|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
868-991 |
1.27e-50 |
|
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365.
Pssm-ID: 464333 [Multi-domain] Cd Length: 138 Bit Score: 175.26 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 868 MDLRWQIHHSEKNWNREKVELLDRLDRDRQEWERQKKEFLWRIEQLQKENSPRR------------GGSFLCDQKDGNVR 935
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRRkinmnerakvidGEKFVPDQKESSSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2052734496 936 PFPHQGSLRMPR--PVAMWPCADADSIPFEDRPLSKLKESDRCSASENLYLDALSLDD 991
Cdd:pfam14818 81 PFPDSGQCEFPRmnHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
141-235 |
5.37e-37 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 134.73 E-value: 5.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 141 DSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANI 220
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 2052734496 221 LGRKIVELEVENRGL 235
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
270-362 |
1.75e-36 |
|
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, SOGA2, and SOGA3. SOGA1 regulates autophagy by playing a role in the reduction of glucose production in an adiponectin and insulin dependent manner.
Pssm-ID: 463264 [Multi-domain] Cd Length: 95 Bit Score: 133.19 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 270 SSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPPREPGWLGEGASPGA--GGGAPLQEELKSARLQISE 347
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSdsSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 2052734496 348 LSGKVLKLQHENHAL 362
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-296 |
1.98e-11 |
|
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: 69.32 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAK 88
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 89 AEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKLGR 168
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 169 EKDELEQELQKYKSLYGDVDSPLptgeaggppstreAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQER 248
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEAL-------------ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2052734496 249 EGPGRDHAPSIPTSPFGDSLEsstELRRHLQFVEEEAELLRRSISEIE 296
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-356 |
2.26e-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: 62.38 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 58 IRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRS-------TREM 130
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEEriaqlskELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 131 YKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDvdsplpTGEAGGPPSTREAELKLR 210
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL------LNEEAANLRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 211 LKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHApsiptspfgdsLESSTELRRHLQFVEEEAELLRR 290
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-----------LNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2052734496 291 SISEIEDHNRQLTHELSKfkfepprepgwlgegaspgagggapLQEELKSARLQISELSGKVLKLQ 356
Cdd:TIGR02168 902 ELRELESKRSELRRELEE-------------------------LREKLAQLELRLEGLEVRIDNLQ 942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-415 |
3.72e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNcRILQYRLRKAEQKSLKVAetgqvdgelIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENE 94
Cdd:COG1196 201 QLEPLERQAEKAERY-RELKEELKELEAELLLLK---------LRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 95 TLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELE 174
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 175 QELQkykslygdvdsplptgeaggppSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRD 254
Cdd:COG1196 351 EELE----------------------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 255 HApsiptspfgdslESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKfkfepprepgwlgegaspgaggGAPL 334
Cdd:COG1196 409 EE------------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE----------------------EAEL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 335 QEELKSARLQISELSGKVLKLQHENHALLSNIQRCDLAAHLGLRApsprdsdAESDAGKKESDGEESRLPQPKREGPVGG 414
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-------EADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
.
gi 2052734496 415 E 415
Cdd:COG1196 528 V 528
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
83-358 |
1.65e-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: 56.23 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 83 EEKRAKAEDENETLRQQMIEVEISKQALQNELERLKesslKRRSTREMYKEKKTFNQDDSADLRC-QLQFAKEEAFLMRK 161
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR----REREKAERYQALLKEKREYEGYELLkEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 162 KMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANI----------------LGRKI 225
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaslersiaekereledAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 226 VELEVENRGLKAEMEDMRGQQEREGPGRDHApsipTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHE 305
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2052734496 306 LSKFKFEPPRepgwLGEGASPGAGGGAPLQEELKSARLQISELSGKVLKLQHE 358
Cdd:TIGR02169 401 INELKRELDR----LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-312 |
2.35e-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: 55.83 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 10 EEDVYQLQELRRELDRANKNCRI-----LQYRLRKAEQKSLKVAETGQVDGELIRSLEQdLKVAKDVSVRLHHELktvEE 84
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERqaekaERYKELKAELRELELALLVLRLEELREELEE-LQEELKEAEEELEEL---TA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 85 KRAKAEDENETLRQQMIEVEISKQALQNELERLKE--SSLKRRstREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKK 162
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQ--KQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 163 MAKLGREKDELEQELQkykslygDVDSPLPTGEAggppstREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDM 242
Cdd:TIGR02168 339 LAELEEKLEELKEELE-------SLEAELEELEA------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2052734496 243 RGQQER--------EGPGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFE 312
Cdd:TIGR02168 406 EARLERledrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-301 |
9.35e-06 |
|
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: 50.45 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 3 EMRDSYLEEDVYQLQELRRELDRankncRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKvakdvsvRLHHElktv 82
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEA-----RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN-------RLTLE---- 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 83 eekRAKAEDENETLRQQMIEVEISKQALQNELERLKessLKRRSTREMYKEKKTFnqddSADLRCQLQFAKEEAFLMRKK 162
Cdd:TIGR02169 828 ---KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN---GKKEELEEELEELEAA----LRDLESRLGDLKKERDELEAQ 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 163 MAKLGREKDELEQELQKYKSLYGDVDSPLptGEAGGPPSTREAELKLRLKLVEEEANI--LGRKIVELEVENRGLkaEME 240
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEIPEEELSLedVQAELQRVEEEIRAL--EPV 973
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2052734496 241 DMRGQQEREgpgrdhapsiptspfgDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQ 301
Cdd:TIGR02169 974 NMLAIQEYE----------------EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
15-267 |
1.07e-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: 49.76 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDvsvrlhhELKTVEEKRAKAEDENE 94
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALAR-------RIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 95 TLRQQMIEVEISKQALQNELERLkesslkrrsTREMYKEKKT------FNQDDSAD-------LRCQLQFAKEEAFLMRK 161
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAEL---------LRALYRLGRQpplallLSPEDFLDavrrlqyLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 162 KMAKLGREKDELEQELQKYKSLYGDVdsplptgeaggppSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMED 241
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAEL-------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|....*..
gi 2052734496 242 MRGQQER-EGPGRDHAPSIPTSPFGDS 267
Cdd:COG4942 225 LEALIARlEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-378 |
1.11e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 92 ENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKLGREKD 171
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 172 ELEQELQKYKSLYGDVDSPLPTGEAggppstREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEmedmrgqqeregp 251
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEA------EIEELEAQIEQLKEELKALREALDELRAELTLLNEE------------- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 252 grdhapsiptspFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKfEPPREpgwLGEGASPGAGGG 331
Cdd:TIGR02168 819 ------------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE-ELIEE---LESELEALLNER 882
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2052734496 332 APLQEELKSARLQISELSGKVLKLQHENHALLSNIQRC-DLAAHLGLR 378
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELrEKLAQLELR 930
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
9-308 |
1.25e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAK 88
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 89 AEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDS--ADLRCQLQFAKEEAFLMRKKMAKL 166
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEllKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 167 GREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPST---REAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMR 243
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEellEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2052734496 244 GQQEREGPGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSK 308
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
10-365 |
1.85e-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: 49.25 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 10 EEDVYQLQELRRELDRANKNCRILQYRLR--KAEQKSLKvaetGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRA 87
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN----NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 88 KAEDENETLRQQMIEVEISKQALQNELERlKESSLKR-RSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKL 166
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEE-KQNEIEKlKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 167 GREKDELEQELQKYKSLYGDVDSPLPTGEaggppsTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMrgQQ 246
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLT------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK--QK 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 247 EREGPGRDHapSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFepprepgwlgegasp 326
Cdd:TIGR04523 490 ELKSKEKEL--KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF--------------- 552
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2052734496 327 gagggaplqeELKSARL--QISELSGKVLKLQHENHALLSN 365
Cdd:TIGR04523 553 ----------ELKKENLekEIDEKNKEIEELKQTQKSLKKK 583
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-302 |
1.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 1 MEEMRDSYLEEDVYQLQELRREldranKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELK 80
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 81 TVEEKRAKAEdenETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLqfAKEEAFLMR 160
Cdd:PTZ00121 1669 KAEEDKKKAE---EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE--AKKEAEEDK 1743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 161 KKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANILGRKIVELEVENRG-----L 235
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnlvinD 1823
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2052734496 236 KAEMEDMRGQQ--EREGPGRDHAPSIPTSPFGDSLESSTELRRHLQFvEEEAELLRRSISEIE--DHNRQL 302
Cdd:PTZ00121 1824 SKEMEDSAIKEvaDSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF-NKEKDLKEDDEEEIEeaDEIEKI 1893
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
15-261 |
2.36e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENE 94
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEE-------LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 95 TLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQfakeeaflmRKKMAKLGREKDELE 174
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ---------ALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 175 QELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRD 254
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
....*..
gi 2052734496 255 HAPSIPT 261
Cdd:COG4372 270 EKDTEEE 276
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-310 |
2.94e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 2 EEMRDSYLEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVD--GELIRSLEQDLKVakdvsvrlhHEL 79
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKelAEQLKELEEKLKK---------YNL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 80 KTVEEKrakaEDENETLRQQMIEVEISKQALQNELERLKEssLKRRStREMYKEKKTfnqddsadlrcqlqfAKEEAFLM 159
Cdd:PRK03918 518 EELEKK----AEEYEKLKEKLIKLKGEIKSLKKELEKLEE--LKKKL-AELEKKLDE---------------LEEELAEL 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 160 RKKMAKLGREK-DELEQELQKYKSLYGDVDsplptgEAGGPPSTREAELKlRLKLVEEEANILGRKIVELEVENRGLKAE 238
Cdd:PRK03918 576 LKELEELGFESvEELEERLKELEPFYNEYL------ELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKE 648
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2052734496 239 MEDMRGQQEREgpgrdhapsiptsPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK 310
Cdd:PRK03918 649 LEELEKKYSEE-------------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-310 |
7.15e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 16 LQELRRELDRankncrilqyrlRKAEQKSLkVAETGQVDgELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENET 95
Cdd:PRK03918 167 LGEVIKEIKR------------RIERLEKF-IKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 96 L---RQQMIEVEISKQALQNELERLKEsslKRRSTREMYKEKKtfnqDDSADLRCQ------LQFAKEEAFLMRKKMAKL 166
Cdd:PRK03918 233 LeelKEEIEELEKELESLEGSKRKLEE---KIRELEERIEELK----KEIEELEEKvkelkeLKEKAEEYIKLSEFYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 167 GREKDELEQELQKYKSLYGDVDSPLPTGEAggpPSTREAELKLRLKLVEEEANILGRKIVELEVenrgLKAEMEDMRGQQ 246
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEE---KEERLEELKKKLKELEKRLEELEERHELYEE----AKAKKEELERLK 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2052734496 247 EREGPgrdhapsiptspfgdslESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK 310
Cdd:PRK03918 379 KRLTG-----------------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-310 |
1.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 9 LEEDVYQLQELRRELDRANKNCRILQYRLR---------KAEQKSL--KVAETGQVDG------ELIRSLEQDLKVAKDV 71
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIReleerieelKKEIEELeeKVKELKELKEkaeeyiKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 72 SVRL---HHELKTVEEKRAKAEDENETLRqqmiEVEISKQALQNELERLKESSLK----RRSTREMYKEKKTFNQDDSAD 144
Cdd:PRK03918 313 EKRLsrlEEEINGIEERIKELEEKEERLE----ELKKKLKELEKRLEELEERHELyeeaKAKKEELERLKKRLTGLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 145 LRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANILGRK 224
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 225 IvELEVENRGLKAEMEDMRGQQEREgpgRDHAPSIPTSPFGDSLESSTEL--RRHLQFVEEEAELLRRSISEIEDHNRQL 302
Cdd:PRK03918 469 K-EIEEKERKLRKELRELEKVLKKE---SELIKLKELAEQLKELEEKLKKynLEELEKKAEEYEKLKEKLIKLKGEIKSL 544
|
....*...
gi 2052734496 303 THELSKFK 310
Cdd:PRK03918 545 KKELEKLE 552
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9-199 |
1.32e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGElIRSLEQDLKVAKDVSVrlhhELKTVEEKRAK 88
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-IAELEAELERLDASSD----DLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 89 AEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKM----- 163
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLeerid 776
|
170 180 190
....*....|....*....|....*....|....*....
gi 2052734496 164 ---AKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGP 199
Cdd:COG4913 777 alrARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
15-179 |
1.50e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 46.67 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNcriLQYRLRKAEQKSLKVAETGQVD----GELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAE 90
Cdd:pfam07111 482 ELEQLREERNRLDAE---LQLSAHLIQQEVGRAREQGEAErqqlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQEST 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 91 DENETLRQQMI-EVEISKQALQN---ELE-RLKE--SSLKRR---STREMYK---------EKKTFNQDDSADL-RCQLQ 150
Cdd:pfam07111 559 EEAASLRQELTqQQEIYGQALQEkvaEVEtRLREqlSDTKRRlneARREQAKavvslrqiqHRATQEKERNQELrRLQDE 638
|
170 180
....*....|....*....|....*....
gi 2052734496 151 FAKEEAFLMRKKMAKLGREKDELEQELQK 179
Cdd:pfam07111 639 ARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1-175 |
2.34e-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: 45.88 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 1 MEEMRDSYLEEDVYQLQELRRELDRANKN--CRILQYRLRKAEQKSLKVAETgQVDGELIRSLEQDLKVAKDVSVRLHHE 78
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEARQRevRRLEEERAREMERVRLEEQER-QQQVERLRQQEEERKRKKLELEKEKRD 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 79 LKTVEEKRAKA-EDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQ-DDSADLRCQLQFAKEEa 156
Cdd:pfam17380 486 RKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEE- 564
|
170
....*....|....*....
gi 2052734496 157 flmRKKMAKLGREKDELEQ 175
Cdd:pfam17380 565 ---RSRLEAMEREREMMRQ 580
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-302 |
4.33e-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: 45.06 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 71 VSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQ 150
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 151 FAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDV-----DSPLPTGEAGGPP----------STREAELKLRLKLVE 215
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKleeevsrieaRLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 216 EEanILGRKIVELEVENRGLKaEMEDMRGQQEREGPGRdhapsiptspFGDSLESSTELRRHLQFVEEEAELLRRSISEI 295
Cdd:TIGR02169 828 KE--YLEKEIQELQEQRIDLK-EQIKSIEKEIENLNGK----------KEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
....*..
gi 2052734496 296 EDHNRQL 302
Cdd:TIGR02169 895 EAQLREL 901
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-244 |
4.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEqkslkvaetgqvdgELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAK 88
Cdd:PRK03918 226 LEKEVKELEELKEEIEELEKELESLEGSKRKLE--------------EKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 89 AEdENETLRQQMIEVEISKQALQNELERLKEsslKRRSTREMYKEkktfnqddsadlrcqLQFAKEEAFLMRKKMAKLGR 168
Cdd:PRK03918 292 AE-EYIKLSEFYEEYLDELREIEKRLSRLEE---EINGIEERIKE---------------LEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 169 EKDELEQELQKY---KSLYGDVDSpLPTGEAGGPPSTREAELKL---RLKLVEEEANILGRKIVELEVENRGLKAEMEDM 242
Cdd:PRK03918 353 RLEELEERHELYeeaKAKKEELER-LKKRLTGLTPEKLEKELEElekAKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
|
..
gi 2052734496 243 RG 244
Cdd:PRK03918 432 KK 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-918 |
4.68e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 32 ILQYRLRK--AEQKslkvaetgqvdgelIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENEtLRQQMIEVEIS--- 106
Cdd:TIGR02168 167 ISKYKERRkeTERK--------------LERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELAllv 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 107 --KQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLY 184
Cdd:TIGR02168 232 lrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 185 GDVDSPLPTGEAggppstREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEregpgrdhapsiptspf 264
Cdd:TIGR02168 312 ANLERQLEELEA------QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----------------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 265 gdslesstELRRHLQFVEEEAELLRRSISEIEdhnRQLThelskfkfepprepgwlgegaspgagggaPLQEELKSARLQ 344
Cdd:TIGR02168 369 --------ELESRLEELEEQLETLRSKVAQLE---LQIA-----------------------------SLNNEIERLEAR 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 345 ISELSGKVLKLQHENHALLSNIQRCDLAAHlglrapspRDSDAESDAGKKESDGEESRLPQPKregpvggESDSEEMFEK 424
Cdd:TIGR02168 409 LERLEDRRERLQQEIEELLKKLEEAELKEL--------QAELEELEEELEELQEELERLEEAL-------EELREELEEA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 425 TSGFGSGKPSEASepcptelLKAREDSeyLVTLKHEAQRLERTVERLitdtdsFLHDAGLRGGAPLPGPGLQGEEEQ--- 501
Cdd:TIGR02168 474 EQALDAAERELAQ-------LQARLDS--LERLQENLEGFSEGVKAL------LKNQSGLSGILGVLSELISVDEGYeaa 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 502 -----GEGDQQ-----EPQLLGTINAkMKAFKKELQAFLEQVNRIGDGL--SPLPHLTESSSFLSTVTSVSRDSPignlg 569
Cdd:TIGR02168 539 ieaalGGRLQAvvvenLNAAKKAIAF-LKQNELGRVTFLPLDSIKGTEIqgNDREILKNIEGFLGVAKDLVKFDP----- 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 570 kELGPDLQSRLkeqleWQLGPArgderESLR--LRAARELHRRA-----DGD--------TGSHGLGGQTCFSLEMEEEH 634
Cdd:TIGR02168 613 -KLRKALSYLL-----GGVLVV-----DDLDnaLELAKKLRPGYrivtlDGDlvrpggviTGGSAKTNSSILERRREIEE 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 635 LyalrWKELEMhslalqntlhertwsdeknlMQQELRSLKQNIFLFYVKLRWLLKHWRQGKQmeeeGEEFTEGEHPETLS 714
Cdd:TIGR02168 682 L----EEKIEE--------------------LEEKIAELEKALAELRKELEELEEELEQLRK----ELEELSRQISALRK 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 715 RLGELGVQGGHQADGPDHDSDRGCGFPVGEHSPHSRVQIGDHSLRLQTADRGQPHKQVVENQQLFSAFKALLEDFRAELR 794
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 795 EDERARLRLQ---QQYASDKAAWDVEWAVLKCRLEQLEEKTENKLGELGSSAESKGALKKEREVHQKLLADSHSLVMDLR 871
Cdd:TIGR02168 814 LLNEEAANLRerlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 2052734496 872 wqihhseknwnrekvELLDRLDRDRQEWERQKKEFLWRIEQLQKENS 918
Cdd:TIGR02168 894 ---------------SELEELSEELRELESKRSELRRELEELREKLA 925
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
15-191 |
4.85e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNCRILQYRLRKAEQKS------LKVAE-TGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRA 87
Cdd:pfam00261 44 RIQLLEEELERTEERLAEALEKLEEAEKAAdesergRKVLEnRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 88 KAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAFLMRKKMAKLG 167
Cdd:pfam00261 124 VVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLE 203
|
170 180
....*....|....*....|....
gi 2052734496 168 REKDELEQELQKYKSLYGDVDSPL 191
Cdd:pfam00261 204 KEVDRLEDELEAEKEKYKAISEEL 227
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
13-302 |
6.38e-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: 44.34 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 13 VYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQ--VDGELIRSLEQDlkvaKDVSVRLHHELKTVEEKRA--- 87
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRklEEAEKARQAEMD----RQAAIYAEQERMAMEREREler 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 88 -KAED---ENETLRQQMIEVEISKqalQNELERLK--------------ESSLKRRSTREMYKEKKTFNQDDSADLRCQL 149
Cdd:pfam17380 353 iRQEErkrELERIRQEEIAMEISR---MRELERLQmerqqknervrqelEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 150 QFAKEEAflMRKKMAKLGRE-----KDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANILGRK 224
Cdd:pfam17380 430 EEARQRE--VRRLEEERAREmervrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 225 IVELEVENRGLKAEMEDMRG----QQER---EGPGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRsISEIED 297
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKaiyeEERRreaEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ-IVESEK 586
|
....*
gi 2052734496 298 HNRQL 302
Cdd:pfam17380 587 ARAEY 591
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
15-248 |
8.28e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNCRILQYRLRKAEQkslkvaetgqvdgeLIRSLEQDlkvakdvsvrlHHELKTVEEKRAKAEDENE 94
Cdd:pfam05557 126 ELQSTNSELEELQERLDLLKAKASEAEQ--------------LRQNLEKQ-----------QSSLAEAEQRIKELEFEIQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 95 TLRQQMIEVEISKQAL------QNELERLKESSLKRRSTRE---MYKEKKtfnqddsADLRCQLQfaKEEAflMRKKMAK 165
Cdd:pfam05557 181 SQEQDSEIVKNSKSELaripelEKELERLREHNKHLNENIEnklLLKEEV-------EDLKRKLE--REEK--YREEAAT 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 166 LGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPP----STREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMED 241
Cdd:pfam05557 250 LELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED 329
|
....*..
gi 2052734496 242 MRGQQER 248
Cdd:pfam05557 330 LNKKLKR 336
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-182 |
1.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNCRILQYRLRKAEqkslkvAETGQVDGELIRSLEQDLKVAKDvsvRLHHELKTVEEKRAKAEDENE 94
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAELEELRAELA---RLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 95 TLRQQMIEVE-ISKQALQNELERLKESSLKRRSTREMYKE------------KKTFN------QDDSADLRCQLQFAKEE 155
Cdd:COG4913 327 ELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAllaalglplpasAEEFAalraeaAALLEALEEELEALEEA 406
|
170 180
....*....|....*....|....*..
gi 2052734496 156 AFLMRKKMAKLGREKDELEQELQKYKS 182
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
139-368 |
1.70e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 139 QDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeaggppSTREAELKLRLKLVEEEA 218
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-------------ARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 219 NILGRKIVELEVENRGLKAEMEDMRGQQEREgpGRDHAPSIPTSP--FGDSLESSTELRRHLQFVEEEAELLRRSISEIE 296
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRL--GRQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2052734496 297 DHNRQLTHELSKfkfepprepgwLGEGASPGAGGGAPLQEELKSARLQISELSGKVLKLQHENHALLSNIQR 368
Cdd:COG4942 164 ALRAELEAERAE-----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
10-249 |
1.75e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 10 EEDVYQLQELRRELDRANKncrilQYRLRKAEQK----SLKVAETGQVDGELIRSLE----QDLKVAKDVsvRLHHELKT 81
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKK-----ADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEkkkaDELKKAEEL--KKAEEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 82 VEEKRAKAEDENETLR--------------QQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQ---DDSAD 144
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRkaeeakkaeearieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQlkkKEAEE 1645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 145 LRCQLQFAKEEaflmRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAggppSTREAELKLRLKLVEEEANILGRK 224
Cdd:PTZ00121 1646 KKKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA----LKKEAEEAKKAEELKKKEAEEKKK 1717
|
250 260
....*....|....*....|....*
gi 2052734496 225 IVELEVENRGLKAEMEDMRGQQERE 249
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
9-311 |
2.01e-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: 42.70 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVakdvsvrLHHELKTVEEKRAK 88
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL-------LEKEIERLKETIIK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 89 AEDENETLRQQMIEVEI-------SKQALQNELERLKESSLKRRSTREmyKEKKTFNQDDSadlrcQLQFAKEEAFLMRK 161
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELiiknldnTRESLETQLKVLSRSINKIKQNLE--QKQKELKSKEK-----ELKKLNEEKKELEE 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 162 KMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppSTREAELK-----LRLKLVEEEANILGRKIVELEVENRGLK 236
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEKKEKESKI---------SDLEDELNkddfeLKKENLEKEIDEKNKEIEELKQTQKSLK 581
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2052734496 237 A---EMEDMRGQQEREgpgrdhapsiptspfgdslesSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKF 311
Cdd:TIGR04523 582 KkqeEKQELIDQKEKE---------------------KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-471 |
2.29e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAK 88
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 89 AEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQDDSADLRCQLQFAKEEAflmRKKMAKLGR 168
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL---AELLEELAE 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 169 EKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQER 248
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 249 EGPGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSisEIEDHNRQLTHELSKFKFEPPREPGWLGEGASPGA 328
Cdd:COG1196 569 AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 329 GGGAPLQEELKSARLQISELSGKVLKLQHENHALLSNIQRCDLAAHLGLRAPSPRDSDAESDAGKKESDGEESRLPQPKR 408
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2052734496 409 EGPVGGESDSEEMFEktsgfgsgkpSEASEPCPTELLKAREDSEYLVTLKHEAQRLERTVERL 471
Cdd:COG1196 727 EEQLEAEREELLEEL----------LEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1-183 |
2.85e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 1 MEEMRDSYLEEDVYQLQE------LRRELDRANKNCRILQ--------YRLRKAEQKSL-------------KVAETGQV 53
Cdd:COG5022 736 LEDMRDAKLDNIATRIQRairgryLRRRYLQALKRIKKIQviqhgfrlRRLVDYELKWRlfiklqpllsllgSRKEYRSY 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 54 DgELIRSLEQDLKVAKDVSVRLHHELKTVEE-------------KRAKAEDENETLRQQMIEVEISK---QALQNELERL 117
Cdd:COG5022 816 L-ACIIKLQKTIKREKKLRETEEVEFSLKAEvliqkfgrslkakKRFSLLKKETIYLQSAQRVELAErqlQELKIDVKSI 894
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2052734496 118 KESSLKRRSTREMYKEkktFNQDDSADLRCQLQFaKEEAFLMRKKMAKLGREKDELEQELQKYKSL 183
Cdd:COG5022 895 SSLKLVNLELESEIIE---LKKSLSSDLIENLEF-KTELIARLKKLLNNIDLEEGPSIEYVKLPEL 956
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
60-535 |
5.55e-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: 41.57 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 60 SLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVE------ISKQALQNELERLKESSLKRRSTREM--- 130
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdvCGSQDEESDLERLKEEIEKSSKQRAMlag 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 131 --------------------------YKEKKTFNQDdSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLY 184
Cdd:TIGR00606 661 atavysqfitqltdenqsccpvcqrvFQTEAELQEF-ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 185 GDVDSPLP-TGEAGGPPSTREAELKLRLklvEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSP 263
Cdd:TIGR00606 740 DLKEKEIPeLRNKLQKVNRDIQRLKNDI---EEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 264 FGDSLESSTELRrhlQFVEEEAELLRRSISEIEDhNRQLTHELSKfkfepprepgwlgegaspGAGGGAPLQEELKSARL 343
Cdd:TIGR00606 817 GSDLDRTVQQVN---QEKQEKQHELDTVVSKIEL-NRKLIQDQQE------------------QIQHLKSKTNELKSEKL 874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 344 QISELSGKVLKLQHENHALLSNIQRCDLAAHLGLRAPSPRDSDAESDAGKKESDGEESRLPQPKREGPVggeSDSEEMFE 423
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIKEKVK 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 424 KTSGFGSGKPSEASEPCPTELL-KAREDSEYLVTLKHEAQRLERTVERLITDTDSFlhdaglrggaplpgpglqGEEEQG 502
Cdd:TIGR00606 952 NIHGYMKDIENKIQDGKDDYLKqKETELNTVNAQLEECEKHQEKINEDMRLMRQDI------------------DTQKIQ 1013
|
490 500 510
....*....|....*....|....*....|...
gi 2052734496 503 EGDQQEPQLLGTINAKMKAFKKELQAFLEQVNR 535
Cdd:TIGR00606 1014 ERWLQDNLTLRKRENELKEVEEELKQHLKEMGQ 1046
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-124 |
6.97e-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: 41.21 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 16 LQELRRELDRANKNCRILQYRLRKAEQKslkvaetgqvdgelIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENET 95
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEE--------------LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
90 100 110
....*....|....*....|....*....|.
gi 2052734496 96 LRQQMIEVEISKQALQNELERLKE--SSLKR 124
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKelSKLQR 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
74-305 |
7.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 74 RLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQnELERLKESSLKRRSTREMYKEKKTF------NQDDSADLRC 147
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAElerldaSSDDLAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 148 QLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTReAELKLRL------KLVEEEANIL 221
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-ALLEERFaaalgdAVERELRENL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 222 GRKIVELEVENRGLKAEMEDMRGQQEREGPGrdhapsiPTSPFGDSLESSTELRRHLQFVEEE---------AELLRR-S 291
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAFNREWPA-------ETADLDADLESLPEYLALLDRLEEDglpeyeerfKELLNEnS 844
|
250
....*....|....
gi 2052734496 292 ISEIEDHNRQLTHE 305
Cdd:COG4913 845 IEFVADLLSKLRRA 858
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
14-191 |
7.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 14 YQLQELRRELDRANKNCRILQYRLRKAEQKslkvaetgqvdgelIRSLEQDLKVAKDvsvrlhhELKTVEEKRAKAEDEN 93
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDE--------------LAALEARLEAAKT-------ELEDLEKEIKRLELEI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 94 ETLRQ-------QMIEVEISK--QALQNELERLKesslKRRSTRE------MYK-EKKtfnQDDSADLRCQLQFAKEEaf 157
Cdd:COG1579 69 EEVEArikkyeeQLGNVRNNKeyEALQKEIESLK----RRISDLEdeilelMERiEEL---EEELAELEAELAELEAE-- 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 2052734496 158 lMRKKMAKLGREKDELEQELQKYKS----LYGDVDSPL 191
Cdd:COG1579 140 -LEEKKAELDEELAELEAELEELEAereeLAAKIPPEL 176
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
74-241 |
7.61e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 74 RLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEK--KTFNQDDSADLRCQLQF 151
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 152 AKEEAFLMRKKMAKLGREKDELEQELQKYKSLYgdvdsplptgeaggppSTREAELKLRLKLVEEEANILGRKIVELEVE 231
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAEL----------------AELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|
gi 2052734496 232 NRGLKAEMED 241
Cdd:COG1579 165 REELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
15-247 |
8.11e-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: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 15 QLQELRRELDRANKNCRILQYRLRKAEQKSLK-VAETGQVDGElIRSLEQDLKvakdvsvRLHHELKTVEEKRAKAEDEN 93
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKlEAEIDKLLAE-IEELEREIE-------EERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 94 ETLRQQMIEVEISKQALQNELERLKESslKRRSTREMYKEKKTFN--QDDSADLRCQLQFAKEEAFLMRKKMAKLGREKD 171
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREK--LEKLKREINELKRELDrlQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 172 ELEQEL----QKYKSLYGDVDsplptgeaggppSTREAELKLRLKL--VEEEANILGRKIVELEVENRGLKAEMEDMRGQ 245
Cdd:TIGR02169 445 DKALEIkkqeWKLEQLAADLS------------KYEQELYDLKEEYdrVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
..
gi 2052734496 246 QE 247
Cdd:TIGR02169 513 EE 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-297 |
8.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 1 MEEMRDSYLEEdvyqLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLE---------QDLKVAKDV 71
Cdd:PRK03918 298 LSEFYEEYLDE----LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerhelyEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 72 SVRLH------------HELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLK-----------------ESSL 122
Cdd:PRK03918 374 LERLKkrltgltpekleKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteehRKEL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 123 KRRSTREM---YKEKKTFNQDDSaDLRCQLQ-----FAKEEAFLMRKKMAKLGRE---------KDELEQELQKYKSLYG 185
Cdd:PRK03918 454 LEEYTAELkriEKELKEIEEKER-KLRKELRelekvLKKESELIKLKELAEQLKEleeklkkynLEELEKKAEEYEKLKE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 186 DVDsplptgEAGGPPST------REAELKLRLKLVEEEANILGRKIVEL--EVENRGLKAEMEDMRGQQEREgpgrdhap 257
Cdd:PRK03918 533 KLI------KLKGEIKSlkkeleKLEELKKKLAELEKKLDELEEELAELlkELEELGFESVEELEERLKELE-------- 598
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2052734496 258 siptsPFGDSLESSTELRRHLQFVEEEAELLRRSISEIED 297
Cdd:PRK03918 599 -----PFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
16-179 |
8.95e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 38.74 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 16 LQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQ----VD-----------GELIRSLEQDLKVAKDVSVRLHHELK 80
Cdd:pfam13870 1 MRAKRNELSKLRLELITLKHTLAKIQEKLEQKEELGEgltmIDflqlqienqalNEKIEERNKELKRLKLKVTNTVHALT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 81 TVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKEsslkrrsTREMYKekktfnqDDSADLRCQL----------Q 150
Cdd:pfam13870 81 HLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKL-------ERDKLR-------KQNKKLRQQGgllhvpallhD 146
|
170 180 190
....*....|....*....|....*....|.
gi 2052734496 151 FAKEEAFL--MRKKMAKLGREKDELEQELQK 179
Cdd:pfam13870 147 YDKTKAEVeeKRKSVKKLRRKVKILEMRIKE 177
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
31-133 |
9.36e-03 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 38.87 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 31 RILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL-----KVAKDVSVRLHHELKTVEEKRAKAED---ENETLRQQMIE 102
Cdd:pfam15035 24 KVLQYKKRCSELEQQLLEKTSELEKTELLLRKLTLeprlqRLEREHSADLEEALIRLEEERQRSESlsqVNSLLREQLEQ 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2052734496 103 VEISKQALQNELERL-------------KESSLKRRstREMYKE 133
Cdd:pfam15035 104 ASRANEALREDLQKLtndwerareeleqKESEWRKE--EEAFNE 145
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
7-184 |
9.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 7 SYLEEdvyQLQELRRELDRANKncRILQYRlrkAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKR 86
Cdd:COG3206 178 EFLEE---QLPELRKELEEAEA--ALEEFR---QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 87 AKAEDEN---------ETLRQQMIEVEISK--------------QALQNELERLKESSLKR-RSTREMYKEKKTFNQDDS 142
Cdd:COG3206 250 GSGPDALpellqspviQQLRAQLAELEAELaelsarytpnhpdvIALRAQIAALRAQLQQEaQRILASLEAELEALQARE 329
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2052734496 143 ADLRCQLQFAKEEAflmrKKMAKLGREKDELEQELQKYKSLY 184
Cdd:COG3206 330 ASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELY 367
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
38-296 |
9.46e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 38 RKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERL 117
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 118 KEsSLKRRstremykekktfnQDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeag 197
Cdd:COG4372 86 NE-QLQAA-------------QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052734496 198 gppSTREAELK-LRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLESSTELRR 276
Cdd:COG4372 146 ---AEREEELKeLEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260
....*....|....*....|
gi 2052734496 277 HLQFVEEEAELLRRSISEIE 296
Cdd:COG4372 223 AKDSLEAKLGLALSALLDAL 242
|
|
| |
