRSK 387
|
....*..
gi 2462572620 242 VFDLEQQ 248
Cdd:TIGR02168 388 VAQLELQ 394
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-271 |
4.22e-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: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEgamHEKLIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQ 111
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 112 FSRMEETVRNLLQSQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKL------L 185
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEA------EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELeeaeeaL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 186 LERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSD 265
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
....*.
gi 2462572620 266 LLLQKL 271
Cdd:COG1196 489 AAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
32-304 |
3.96e-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: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 32 IEHLLTQLEEQHRSLwreklavaRLQREVAQRtsegamHEKLIHELEE-ERHLRLqseKRLQEVTLESERNRIQMRSLQQ 110
Cdd:COG1196 191 LEDILGELERQLEPL--------ERQAEKAER------YRELKEELKElEAELLL---LKLRELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 111 QFSRMEETVRNLlqsqgspEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEgKEKTKLLLERLK 190
Cdd:COG1196 254 ELEELEAELAEL-------EAELEEL------RLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 191 ALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQK 270
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270
....*....|....*....|....*....|....
gi 2462572620 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 2462572620 31 YIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSE----KRLQEVTLESERNRIQMR 106
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 107 SLQQQFSRMEETVRNLL-QSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKLL 185
Cdd:COG1196 313 ELEERLEELEEELAELEeELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462572620 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 |
2.65e-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: 49.28 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNR--------- 102
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeeleaqieq 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 103 --IQMRSLQQQFSRMEETVRNLLQSQGSPEQKKEETVNIMVYQEKLSEE-ERKHKEALEDLHMVVDEDSRSESSSTDEgK 179
Cdd:TIGR02168 794 lkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEELEELIEEL-E 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 180 EKTKLLLERLKALEAENSALALENENQREQyercLDEVANQVVQALLTQKDLREECVKLKTRVFDLEQQNRTLsilfQQR 259
Cdd:TIGR02168 873 SELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL----QER 944
|
..
gi 2462572620 260 VR 261
Cdd:TIGR02168 945 LS 946
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
33-306 |
4.42e-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: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 33 EHLLTQLEEQHRSLWReklavaRLQREVAQRTSEGAMHEKLIHELEEERhLRLQSEKRLQEVTLES---ERNRIQMRSLQ 109
Cdd:pfam17380 299 ERLRQEKEEKAREVER------RRKLEEAEKARQAEMDRQAAIYAEQER-MAMERERELERIRQEErkrELERIRQEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 110 QQFSRMEETVRNLLQSQGSPEQKKEETVniMVYQEKLSEEERKHKEALEDLHMvvdedsRSESSSTDEGKEKTKLLLERL 189
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELE--AARKVKILEEERQRKIQQQKVEM------EQIRAEQEEARQREVRRLEEE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 190 KALEAENsaLALENENQREQYERCLDEVANQVVQALLTQKDLRE--ECVKLKTRVFDLEQQNRTLSILFQQRVRptsdll 267
Cdd:pfam17380 444 RAREMER--VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEERKQAMIEEERKR------ 515
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462572620 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 2462572620 18 LDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEErHLRLQSEKRLQEVTLE 97
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 98 SERNRI-----QMRSLQQQFSRMEETV----RNLLQSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDS 168
Cdd:TIGR02168 828 SLERRIaaterRLEDLEEQIEELSEDIeslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462572620 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 2462572620 7 LEKRDFGKRLSldsSLVEYMDSNKYIEHLLTQLEEQHRSLwrekLAVARLQREVAQRTSEGAMHEKLIHELE-EERHLRL 85
Cdd:COG4913 218 LEEPDTFEAAD---ALVEHFDDLERAHEALEDAREQIELL----EPIRELAERYAAARERLAELEYLRAALRlWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 86 QS-EKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQS-QGSPEQKKEEtvnimvYQEKLSEEERKHKEALEDLhmv 163
Cdd:COG4913 291 ELlEAELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQ------LEREIERLERELEERERRR--- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 164 vdedsrsessstdegkEKTKLLLERLKaLEAENSALALEN-----ENQREQYERCLDEVANQVVQALLTQKDLREECVKL 238
Cdd:COG4913 362 ----------------ARLEALLAALG-LPLPASAEEFAAlraeaAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
250 260 270
....*....|....*....|....*....|...
gi 2462572620 239 KTRVFDLEQQNRTLSiLFQQRVRptsDLLLQKL 271
Cdd:COG4913 425 EAEIASLERRKSNIP-ARLLALR---DALAEAL 453
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
11-254 |
1.50e-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: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 11 DFGKRLSLDSSL----VEYMDSNKYIEhllTQLEEQHRSLWREKLAVARLQREVAQRTSE-----GAMHEKLI---HELE 78
Cdd:pfam12128 249 EFNTLESAELRLshlhFGYKSDETLIA---SRQEERQETSAELNQLLRTLDDQWKEKRDElngelSAADAAVAkdrSELE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 79 --EERHLRLQSEkRLQEVTLESErnriQMRSLQQQFSRMEETVRNLLQSQGSPEQK-------------------KEETV 137
Cdd:pfam12128 326 alEDQHGAFLDA-DIETAAADQE----QLPSWQSELENLEERLKALTGKHQDVTAKynrrrskikeqnnrdiagiKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 138 NIMVYQEKLSEEERKHKEALEDlhmVVDEDSRSESSSTDEGKEKTKLLLERLKALEAENSALALENENQREQYERClDEV 217
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQALES---ELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERI-ERA 476
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462572620 218 ANQVVQALLTQKDLREECVKLKTRvfdLEQQNRTLSI 254
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKR---RDQASEALRQ 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
53-261 |
1.52e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 53 VARLQREVAQ------RTSEGAMHEklIHELEEERHLRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNL--LQ 124
Cdd:COG4717 48 LERLEKEADElfkpqgRKPELNLKE--LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 125 SQGSPEQKKEETvnimvyQEKLSEEERKHKEALEDLHMVVDEDSRSessstdegKEKTKLLLERLKALEAENSALALENE 204
Cdd:COG4717 126 QLLPLYQELEAL------EAELAELPERLEELEERLEELRELEEEL--------EELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462572620 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 |
1.57e-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: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 19 DSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVA-RLQRE-------------VAQRTSEgamHEKLIHELE------ 78
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQeQLQAEtelcaeaeemrarLAARKQE---LEEILHELEsrleee 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 79 EERHLRLQSE-KRLQ------EVTLESE---RNRIQMR--SLQQQFSRMEETVrNLLQSQGSPEQKK----EETVNIMVY 142
Cdd:pfam01576 88 EERSQQLQNEkKKMQqhiqdlEEQLDEEeaaRQKLQLEkvTTEAKIKKLEEDI-LLLEDQNSKLSKErkllEERISEFTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 143 QekLSEEERKHK--EALEDLHMVVDEDSRSESSStdegKEKTKLLLERLK-ALEAENSAL 199
Cdd:pfam01576 167 N--LAEEEEKAKslSKLKNKHEAMISDLEERLKK----EEKGRQELEKAKrKLEGESTDL 220
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
680-1105 |
1.79e-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: 43.02 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 680 EFSSHQTGVVTVTRNEISINSTPAGPKAEHTELLPQGIACLQPRAAArDYTFFKRSEEDTEknIPKDNVDNVPRVSTESF 759
Cdd:pfam17823 89 EHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIA-ALPSEAFSAPRAA--ACRANASAAPRAAIAAA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 760 SSrTVTQNPQQQKLVKPTHNIScQSNSRSSAPMGIYQKQNLTKIPPRGKSSPQKSKlMEPEATTLLPSSGLVTLekspal 839
Cdd:pfam17823 166 SA-PHAASPAPRTAASSTTAAS-STTAASSAPTTAASSAPATLTPARGISTAATAT-GHPAAGTALAAVGNSSP------ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 840 APGKLSRFMKTESSGPLFELRSDPHIPKHSAQLPHSSRmpsrrdwvqcPKSQTPG-SRSRPAIESSDSGEPPTRDEHCGS 918
Cdd:pfam17823 237 AAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGD----------PHARRLSpAKHMPSDTMARNPAAPMGAQAQGP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 919 GPEAGVKspspppppgrsvsllarpsydySPAPSSTKSETRVPSETARTPFKSPLLKGTSAPVISsnpaTTEVQRKKPSV 998
Cdd:pfam17823 307 IIQVSTD----------------------QPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAVVT----TTKAQAKEPSA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 999 AFKKPIFTHPMPSPEAVIQTRCPAHAPsssFTVMALGPpkvspkrGVPKTsPRQ--TLGTPQRDIGLQTPRISPSTHEPl 1076
Cdd:pfam17823 361 SPVPVLHTSMIPEVEATSPTTQPSPLL---PTQGAAGP-------GILLA-PEQvaTEATAGTASAGPTPRSSGDPKTL- 428
|
410 420
....*....|....*....|....*....
gi 2462572620 1077 emtSSKSVSPGRKGQLYDSASTPPKPSFL 1105
Cdd:pfam17823 429 ---AMASCQLSTQGQYLVVTTDPLTPALV 454
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
722-1196 |
1.96e-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: 43.37 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 722 PRAAARDYTFFKR----SEEDTEKNIPKDNVD----------NVPRVSTESFSSRTVTQNPQQQKLVKPTHNISCQSNSR 787
Cdd:pfam05109 290 PKASGGDYCIQSNivfsDEIPASQDMPTNTTDityvgdnatySVPMVTSEDANSPNVTVTAFWAWPNNTETDFKCKWTLT 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 788 SSAPMGI------YQKQNLTKIPPRGKSSPQKSKLMEPEATTLLPSSGLVTLEKSPalapgklsrfmKTESSGPLFElRS 861
Cdd:pfam05109 370 SGTPSGCenisgaFASNRTFDITVSGLGTAPKTLIITRTATNATTTTHKVIFSKAP-----------ESTTTSPTLN-TT 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 862 DPHIPKHSAQLPHSSRMPSrrdwvqcpkSQTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAGVKSPSPPPPPGRSVSLLA 941
Cdd:pfam05109 438 GFAAPNTTTGLPSSTHVPT---------NLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTS 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 942 RPSYDYSPAPSSTkseTRVPSETARTPFKSPLLKGTSAPVISSNPATTEVQRKKPSVAFKKPIFTHPM---PSPEAVIQT 1018
Cdd:pfam05109 509 PTSAVTTPTPNAT---SPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTlgkTSPTSAVTT 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1019 RCP--------AHAPSSSFTVMALGPPKVSPKRGVPKTSPRQTLGTPQRDIGLQTPR------------ISPST------ 1072
Cdd:pfam05109 586 PTPnatsptvgETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSsmslrpssisetLSPSTsdnsts 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 1073 HEPLEMTSSKS-------VSPGRKGQLYDSASTP-PKP------SFLGVNESPSSQVSSSSSSSSPAKSHNSPHGcqsah 1138
Cdd:pfam05109 666 HMPLLTSAHPTggenitqVTPASTSTHHVSTSSPaPRPgttsqaSGPGNSSTSTKPGEVNVTKGTPPKNATSPQA----- 740
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462572620 1139 EKGLKTRLPVGLKVLMKSpqllrkSSTVPGKHekdSLNEASKSSVAVNKSKPEDSKNP 1196
Cdd:pfam05109 741 PSGQKTAVPTVTSTGGKA------NSTTGGKH---TTGHGARTSTEPTTDYGGDSTTP 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-258 |
2.08e-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: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 30 KYIEHLLTQLEEQHRSLWREklaVARLQREVAQRtsegamhEKLIHELEEERHlrlQSEKRLQEVTLESERNRIQMRSLQ 109
Cdd:COG4942 37 AELEKELAALKKEEKALLKQ---LAALERRIAAL-------ARRIRALEQELA---ALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 110 QQFSRM--------EETVRNLLQSQGSPEQkkeeTVNIMVYQEKLSEEERKHKEALedlhmvvdedsrsessstdegKEK 181
Cdd:COG4942 104 EELAELlralyrlgRQPPLALLLSPEDFLD----AVRRLQYLKYLAPARREQAEEL---------------------RAD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462572620 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 2462572620 48 REKLAvaRLQREVAQRTSEGAMHEKLIHELEEERHlRLQSEKRLQEVTLESERNRIQMRSLQQQFSRMEETVRNLLQSQG 127
Cdd:COG4913 609 RAKLA--ALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 128 SPEQKKEEtvnimvyQEKLSEEERKHKEALEDLhmvvdedsrsESSSTDEGKEKTKLLLERLKALEAENSALALENENQR 207
Cdd:COG4913 686 DLAALEEQ-------LEELEAELEELEEELDEL----------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462572620 208 EQYERCLDEVANQVVQALLtQKDLREECVKLKTRVFDLEQQ 248
Cdd:COG4913 749 ALLEERFAAALGDAVEREL-RENLEERIDALRARLNRAEEE 788
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
804-1075 |
2.59e-03 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 804 PPRGKSSPQKSKlmEPEATtllpSSGLVTLEKSPAL--APGKLSRFMKTESSGPLFELRSDPHIPKhSAQLPHSSRMPSR 881
Cdd:PTZ00449 536 DSKESDEPKEGG--KPGET----KEGEVGKKPGPAKehKPSKIPTLSKKPEFPKDPKHPKDPEEPK-KPKRPRSAQRPTR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 882 RDWVQCPKS-QTPGSRSRPAIESSDSGEPPTRDEHCGSGPEAgvKSPSPPPPPGRSVSLLARPSY------DYSPAPSST 954
Cdd:PTZ00449 609 PKSPKLPELlDIPKSPKRPESPKSPKRPPPPQRPSSPERPEG--PKIIKSPKPPKSPKPPFDPKFkekfydDYLDAAAKS 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 955 KsETRVP---------------SETARTPFKSPllkGTSAPVISSNPATTEVQRKKPSVAFKKPIFTHPMPSPEAVIQTR 1019
Cdd:PTZ00449 687 K-ETKTTvvldesfesilketlPETPGTPFTTP---RPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHE 762
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572620 1020 CPAHAPSSSFTVMALGPPKVSPKRGVPktsprqtlgtpqrDIGLQTPRiSPSTHEP 1075
Cdd:PTZ00449 763 TPADTPLPDILAEEFKEEDIHAETGEP-------------DEAMKRPD-SPSEHED 804
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
32-252 |
2.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 32 IEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESERNRI----QMRS 107
Cdd:COG4372 75 LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAereeELKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 108 LQQQFSRMEETVRNLLQS-QGSPEQKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKEKTKLLL 186
Cdd:COG4372 155 LEEQLESLQEELAALEQElQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLA 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462572620 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 |
3.12e-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: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 7 LEKRDFGKRLSLDSSLVEYMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLRLQ 86
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 87 SEKRLQEVTLESERNRIQmRSLQQQFSRMEETVRNLLQSQGSPEQKKEETVNIMVYQEKLSEEERKHKEALEdlhmvvde 166
Cdd:pfam02463 772 KEKELAEEREKTEKLKVE-EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL-------- 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 167 dsrsessstDEGKEKTKLLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVKLKTRVFDLE 246
Cdd:pfam02463 843 ---------KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLE 913
|
....*...
gi 2462572620 247 QQNRTLSI 254
Cdd:pfam02463 914 EKENEIEE 921
|
|
| 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 2462572620 8 EKRDFGKRLSLDSSLVE--YMDSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTsegamheKLIHELEEERHLRL 85
Cdd:pfam05483 265 ESRDKANQLEEKTKLQDenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAT-------KTICQLTEEKEAQM 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 86 QsekrlqevtlESERNRIQMRSLQQQFSRMEETVRNLLQSQGSPEQKKEETVNI--MVYQEKLSEEE-----RKHKEA-L 157
Cdd:pfam05483 338 E----------ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIitMELQKKSSELEemtkfKNNKEVeL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 158 EDLHMVVDEDSRSESSstdegKEKTKLLLERLKALEAENSALALENENQREQYERCLDEVANQVVQALLTQKDLREECVK 237
Cdd:pfam05483 408 EELKKILAEDEKLLDE-----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEK 482
|
250 260 270
....*....|....*....|....*....|..
gi 2462572620 238 LKTRVFDLEQQNRTLSILFQQRVRPTSDLLLQ 269
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASDMTLE 514
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
33-263 |
5.13e-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: 41.88 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 33 EHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELE---------EERHLRLQSEKRLQEVTLESERNRI 103
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQR 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 104 -----QMRSLQQQFSRM-----------------EETVRNLLQSQGSPEQ-----------KKEETVN---IMVYQEKLS 147
Cdd:TIGR00618 559 aslkeQMQEIQQSFSILtqcdnrskedipnlqniTVRLQDLTEKLSEAEDmlaceqhallrKLQPEQDlqdVRLHLQQCS 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 148 EEERKHKEALEDLHMVVDEDSRSESSSTDegKEKTKLLLERLKALEAENSALALENENQREQYERClDEVANQVVQALLT 227
Cdd:TIGR00618 639 QELALKLTALHALQLTLTQERVREHALSI--RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEE 715
|
250 260 270
....*....|....*....|....*....|....*....
gi 2462572620 228 QKDLREE-CVKLKTRVFDLEQQNRTLSILFQ--QRVRPT 263
Cdd:TIGR00618 716 YDREFNEiENASSSLGSDLAAREDALNQSLKelMHQART 754
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
5-234 |
7.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 5 RQLEKRDFGKRLSLDSSLveymdSNKYIEHLLTQLEEQHRSLWREKLAVARLQREVAQRTSEGAMHEKLIHELEEERHLR 84
Cdd:COG4717 317 EEEELEELLAALGLPPDL-----SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 85 LQSEKRlqevtlesERNRIQMRSLQQQFSRMEETVRNLLQsQGSPEQKKEETVNImvyQEKLSEEERKHKEaledlhmvv 164
Cdd:COG4717 392 EQAEEY--------QELKEELEELEEQLEELLGELEELLE-ALDEEELEEELEEL---EEELEELEEELEE--------- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 165 dedsrsessstdegkektklLLERLKALEAENSALALENE--NQREQYERCLDEV--------ANQVVQALL--TQKDLR 232
Cdd:COG4717 451 --------------------LREELAELEAELEQLEEDGElaELLQELEELKAELrelaeewaALKLALELLeeAREEYR 510
|
..
gi 2462572620 233 EE 234
Cdd:COG4717 511 EE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-228 |
7.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 35 LLTQLEEQHRSLWRE-----KLAVARLQrEVAQRTSEGAMHEKLIHELEEERHlrlQSEKRLQEV-----TLESERNRI- 103
Cdd:COG4717 47 LLERLEKEADELFKPqgrkpELNLKELK-ELEEELKEAEEKEEEYAELQEELE---ELEEELEELeaeleELREELEKLe 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 104 QMRSLQQQFSRMEETVRNLLQSQGSPE---QKKEETVNIMVYQEKLSEEERKHKEALEDLHMVVDEDSRSESSSTDEGKE 180
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462572620 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 2462572620 31 YIEHLLTQLEEQHRSLWREKLA----VARLQREVAQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTL 96
Cdd:cd19543 175 YIAWLQRQDKEAAEAYWREYLAgfeePTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTL 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
43-160 |
8.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462572620 43 HRSLWREKLAVARLQREV----AQRTSEGAMHEKLIHELEEERHLRLQSEKRLQEVTLESER--NRIQMR--SLQQQFSR 114
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKleKRLLQKeeNLDRKLEL 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462572620 115 MEETVRNLLQSQGSPEQKKEEtvnimvYQEKLSEEERKHKEALEDL 160
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQE------LEKKEEELEELIEEQLQEL 144
|
|
| |
