|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
1024-1147 |
7.08e-51 |
|
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: 176.03 E-value: 7.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 1024 MDLRWQIHHSEKNWNREKVELLDRLDRDRQEWERQKKEFLWRIEQLQKENSPRR------------GGSFLCDQKDGNVR 1091
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRRkinmnerakvidGEKFVPDQKESSSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603757 1092 PFPHQGSLRMPR--PVAMWPCADADSIPFEDRPLSKLKESDRCSASENLYLDALSLDD 1147
Cdd:pfam14818 81 PFPDSGQCEFPRmnHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
218-312 |
3.57e-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: 135.50 E-value: 3.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 218 DSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANI 297
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1034603757 298 LGRKIVELEVENRGL 312
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
347-439 |
1.16e-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: 133.96 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 347 SSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPPREPGWLGEGASPGA--GGGAPLQEELKSARLQISE 424
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSdsSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1034603757 425 LSGKVLKLQHENHAL 439
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-373 |
1.04e-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: 70.47 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 44 ELDELRAEMEEMRDSYLEEDVyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKvakdvs 123
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA------ 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 124 vRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKE--SSLKRR--STREMYKEKKTFNQQNGgmERPG 199
Cdd:TIGR02168 751 -QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelKALREAldELRAELTLLNEEAANLR--ERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 200 NCRPATKTQRKLAPRRKDDSADLRCQLQFAKEEaflmrkkMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppst 279
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAE-------IEELEELIEELESELEALLNERASLEEAL----------- 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 280 reAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLEsstELRRHLQFVE 359
Cdd:TIGR02168 890 --ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIE 964
|
330
....*....|....
gi 1034603757 360 EEAELLRRSISEIE 373
Cdd:TIGR02168 965 DDEEEARRRLKRLE 978
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-259 |
4.15e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEMRDSY--LEedvyQLQELRRELDRANKNCRILQYRLRKAEqkslkvAETGQVDGELIRSLEQDLKVAK 120
Cdd:COG4913 235 DDLERAHEALEDAREQIelLE----PIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 121 DvsvRLHHELKTVEEKRAKAEDENETLRQQMIEVE-ISKQALQNELERLKESSLKRRSTREMYKEKktfnQQNGGMERPG 199
Cdd:COG4913 305 A---RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL----LAALGLPLPA 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 200 NcRPATKTQRKLAPRRKDDSADLRCQLQfakEEAFLMRKKMAKLGREKDELEQELQKYKS 259
Cdd:COG4913 378 S-AEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-433 |
4.67e-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: 58.53 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 109 IRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSlkRRSTREMYKEKKTF 188
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV--EQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 189 NQQNGgmERPGNCRPATKTQRKLApRRKDDSADLRCQLQFAKEEaflmrkkMAKLGREKDELEQELQKYKSLYGDVdspl 268
Cdd:TIGR02168 757 TELEA--EIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEE-------LKALREALDELRAELTLLNEEAANL---- 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 269 ptgeaggppSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHApsiptspfgdsLESS 348
Cdd:TIGR02168 823 ---------RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-----------LNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 349 TELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKfkfepprepgwlgegaspgagggapLQEELKSARLQISELSGK 428
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEE-------------------------LREKLAQLELRLEGLEVR 937
|
....*
gi 1034603757 429 VLKLQ 433
Cdd:TIGR02168 938 IDNLQ 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-259 |
9.49e-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: 57.37 E-value: 9.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 44 ELDELRAEMEEMRDSY--LEEDVY-----------QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIR 110
Cdd:TIGR02168 268 KLEELRLEVSELEEEIeeLQKELYalaneisrleqQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 111 SLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKE--SSLKRRSTRemykekktf 188
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEArlERLEDRRER--------- 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034603757 189 NQQNGGMERPGNCRPATKTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKS 259
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
34-425 |
2.06e-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: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 34 RVEGAAPFSDELDELRAEMEEMR------DSYLEEDVYQLQELRRELDRANKNcRILQYRLRKAEQ----KSLKVAETG- 102
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEenierlDLIIDEKRQQLERLRREREKAERY-QALLKEKREYEGyellKEKEALERQk 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 103 -QVDGElIRSLEQDLkvaKDVSVRLHHELKTVEEKRAKAEDENEtlrqqmievEISKQAlQNELERLKESSLKRRSTREM 181
Cdd:TIGR02169 240 eAIERQ-LASLEEEL---EKLTEEISELEKRLEEIEQLLEELNK---------KIKDLG-EEEQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 182 YKEKKTFNQQNggmerpgncrpatktQRKLAPRRKDDSADLRCQlqfaKEEAFLMRKKMAKLGREKDELEQELQKYKSLY 261
Cdd:TIGR02169 306 LERSIAEKERE---------------LEDAEERLAKLEAEIDKL----LAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 262 GDVDSPLptgeagGPPSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMedmrgqQEREGPGRDHAPSIPtspf 341
Cdd:TIGR02169 367 EDLRAEL------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL------QRLSEELADLNAAIA---- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 342 gDSLESSTELrrhlqfvEEEAELLRRSISEIEDHNRQLTHELSKFKFEpprepgwlgegASPGAGGGAPLQEELKSARLQ 421
Cdd:TIGR02169 431 -GIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAADLSKYEQE-----------LYDLKEEYDRVEKELSKLQRE 491
|
....
gi 1034603757 422 ISEL 425
Cdd:TIGR02169 492 LAEA 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-435 |
4.75e-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: 55.07 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 134 EEKRAKAEDENETLRQQMIEVEISKQALQNELERLKesslKRRSTREMYKEKKTFNQQNGGMERPGNCRPATKTQRKLAP 213
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR----REREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 214 RRkddsADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSlygdvDSPLPTGEAGGPPSTREAELKLRLKLVEE 293
Cdd:TIGR02169 245 QL----ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE-----EEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 294 EANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHApsipTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIE 373
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034603757 374 DHNRQLTHELSKFKFEPPRepgwLGEGASPGAGGGAPLQEELKSARLQISELSGKVLKLQHE 435
Cdd:TIGR02169 392 EKLEKLKREINELKRELDR----LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
61-389 |
1.19e-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: 53.91 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 61 EEDVYQLQELRRELDRANKNCRI-----LQYRLRKAEQKSLKVAETGQVDGELIRSLEQdLKVAKDVSVRLHHELktvEE 135
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERqaekaERYKELKAELRELELALLVLRLEELREELEE-LQEELKEAEEELEEL---TA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 136 KRAKAEDENETLRQQMIEVEISKQALQNELERLKE--SSLKRRstREMYKEKKTFNQQNggmerpgncRPATKTQRKLAP 213
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQ--KQILRERLANLERQ---------LEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 214 RRKD----DSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeaggppSTREAELKLRLK 289
Cdd:TIGR02168 330 SKLDelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL-------------RSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 290 LVEEEANILGRKIVELEVENRGLKAEMEDMRGQQERegpgrdHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSI 369
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE------AELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340
....*....|....*....|
gi 1034603757 370 SEIEDHNRQLTHELSKFKFE 389
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQAR 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-387 |
1.20e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 42 SDELDELRAEMEEMRDSY--LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQdLKVA 119
Cdd:PRK03918 213 SSELPELREELEKLEKEVkeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 120 KDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQ-NGGMERP 198
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 199 GNCRpatKTQRKLAPRRKDDSADLRCQLQFAKEEaflMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPS 278
Cdd:PRK03918 372 EELE---RLKKRLTGLTPEKLEKELEELEKAKEE---IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 279 TREAELKLRLKLVEEEANILGRKIvELEVENRGLKAEMEDMRGQQEREgpgRDHAPSIPTSPFGDSLESSTEL--RRHLQ 356
Cdd:PRK03918 446 TEEHRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRELEKVLKKE---SELIKLKELAEQLKELEEKLKKynLEELE 521
|
330 340 350
....*....|....*....|....*....|.
gi 1034603757 357 FVEEEAELLRRSISEIEDHNRQLTHELSKFK 387
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-326 |
1.54e-06 |
|
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: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 42 SDELDELRAEMEEMRDSYLEEdvyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKD 121
Cdd:COG1196 219 KEELKELEAELLLLKLRELEA---ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 122 VSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQNggmerpgnc 201
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA--------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 202 rpATKTQRKLAPRRKDDSADLRcQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLpTGEAGGPPSTRE 281
Cdd:COG1196 367 --LLEAEAELAEAEEELEELAE-ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL-AELEEEEEEEEE 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034603757 282 AELKLRLKLVEEEANILG--RKIVELEVENRGLKAEMEDMRGQQERE 326
Cdd:COG1196 443 ALEEAAEEEAELEEEEEAllELLAELLEEAALLEAALAELLEELAEA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-378 |
5.88e-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: 51.61 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 28 SWAPTSRVEGAAPFSDELDELRAEMEEMRD--SYLEEDVYQLQ----ELRRELDRANKNCRILQYRLRKAEQKSLKVAET 101
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRelSSLQSELRRIEnrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 102 GQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETL-----RQQMIEVEISKQALQNELERLK------E 170
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEarlreiE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 171 SSLKRRSTREMYKEKKTFNQQNGgmerpgncRPATKTQRKLAPRRKDDS------------------ADLRCQLQFAKEE 232
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQ--------RIDLKEQIKSIEKEIENLngkkeeleeeleeleaalRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 233 AFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptGEAGGPPSTREAELKLRLKLVEEEANI--LGRKIVELEVENR 310
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEIPEEELSLedVQAELQRVEEEIR 968
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603757 311 GLkaEMEDMRGQQEREgpgrdhapsiptspfgDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQ 378
Cdd:TIGR02169 969 AL--EPVNMLAIQEYE----------------EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-194 |
6.90e-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: 51.22 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 39 APFSDELDELRAEMEEMRDSYLEEDVyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKV 118
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034603757 119 AKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERL-KESSLKRRSTREMYKEKKTFNQQNGG 194
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVRG 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-387 |
8.24e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 34 RVEGAAPFSDELDELRAEMEEMRDSYLEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKslkVAETGQVDGELIRSLE 113
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR---IGELKKEIKELKKAIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 114 QdLKVAK----------------DVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEiSKQALQNELERLK-------- 169
Cdd:PRK03918 430 E-LKKAKgkcpvcgrelteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELE-KVLKKESELIKLKelaeqlke 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 170 -ESSLKRRSTREMYKEKKTF---NQQNGGMErpGNCRPATKTQRKLAPRRKdDSADLRCQLQFAKEEAFLMRKKMAKLGR 245
Cdd:PRK03918 508 lEEKLKKYNLEELEKKAEEYeklKEKLIKLK--GEIKSLKKELEKLEELKK-KLAELEKKLDELEEELAELLKELEELGF 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 246 EK-DELEQELQKYKSLYGDVDsplptgEAGGPPSTREAELKlRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQE 324
Cdd:PRK03918 585 ESvEELEERLKELEPFYNEYL------ELKDAEKELEREEK-ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS 657
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034603757 325 REgpgrdhapsiptsPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFK 387
Cdd:PRK03918 658 EE-------------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
33-385 |
1.11e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 33 SRVEGAAPFSDELDELRAEMEEMRDSYLEEDVYQLQELRRELDRANKNCRILQYRLRKAEQK-SLKVAETGQVDGELiRS 111
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEElEQARSELEQLEEEL-EE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 112 LEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQ 191
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 192 N-GGMERPGNCRPATKTQRKLAPRRKddsaDLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPT 270
Cdd:COG4372 165 ElAALEQELQALSEAEAEQALDELLK----EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 271 GEAGGPPST---REAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLES 347
Cdd:COG4372 241 ALELEEDKEellEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034603757 348 STELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSK 385
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-258 |
1.50e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 49 RAEMEEMRDSYLEEDVYQLQELRREldranKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHH 128
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 129 ELKTVEEKRAKAEdenETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKE---KKTFNQQNGGMERPGncRPAT 205
Cdd:PTZ00121 1666 EAKKAEEDKKKAE---EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEENKIKAEEAK--KEAE 1740
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034603757 206 KTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYK 258
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
43-612 |
2.30e-05 |
|
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: 49.66 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEMRD-SYLEEDVYQLQELRRelDRANKNCRILQYRLRKAEQKSLKVAE---TGQVDgELIRSLEQDLKV 118
Cdd:TIGR00606 512 DLDRKLRKLDQEMEQlNHHTTTRTQMEMLTK--DKMDKDEQIRKIKSRHSDELTSLLGYfpnKKQLE-DWLHSKSKEINQ 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 119 AKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVE------ISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQ- 191
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdvCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQf 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 192 -NGGMERPGNCRPATKTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLP- 269
Cdd:TIGR00606 669 iTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPe 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 270 TGEAGGPPSTREAELKLRLklvEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLESST 349
Cdd:TIGR00606 749 LRNKLQKVNRDIQRLKNDI---EEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQ 825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 350 ELRrhlQFVEEEAELLRRSISEIEDhNRQLTHELSKfkfepprepgwlgegaspGAGGGAPLQEELKSARLQISELSGKV 429
Cdd:TIGR00606 826 QVN---QEKQEKQHELDTVVSKIEL-NRKLIQDQQE------------------QIQHLKSKTNELKSEKLQIGTNLQRR 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 430 LKLQHENHALLSNIQRCDLAAHLGLRAPSPRDSDAESDAGKKESDGEESRLPQPKREGPVggeSDSEEMFEKTSGFGSGK 509
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIKEKVKNIHGYMKDI 960
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 510 PSEASEPCPTELL-KAREDSEYLVTLKHEAQRLERTVERLITDTDSFlhdaglrggaplpgpglqGEEEQGEGDQQEPQL 588
Cdd:TIGR00606 961 ENKIQDGKDDYLKqKETELNTVNAQLEECEKHQEKINEDMRLMRQDI------------------DTQKIQERWLQDNLT 1022
|
570 580
....*....|....*....|....
gi 1034603757 589 LGTINAKMKAFKKELQAFLEQVNR 612
Cdd:TIGR00606 1023 LRKRENELKEVEEELKQHLKEMGQ 1046
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-326 |
2.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 46 DELRAEMEEMRDSylEEDVYQLQELRRELDRANKNCRILQY--RLRKAEQK----SLKVAETGQVDGELIRSLE----QD 115
Cdd:PTZ00121 1473 DEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAkkadEAKKAEEAKKADEAKKAEEkkkaDE 1550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 116 LKVAKDVsvRLHHELKTVEEKRAKAEDENETLRQqmieVEISKQAlqnELERLKESSLKRRSTREMYKEKktFNQQNGGM 195
Cdd:PTZ00121 1551 LKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRK----AEEAKKA---EEARIEEVMKLYEEEKKMKAEE--AKKAEEAK 1619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 196 ERPGNCRPATKTQRKLAPRRKDDSADLRCQLQFAKEEaflmRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAgg 275
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-- 1693
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1034603757 276 ppSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQERE 326
Cdd:PTZ00121 1694 --LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-176 |
3.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEMRDSYLEEDVYQLQELRRELDRANKncrilqyRLRKAEQKSLKVAetgqvdgELIRSLEQDLKVAKDV 122
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLE-------ALLAALGLPLPASAEE 381
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034603757 123 SVRLHHELKtveEKRAKAEDENETLRQQMIEVEISKQALQNELERLKE--SSLKRR 176
Cdd:COG4913 382 FAALRAEAA---ALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
38-308 |
8.31e-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: 47.07 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 38 AAPFSDELDELRAEMEEMRDsyleedvyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLK 117
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQ--------EIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 118 VAKDvsvrlhhELKTVEEKRAKAEDENETLRQQMIEV--EISKQALQNELERLkessLKRRSTREMYKEKKTFNQQNggm 195
Cdd:COG4942 80 ALEA-------ELAELEKEIAELRAELEAQKEELAELlrALYRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLA--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 196 erpgncrPATKTQRKLAPRRKDDSADLRCQLQFAKEEaflMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeagg 275
Cdd:COG4942 146 -------PARREQAEELRADLAELAALRAELEAERAE---LEALLAELEEERAALEALKAERQKLLARL----------- 204
|
250 260 270
....*....|....*....|....*....|...
gi 1034603757 276 ppSTREAELKLRLKLVEEEANILGRKIVELEVE 308
Cdd:COG4942 205 --EKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
43-379 |
8.34e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEMRDSY--LEEDVYQLQELRRELDRA---NKNCRILQYRLRKAEQKSLKVAETGQVDGEL--------- 108
Cdd:COG4717 71 KELKELEEELKEAEEKEeeYAELQEELEELEEELEELeaeLEELREELEKLEKLLQLLPLYQELEALEAELaelperlee 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 109 --------------IRSLEQDLKVAK--------DVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELE 166
Cdd:COG4717 151 leerleelreleeeLEELEAELAELQeeleelleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 167 RLKESSLKRRSTREMYKEKKTFNQQNGGMERPGNCRPATKTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGR- 245
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQAl 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 246 -EKDELEQ-ELQKYKSLYGdVDSPLPTGEAGGPPST-----------REAELKLRLKLVEEEANILG-----------RK 301
Cdd:COG4717 311 pALEELEEeELEELLAALG-LPPDLSPEELLELLDRieelqellreaEELEEELQLEELEQEIAALLaeagvedeeelRA 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034603757 302 IVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTspfGDSLES-STELRRHLQFVEEEAELLRRSISEIEDHNRQL 379
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALD---EEELEEeLEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
64-379 |
9.17e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.43 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 64 VYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQ--VDGELIRSLEQDlkvaKDVSVRLHHELKTVEEKRA--- 138
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRklEEAEKARQAEMD----RQAAIYAEQERMAMEREREler 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 139 -KAED---ENETLRQQMIEVEISK----QALQNEL----ERLKESSLKRRSTREMYKEK-KTFNQQNGGME--RPGNCRP 203
Cdd:pfam17380 353 iRQEErkrELERIRQEEIAMEISRmrelERLQMERqqknERVRQELEAARKVKILEEERqRKIQQQKVEMEqiRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 204 ATKTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppstrEAE 283
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL------------EKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 284 LKLRLKLVEEEANilGRKIVELEVENRGLKAEMEDMRGQQEREgpGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAE 363
Cdd:pfam17380 501 LEERKQAMIEEER--KRKLLEKEMEERQKAIYEEERRREAEEE--RRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
330
....*....|....*.
gi 1034603757 364 LLRRsISEIEDHNRQL 379
Cdd:pfam17380 577 MMRQ-IVESEKARAEY 591
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-276 |
9.94e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 45 LDELRAEMEEmrdsyLEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGElIRSLEQDLKVAKDVSV 124
Cdd:COG4913 612 LAALEAELAE-----LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE-IAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 125 rlhhELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKEsslkrrstremykEKKTFNQQNGGMERPGNCRPA 204
Cdd:COG4913 686 ----DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE-------------ELDELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034603757 205 TKTQRKLA-----PRRKDDSADLRCQLQFAKeeaflmrkkmAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGP 276
Cdd:COG4913 749 ALLEERFAaalgdAVERELRENLEERIDALR----------ARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
66-256 |
1.20e-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: 47.05 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 66 QLQELRRELDRANKNcriLQYRLRKAEQKSLKVAETGQVD----GELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAE 141
Cdd:pfam07111 482 ELEQLREERNRLDAE---LQLSAHLIQQEVGRAREQGEAErqqlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQEST 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 142 DENETLRQQMI-EVEISKQALQN---ELE-RLKE--SSLKRR---STREMYKEKKTFNQqnggmerpgncrpatkTQRKl 211
Cdd:pfam07111 559 EEAASLRQELTqQQEIYGQALQEkvaEVEtRLREqlSDTKRRlneARREQAKAVVSLRQ----------------IQHR- 621
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034603757 212 APRRKDDSADL-RCQLQFAKEEAFLMRKKMAKLGREKDELEQELQK 256
Cdd:pfam07111 622 ATQEKERNQELrRLQDEARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
41-336 |
1.79e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 41 FSDELDELR---AEMEEMRDSYLEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLk 117
Cdd:TIGR00606 243 YENELDPLKnrlKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 118 vakdvsVRLHHELKtveekraKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNqqngGMER 197
Cdd:TIGR00606 322 ------VDCQRELE-------KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD----GFER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 198 PGNCRPATKTQRKLAPRRKDDSA--------DLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLP 269
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAktaaqlcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603757 270 TGEaGGPPSTREAELKLR-----LKLVEEEANILGRKIVELEVEN------RGLKAEMEDMRgQQEREGPGRDHAPSI 336
Cdd:TIGR00606 465 QLE-GSSDRILELDQELRkaereLSKAEKNSLTETLKKEVKSLQNekadldRKLRKLDQEME-QLNHHTTTRTQMEML 540
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
49-336 |
1.83e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 49 RAEME-EMRDSYLEedvyqLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQvdgELIRSLeQDLKVAKDvsvRLH 127
Cdd:pfam15921 592 KAQLEkEINDRRLE-----LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS---ERLRAV-KDIKQERD---QLL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 128 HELKTVEEKRAKAEDENETL----RQQMIEVEISKQALQNELerlkesslkRRSTREMYKEKKTFNQQNGGmerPGNC-R 202
Cdd:pfam15921 660 NEVKTSRNELNSLSEDYEVLkrnfRNKSEEMETTTNKLKMQL---------KSAQSELEQTRNTLKSMEGS---DGHAmK 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 203 PATKTQRKLAPRRKDDSAdLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeAGGPPSTREA 282
Cdd:pfam15921 728 VAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM--------AGELEVLRSQ 798
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034603757 283 ELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQ-------QEREGPGRDHAPSI 336
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKlqhtldvKELQGPGYTSNSSM 859
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
67-387 |
3.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 67 LQELRRELDRankncrilqyrlRKAEQKSLkVAETGQVDgELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENET 146
Cdd:PRK03918 167 LGEVIKEIKR------------RIERLEKF-IKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 147 L---RQQMIEVEISKQALQNELERLKEsslKRRSTREMYKEKKtfnqqnggmerpgncrpatKTQRKLAPRRKDDSadlr 223
Cdd:PRK03918 233 LeelKEEIEELEKELESLEGSKRKLEE---KIRELEERIEELK-------------------KEIEELEEKVKELK---- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 224 cQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAggpPSTREAELKLRLKLVEEEANILGRKIV 303
Cdd:PRK03918 287 -ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE---KEERLEELKKKLKELEKRLEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 304 ELEVenrgLKAEMEDMRGQQEREGPgrdhapsiptspfgdslESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHEL 383
Cdd:PRK03918 363 LYEE----AKAKKEELERLKKRLTG-----------------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
....
gi 1034603757 384 SKFK 387
Cdd:PRK03918 422 KELK 425
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
42-442 |
7.09e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 42 SDELDELRAEMEEMRD------SYLEEDVYQLQELRRELDRANKNCRILQYRLR--KAEQKSLKvaetGQVDGELIRSLE 113
Cdd:TIGR04523 238 QQEINEKTTEISNTQTqlnqlkDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN----NQKEQDWNKELK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 114 QDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERlKESSLKRrstreMYKEKKTFNQQNg 193
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE-KQNEIEK-----LKKENQSYKQEI- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 194 gmerpgncrpatktqRKLaprrKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEa 273
Cdd:TIGR04523 387 ---------------KNL----ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 274 ggppsTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMrgQQEREGPGRDHapSIPTSPFGDSLESSTELRR 353
Cdd:TIGR04523 447 -----NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK--QKELKSKEKEL--KKLNEEKKELEEKVKDLTK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 354 HLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFepprepgwlgegaspgagggaplqeELKSARL--QISELSGKVLK 431
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDF-------------------------ELKKENLekEIDEKNKEIEE 572
|
410
....*....|.
gi 1034603757 432 LQHENHALLSN 442
Cdd:TIGR04523 573 LKQTQKSLKKK 583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
41-190 |
1.06e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 41 FSDELDELRAEMEEMRDSYLEEDVyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVA- 119
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEE-QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAe 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034603757 120 -KDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQ 190
Cdd:TIGR02168 435 lKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
44-185 |
1.31e-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: 42.22 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 44 ELDELRAEMEEMRDSYLEEDVyQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDG---ElIRSLEQDLKVAK 120
Cdd:COG1579 32 ELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqkE-IESLKRRISDLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034603757 121 DVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVeisKQALQNELERLKESSLKRRSTREMYKEK 185
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELEELEAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
42-324 |
1.32e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 42 SDELDELRAEMEEMRDSYLEEDVYQLQELRRELDRANKNCRILQYRLRKAEQK------SLKVAETGQVDGELIRSLEQD 115
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEleeleeELEQLENELEAAALEERLKEA 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 116 LKVAKDVSVRLHHE----------------------------LKTVEEKRAKAEDENETLRQQMIEvEISKQALQNELER 167
Cdd:COG4717 249 RLLLLIAAALLALLglggsllsliltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALE-ELEEEELEELLAA 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 168 LK-ESSLKRRSTREMYKEKKTFNQQNGGMERpgncrpaTKTQRKLAPRRKDDSADLRcQLQFAKEEAFLMRkkmAKLGRE 246
Cdd:COG4717 328 LGlPPDLSPEELLELLDRIEELQELLREAEE-------LEEELQLEELEQEIAALLA-EAGVEDEEELRAA---LEQAEE 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603757 247 KDELEQELQKYKSLYGDVDSPLPTGEAGGPpstrEAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQE 324
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALD----EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
44-191 |
1.51e-03 |
|
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: 43.57 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 44 ELDELRAEMEEMRdsylEEDVYQLQELR-RELDRankncrilqyrLRKAEQKSlkvaetgQVDGELIRSLEQDLKVAKDV 122
Cdd:pfam17380 421 EMEQIRAEQEEAR----QREVRRLEEERaREMER-----------VRLEEQER-------QQQVERLRQQEEERKRKKLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 123 SVRLHHELKTVEEKRAKA-EDENETLRQQMIEVEISKQALQNELE----------RLKESSLKRRSTREMyKEKKTFNQQ 191
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEerqkaiyeeeRRREAEEERRKQQEM-EERRRIQEQ 557
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
43-387 |
1.71e-03 |
|
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: 43.19 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEmRDSYLEEDVYQLQELRRELDRANKNCRILQYRLR--KAEQKSLKVAEtgQVDGELIRSL---EQDLK 117
Cdd:pfam05557 111 NELSELRRQIQR-AELELQSTNSELEELQERLDLLKAKASEAEQLRQnlEKQQSSLAEAE--QRIKELEFEIqsqEQDSE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 118 VAKDVSV-------------RLHHELK--------------TVEEKRAKAEDEnETLRQQMIEVEISKQALQNEL---ER 167
Cdd:pfam05557 188 IVKNSKSelaripelekeleRLREHNKhlnenienklllkeEVEDLKRKLERE-EKYREEAATLELEKEKLEQELqswVK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 168 LKESS--------LKRRSTREMYKEKKTFNQQNGGMERpgNCRPATKTQRKLAPRRKDDSA---DLRCQLQFAKEEAFLM 236
Cdd:pfam05557 267 LAQDTglnlrspeDLSRRIEQLQQREIVLKEENSSLTS--SARQLEKARRELEQELAQYLKkieDLNKKLKRHKALVRRL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 237 RKKMAKLGREKDELEQELQKYkslygdvDSPLPTGEAGGPPSTREAEL-------KLRLKLVEEEANILGRKIVELEVEN 309
Cdd:pfam05557 345 QRRVLLLTKERDGYRAILESY-------DKELTMSNYSPQLLERIEEAedmtqkmQAHNEEMEAQLSVAEEELGGYKQQA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 310 RGLKAEMEDMRGQQEREGPGRdhapsiptspfgdSLESSTELRRHLQFVEEEAELLRRSI----SEIEDHNRQLTHELSK 385
Cdd:pfam05557 418 QTLERELQALRQQESLADPSY-------------SKEEVDSLRRKLETLELERQRLREQKneleMELERRCLQGDYDPKK 484
|
..
gi 1034603757 386 FK 387
Cdd:pfam05557 485 TK 486
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
26-320 |
3.13e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.31 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 26 RVSWAPTSRVEGAAPFSDELDELRAEMEEMRDSYLEEdvyQLQELRRELDRA---------NKNCRILQ---YRLRKAEQ 93
Cdd:NF033838 33 GVVHAEEVRGGNNPTVTSSGNESQKEHAKEVESHLEK---ILSEIQKSLDKRkhtqnvalnKKLSDIKTeylYELNVLKE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 94 KSlKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENE-------TLRQQMIEVEISKQAL---QN 163
Cdd:NF033838 110 KS-EAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEedrrnypTNTYKTLELEIAESDVevkKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 164 ELERLKESSLKRRSTREMYKEKKTFNQQNGGMERPGNcrpaTKTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAkl 243
Cdd:NF033838 189 ELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEK----IKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPK-- 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034603757 244 GREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTreaELKLRLKLVEEEanilgrKIVElEVENRGLKAEMEDMR 320
Cdd:NF033838 263 RRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSP---SLKPEKKVAEAE------KKVE-EAKKKAKDQKEEDRR 329
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-548 |
3.51e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEMRDSY---------LEEDVY----QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELI 109
Cdd:COG1196 274 LELEELELELEEAQAEEyellaelarLEQDIArleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 110 RSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFN 189
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 190 QQNGGMERpgncRPATKTQRKLApRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLY----GDVD 265
Cdd:COG1196 434 EEEEEEEE----EALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadyeGFLE 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 266 SPLPTGEAGGPPSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSL 345
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAAL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 346 ESSTELRRHLQFVEEEAELLRRSisEIEDHNRQLTHELSKFKFEPPREPGWLGEGASPGAGGGAPLQEELKSARLQISEL 425
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREA--DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 426 SGKVLKLQHENHALLSNIQRCDLAAHLGLRAPSPRDSDAESDAGKKESDGEESRLPQPKREGPVGGESDSEEMFEktsgf 505
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL----- 741
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1034603757 506 gsgkpSEASEPCPTELLKAREDSEYLVTLKHEAQRLERTVERL 548
Cdd:COG1196 742 -----LEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-377 |
4.01e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 45 LDELRAEMEEMRDSYLEEDV----YQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGqvdgELIRSLEQdlkvak 120
Cdd:PRK02224 189 LDQLKAQIEEKEEKDLHERLngleSELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----EELETLEA------ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 121 dvsvrlhhELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNEL-ERLKESSLKRRSTREMYKEKKTFNQQNGGMERP- 198
Cdd:PRK02224 259 --------EIEDLRETIAETEREREELAEEVRDLRERLEELEEERdDLLAEAGLDDADAEAVEARREELEDRDEELRDRl 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 199 GNCRPATKTQRKLAPRRKDDSADLRCQLQFAKEEAflmrkkmAKLGREKDELEQELQKYKSLYGDVDSPLPTGEA--GGP 276
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEA-------AELESELEEAREAVEDRREEIEELEEEIEELRErfGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 277 PSTREaELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQErEGPGRDHAPSIPTSPFGDSLESSTELRRHLq 356
Cdd:PRK02224 404 PVDLG-NAEDFLEELREERDELREREAELEATLRTARERVEEAEALLE-AGKCPECGQPVEGSPHVETIEEDRERVEEL- 480
|
330 340
....*....|....*....|..
gi 1034603757 357 fvEEEAELLRRSISEIED-HNR 377
Cdd:PRK02224 481 --EAELEDLEEEVEEVEErLER 500
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
41-261 |
4.40e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 41 FSDELDELRAEMEEMRDSYLEEdvyQLQELRRELDRANKncRILQYRlrkAEQKSLKVAETGQVDGELIRSLEQDLKVAK 120
Cdd:COG3206 161 YLEQNLELRREEARKALEFLEE---QLPELRKELEEAEA--ALEEFR---QKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 121 DVSVRLHHELKTVEEKRAKAEDEN---------ETLRQQMIEVEiskQALQNELERLKESSLKRRSTREMYKEKKTFNQQ 191
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALpellqspviQQLRAQLAELE---AELAELSARYTPNHPDVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 192 nggmeRPGNCRPATKTQRKLAPRRKddsADLRCQLQFAKEEAflmrKKMAKLGREKDELEQELQKYKSLY 261
Cdd:COG3206 310 -----EAQRILASLEAELEALQARE---ASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELY 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-445 |
5.05e-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: 41.29 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 217 DDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYkslygdvdsplptgeaggppSTREAELKLRLKLVEEEAN 296
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------------------ERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 297 ILGRKIVELEVENRGLKAEMEDMRGQQER-----EGPGRDHAPSIPTSP--FGDSLESSTELRRHLQFVEEEAELLRRSI 369
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAEllralYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034603757 370 SEIEDHNRQLTHELSKfkfepprepgwLGEGASPGAGGGAPLQEELKSARLQISELSGKVLKLQHENHALLSNIQR 445
Cdd:COG4942 160 AELAALRAELEAERAE-----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
43-170 |
5.25e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEMRDSYL--EEDVYQLQELRRELDRANKNCRILQYRLRKAEQ-------------KSLKVAETGQVDG- 106
Cdd:pfam06160 305 EQNKELKEELERVQQSYTlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVayselqeeleeilEQLEEIEEEQEEFk 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 107 ELIRSLEQDLKVAKDVSVRLHHELKTVE---EKR-------------AKAEDENETLRQQMIEV-----EISKQAL--QN 163
Cdd:pfam06160 385 ESLQSLRKDELEAREKLDEFKLELREIKrlvEKSnlpglpesyldyfFDVSDEIEDLADELNEVplnmdEVNRLLDeaQD 464
|
....*..
gi 1034603757 164 ELERLKE 170
Cdd:pfam06160 465 DVDTLYE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-385 |
5.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 43 DELDELRAEMEEMRDSyLEEDV-----YQlqELRRELDRANKNCRILQYRLRKAEQKSLKvaetgqvdgELIRSLEQDLK 117
Cdd:COG1196 189 ERLEDILGELERQLEP-LERQAekaerYR--ELKEELKELEAELLLLKLRELEAELEELE---------AELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 118 VAKdvsvrlhhelKTVEEKRAKAedenETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQNggMER 197
Cdd:COG1196 257 ELE----------AELAELEAEL----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER--LEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 198 pgncrpATKTQRKLAPRRKDDSAdlrcQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDsplptgeaggpp 277
Cdd:COG1196 321 ------LEEELAELEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------------ 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 278 STREAELKLRLKLVEEEANILgRKIVELEVENRGLKAEMEDMRGQQEREGpgrdhapsiptspfGDSLESSTELRRHLQF 357
Cdd:COG1196 379 EELEELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELE--------------EALAELEEEEEEEEEA 443
|
330 340
....*....|....*....|....*...
gi 1034603757 358 VEEEAELLRRSISEIEDHNRQLTHELSK 385
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
67-170 |
7.18e-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: 39.51 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 67 LQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQ----VD-----------GELIRSLEQDLKVAKDVSVRLHHELK 131
Cdd:pfam13870 1 MRAKRNELSKLRLELITLKHTLAKIQEKLEQKEELGEgltmIDflqlqienqalNEKIEERNKELKRLKLKVTNTVHALT 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1034603757 132 TVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKE 170
Cdd:pfam13870 81 HLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKL 119
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
82-184 |
8.34e-03 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 39.25 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603757 82 RILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL-----KVAKDVSVRLHHELKTVEEKRAKAED---ENETLRQQMIE 153
Cdd:pfam15035 24 KVLQYKKRCSELEQQLLEKTSELEKTELLLRKLTLeprlqRLEREHSADLEEALIRLEEERQRSESlsqVNSLLREQLEQ 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034603757 154 VEISKQALQNELERL-------------KESSLKRRstREMYKE 184
Cdd:pfam15035 104 ASRANEALREDLQKLtndwerareeleqKESEWRKE--EEAFNE 145
|
|
| |
