|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
234-320 |
3.58e-23 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 92.80 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 234 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 313
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 2217352044 314 SQLNRLN 320
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
232-320 |
1.44e-10 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 57.69 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 232 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 311
Cdd:pfam16516 12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91
|
....*....
gi 2217352044 312 SQSQLNRLN 320
Cdd:pfam16516 92 LQRQNQQLK 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-340 |
5.01e-10 |
|
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: 61.61 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 110 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 189
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 190 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 269
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217352044 270 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR02168 836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
146-340 |
4.24e-09 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 146 ERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRED-----------DRQRDLTRDRLQREEKEKERLNEELHELKE- 213
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEa 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 214 ----ENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEEMRTEMEVLKQQvQIYEEDFK 289
Cdd:TIGR02169 781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ----------KLNRLTLEKEYLEKEIQELQEQ-RIDLKEQI 849
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217352044 290 KERSDR-ERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR02169 850 KSIEKEiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-339 |
8.02e-09 |
|
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: 57.76 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 123 QRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRdltRDRLQREEKEKE 202
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---EAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 203 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 282
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----------LDELRAELTLLNEEAA 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217352044 283 IYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-339 |
1.15e-08 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 101 AEPSTRKNLMNSLEQKIRCLEKQ----RKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRK 176
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 177 DDRQRE--DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLnKALQDALNIKCSFS 254
Cdd:TIGR02169 774 LHKLEEalNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL-QEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 255 EDCLRKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLE 334
Cdd:TIGR02169 853 EKEIENLNGKK--EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
....*
gi 2217352044 335 KQLKQ 339
Cdd:TIGR02169 931 EELSE 935
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-339 |
2.65e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 113 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 192
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 268
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217352044 269 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-310 |
5.57e-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: 55.06 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 106 RKNLMNSLEQK---IRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE 182
Cdd:TIGR02168 311 LANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 183 DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEikRLNKALQDAlnikcsfsedclrksr 262
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE--ELEEELEEL---------------- 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217352044 263 vEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINE 310
Cdd:TIGR02168 453 -QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-339 |
2.50e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 125 KELLEVNQQWDQQFRSMKElYERKVAELKTKLDAAERFLSTrekdpHQRQRKDDRQREDDRQRDL--TRDRLQREEKEKE 202
Cdd:TIGR02168 232 LRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEE-----LRLEVSELEEEIEELQKELyaLANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 203 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 282
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----------LEELEAELEELESRLE 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217352044 283 IYEEDFKKERSDR---------------------ERLNQEKEELQQINETSQSQLnrLNSQIKACQMEKEKLEKQLKQ 339
Cdd:TIGR02168 376 ELEEQLETLRSKVaqlelqiaslnneierlearlERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
179-339 |
7.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 179 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 258
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 259 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:COG1196 284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
.
gi 2217352044 339 Q 339
Cdd:COG1196 355 E 355
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
114-308 |
2.97e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 114 EQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERkvaeLKTKLDAAERFLSTREKD----PHQRQRkddRQREDDRQR-D 188
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA----LQERREALQRLAEYSWDEidvaSAEREI---AELEAELERlD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 189 LTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLrksrvefchE 268
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---------E 752
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217352044 269 EMRTEmEVLKQQVQIYEEDFKKERSD-RERLNQEKEELQQI 308
Cdd:COG4913 753 ERFAA-ALGDAVERELRENLEERIDAlRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
120-339 |
4.75e-06 |
|
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: 48.22 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 120 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKdphqrqrkddRQREDDRQRDLTRDRLQREEK 199
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALAR----------RIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 200 EKERLNEELHELKEEnkllkgkntLANKEKEHYeceikRLNKALQDALNIKCSFSEDCLRKSRVefcheeMRTEMEVLKQ 279
Cdd:COG4942 91 EIAELRAELEAQKEE---------LAELLRALY-----RLGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARRE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 280 QVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
107-324 |
1.32e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 107 KNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLStrEKDPHQRQRKDDRQREDDrq 186
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-TKKISSLKEKIEKLESEKK--EKESKISDLEDELNKDDF-- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 187 rDLTRDRLqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRKSRVEfc 266
Cdd:TIGR04523 553 -ELKKENL---EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAKKE-- 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217352044 267 HEEMRTEM-------EVLKQQVQIYEEDFKKERSDRERLNQE----KEELQQINETSQSQLNRLNSQIK 324
Cdd:TIGR04523 626 NEKLSSIIknikskkNKLKQEVKQIKETIKEIRNKWPEIIKKikesKTKIDDIIELMKDWLKELSLHYK 694
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-329 |
1.94e-05 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 110 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELktklDAAERFLST--REKDPHQRQRKDDRQREDDRQR 187
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEerKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 188 DL---------TRDRLQREEKEKERLNEELHELKEENKLLKgkntlanKEKEHYECEIKRLNKALQDALNIKCSFSEDcl 258
Cdd:TIGR02169 372 ELeevdkefaeTRDELKDYREKLEKLKREINELKRELDRLQ-------EELQRLSEELADLNAAIAGIEAKINELEEE-- 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217352044 259 rksrvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQME 329
Cdd:TIGR02169 443 --------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
86-315 |
2.48e-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: 46.66 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 86 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 165
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 166 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 245
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 246 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 315
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
158-339 |
2.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 158 AAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIK 237
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 238 RlnKALQDALNIKCSFSEDCLRKSRVefcHEEMRTEMEVLKQQVQIYEEDFKKERSD-----RERLNQEKEELQQInets 312
Cdd:COG4717 134 L--EALEAELAELPERLEELEERLEE---LRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEEL---- 204
|
170 180
....*....|....*....|....*..
gi 2217352044 313 QSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-325 |
6.18e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 113 LEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD 192
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKcsfsedclrksrvefcHEEMRT 272
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----------------EEEEEA 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217352044 273 EMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKA 325
Cdd:COG1196 444 LEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
133-317 |
6.73e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.09 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 133 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 210
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 211 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 290
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169
|
170 180
....*....|....*....|....*....
gi 2217352044 291 ERSDRERLNQE--KEELQQINETSQSQLN 317
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
73-315 |
9.04e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 73 GKTaSMAHFVQGtsrMIAAESSTEHKECAEPSTRKNLMNSleQKIRCLEKQRKELLEVNQQWDQQfrsmkelyERKVAEL 152
Cdd:COG4717 35 GKS-TLLAFIRA---MLLERLEKEADELFKPQGRKPELNL--KELKELEEELKEAEEKEEEYAEL--------QEELEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 153 KTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKE-ENKLLKGKNTLANKEKEH 231
Cdd:COG4717 101 EEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRElEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 232 YECEIKRLNKALQDAlnikcsfsedclrksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 311
Cdd:COG4717 180 EELLEQLSLATEEEL---------------------QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
....
gi 2217352044 312 SQSQ 315
Cdd:COG4717 239 AALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-339 |
9.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 165 TRE---KDPHQRQRKDDRQReddRQRDL-----TRDRLQREEKEKERLNEELHELKEENKLLKgkntlankekehyecEI 236
Cdd:COG4913 578 TRAgqvKGNGTRHEKDDRRR---IRSRYvlgfdNRAKLAALEAELAELEEELAEAEERLEALE---------------AE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 237 KRLNKALQDALNIKCSFSEDCLRksrvefcHEEMRTEMEVLKQQVQIYEEDfkkeRSDRERLNQEKEELQQINETSQSQL 316
Cdd:COG4913 640 LDALQERREALQRLAEYSWDEID-------VASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEEL 708
|
170 180
....*....|....*....|...
gi 2217352044 317 NRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDE 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-340 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 111 NSLEQKIRCLEKQRKELLEVNQQWDqqfrsmkelyerKVAELKTKLDAAERFLSTRekDPHQRQRKDD--RQREDDRQRD 188
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAE------------RYAAARERLAELEYLRAAL--RLWFAQRRLEllEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 189 LTR--DRLQREEKEKERLNEELHELKEEnkllkgKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsedclrksrvefc 266
Cdd:COG4913 304 LARleAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLERELEERERR----------------- 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217352044 267 HEEMRTEMEVLKQQVQIYEEDFKKErsdRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
136-340 |
1.35e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 136 QQFRSMKELYERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEEN 215
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 216 KLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKE---- 291
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkni 953
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217352044 292 ---RSDRERLNQEKEELQQINEtsQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:TIGR00606 954 hgyMKDIENKIQDGKDDYLKQK--ETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-339 |
1.49e-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: 44.28 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 179 RQREDDRQRDLTRDRLqreekekERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCL 258
Cdd:TIGR02168 173 RRKETERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 259 RKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:TIGR02168 242 EELQEEL--KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
.
gi 2217352044 339 Q 339
Cdd:TIGR02168 320 E 320
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-341 |
1.55e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 102 EPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYE------------------------RKVAELKTKLD 157
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekeierlketiiknnseikdltNQDSVKELIIK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 158 AAERFLSTREK--DPHQRQRKDDRQREDDRQRDLTRDrlqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECE 235
Cdd:TIGR04523 458 NLDNTRESLETqlKVLSRSINKIKQNLEQKQKELKSK-----EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 236 IKRLNKALQDaLNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQ--------------VQIYEEDFKKERSDRERLNQE 301
Cdd:TIGR04523 533 KKEKESKISD-LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTqkslkkkqeekqelIDQKEKEKKDLIKEIEEKEKK 611
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2217352044 302 KEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQMY 341
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
116-246 |
1.62e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 116 KIRCLEKQRKELL-EVNQQWDQQFRSMKELYERKVaELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLtRDRL 194
Cdd:COG4717 364 QLEELEQEIAALLaEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL-EEEL 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2217352044 195 QREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 246
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-340 |
1.91e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 91 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS---MKELYERKVAELKTKLDAAERFLSTRE 167
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 168 KDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKllKGKNTLANKEKEHYECEikrlnkalqdal 247
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--KAAEALKKEAEEAKKAE------------ 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 248 NIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQvqiyEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQ 327
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
250
....*....|...
gi 2217352044 328 MEKEKLEKQLKQM 340
Cdd:PTZ00121 1782 EEELDEEDEKRRM 1794
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
193-339 |
3.06e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 193 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 272
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217352044 273 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:smart00787 205 ELDRAK-------EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
122-335 |
3.91e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 122 KQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLdaAERFLSTREKDPHQRQRKDDRQREDDRQR-DLTRDRLQREEKE 200
Cdd:COG5022 813 RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVL--IQKFGRSLKAKKRFSLLKKETIYLQSAQRvELAERQLQELKID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 201 KERLNEeLHE--LKEENKLLKGKNTLANKEKEHYECEIKRLNKaLQDALNiKCSFSEDCLRKSRVEFCHEEMRTEMEVLK 278
Cdd:COG5022 891 VKSISS-LKLvnLELESEIIELKKSLSSDLIENLEFKTELIAR-LKKLLN-NIDLEEGPSIEYVKLPELNKLHEVESKLK 967
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217352044 279 QQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLnrlnSQIKACQMEKEKLEK 335
Cdd:COG5022 968 ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS----KQYGALQESTKQLKE 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-339 |
4.18e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 181 REDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRK 260
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-KLELLLSNLKKKIQK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 261 srvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQ-QINETSQSQlNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:TIGR04523 213 ------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtQLNQLKDEQ-NKIKKQLSEKQKELEQNNKKIKE 285
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
106-246 |
4.79e-04 |
|
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: 42.40 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 106 RKNLMNSLEQKIRCLeKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRkddrqreddr 185
Cdd:pfam05483 519 QEDIINCKKQEERML-KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK---------- 587
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217352044 186 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 246
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
121-339 |
5.91e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 121 EKQRKELLEVNQQwdQQFRSMKELYERKVaELKTKLDAAER-----------FLSTREKDPHQRQRKDDRQREDDRQRDL 189
Cdd:pfam17380 286 ERQQQEKFEKMEQ--ERLRQEKEEKAREV-ERRRKLEEAEKarqaemdrqaaIYAEQERMAMERERELERIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 190 TRDRLQREEKEKERLnEELHELKEENKllkgkntlANKEKEHYECEIKRLNKALQdalnikcsfsedclrKSRVEFCHEE 269
Cdd:pfam17380 363 ERIRQEEIAMEISRM-RELERLQMERQ--------QKNERVRQELEAARKVKILE---------------EERQRKIQQQ 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217352044 270 MRTEMEVLKQQVQIYEEDFKKERSDRERlnqEKEELQQINETSQSQLNRLNSQ-----IKACQMEKEKLEKQLKQ 339
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERLRQQeeerkRKKLELEKEKRDRKRAE 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-338 |
5.95e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 91 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKEllEVNQQWDQQFRSMKELYE-----------RKVAELKTKLDAA 159
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD--EAKKKAEEDKKKADELKKaaaakkkadeaKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 160 ERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEK-------ERLNEELHELKEENKLLKGKNTLANKEKEHY 232
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeakkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 233 ECEIKRLNKALQDALNIKcsfSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS 312
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
250 260
....*....|....*....|....*.
gi 2217352044 313 QSQLNRLNSQIKACQMEKEKLEKQLK 338
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
79-218 |
5.98e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 79 AHFVQGTS------RMIAAESSTEHKECAEPSTRKNLM-NSLEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAE 151
Cdd:COG2433 370 ARVIRGLSieealeELIEKELPEEEPEAEREKEHEERElTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIER 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217352044 152 LKTKLdaaeRFLSTREKDPHQRQRK-DDRQREDDRqrdLTRdRLQREEKEKERLNEELHELKEENKLL 218
Cdd:COG2433 446 LEREL----SEARSEERREIRKDREiSRLDREIER---LER-ELEEERERIEELKRKLERLKELWKLE 505
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
172-339 |
6.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 172 QRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----- 246
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 247 ------------LNIKcSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQS 314
Cdd:COG3883 97 rsggsvsyldvlLGSE-SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|..
gi 2217352044 315 Q-------LNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:COG3883 176 QqaeqealLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
112-212 |
7.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 112 SLEQKIRCLEKQRKElleVNQQWDQqfrsmkelYERKVAELKTKLDA-AERFLSTREKDPHQRQRKDDRQREDDRQRDLT 190
Cdd:COG4913 342 QLEREIERLERELEE---RERRRAR--------LEALLAALGLPLPAsAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90 100
....*....|....*....|..
gi 2217352044 191 RDRLQREEKEKERLNEELHELK 212
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
112-338 |
1.00e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 112 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTR 191
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 192 DRLQREEKEKERLNEElhelKEENKLLKGKNTLANKEKEHYECE------IKRLNKALQDALNIKCSFSEDCLRKSRVEF 265
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQ----KEQDWNKELKSELKNQEKKLEEIQnqisqnNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217352044 266 CHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINEtsqsqlnRLNSQIKACQMEKEKLEKQLK 338
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-------QKDEQIKKLQQEKELLEKEIE 429
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
87-305 |
1.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 87 RMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEvnqqwdqqfrSMKELyERKVAELKTKLdaaeRFLSTR 166
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE----------KIREL-EERIEELKKEI----EELEEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 167 EKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLN------ 240
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerh 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217352044 241 KALQDALNIKCSFSEdcLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEEL 305
Cdd:PRK03918 362 ELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-246 |
1.35e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 106 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDphQRQRKDDRQREDDR 185
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLER--LERLEEELEELEEA 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217352044 186 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 246
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
120-339 |
1.42e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 120 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAErflSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEK 199
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL-NEQISQLKKELTNSE---SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 200 EKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLnkaLQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQ 279
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL---KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217352044 280 QVQIYEEDFKKERSDRERLNQE-----KEELQQINETSQS--QLNRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEKKELeeKVKDLTKKISSLKEKIEKLESEKKE 535
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
91-339 |
1.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 91 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyeRKVAELKTKLDAAERFLSTREKDp 170
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA--KKAAEAKKKADEAKKAEEAKKAD- 1525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 171 HQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIK 250
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 251 CSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINET---SQSQLNRLNSQIKACQ 327
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKAAEeakKAEEDKKKAEEAKKAE 1684
|
250
....*....|..
gi 2217352044 328 MEKEKLEKQLKQ 339
Cdd:PTZ00121 1685 EDEKKAAEALKK 1696
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-306 |
1.71e-03 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 110 MNSLEQKIRCLEKQRKELLEVNQQWDQQfrsmKELYERKVAELKTKLDAAERflstrEKDPHQRQRKDDRQREDDRQRDl 189
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEE-----ELEELEAALRDLESRLGDLKKE- 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 190 tRDRLQRE----EKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsEDClrKSRVEF 265
Cdd:TIGR02169 891 -RDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-----EDV--QAELQR 962
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217352044 266 CHEEMRTEMEVLKQQVQIYEE---DFKKERSDRERLNQEKEELQ 306
Cdd:TIGR02169 963 VEEEIRALEPVNMLAIQEYEEvlkRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-335 |
1.73e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 108 NLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERflstrekdphQRQRKDDRQREDDRQR 187
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELES----------ELEALLNERASLEEAL 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 188 DLTRDRLQREEKEKERLNEELHELKEEnklLKGKNTLANKEKEhyeceikRLNKALQDALNIKCSFSEdclrksrvefch 267
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLEL-------RLEGLEVRIDNLQERLSE------------ 947
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217352044 268 eEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS-------QSQLNRLNSQIKACQMEKEKLEK 335
Cdd:TIGR02168 948 -EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAieeyeelKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
95-298 |
1.74e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 95 TEHKEC--AEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKElyerKVAELKTKLDAAERFLSTREKDPHQ 172
Cdd:pfam10174 372 TEEKSTlaGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE----RVKSLQTDSSNTDTALTTLEEALSE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 173 RQRKDDRQREddrQRDltRDRLQREEkEKERLNEELHELKEENKLLKG----KNTLANKEKEHYECE----IKRLNKALQ 244
Cdd:pfam10174 448 KERIIERLKE---QRE--REDRERLE-ELESLKKENKDLKEKVSALQPelteKESSLIDLKEHASSLassgLKKDSKLKS 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217352044 245 DALNIK-----CSFSEDCLRKSR----VEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERL 298
Cdd:pfam10174 522 LEIAVEqkkeeCSKLENQLKKAHnaeeAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
|
| Cas7_I-C |
cd09687 |
CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly ... |
176-338 |
1.92e-03 |
|
CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Cst2/DevR family
Pssm-ID: 187818 Cd Length: 302 Bit Score: 40.12 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 176 KDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHyecEIKRLnkalqdaLNIKCSFSE 255
Cdd:cd09687 158 EVGIEEKKCNPRGRLEYRLPKEEKEKRRANNLLKAIRNLSGGAKQARRLEDLSPKF---VVLGV-------LNGKNPFFL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 256 DCLrksRVEFCHEEMRTEMEVLKQQVqiyeEDFKKERSDRERLNQEKEELQqiNETSQSQLNRLNSQIKACQMEKEKLEK 335
Cdd:cd09687 228 NSL---RVEEGKSALKIDVELIVTAL----EDFSEKIEDLEHIGLLKGKFA--NELEEIKELLADGGVESEVGIFEEIEK 298
|
...
gi 2217352044 336 QLK 338
Cdd:cd09687 299 AVE 301
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-340 |
2.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 106 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS--MKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE- 182
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELREleKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEk 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 183 --------DDRQRDLTRD--RLQREEKEKERLNEELHELKEENKLLKGK-NTLANKEKEHYECEIKRLNKALQDALNIKC 251
Cdd:PRK03918 530 lkekliklKGEIKSLKKEleKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 252 SFSEDCLRKSRVEFCHEEM----------RTEMEVLKQQVQIYEEDFKKErsDRERLNQEKEELQQINETSQSQLNRLNS 321
Cdd:PRK03918 610 AEKELEREEKELKKLEEELdkafeelaetEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEK 687
|
250
....*....|....*....
gi 2217352044 322 QIKACQMEKEKLEKQLKQM 340
Cdd:PRK03918 688 RREEIKKTLEKLKEELEER 706
|
|
| tape_meas_lam_C |
TIGR01541 |
phage tail tape measure protein, lambda family; This model represents a relatively ... |
112-212 |
2.53e-03 |
|
phage tail tape measure protein, lambda family; This model represents a relatively well-conserved region near the C-terminus of the tape measure protein of a lambda and related phage. This protein, which controls phage tail length, is typically about 1000 residues in length. Both low-complexity sequence and insertion/deletion events appear common in this family. Mutational studies suggest a ruler or template role in the determination of phage tail length. Similar behavior is attributed to proteins from distantly related or unrelated families in other phage. [Mobile and extrachromosomal element functions, Prophage functions]
Pssm-ID: 273681 [Multi-domain] Cd Length: 332 Bit Score: 39.82 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 112 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDA-------AERFLSTREKDPHQRQRKDDRQREDD 184
Cdd:TIGR01541 28 SRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIRAQNKRQLDRfglgdkqRERLDARLQIDRTFRKQQRDLNKAMT 107
|
90 100
....*....|....*....|....*....
gi 2217352044 185 RQRDLTRDRLQREE-KEKERLNEELHELK 212
Cdd:TIGR01541 108 AKGLAGSDLYKEQLaAIKASLNEALAELH 136
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
180-339 |
2.69e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 38.89 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 180 QREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKG-----KNTLA------NKEKEHYECEIKRLNKALQDAL- 247
Cdd:pfam05010 3 QKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKivaefEKTIAqmieekQKQKELEHAEIQKVLEEKDQALa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 248 ---NIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKE--RSDR------ERLNQEKEELQQINETSQSQL 316
Cdd:pfam05010 83 dlnSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEeqRYQAlkahaeEKLDQANEEIAQVRSKAKAET 162
|
170 180
....*....|....*....|...
gi 2217352044 317 NRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:pfam05010 163 AALQASLRKEQMKVQSLERQLEQ 185
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
107-319 |
4.52e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 107 KNLMNSLEQKIRCL---EKQRKELLEVNQQWDQQFRSMKElYERKVAELKTKLD--AAERF--LSTREKDPHQRQRKDDR 179
Cdd:PRK11281 59 KLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQ-AQAELEALKDDNDeeTRETLstLSLRQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 180 QredDRQRDLT---------RDRLQREEKEkerLNEELHELKEENKLLkgKNTLANKEKEHYEcEIKRLNkALQDALNIK 250
Cdd:PRK11281 138 Q---NAQNDLAeynsqlvslQTQPERAQAA---LYANSQRLQQIRNLL--KGGKVGGKALRPS-QRVLLQ-AEQALLNAQ 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217352044 251 CSFSEDCLR---------KSRvefcHEEMRTEMEVLKQQVQIYEEDFKKERsdRERLNQEKEELQQINETSQSQLNRL 319
Cdd:PRK11281 208 NDLQRKSLEgntqlqdllQKQ----RDYLTARIQRLEHQLQLLQEAINSKR--LTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
184-340 |
5.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 184 DRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDAlnikcsfsedclrksrv 263
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA----------------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217352044 264 efcheemRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:COG4372 93 -------QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
125-319 |
5.68e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 125 KELLEvnqqwdqQFRSMKELYERkVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERL 204
Cdd:COG3096 498 RELLR-------RYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 205 NEELHELKEENKLLKgkntlanKEKEHYECEIKRLNK------ALQDALNIKCsfsedclrksrvEFCHEEMRTEMEVLK 278
Cdd:COG3096 570 EEQAAEAVEQRSELR-------QQLEQLRARIKELAArapawlAAQDALERLR------------EQSGEALADSQEVTA 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217352044 279 --QQVQIYEEDFKKERSD----RERLNQEKEELQQINETSQSQLNRL 319
Cdd:COG3096 631 amQQLLEREREATVERDElaarKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-225 |
5.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 110 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDL 189
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEEL-EAELAELQEELEELLEQLSLATEE-ELQDLAEELEELQQRLAEL 211
|
90 100 110
....*....|....*....|....*....|....*.
gi 2217352044 190 tRDRLQREEKEKERLNEELHELKEENKLLKGKNTLA 225
Cdd:COG4717 212 -EEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
105-339 |
6.15e-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: 39.18 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 105 TRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyerkvaELKTKLDAAERFLSTREKDPHQRQRKDDRQREDD 184
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY------QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 185 RQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQ---DALNIKCSFSEDCLRKS 261
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrkvDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217352044 262 RVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQL-NRLNSQIKACQMEKEKLEKQLKQ 339
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEsERLSSAAKLKEEELELKSEEEKE 406
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
268-341 |
8.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.27 E-value: 8.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217352044 268 EEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQME----KEKLEKQLKQMY 341
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieerREELGERARALY 96
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
107-340 |
9.22e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 37.97 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 107 KNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYE---RKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRED 183
Cdd:COG1340 28 KEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDelnEKVKELKEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217352044 184 DRQRDLTRDRLQREEKEKERlneELHELKEENKLLKgknTLANKEKehyecEIKRLNKALQDALNIKCSFSEdcLRKSRV 263
Cdd:COG1340 108 GGSIDKLRKEIERLEWRQQT---EVLSPEEEKELVE---KIKELEK-----ELEKAKKALEKNEKLKELRAE--LKELRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217352044 264 EFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 340
Cdd:COG1340 175 EA--EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249
|
|
| |
