|
Name |
Accession |
Description |
Interval |
E-value |
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
231-317 |
2.45e-23 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 93.18 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 231 CEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQ 310
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 2462598919 311 SQLNRLN 317
Cdd:cd09803 81 RENQELK 87
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
229-317 |
1.02e-10 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 58.07 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 229 YECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 308
Cdd:pfam16516 12 YKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEY 91
|
....*....
gi 2462598919 309 SQSQLNRLN 317
Cdd:pfam16516 92 LQRQNQQLK 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-337 |
4.72e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 107 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDL 186
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 187 TRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEE 266
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----------RLESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462598919 267 MRTEMEVLKQQvqiyeedFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 337
Cdd:TIGR02168 836 TERRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
143-337 |
3.53e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 143 ERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRED-----------DRQRDLTRDRLQREEKEKERLNEELHELKE- 210
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEa 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 211 ----ENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNikcsfsedclRKSRVEFCHEEMRTEMEVLKQQvQIYEEDFK 286
Cdd:TIGR02169 781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ----------KLNRLTLEKEYLEKEIQELQEQ-RIDLKEQI 849
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462598919 287 KERSDR-ERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 337
Cdd:TIGR02169 850 KSIEKEiENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
61-336 |
6.62e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 61 GSCDYKKTPGKTASMAHFVQGTSRMIAAESStehkecaEPSTRKNLMNSLEQKIRCLEKQ----RKELLEVNQQWDQQFR 136
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQS-------ELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 137 SMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE--DDRQRDLTRDRLQREEKEKERLNEELHELKEENKL 214
Cdd:TIGR02169 738 RLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEalNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 215 LKGKNTLANKEKEHYECEIKRLnKALQDALNIKCSFSEDCLRKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRER 294
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQEL-QEQRIDLKEQIKSIEKEIENLNGKK--EELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462598919 295 LNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-336 |
6.75e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 120 QRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRdltRDRLQREEKEKE 199
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL---EAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 200 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 279
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----------LDELRAELTLLNEEAA 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598919 280 IYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-336 |
2.55e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 110 LEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAELKTKLDAAERFLSTREKdphQRQRKDDRQREDDRQRDLTRD 189
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 190 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----LNIKCSFSEDCLRKSRVEFCHE 265
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAeealLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462598919 266 EMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
103-307 |
4.82e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 103 RKNLMNSLEQK---IRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE 179
Cdd:TIGR02168 311 LANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 180 DDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEikRLNKALQDAlnikcsfsedclrksr 259
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE--ELEEELEEL---------------- 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462598919 260 vEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINE 307
Cdd:TIGR02168 453 -QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-336 |
2.32e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 122 KELLEVNQQWDQQFRSMKElYERKVAELKTKLDAAERFLSTrekdpHQRQRKDDRQREDDRQRDL--TRDRLQREEKEKE 199
Cdd:TIGR02168 232 LRLEELREELEELQEELKE-AEEELEELTAELQELEEKLEE-----LRLEVSELEEEIEELQKELyaLANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 200 RLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDclrksrvefcHEEMRTEMEVLKQQVQ 279
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE----------LEELEAELEELESRLE 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462598919 280 IYEEDFKKERSDR---------------------ERLNQEKEELQQINETSQSQLnrLNSQIKACQMEKEKLEKQLKQ 336
Cdd:TIGR02168 376 ELEEQLETLRSKVaqlelqiaslnneierlearlERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
176-336 |
7.43e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 176 RQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALqdalnikcsfsedcl 255
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 256 rksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 335
Cdd:COG1196 284 ---------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
.
gi 2462598919 336 Q 336
Cdd:COG1196 355 E 355
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
111-305 |
2.81e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 111 EQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERkvaeLKTKLDAAERFLSTREKD----PHQRQRkddRQREDDRQR-D 185
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDA----LQERREALQRLAEYSWDEidvaSAEREI---AELEAELERlD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 186 LTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLrksrvefchE 265
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---------E 752
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462598919 266 EMRTEmEVLKQQVQIYEEDFKKERSD-RERLNQEKEELQQI 305
Cdd:COG4913 753 ERFAA-ALGDAVERELRENLEERIDAlRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
117-336 |
9.69e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 117 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKdphqrqrkddRQREDDRQRDLTRDRLQREEK 196
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALAR----------RIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 197 EKERLNEELHELKEEnkllkgkntLANKEKEHYeceikRLNKALQDALNIKCSFSEDCLRKSRVefcheeMRTEMEVLKQ 276
Cdd:COG4942 91 EIAELRAELEAQKEE---------LAELLRALY-----RLGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARRE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 277 QVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
104-321 |
1.48e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 104 KNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLStrEKDPHQRQRKDDRQREDDrq 183
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL-TKKISSLKEKIEKLESEKK--EKESKISDLEDELNKDDF-- 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 184 rDLTRDRLqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRKSRVEfc 263
Cdd:TIGR04523 553 -ELKKENL---EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE-EKEKKISSLEKELEKAKKE-- 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462598919 264 HEEMRTEM-------EVLKQQVQIYEEDFKKERSDRERLNQE----KEELQQINETSQSQLNRLNSQIK 321
Cdd:TIGR04523 626 NEKLSSIIknikskkNKLKQEVKQIKETIKEIRNKWPEIIKKikesKTKIDDIIELMKDWLKELSLHYK 694
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-326 |
1.53e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 107 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELktklDAAERFLST--REKDPHQRQRKDDRQREDDRQR 184
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI----EELEREIEEerKRRDKLTEEYAELKEELEDLRA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 185 DL---------TRDRLQREEKEKERLNEELHELKEENKLLKgkntlanKEKEHYECEIKRLNKALQDALNIKCSFSEDcl 255
Cdd:TIGR02169 372 ELeevdkefaeTRDELKDYREKLEKLKREINELKRELDRLQ-------EELQRLSEELADLNAAIAGIEAKINELEEE-- 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462598919 256 rksrvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQME 326
Cdd:TIGR02169 443 --------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
83-312 |
2.17e-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: 46.66 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 83 SRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKelleVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLST 162
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRK----IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 163 REKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyeceiKRLNKALQD 242
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR------KLLEKEMEE 524
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 243 ALNikCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEdfkkERSDRERLNQEKEELQQINETSQSQ 312
Cdd:pfam17380 525 RQK--AIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-336 |
3.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 155 AAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIK 234
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 235 RlnKALQDALNIKCSFSEDCLRKSRVefcHEEMRTEMEVLKQQVQIYEEDFKKERSD-----RERLNQEKEELQQInets 309
Cdd:COG4717 134 L--EALEAELAELPERLEELEERLEE---LRELEEELEELEAELAELQEELEELLEQlslatEEELQDLAEELEEL---- 204
|
170 180
....*....|....*....|....*..
gi 2462598919 310 QSQLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-322 |
6.06e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 110 LEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD 189
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 190 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKcsfsedclrksrvefcHEEMRT 269
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE----------------EEEEEA 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462598919 270 EMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKA 322
Cdd:COG1196 444 LEEAAEEEAELEEEE-EALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
130-314 |
6.54e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.09 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 130 QWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRD--RLQREEKEKERLNEELHE 207
Cdd:PRK12705 23 VLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREeeRLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 208 LKEEnkLLKGKNTLANKEKehyecEIKRLNKALQDALNIKCSFSEDCLRKSRVEfcheemRTEMEVLKQQVQIYEEDFKK 287
Cdd:PRK12705 103 LENQ--LEEREKALSAREL-----ELEELEKQLDNELYRVAGLTPEQARKLLLK------LLDAELEEEKAQRVKKIEEE 169
|
170 180
....*....|....*....|....*....
gi 2462598919 288 ERSDRERLNQE--KEELQQINETSQSQLN 314
Cdd:PRK12705 170 ADLEAERKAQNilAQAMQRIASETASDLS 198
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-336 |
8.93e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 162 TRE---KDPHQRQRKDDRQReddRQRDL-----TRDRLQREEKEKERLNEELHELKEENKLLKgkntlankekehyecEI 233
Cdd:COG4913 578 TRAgqvKGNGTRHEKDDRRR---IRSRYvlgfdNRAKLAALEAELAELEEELAEAEERLEALE---------------AE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 234 KRLNKALQDALNIKCSFSEDCLRksrvefcHEEMRTEMEVLKQQVQIYEEDfkkeRSDRERLNQEKEELQQINETSQSQL 313
Cdd:COG4913 640 LDALQERREALQRLAEYSWDEID-------VASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEEL 708
|
170 180
....*....|....*....|...
gi 2462598919 314 NRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDE 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-337 |
9.91e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 108 NSLEQKIRCLEKQRKELLEVNQQWDqqfrsmkelyerKVAELKTKLDAAERFLSTRekDPHQRQRKDD--RQREDDRQRD 185
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAE------------RYAAARERLAELEYLRAAL--RLWFAQRRLEllEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 186 LTR--DRLQREEKEKERLNEELHELKEEnkllkgKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsedclrksrvefc 263
Cdd:COG4913 304 LARleAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLERELEERERR----------------- 360
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462598919 264 HEEMRTEMEVLKQQVQIYEEDFKKErsdRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 337
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
70-312 |
1.05e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 70 GKTaSMAHFVQGtsrMIAAESSTEHKECAEPSTRKNLMNSleQKIRCLEKQRKELLEVNQQWDQQfrsmkelyERKVAEL 149
Cdd:COG4717 35 GKS-TLLAFIRA---MLLERLEKEADELFKPQGRKPELNL--KELKELEEELKEAEEKEEEYAEL--------QEELEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 150 KTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKE-ENKLLKGKNTLANKEKEH 228
Cdd:COG4717 101 EEELEELEAELEELREE-LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRElEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 229 YECEIKRLNKALQDAlnikcsfsedclrksrvefchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINET 308
Cdd:COG4717 180 EELLEQLSLATEEEL---------------------QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
....
gi 2462598919 309 SQSQ 312
Cdd:COG4717 239 AALE 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
88-337 |
1.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 88 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS---MKELYERKVAELKTKLDAAERFLSTRE 164
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeaKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 165 KDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKllKGKNTLANKEKEHYECEikrlnkalqdal 244
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK--KAAEALKKEAEEAKKAE------------ 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 245 NIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQvqiyEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQ 324
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
250
....*....|...
gi 2462598919 325 MEKEKLEKQLKQM 337
Cdd:PTZ00121 1782 EEELDEEDEKRRM 1794
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
118-336 |
1.09e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 118 EKQRKELLEVNQQwdQQFRSMKELYERKVaELKTKLDAAER-----------FLSTREKDPHQRQRKDDRQREDDRQRDL 186
Cdd:pfam17380 286 ERQQQEKFEKMEQ--ERLRQEKEEKAREV-ERRRKLEEAEKarqaemdrqaaIYAEQERMAMERERELERIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 187 TRDRLQREEKEKERLNE-ELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHE 265
Cdd:pfam17380 363 ERIRQEEIAMEISRMRElERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462598919 266 EMRTEMEVLK-------QQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:pfam17380 443 ERAREMERVRleeqerqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK 520
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
133-337 |
1.16e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 133 QQFRSMKELYERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEEN 212
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 213 KLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKE---- 288
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkni 953
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462598919 289 ---RSDRERLNQEKEELQQINEtsQSQLNRLNSQIKACQMEKEKLEKQLKQM 337
Cdd:TIGR00606 954 hgyMKDIENKIQDGKDDYLKQK--ETELNTVNAQLEECEKHQEKINEDMRLM 1003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-336 |
1.37e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 176 RQREDDRQRDLTRDRLqreekekERLNEELHELKEENKLLKGKNTLANKEKEhYECEIKRLNKALQdALNIKcsFSEDCL 255
Cdd:TIGR02168 173 RRKETERKLERTRENL-------DRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALL-VLRLE--ELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 256 RKSRVEFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLK 335
Cdd:TIGR02168 242 EELQEEL--KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
.
gi 2462598919 336 Q 336
Cdd:TIGR02168 320 E 320
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
99-338 |
1.75e-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: 43.86 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 99 EPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYE------------------------RKVAELKTKLD 154
Cdd:TIGR04523 378 ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEllekeierlketiiknnseikdltNQDSVKELIIK 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 155 AAERFLSTREK--DPHQRQRKDDRQREDDRQRDLTRDrlqreEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECE 232
Cdd:TIGR04523 458 NLDNTRESLETqlKVLSRSINKIKQNLEQKQKELKSK-----EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 233 IKRLNKALQDaLNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQ--------------VQIYEEDFKKERSDRERLNQE 298
Cdd:TIGR04523 533 KKEKESKISD-LEDELNKDDFELKKENLEKEIDEKNKEIEELKQTqkslkkkqeekqelIDQKEKEKKDLIKEIEEKEKK 611
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462598919 299 KEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQMY 338
Cdd:TIGR04523 612 ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
113-243 |
1.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 113 KIRCLEKQRKELL-EVNQQWDQQFRSMKELYERKVaELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLtRDRL 191
Cdd:COG4717 364 QLEELEQEIAALLaEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL-EEEL 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462598919 192 QREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 243
Cdd:COG4717 442 EELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
190-336 |
3.03e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 190 RLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEhyecEIKRLNKALQDALNIkcsfsedcLRKSrVEFCHEEMRT 269
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKP----KLRDRKDALEEELRQ--------LKQL-EDELEDCDPT 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598919 270 EMEVLKqqvqiyeEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:smart00787 205 ELDRAK-------EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQ 264
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
88-335 |
3.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 88 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKEllEVNQQWDQQFRSMKELYE-----------RKVAELKTKLDAA 156
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD--EAKKKAEEDKKKADELKKaaaakkkadeaKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 157 ERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEK-------ERLNEELHELKEENKLLKGKNTLANKEKEHY 229
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeakkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 230 ECEIKRLNKALQDALNIKcsfSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS 309
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAK---KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
250 260
....*....|....*....|....*.
gi 2462598919 310 QSQLNRLNSQIKACQMEKEKLEKQLK 335
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
103-243 |
3.53e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 103 RKNLMNSLEQKIRCLeKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRkddrqreddr 182
Cdd:pfam05483 519 QEDIINCKKQEERML-KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK---------- 587
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462598919 183 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 243
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
119-332 |
3.58e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 119 KQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLdaAERFLSTREKDPHQRQRKDDRQREDDRQR-DLTRDRLQREEKE 197
Cdd:COG5022 813 RSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVL--IQKFGRSLKAKKRFSLLKKETIYLQSAQRvELAERQLQELKID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 198 KERLNEeLHE--LKEENKLLKGKNTLANKEKEHYECEIKRLNKaLQDALNiKCSFSEDCLRKSRVEFCHEEMRTEMEVLK 275
Cdd:COG5022 891 VKSISS-LKLvnLELESEIIELKKSLSSDLIENLEFKTELIAR-LKKLLN-NIDLEEGPSIEYVKLPELNKLHEVESKLK 967
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598919 276 QQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLnrlnSQIKACQMEKEKLEK 332
Cdd:COG5022 968 ETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS----KQYGALQESTKQLKE 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
178-336 |
4.67e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 178 REDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQdALNIKCSFSEDCLRK 257
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL-KLELLLSNLKKKIQK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 258 srvefcHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQ-QINETSQSQlNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:TIGR04523 213 ------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQtQLNQLKDEQ-NKIKKQLSEKQKELEQNNKKIKE 285
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
76-215 |
5.57e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 76 AHFVQGTS------RMIAAESSTEHKECAEPSTRKNLM-NSLEQKIRCLEKQRKELLEVNQQWDQQFRSMkelyERKVAE 148
Cdd:COG2433 370 ARVIRGLSieealeELIEKELPEEEPEAEREKEHEERElTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIER 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462598919 149 LKTKLdaaeRFLSTREKDPHQRQRK-DDRQREDDRqrdLTRdRLQREEKEKERLNEELHELKEENKLL 215
Cdd:COG2433 446 LEREL----SEARSEERREIRKDREiSRLDREIER---LER-ELEEERERIEELKRKLERLKELWKLE 505
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
109-209 |
6.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 109 SLEQKIRCLEKQRKElleVNQQWDQqfrsmkelYERKVAELKTKLDA-AERFLSTREKDPHQRQRKDDRQREDDRQRDLT 187
Cdd:COG4913 342 QLEREIERLERELEE---RERRRAR--------LEALLAALGLPLPAsAEEFAALRAEAAALLEALEEELEALEEALAEA 410
|
90 100
....*....|....*....|..
gi 2462598919 188 RDRLQREEKEKERLNEELHELK 209
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLE 432
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
169-336 |
8.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 169 QRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA----- 243
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 244 ------------LNIKcSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQS 311
Cdd:COG3883 97 rsggsvsyldvlLGSE-SFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190
....*....|....*....|....*....|..
gi 2462598919 312 Q-------LNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:COG3883 176 QqaeqealLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
88-336 |
9.27e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 88 AESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyeRKVAELKTKLDAAERflsTREKDP 167
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA--KKAAEAKKKADEAKK---AEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 168 HQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLN--EELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALN 245
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 246 IKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDfKKERSDRERLNQEKEELQQINET---SQSQLNRLNSQIKA 322
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE-AEEKKKAEELKKAEEENKIKAAEeakKAEEDKKKAEEAKK 1682
|
250
....*....|....
gi 2462598919 323 CQMEKEKLEKQLKQ 336
Cdd:PTZ00121 1683 AEEDEKKAAEALKK 1696
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
84-302 |
1.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 84 RMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEvnqqwdqqfrSMKELyERKVAELKTKLdaaeRFLSTR 163
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE----------KIREL-EERIEELKKEI----EELEEK 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 164 EKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLN------ 237
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEeleerh 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462598919 238 KALQDALNIKCSFSEdcLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEEL 302
Cdd:PRK03918 362 ELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
109-335 |
1.16e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 109 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTR 188
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 189 DRLQREEKEKERLNEElhelKEENKLLKGKNTLANKEKEHYECE------IKRLNKALQDALNIKCSFSEDCLRKSRVEF 262
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQ----KEQDWNKELKSELKNQEKKLEEIQnqisqnNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462598919 263 CHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINEtsqsqlnRLNSQIKACQMEKEKLEKQLK 335
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ-------QKDEQIKKLQQEKELLEKEIE 429
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
107-303 |
1.34e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 107 MNSLEQKIRCLEKQRKELLEVNQQWDQQfrsmKELYERKVAELKTKLDAAERflstrEKDPHQRQRKDDRQREDDRQRDl 186
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEE-----ELEELEAALRDLESRLGDLKKE- 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 187 tRDRLQRE----EKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIkcsfsEDClrKSRVEF 262
Cdd:TIGR02169 891 -RDELEAQlrelERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-----EDV--QAELQR 962
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462598919 263 CHEEMRTEMEVLKQQVQIYEE---DFKKERSDRERLNQEKEELQ 303
Cdd:TIGR02169 963 VEEEIRALEPVNMLAIQEYEEvlkRLDELKEKRAKLEEERKAIL 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
103-243 |
1.35e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 103 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDphQRQRKDDRQREDDR 182
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLER--LERLEEELEELEEA 429
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462598919 183 QRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDA 243
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
92-295 |
1.40e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 92 TEHKEC--AEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKElyerKVAELKTKLDAAERFLSTREKDPHQ 169
Cdd:pfam10174 372 TEEKSTlaGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE----RVKSLQTDSSNTDTALTTLEEALSE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 170 RQRKDDRQREddrQRDltRDRLQREEkEKERLNEELHELKEENKLLKG----KNTLANKEKEHYECE----IKRLNKALQ 241
Cdd:pfam10174 448 KERIIERLKE---QRE--REDRERLE-ELESLKKENKDLKEKVSALQPelteKESSLIDLKEHASSLassgLKKDSKLKS 521
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462598919 242 DALNIK-----CSFSEDCLRKSR----VEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERL 295
Cdd:pfam10174 522 LEIAVEqkkeeCSKLENQLKKAHnaeeAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
117-336 |
1.55e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 117 LEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAErflSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEK 196
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQL-NEQISQLKKELTNSE---SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 197 EKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLnkaLQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQ 276
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL---KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598919 277 QVQIYEEDFKKERSDRERLNQE-----KEELQQINETSQS--QLNRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKElkskeKELKKLNEEKKELeeKVKDLTKKISSLKEKIEKLESEKKE 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-332 |
1.58e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 105 NLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERflstrekdphQRQRKDDRQREDDRQR 184
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELES----------ELEALLNERASLEEAL 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 185 DLTRDRLQREEKEKERLNEELHELKEEnklLKGKNTLANKEKEhyeceikRLNKALQDALNIKCSFSEdclrksrvefch 264
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLEL-------RLEGLEVRIDNLQERLSE------------ 947
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462598919 265 eEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETS-------QSQLNRLNSQIKACQMEKEKLEK 332
Cdd:TIGR02168 948 -EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAieeyeelKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| Cas7_I-C |
cd09687 |
CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly ... |
173-335 |
1.59e-03 |
|
CRISPR/Cas system-associated RAMP superfamily protein Cas7; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas7 is a RAMP superfamily protein; Subunit of the Cascade complex; also known as Cst2/DevR family
Pssm-ID: 187818 Cd Length: 302 Bit Score: 40.12 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 173 KDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKehyECEIKRLnkalqdaLNIKCSFSE 252
Cdd:cd09687 158 EVGIEEKKCNPRGRLEYRLPKEEKEKRRANNLLKAIRNLSGGAKQARRLEDLSP---KFVVLGV-------LNGKNPFFL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 253 DCLrksRVEFCHEEMRTEMEVLKQQVqiyeEDFKKERSDRERLNQEKEELQqiNETSQSQLNRLNSQIKACQMEKEKLEK 332
Cdd:cd09687 228 NSL---RVEEGKSALKIDVELIVTAL----EDFSEKIEDLEHIGLLKGKFA--NELEEIKELLADGGVESEVGIFEEIEK 298
|
...
gi 2462598919 333 QLK 335
Cdd:cd09687 299 AVE 301
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
103-337 |
2.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 103 RKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRS--MKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRE- 179
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELREleKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEk 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 180 --------DDRQRDLTRD--RLQREEKEKERLNEELHELKEENKLLKGK-NTLANKEKEHYECEIKRLNKALQDALNIKC 248
Cdd:PRK03918 530 lkekliklKGEIKSLKKEleKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 249 SFSEDCLRKSRVEFCHEEM----------RTEMEVLKQQVQIYEEDFKKErsDRERLNQEKEELQQINETSQSQLNRLNS 318
Cdd:PRK03918 610 AEKELEREEKELKKLEEELdkafeelaetEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELEK 687
|
250
....*....|....*....
gi 2462598919 319 QIKACQMEKEKLEKQLKQM 337
Cdd:PRK03918 688 RREEIKKTLEKLKEELEER 706
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
177-336 |
2.35e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 38.89 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 177 QREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKG-----KNTLA------NKEKEHYECEIKRLNKALQDAL- 244
Cdd:pfam05010 3 QKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKivaefEKTIAqmieekQKQKELEHAEIQKVLEEKDQALa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 245 ---NIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKE--RSDR------ERLNQEKEELQQINETSQSQL 313
Cdd:pfam05010 83 dlnSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEeqRYQAlkahaeEKLDQANEEIAQVRSKAKAET 162
|
170 180
....*....|....*....|...
gi 2462598919 314 NRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:pfam05010 163 AALQASLRKEQMKVQSLERQLEQ 185
|
|
| tape_meas_lam_C |
TIGR01541 |
phage tail tape measure protein, lambda family; This model represents a relatively ... |
109-209 |
2.51e-03 |
|
phage tail tape measure protein, lambda family; This model represents a relatively well-conserved region near the C-terminus of the tape measure protein of a lambda and related phage. This protein, which controls phage tail length, is typically about 1000 residues in length. Both low-complexity sequence and insertion/deletion events appear common in this family. Mutational studies suggest a ruler or template role in the determination of phage tail length. Similar behavior is attributed to proteins from distantly related or unrelated families in other phage. [Mobile and extrachromosomal element functions, Prophage functions]
Pssm-ID: 273681 [Multi-domain] Cd Length: 332 Bit Score: 39.82 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 109 SLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDA-------AERFLSTREKDPHQRQRKDDRQREDD 181
Cdd:TIGR01541 28 SRSDEIIALIKLEKLLEEAEQKALEALKKLAEATASIRAQNKRQLDRfglgdkqRERLDARLQIDRTFRKQQRDLNKAMT 107
|
90 100
....*....|....*....|....*....
gi 2462598919 182 RQRDLTRDRLQREE-KEKERLNEELHELK 209
Cdd:TIGR01541 108 AKGLAGSDLYKEQLaAIKASLNEALAELH 136
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
45-202 |
4.69e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 39.34 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 45 ILQQKNLLALSTLKCPGSCDYKKTPGKTASMAHFVQGtsrMIAAESSTEHKECAEPSTRKNLMNSLEQKIrcLEKQRKEL 124
Cdd:PTZ00266 388 ITSVTSVASVASVASVPSKDDRKYPQDGATHCHAVNG---HYGGRVDKDHAERARIEKENAHRKALEMKI--LEKKRIER 462
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462598919 125 LEvnqqwdqqfRSMKELYERKvaelktKLDAAERFLSTREKDPHQRQRKDDRQRED-DRQRDLTRDRLQREEKEKERLN 202
Cdd:PTZ00266 463 LE---------REERERLERE------RMERIERERLERERLERERLERDRLERDRlDRLERERVDRLERDRLEKARRN 526
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
122-316 |
5.62e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.17 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 122 KELLEvnqqwdqQFRSMKELYERkVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERL 201
Cdd:COG3096 498 RELLR-------RYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 202 NEELHELKEENKLLKgkntlanKEKEHYECEIKRLNK------ALQDALNIKCsfsedclrksrvEFCHEEMRTEMEVLK 275
Cdd:COG3096 570 EEQAAEAVEQRSELR-------QQLEQLRARIKELAArapawlAAQDALERLR------------EQSGEALADSQEVTA 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462598919 276 --QQVQIYEEDFKKERSD----RERLNQEKEELQQINETSQSQLNRL 316
Cdd:COG3096 631 amQQLLEREREATVERDElaarKQALESQIERLSQPGGAEDPRLLAL 677
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
102-336 |
6.09e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.18 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 102 TRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyerkvaELKTKLDAAERFLSTREKDPHQRQRKDDRQREDD 181
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY------QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 182 RQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQ---DALNIKCSFSEDCLRKS 258
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrkvDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462598919 259 RVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQL-NRLNSQIKACQMEKEKLEKQLKQ 336
Cdd:pfam02463 328 KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEsERLSSAAKLKEEELELKSEEEKE 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
107-222 |
6.21e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 107 MNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELyERKVAELKTKLDAAERFLSTREKDpHQRQRKDDRQREDDRQRDL 186
Cdd:COG4717 134 LEALEAELAELPERLEELEERLEELRELEEELEEL-EAELAELQEELEELLEQLSLATEE-ELQDLAEELEELQQRLAEL 211
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462598919 187 tRDRLQREEKEKERLNEELHELKEENKLLKGKNTLA 222
Cdd:COG4717 212 -EEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
181-337 |
6.68e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 181 DRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDAlnikcsfsedclrksrv 260
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA----------------- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598919 261 efcheemRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 337
Cdd:COG4372 93 -------QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
104-316 |
7.12e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 38.74 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 104 KNLMNSLEQKIRCL---EKQRKELLEVNQQWDQQFRSMKElYERKVAELKTKLD--AAERF--LSTREKDPHQRQRKDDR 176
Cdd:PRK11281 59 KLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQ-AQAELEALKDDNDeeTRETLstLSLRQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 177 QredDRQRDLT---------RDRLQREEKEkerLNEELHELKEENKLLkgKNTLANKEKEHYEcEIKRLNkALQDALNIK 247
Cdd:PRK11281 138 Q---NAQNDLAeynsqlvslQTQPERAQAA---LYANSQRLQQIRNLL--KGGKVGGKALRPS-QRVLLQ-AEQALLNAQ 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462598919 248 CSFSEDCLR---------KSRvefcHEEMRTEMEVLKQQVQIYEEDFKKERsdRERLNQEKEELQQINETSQSQLNRL 316
Cdd:PRK11281 208 NDLQRKSLEgntqlqdllQKQ----RDYLTARIQRLEHQLQLLQEAINSKR--LTLSEKTVQEAQSQDEAARIQANPL 279
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
104-337 |
8.42e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 37.97 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 104 KNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYE---RKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQRED 180
Cdd:COG1340 28 KEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDelnEKVKELKEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462598919 181 DRQRDLTRDRLQREEKEKERlneELHELKEENKLLKgknTLANKEKehyecEIKRLNKALQDALNIKCSFSEdcLRKSRV 260
Cdd:COG1340 108 GGSIDKLRKEIERLEWRQQT---EVLSPEEEKELVE---KIKELEK-----ELEKAKKALEKNEKLKELRAE--LKELRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462598919 261 EFchEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQM 337
Cdd:COG1340 175 EA--EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249
|
|
| |
