|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
227-313 |
6.21e-21 |
|
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: 85.86 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 227 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 306
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 194375109 307 SQLNRLN 313
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
225-313 |
3.16e-09 |
|
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: 53.83 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 225 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 304
Cdd:pfam16516 12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91
|
....*....
gi 194375109 305 SQSQLNRLN 313
Cdd:pfam16516 92 LQRQNQQLK 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-333 |
3.59e-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: 58.53 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 103 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 182
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 183 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 262
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194375109 263 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 333
Cdd:TIGR02168 836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-332 |
1.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 106 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 185
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 186 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 261
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194375109 262 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-332 |
3.02e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 172 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 251
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 252 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 331
Cdd:COG1196 284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
.
gi 194375109 332 Q 332
Cdd:COG1196 355 E 355
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
126-310 |
2.19e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 126 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 203
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 204 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 283
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169
|
170 180
....*....|....*....|....*....
gi 194375109 284 ERSDRERLNQE--KEELQQINETSQSQLN 310
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
79-308 |
5.59e-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: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 79 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 158
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 159 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 238
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 239 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 308
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-332 |
9.06e-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: 41.58 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 179 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCLRKSRVEF 258
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREELEELQEEL 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194375109 259 chEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:TIGR02168 249 --KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
186-332 |
1.34e-03 |
|
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: 40.39 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 186 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 265
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194375109 266 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:smart00787 205 ELDRAK-------EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
227-313 |
6.21e-21 |
|
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: 85.86 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 227 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 306
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 194375109 307 SQLNRLN 313
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
225-313 |
3.16e-09 |
|
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: 53.83 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 225 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 304
Cdd:pfam16516 12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91
|
....*....
gi 194375109 305 SQSQLNRLN 313
Cdd:pfam16516 92 LQRQNQQLK 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-333 |
3.59e-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: 58.53 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 103 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 182
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 183 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 262
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194375109 263 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 333
Cdd:TIGR02168 836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
116-332 |
5.45e-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: 54.68 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 116 QRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRdltRDRLQREEKEKE 195
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---EAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 196 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 275
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----------LDELRAELTLLNEEAA 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 194375109 276 IYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
139-333 |
7.28e-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: 54.30 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 139 ERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRED-----------DRQRDLTRDRLQREEKEKERLNEELHELKE- 206
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEa 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 207 ----ENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFK 282
Cdd:TIGR02169 781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ----------KLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 194375109 283 KERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 333
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-332 |
1.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 106 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 185
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 186 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 261
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194375109 262 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
94-332 |
1.86e-07 |
|
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: 53.15 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 94 AEPSTRKNLMNSLEQKIRCLEKQ----RKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRK 169
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEED 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 170 DDRQRE--DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLnKALQDALNIKCSFS 247
Cdd:TIGR02169 774 LHKLEEalNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL-QEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 248 EDCLRKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLE 327
Cdd:TIGR02169 853 EKEIENLNGKK--EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
....*
gi 194375109 328 KQLKQ 332
Cdd:TIGR02169 931 EELSE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-303 |
3.92e-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: 51.98 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 99 RKNLMNSLEQK---IRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE 175
Cdd:TIGR02168 311 LANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 176 DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEikRLNKALQDAlnikcsfsedclrksr 255
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE--ELEEELEEL---------------- 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 194375109 256 vEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINE 303
Cdd:TIGR02168 453 -QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-332 |
3.02e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 172 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 251
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 252 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 331
Cdd:COG1196 284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
.
gi 194375109 332 Q 332
Cdd:COG1196 355 E 355
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
118-332 |
3.46e-06 |
|
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: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 118 KELLEVNQQWDQQFRSMKElYERKVAELKTKLDAAERFLSTrekdpHQRQRKDDRQREDDRQRDL--TRDRLQREEKEKE 195
Cdd:TIGR02168 232 LRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEE-----LRLEVSELEEEIEELQKELyaLANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 196 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 275
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----------LEELEAELEELESRLE 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194375109 276 IYEEDFKKERSDR---------------------ERLNQEKEELQQINETSQSQLnrLNSQIKACQMEKEKLEKQLKQ 332
Cdd:TIGR02168 376 ELEEQLETLRSKVaqlelqiaslnneierlearlERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEE 451
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
107-301 |
1.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 107 EQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERkvaeLKTKLDAAERFLSTREKD----PHQRQRkddRQREDDRQR-D 181
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA----LQERREALQRLAEYSWDEidvaSAEREI---AELEAELERlD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 182 LTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLrksrvefchE 261
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---------E 752
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 194375109 262 EMRTEmEVLKQQVQIYEEDFKKERSD-RERLNQEKEELQQI 301
Cdd:COG4913 753 ERFAA-ALGDAVERELRENLEERIDAlRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
113-332 |
1.76e-05 |
|
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: 46.30 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 113 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKdphqrqrkddRQREDDRQRDLTRDRLQREEK 192
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALAR----------RIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 193 EKERLNEELHELKEEnkllkgkntLANKEKEHYeceikRLNKALQDALNIKCSFSEDCLRKSRVefcheeMRTEMEVLKQ 272
Cdd:COG4942 91 EIAELRAELEAQKEE---------LAELLRALY-----RLGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARRE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 273 QVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
151-332 |
1.92e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 151 AAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIK 230
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 231 RlnKALQDALNIKCSFSEDCLRKSRVefcHEEMRTEMEVLKQQVQIYEEDFKKERSD-----RERLNQEKEELQQInets 305
Cdd:COG4717 134 L--EALEAELAELPERLEELEERLEE---LRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEEL---- 204
|
170 180
....*....|....*....|....*..
gi 194375109 306 QSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
126-310 |
2.19e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 126 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 203
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 204 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 283
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169
|
170 180
....*....|....*....|....*....
gi 194375109 284 ERSDRERLNQE--KEELQQINETSQSQLN 310
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-318 |
2.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 106 LEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD 185
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 186 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKcsfsedclrksrvefcHEEMRT 265
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----------------EEEEEA 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 194375109 266 EMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKA 318
Cdd:COG1196 444 LEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-322 |
3.11e-04 |
|
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: 42.75 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 103 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELktklDAAERFLST--REKDPHQRQRKDDRQREDDRQR 180
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEerKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 181 DL---------TRDRLQREEKEKERLNEELHELKEENKLLKgkntlanKEKEHYECEIKRLNKALQDALNIKCSFSEDcl 251
Cdd:TIGR02169 372 ELeevdkefaeTRDELKDYREKLEKLKREINELKRELDRLQ-------EELQRLSEELADLNAAIAGIEAKINELEEE-- 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194375109 252 rksrvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQME 322
Cdd:TIGR02169 443 --------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
161-332 |
3.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 161 KDPHQRQRKDDRQReddRQRDL-----TRDRLQREEKEKERLNEELHELKEENKLLKgkntlankekehyecEIKRLNKA 235
Cdd:COG4913 584 KGNGTRHEKDDRRR---IRSRYvlgfdNRAKLAALEAELAELEEELAEAEERLEALE---------------AELDALQE 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 236 LQDALNIKCSFSEDCLRksrvefcHEEMRTEMEVLKQQVQIYEEDfkkeRSDRERLNQEKEELQQINETSQSQLNRLNSQ 315
Cdd:COG4913 646 RREALQRLAEYSWDEID-------VASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGE 714
|
170
....*....|....*..
gi 194375109 316 IKACQMEKEKLEKQLKQ 332
Cdd:COG4913 715 IGRLEKELEQAEEELDE 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-333 |
4.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 104 NSLEQKIRCLEKQRKELLEVNQQWDqqfrsmkelyerKVAELKTKLDAAERFLSTRekDPHQRQRKDD--RQREDDRQRD 181
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAE------------RYAAARERLAELEYLRAAL--RLWFAQRRLEllEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 182 LTR--DRLQREEKEKERLNEELHELKEEnkllkgKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsedclrksrvefc 259
Cdd:COG4913 304 LARleAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLERELEERERR----------------- 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194375109 260 HEEMRTEMEVLKQQVQIYEEDFKKErsdRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 333
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
79-308 |
5.59e-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: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 79 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 158
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 159 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 238
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 239 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 308
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-239 |
8.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 109 KIRCLEKQRKELL-EVNQQWDQQFRSMKELYERKVaELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLtRDRL 187
Cdd:COG4717 364 QLEELEQEIAALLaEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL-EEEL 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 194375109 188 QREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 239
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
179-332 |
9.06e-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: 41.58 E-value: 9.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 179 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCLRKSRVEF 258
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREELEELQEEL 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194375109 259 chEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:TIGR02168 249 --KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
115-328 |
1.14e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.22 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 115 KQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLdaAERFLSTREKDPHQRQRKDDRQREDDRQR-DLTRDRLQREEKE 193
Cdd:COG5022 813 RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVL--IQKFGRSLKAKKRFSLLKKETIYLQSAQRvELAERQLQELKID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 194 KERLNEeLHE--LKEENKLLKGKNTLANKEKEHYECEIKRLNKaLQDALNiKCSFSEDCLRKSRVEFCHEEMRTEMEVLK 271
Cdd:COG5022 891 VKSISS-LKLvnLELESEIIELKKSLSSDLIENLEFKTELIAR-LKKLLN-NIDLEEGPSIEYVKLPELNKLHEVESKLK 967
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 194375109 272 QQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLnrlnSQIKACQMEKEKLEK 328
Cdd:COG5022 968 ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS----KQYGALQESTKQLKE 1020
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
66-308 |
1.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 66 GKTaSMAHFVQGtsrMIAAESSTEHKECAEPSTRKNLMNSleQKIRCLEKQRKELLEVNQQWDQQfrsmkelyERKVAEL 145
Cdd:COG4717 35 GKS-TLLAFIRA---MLLERLEKEADELFKPQGRKPELNL--KELKELEEELKEAEEKEEEYAEL--------QEELEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 146 KTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKE-ENKLLKGKNTLANKEKEH 224
Cdd:COG4717 101 EEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRElEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 225 YECEIKRLNKALQDAlnikcsfsedclrksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 304
Cdd:COG4717 180 EELLEQLSLATEEEL---------------------QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
....
gi 194375109 305 SQSQ 308
Cdd:COG4717 239 AALE 242
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
186-332 |
1.34e-03 |
|
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: 40.39 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 186 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 265
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194375109 266 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:smart00787 205 ELDRAK-------EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
165-332 |
1.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 165 QRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----- 239
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 240 ------------LNIKcSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQS 307
Cdd:COG3883 97 rsggsvsyldvlLGSE-SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|..
gi 194375109 308 Q-------LNRLNSQIKACQMEKEKLEKQLKQ 332
Cdd:COG3883 176 QqaeqealLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
129-333 |
1.71e-03 |
|
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: 40.42 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 129 QQFRSMKELYERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEEN 208
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 209 KLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKE---- 284
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkni 953
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 194375109 285 ---RSDRERLNQEKEELQQINEtsQSQLNRLNSQIKACQMEKEKLEKQLKQM 333
Cdd:TIGR00606 954 hgyMKDIENKIQDGKDDYLKQK--ETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
105-205 |
1.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 105 SLEQKIRCLEKQRKElleVNQQWDQqfrsmkelYERKVAELKTKLDA-AERFLSTREKDPHQRQRKDDRQREDDRQRDLT 183
Cdd:COG4913 342 QLEREIERLERELEE---RERRRAR--------LEALLAALGLPLPAsAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90 100
....*....|....*....|..
gi 194375109 184 RDRLQREEKEKERLNEELHELK 205
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLE 432
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
72-211 |
1.76e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 72 AHFVQGTS------RMIAAESSTEHKECAEPSTRKNLM-NSLEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAE 144
Cdd:COG2433 370 ARVIRGLSieealeELIEKELPEEEPEAEREKEHEERElTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIER 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194375109 145 LKTKLdaaeRFLSTREKDPHQRQRK-DDRQREDDRqrdLTRdRLQREEKEKERLNEELHELKEENKLL 211
Cdd:COG2433 446 LEREL----SEARSEERREIRKDREiSRLDREIER---LER-ELEEERERIEELKRKLERLKELWKLE 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
100-317 |
2.00e-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: 40.00 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 100 KNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLStrEKDPHQRQRKDDRQREDDrq 179
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-TKKISSLKEKIEKLESEKK--EKESKISDLEDELNKDDF-- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 180 rDLTRDRLqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRKSRVEfc 259
Cdd:TIGR04523 553 -ELKKENL---EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAKKE-- 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194375109 260 HEEMRTEM-------EVLKQQVQIYEEDFKKERSDRERLNQE----KEELQQINETSQSQLNRLNSQIK 317
Cdd:TIGR04523 626 NEKLSSIIknikskkNKLKQEVKQIKETIKEIRNKWPEIIKKikesKTKIDDIIELMKDWLKELSLHYK 694
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
100-312 |
2.02e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.28 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 100 KNLMNSLEQKIRCL---EKQRKELLEVNQQWDQQFRSMKElYERKVAELKTKLD--AAERF--LSTREKDPHQRQRKDDR 172
Cdd:PRK11281 59 KLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQ-AQAELEALKDDNDeeTRETLstLSLRQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 173 QredDRQRDLT---------RDRLQREEKEkerLNEELHELKEENKLLkgKNTLANKEKEHYEcEIKRLNkALQDALNIK 243
Cdd:PRK11281 138 Q---NAQNDLAeynsqlvslQTQPERAQAA---LYANSQRLQQIRNLL--KGGKVGGKALRPS-QRVLLQ-AEQALLNAQ 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194375109 244 CSFSEDCLR---------KSRvefcHEEMRTEMEVLKQQVQIYEEDFKKERsdRERLNQEKEELQQINETSQSQLNRL 312
Cdd:PRK11281 208 NDLQRKSLEgntqlqdllQKQ----RDYLTARIQRLEHQLQLLQEAINSKR--LTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| tape_meas_lam_C |
TIGR01541 |
phage tail tape measure protein, lambda family; This model represents a relatively ... |
105-205 |
2.85e-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: 39.44 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 105 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDA-------AERFLSTREKDPHQRQRKDDRQREDD 177
Cdd:TIGR01541 28 SRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIRAQNKRQLDRfglgdkqRERLDARLQIDRTFRKQQRDLNKAMT 107
|
90 100
....*....|....*....|....*....
gi 194375109 178 RQRDLTRDRLQREE-KEKERLNEELHELK 205
Cdd:TIGR01541 108 AKGLAGSDLYKEQLaAIKASLNEALAELH 136
|
|
| Cas7_I-C |
cd09687 |
CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly ... |
169-331 |
3.59e-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: 38.96 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 169 KDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceikrlnKALQDALNIKCSFSE 248
Cdd:cd09687 158 EVGIEEKKCNPRGRLEYRLPKEEKEKRRANNLLKAIRNLSGGAKQARRLEDLSPK----------FVVLGVLNGKNPFFL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 249 DCLrksRVEFCHEEMRTEMEVLKQQVqiyeEDFKKERSDRERLNQEKEELQqiNETSQSQLNRLNSQIKACQMEKEKLEK 328
Cdd:cd09687 228 NSL---RVEEGKSALKIDVELIVTAL----EDFSEKIEDLEHIGLLKGKFA--NELEEIKELLADGGVESEVGIFEEIEK 298
|
...
gi 194375109 329 QLK 331
Cdd:cd09687 299 AVE 301
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
99-239 |
4.15e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 99 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDphQRQRKDDRQREDDR 178
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLER--LERLEEELEELEEA 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194375109 179 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 239
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
84-333 |
4.52e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 84 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS---MKELYERKVAELKTKLDAAERFLSTRE 160
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 161 KDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKllKGKNTLANKEKEHYECEikrlnkalqdal 240
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--KAAEALKKEAEEAKKAE------------ 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 241 NIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQvqiyEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQ 320
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
250
....*....|...
gi 194375109 321 MEKEKLEKQLKQM 333
Cdd:PTZ00121 1782 EEELDEEDEKRRM 1794
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
99-239 |
9.39e-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: 38.16 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194375109 99 RKNLMNSLEQKIRCLeKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRkddrqreddr 178
Cdd:pfam05483 519 QEDIINCKKQEERML-KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK---------- 587
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194375109 179 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 239
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
|
|
| |
