|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
973-1096 |
7.28e-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: 7.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 973 MDLRWQIHHSEKNWNREKVELLDRLDRDRQEWERQKKEFLWRIEQLQKENSPRR------------GGSFLCDQKDGNVR 1040
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRRkinmnerakvidGEKFVPDQKESSSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603763 1041 PFPHQGSLRMPR--PVAMWPCADADSIPFEDRPLSKLKESDRCSASENLYLDALSLDD 1096
Cdd:pfam14818 81 PFPDSGQCEFPRmnHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
167-261 |
3.21e-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: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 167 DSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANI 246
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1034603763 247 LGRKIVELEVENRGL 261
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
296-388 |
1.07e-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: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 296 SSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPPREPGWLGEGASPGA--GGGAPLQEELKSARLQISE 373
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSdsSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1034603763 374 LSGKVLKLQHENHAL 388
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-322 |
1.65e-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: 59.69 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAK 88
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 89 AEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKtfnqqnggmerpgncrpatKTQRKLAPRRKDDS 168
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-------------------AATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 169 ADLRCQLQFAKEEaflmrkkMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppstreAELKLRLKLVEEEANILG 248
Cdd:TIGR02168 848 EELSEDIESLAAE-------IEELEELIEELESELEALLNERASLEEAL-------------ALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034603763 249 RKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLEsstELRRHLQFVEEEAELLRRSISEIE 322
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLE 978
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-208 |
1.13e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNCRILQYRLRKAEqkslkvAETGQVDGELIRSLEQDLKVAKDvsvRLHHELKTVEEKRAKAEDENE 94
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAELEELRAELA---RLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 95 TLRQQMIEVE-ISKQALQNELERLKESSLKRRSTREMYKEKktfnQQNGGMERPGNcRPATKTQRKLAPRRKDDSADLRC 173
Cdd:COG4913 327 ELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL----LAALGLPLPAS-AEEFAALRAEAAALLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|....*
gi 1034603763 174 QLQfakEEAFLMRKKMAKLGREKDELEQELQKYKS 208
Cdd:COG4913 402 ALE---EALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-207 |
4.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 1 MEEMRDSYLEEDVYQLQELRREldranKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELK 80
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 81 TVEEKRAKAEdenETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKE---KKTFNQQNGGMERPGncRPATKTQ 157
Cdd:PTZ00121 1669 KAEEDKKKAE---EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEENKIKAEEAK--KEAEEDK 1743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034603763 158 RKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYK 207
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
15-205 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNcriLQYRLRKAEQKSLKVAETGQVD----GELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAE 90
Cdd:pfam07111 482 ELEQLREERNRLDAE---LQLSAHLIQQEVGRAREQGEAErqqlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQEST 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 91 DENETLRQQMI-EVEISKQALQN---ELE-RLKE--SSLKRR---STREMYKEKKTFNQqnggmerpgncrpatkTQRKl 160
Cdd:pfam07111 559 EEAASLRQELTqQQEIYGQALQEkvaEVEtRLREqlSDTKRRlneARREQAKAVVSLRQ----------------IQHR- 621
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034603763 161 APRRKDDSADL-RCQLQFAKEEAFLMRKKMAKLGREKDELEQELQK 205
Cdd:pfam07111 622 ATQEKERNQELrRLQDEARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4482 |
pfam14818 |
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
973-1096 |
7.28e-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: 7.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 973 MDLRWQIHHSEKNWNREKVELLDRLDRDRQEWERQKKEFLWRIEQLQKENSPRR------------GGSFLCDQKDGNVR 1040
Cdd:pfam14818 1 MDLRWQLQHTEKNWHREKMELLDRFDRERQEWESQKKIMQKKIEQLQREVSLRRkinmnerakvidGEKFVPDQKESSSP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034603763 1041 PFPHQGSLRMPR--PVAMWPCADADSIPFEDRPLSKLKESDRCSASENLYLDALSLDD 1096
Cdd:pfam14818 81 PFPDSGQCEFPRmnHPGSLSKSDSDEESFLDEGNQKLKEQKRCKASENLFLDALSLDN 138
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
167-261 |
3.21e-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: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 167 DSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANI 246
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSDSSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1034603763 247 LGRKIVELEVENRGL 261
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SOGA |
pfam11365 |
Protein SOGA; The SOGA (suppressor of glucose by autophagy) family consists of proteins SOGA1, ... |
296-388 |
1.07e-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: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 296 SSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKFKFEPPREPGWLGEGASPGA--GGGAPLQEELKSARLQISE 373
Cdd:pfam11365 1 SSAELRRQLQFVEEEAELLRRSLSEIEDHNKQLTNELNKYKSKYGPDESSLSDGEGGGSdsSREAELQEELKLARLQINE 80
|
90
....*....|....*
gi 1034603763 374 LSGKVLKLQHENHAL 388
Cdd:pfam11365 81 LSGKVMKLQYENRVL 95
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-322 |
1.65e-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: 59.69 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAK 88
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 89 AEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKtfnqqnggmerpgncrpatKTQRKLAPRRKDDS 168
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-------------------AATERRLEDLEEQI 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 169 ADLRCQLQFAKEEaflmrkkMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppstreAELKLRLKLVEEEANILG 248
Cdd:TIGR02168 848 EELSEDIESLAAE-------IEELEELIEELESELEALLNERASLEEAL-------------ALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034603763 249 RKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLEsstELRRHLQFVEEEAELLRRSISEIE 322
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-382 |
4.44e-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: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 58 IRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKESSlkRRSTREMYKEKKTF 137
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV--EQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 138 NQQNGgmERPGNCRPATKTQRKLApRRKDDSADLRCQLQFAKEEaflmrkkMAKLGREKDELEQELQKYKSLYGDVdspl 217
Cdd:TIGR02168 757 TELEA--EIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEE-------LKALREALDELRAELTLLNEEAANL---- 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 218 ptgeaggppSTREAELKLRLKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHApsiptspfgdsLESS 297
Cdd:TIGR02168 823 ---------RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-----------LNER 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 298 TELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSKfkfepprepgwlgegaspgagggapLQEELKSARLQISELSGK 377
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRRELEE-------------------------LREKLAQLELRLEGLEVR 937
|
....*
gi 1034603763 378 VLKLQ 382
Cdd:TIGR02168 938 IDNLQ 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
83-384 |
4.29e-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: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 83 EEKRAKAEDENETLRQQMIEVEISKQALQNELERLKesslKRRSTREMYKEKKTFNQQNGGMERPGNCRPATKTQRKLAP 162
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR----REREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 163 RRkddsADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSlygdvDSPLPTGEAGGPPSTREAELKLRLKLVEE 242
Cdd:TIGR02169 245 QL----ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE-----EEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 243 EANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHApsipTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIE 322
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKL----TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034603763 323 DHNRQLTHELSKFKFEPPRepgwLGEGASPGAGGGAPLQEELKSARLQISELSGKVLKLQHE 384
Cdd:TIGR02169 392 EKLEKLKREINELKRELDR----LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-338 |
1.17e-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: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 10 EEDVYQLQELRRELDRANKNCRI-----LQYRLRKAEQKSLKVAETGQVDGELIRSLEQdLKVAKDVSVRLHHELktvEE 84
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERqaekaERYKELKAELRELELALLVLRLEELREELEE-LQEELKEAEEELEEL---TA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 85 KRAKAEDENETLRQQMIEVEISKQALQNELERLKE--SSLKRRstREMYKEKKTFNQQNggmerpgncRPATKTQRKLAP 162
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANeiSRLEQQ--KQILRERLANLERQ---------LEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 163 RRKD----DSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeaggppSTREAELKLRLK 238
Cdd:TIGR02168 330 SKLDelaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL-------------RSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 239 LVEEEANILGRKIVELEVENRGLKAEMEDMRGQQERegpgrdHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSI 318
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE------AELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340
....*....|....*....|
gi 1034603763 319 SEIEDHNRQLTHELSKFKFE 338
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQAR 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-208 |
1.13e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNCRILQYRLRKAEqkslkvAETGQVDGELIRSLEQDLKVAKDvsvRLHHELKTVEEKRAKAEDENE 94
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALR------LWFAQRRLELLEAELEELRAELA---RLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 95 TLRQQMIEVE-ISKQALQNELERLKESSLKRRSTREMYKEKktfnQQNGGMERPGNcRPATKTQRKLAPRRKDDSADLRC 173
Cdd:COG4913 327 ELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL----LAALGLPLPAS-AEEFAALRAEAAALLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|....*
gi 1034603763 174 QLQfakEEAFLMRKKMAKLGREKDELEQELQKYKS 208
Cdd:COG4913 402 ALE---EALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
15-334 |
1.52e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENE 94
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEE-------LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 95 TLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQN-GGMERPGNCRPATKTQRKLAPRRKddsaDLRC 173
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQALSEAEAEQALDELLK----EANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 174 QLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPST---REAELKLRLKLVEEEANILGRK 250
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEellEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 251 IVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTH 330
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDND 354
|
....
gi 1034603763 331 ELSK 334
Cdd:COG4372 355 VLEL 358
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
60-561 |
3.26e-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: 48.89 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 60 SLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENETLRQQMIEVE------ISKQALQNELERLKESSLKRRSTREMYKE 133
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdvCGSQDEESDLERLKEEIEKSSKQRAMLAG 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 134 KKTFNQQ--NGGMERPGNCRPATKTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYG 211
Cdd:TIGR00606 661 ATAVYSQfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 212 DVDSPLP-TGEAGGPPSTREAELKLRLklvEEEANILGRKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTSPF 290
Cdd:TIGR00606 741 LKEKEIPeLRNKLQKVNRDIQRLKNDI---EEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 291 GDSLESSTELRrhlQFVEEEAELLRRSISEIEDhNRQLTHELSKfkfepprepgwlgegaspGAGGGAPLQEELKSARLQ 370
Cdd:TIGR00606 818 SDLDRTVQQVN---QEKQEKQHELDTVVSKIEL-NRKLIQDQQE------------------QIQHLKSKTNELKSEKLQ 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 371 ISELSGKVLKLQHENHALLSNIQRCDLAAHLGLRAPSPRDSDAESDAGKKESDGEESRLPQPKREGPVggeSDSEEMFEK 450
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIKEKVKN 952
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 451 TSGFGSGKPSEASEPCPTELL-KAREDSEYLVTLKHEAQRLERTVERLITDTDSFlhdaglrggaplpgpglqGEEEQGE 529
Cdd:TIGR00606 953 IHGYMKDIENKIQDGKDDYLKqKETELNTVNAQLEECEKHQEKINEDMRLMRQDI------------------DTQKIQE 1014
|
490 500 510
....*....|....*....|....*....|..
gi 1034603763 530 GDQQEPQLLGTINAKMKAFKKELQAFLEQVNR 561
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEVEEELKQHLKEMGQ 1046
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-207 |
4.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 1 MEEMRDSYLEEDVYQLQELRREldranKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELK 80
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKA-----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 81 TVEEKRAKAEdenETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKE---KKTFNQQNGGMERPGncRPATKTQ 157
Cdd:PTZ00121 1669 KAEEDKKKAE---EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEENKIKAEEAK--KEAEEDK 1743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034603763 158 RKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYK 207
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-275 |
5.13e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENE 94
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 95 TLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQNggmerpgncrpATKTQRKLAPRRKDDSADLRcQ 174
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-----------LLEAEAELAEAEEELEELAE-E 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 175 LQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLpTGEAGGPPSTREAELKLRLKLVEEEANILG--RKIV 252
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL-AELEEEEEEEEEALEEAAEEEAELEEEEEAllELLA 466
|
250 260
....*....|....*....|...
gi 1034603763 253 ELEVENRGLKAEMEDMRGQQERE 275
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEA 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
15-257 |
9.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETgqvdgelIRSLEQDLKVAKDvsvrlhhELKTVEEKRAKAEDENE 94
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-------LAALERRIAALAR-------RIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 95 TLRQQMIEVEISKQALQNELERLkesslkrrsTREMYKekktfNQQNGGMERPGNCRPATKTQR------KLAPRRKDDS 168
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAEL---------LRALYR-----LGRQPPLALLLSPEDFLDAVRrlqylkYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 169 ADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAggppstREAELKLRLKLVEEEANILG 248
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK------ELAELAAELAELQQEAEELE 226
|
....*....
gi 1034603763 249 RKIVELEVE 257
Cdd:COG4942 227 ALIARLEAE 235
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
15-205 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNcriLQYRLRKAEQKSLKVAETGQVD----GELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAE 90
Cdd:pfam07111 482 ELEQLREERNRLDAE---LQLSAHLIQQEVGRAREQGEAErqqlSEVAQQLEQELQRAQESLASVGQQLEVARQGQQEST 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 91 DENETLRQQMI-EVEISKQALQN---ELE-RLKE--SSLKRR---STREMYKEKKTFNQqnggmerpgncrpatkTQRKl 160
Cdd:pfam07111 559 EEAASLRQELTqQQEIYGQALQEkvaEVEtRLREqlSDTKRRlneARREQAKAVVSLRQ----------------IQHR- 621
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034603763 161 APRRKDDSADL-RCQLQFAKEEAFLMRKKMAKLGREKDELEQELQK 205
Cdd:pfam07111 622 ATQEKERNQELrRLQDEARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
13-328 |
1.16e-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: 47.04 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 13 VYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQ--VDGELIRSLEQDlkvaKDVSVRLHHELKTVEEKRA--- 87
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRklEEAEKARQAEMD----RQAAIYAEQERMAMEREREler 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 88 -KAED---ENETLRQQMIEVEISK----QALQNEL----ERLKESSLKRRSTREMYKEK-KTFNQQNGGME--RPGNCRP 152
Cdd:pfam17380 353 iRQEErkrELERIRQEEIAMEISRmrelERLQMERqqknERVRQELEAARKVKILEEERqRKIQQQKVEMEqiRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 153 ATKTQRKLAPRRKDDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptgeaggppstrEAE 232
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL------------EKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 233 LKLRLKLVEEEANilGRKIVELEVENRGLKAEMEDMRGQQEREgpGRDHAPSIPTSPFGDSLESSTELRRHLQFVEEEAE 312
Cdd:pfam17380 501 LEERKQAMIEEER--KRKLLEKEMEERQKAIYEEERRREAEEE--RRKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
330
....*....|....*.
gi 1034603763 313 LLRRsISEIEDHNRQL 328
Cdd:pfam17380 577 MMRQ-IVESEKARAEY 591
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-334 |
1.30e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNcRILQYRLRKAEQKSLKVAetgqvdgelIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENE 94
Cdd:COG1196 201 QLEPLERQAEKAERY-RELKEELKELEAELLLLK---------LRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 95 TLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQNggMERpgncrpATKTQRKLAPRRKDDSAdlrcQ 174
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER--LEE------LEEELAELEEELEELEE----E 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 175 LQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDsplptgeaggppSTREAELKLRLKLVEEEANILgRKIVEL 254
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------------EELEELAEELLEALRAAAELA-AQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 255 EVENRGLKAEMEDMRGQQEREGpgrdhapsiptspfGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHELSK 334
Cdd:COG1196 406 EEAEEALLERLERLEEELEELE--------------EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-336 |
3.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 16 LQELRRELDRankncrilqyrlRKAEQKSLkVAETGQVDgELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENET 95
Cdd:PRK03918 167 LGEVIKEIKR------------RIERLEKF-IKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 96 L---RQQMIEVEISKQALQNELERLKEsslKRRSTREMYKEKKtfnqqnggmerpgncrpatKTQRKLAPRRKDDSadlr 172
Cdd:PRK03918 233 LeelKEEIEELEKELESLEGSKRKLEE---KIRELEERIEELK-------------------KEIEELEEKVKELK---- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 173 cQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAggpPSTREAELKLRLKLVEEEANILGRKIV 252
Cdd:PRK03918 287 -ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE---KEERLEELKKKLKELEKRLEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 253 ELEVenrgLKAEMEDMRGQQEREGPgrdhapsiptspfgdslESSTELRRHLQFVEEEAELLRRSISEIEDHNRQLTHEL 332
Cdd:PRK03918 363 LYEE----AKAKKEELERLKKRLTG-----------------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
....
gi 1034603763 333 SKFK 336
Cdd:PRK03918 422 KELK 425
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-225 |
3.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 15 QLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAkdvsvRLHHELKTVEEKRAKAEDEN- 93
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAELERLDASSd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 94 --ETLRQQMIEVEISKQALQNELERLKEsslkRRSTREmyKEKKTFNQQnggmerpgncRPATKTQRKLAPRRKDDSADL 171
Cdd:COG4913 686 dlAALEEQLEELEAELEELEEELDELKG----EIGRLE--KELEQAEEE----------LDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034603763 172 RCQLQFAKEEAFLMRKKM------------AKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGP 225
Cdd:COG4913 750 LLEERFAAALGDAVERELrenleeridalrARLNRAEEELERAMRAFNREWPAETADLDADLESLP 815
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-285 |
4.84e-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: 45.11 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 2 EEMRDSYLEedvyqLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQvdgELIRSLeQDLKVAKDvsvRLHHELKT 81
Cdd:pfam15921 597 KEINDRRLE-----LQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS---ERLRAV-KDIKQERD---QLLNEVKT 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 82 VEEKRAKAEDENETL----RQQMIEVEISKQALQNELerlkesslkRRSTREMYKEKKTFNQQNGGmerPGNC-RPATKT 156
Cdd:pfam15921 665 SRNELNSLSEDYEVLkrnfRNKSEEMETTTNKLKMQL---------KSAQSELEQTRNTLKSMEGS---DGHAmKVAMGM 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 157 QRKLAPRRKDDSAdLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVdsplptgeAGGPPSTREAELKLR 236
Cdd:pfam15921 733 QKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM--------AGELEVLRSQERRLK 803
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034603763 237 LKLVEEEANILGRKIVELEVENRGLKAEMEDMRGQ-------QEREGPGRDHAPSI 285
Cdd:pfam15921 804 EKVANMEVALDKASLQFAECQDIIQRQEQESVRLKlqhtldvKELQGPGYTSNSSM 859
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-327 |
5.12e-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: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 16 LQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENET 95
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 96 L-----RQQMIEVEISKQALQNELERLK------ESSLKRRSTREMYKEKKTFNQQNGgmerpgncRPATKTQRKLAPRR 164
Cdd:TIGR02169 784 LearlsHSRIPEIQAELSKLEEEVSRIEarlreiEQKLNRLTLEKEYLEKEIQELQEQ--------RIDLKEQIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 165 KDDS------------------ADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLptGEAGGPP 226
Cdd:TIGR02169 856 IENLngkkeeleeeleeleaalRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL--EALEEEL 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 227 STREAELKLRLKLVEEEANI--LGRKIVELEVENRGLkaEMEDMRGQQEREgpgrdhapsiptspfgDSLESSTELRRHL 304
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEEELSLedVQAELQRVEEEIRAL--EPVNMLAIQEYE----------------EVLKRLDELKEKR 995
|
330 340
....*....|....*....|...
gi 1034603763 305 QFVEEEAELLRRSISEIEDHNRQ 327
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKRE 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-336 |
6.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 9 LEEDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQVDGELIRSLEQdLKVAKDVSVRLHHELKTVEEKRAK 88
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 89 AEDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQ-NGGMERPGNCRpatKTQRKLAPRRKDD 167
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELE---RLKKRLTGLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 168 SADLRCQLQFAKEEaflMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAGGPPSTREAELKLRLKLVEEEANIL 247
Cdd:PRK03918 389 LEKELEELEKAKEE---IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 248 GRKIvELEVENRGLKAEMEDMRGQQEREgpgRDHAPSIPTSPFGDSLESSTEL--RRHLQFVEEEAELLRRSISEIEDHN 325
Cdd:PRK03918 466 KELK-EIEEKERKLRKELRELEKVLKKE---SELIKLKELAEQLKELEEKLKKynLEELEKKAEEYEKLKEKLIKLKGEI 541
|
330
....*....|.
gi 1034603763 326 RQLTHELSKFK 336
Cdd:PRK03918 542 KSLKKELEKLE 552
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
10-275 |
7.55e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 10 EEDVYQLQELRRELDRANKncrilQYRLRKAEQK----SLKVAETGQVDGELIRSLE----QDLKVAKDVsvRLHHELKT 81
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKK-----ADEAKKAEEAkkadEAKKAEEAKKADEAKKAEEkkkaDELKKAEEL--KKAEEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 82 VEEKRAKAEDENETLRQqmieVEISKQAlqnELERLKESSLKRRSTREMYKEKktFNQQNGGMERPGNCRPATKTQRKLA 161
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRK----AEEAKKA---EEARIEEVMKLYEEEKKMKAEE--AKKAEEAKIKAEELKKAEEEKKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 162 PRRKDDSADLRCQLQFAKEEaflmRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEAggppSTREAELKLRLKLVE 241
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA----LKKEAEEAKKAEELK 1708
|
250 260 270
....*....|....*....|....*....|....
gi 1034603763 242 EEANILGRKIVELEVENRGLKAEMEDMRGQQERE 275
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
10-391 |
1.93e-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: 43.09 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 10 EEDVYQLQELRRELDRANKNCRILQYRLR--KAEQKSLKvaetGQVDGELIRSLEQDLKVAKDVSVRLHHELKTVEEKRA 87
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNqlKSEISDLN----NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 88 KAEDENETLRQQMIEVEISKQALQNELERlKESSLKRrstreMYKEKKTFNQQNggmerpgncrpatktqRKLaprrKDD 167
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEE-KQNEIEK-----LKKENQSYKQEI----------------KNL----ESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 168 SADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYKSLYGDVDSPLPTGEaggppsTREAELKLRLKLVEEEANIL 247
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT------NQDSVKELIIKNLDNTRESL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 248 GRKIVELEVENRGLKAEMEDMrgQQEREGPGRDHapSIPTSPFGDSLESSTELRRHLQFVEEEAELLRRSISEIEDHNRQ 327
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQK--QKELKSKEKEL--KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034603763 328 LTHELSKFKFepprepgwlgegaspgagggaplqeELKSARL--QISELSGKVLKLQHENHALLSN 391
Cdd:TIGR04523 543 LEDELNKDDF-------------------------ELKKENLekEIDEKNKEIEELKQTQKSLKKK 583
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1-140 |
4.15e-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: 42.03 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 1 MEEMRDSYLEEDVYQLQELRRELDRANKN--CRILQYRLRKAEQKSLKVAETgQVDGELIRSLEQDLKVAKDVSVRLHHE 78
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEARQRevRRLEEERAREMERVRLEEQER-QQQVERLRQQEEERKRKKLELEKEKRD 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034603763 79 LKTVEEKRAKA-EDENETLRQQMIEVEISKQALQNELE----------RLKESSLKRRSTREMyKEKKTFNQQ 140
Cdd:pfam17380 486 RKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEerqkaiyeeeRRREAEEERRKQQEM-EERRRIQEQ 557
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-394 |
4.80e-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: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 166 DDSADLRCQLQFAKEEAFLMRKKMAKLGREKDELEQELQKYkslygdvdsplptgeaggppSTREAELKLRLKLVEEEAN 245
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------------------ERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 246 ILGRKIVELEVENRGLKAEMEDMRGQQER-----EGPGRDHAPSIPTSP--FGDSLESSTELRRHLQFVEEEAELLRRSI 318
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAEllralYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034603763 319 SEIEDHNRQLTHELSKfkfepprepgwLGEGASPGAGGGAPLQEELKSARLQISELSGKVLKLQHENHALLSNIQR 394
Cdd:COG4942 160 AELAALRAELEAERAE-----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
11-328 |
4.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 11 EDVYQLQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGqvdgELIRSLEQDLKVAKDVSVRLHHELKTVEEKRAK-A 89
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE----EELEELEAELAELQEELEELLEQLSLATEEELQdL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 90 EDENETLRQQMIEVEISKQALQNELERLKESSLKRRSTREMYKEKKTFNQQN-------GGMERPGNCRPATKTQRKLAP 162
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaALLALLGLGGSLLSLILTIAG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 163 RRKDDSADLRCQLQFAKEEAFLMRKKMAKLGR--EKDELEQ-ELQKYKSLYGdVDSPLPTGEAGGPPST----------- 228
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQAlpALEELEEeELEELLAALG-LPPDLSPEELLELLDRieelqellrea 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 229 REAELKLRLKLVEEEANILG-----------RKIVELEVENRGLKAEMEDMRGQQEREGPGRDHAPSIPTspfGDSLES- 296
Cdd:COG4717 357 EELEEELQLEELEQEIAALLaeagvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD---EEELEEe 433
|
330 340 350
....*....|....*....|....*....|..
gi 1034603763 297 STELRRHLQFVEEEAELLRRSISEIEDHNRQL 328
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-143 |
5.58e-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: 41.59 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 16 LQELRRELDRANKNCRILQYRLRKAEQKslkvaetgqvdgelIRSLEQDLKVAKDVSVRLHHELKTVEEKRAKAEDENET 95
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEE--------------LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1034603763 96 LRQQMIEVEISKQALQNELERL-KESSLKRRSTREMYKEKKTFNQQNGG 143
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVeKELSKLQRELAEAEAQARASEERVRG 508
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
16-119 |
8.15e-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: 39.13 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 16 LQELRRELDRANKNCRILQYRLRKAEQKSLKVAETGQ----VD-----------GELIRSLEQDLKVAKDVSVRLHHELK 80
Cdd:pfam13870 1 MRAKRNELSKLRLELITLKHTLAKIQEKLEQKEELGEgltmIDflqlqienqalNEKIEERNKELKRLKLKVTNTVHALT 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1034603763 81 TVEEKRAKAEDENETLRQQMIEVEISKQALQNELERLKE 119
Cdd:pfam13870 81 HLKEKLHFLSAELSRLKKELRERQELLAKLRKELYRVKL 119
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
31-133 |
8.38e-03 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 39.25 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 31 RILQYRLRKAEQKSLKVAETGQVDGELIRSLEQDL-----KVAKDVSVRLHHELKTVEEKRAKAED---ENETLRQQMIE 102
Cdd:pfam15035 24 KVLQYKKRCSELEQQLLEKTSELEKTELLLRKLTLeprlqRLEREHSADLEEALIRLEEERQRSESlsqVNSLLREQLEQ 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034603763 103 VEISKQALQNELERL-------------KESSLKRRstREMYKE 133
Cdd:pfam15035 104 ASRANEALREDLQKLtndwerareeleqKESEWRKE--EEAFNE 145
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-125 |
9.44e-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: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034603763 2 EEMRDSYLEEDVYQLQELRRELDRANKncrilqyRLRKAEQKSLKVAetgqvdgELIRSLEQDLKVAKDVSVRLHHELKt 81
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLEREIERLER-------ELEERERRRARLE-------ALLAALGLPLPASAEEFAALRAEAA- 390
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034603763 82 veEKRAKAEDENETLRQQMIEVEISKQALQNELERLKE--SSLKRR 125
Cdd:COG4913 391 --ALLEALEEELEALEEALAEAEAALRDLRRELRELEAeiASLERR 434
|
|
| |
