|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-339 |
1.45e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 13 DKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKmKELQAVRE 92
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-LELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 93 AlLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEAL 172
Cdd:COG1196 289 E-EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 173 TMVIQADKIKAAEIRSVYHLHQEEITRIkKECEREIRRLEQQLDEKDARRfqlkiAELSAIIRKLEDRNALLSEERNELL 252
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAA-AELAAQLEELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 253 KRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAgiirrpSSLNDLDQSQDEREIDFLKLQI 332
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL------LLLLEAEADYEGFLEGVKAALL 515
|
....*..
gi 1907184491 333 VEQQNLI 339
Cdd:COG1196 516 LAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-338 |
1.06e-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: 64.31 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 7 GSRAKGDKAETLAALQAANE--ELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHavlvtELKTKLHEEKM 84
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 85 KELQAVREALLRQHEAELLRVikikdnENQRLQALLNTLRDGApdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGA 164
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSK------ELTELEAEIEELEERL----------EEAEEELAEAEAEIEELEAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 165 KKQVEEALT---MVIQADKIKAAEIRSVYhlhqEEITRIKKECEREIRRLEQQLDEKDARRFQLK--IAELSAIIRKLED 239
Cdd:TIGR02168 798 LKALREALDelrAELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQIEELSEDIESLAaeIEELEELIEELES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 240 RNALLSEERNELLKRLREAESQYkplldknkrltrknEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslndLDQS 319
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSEL--------------EELSEELRELESKRSELRRELEELREKLAQLE-------LRLE 932
|
330
....*....|....*....
gi 1907184491 320 QDEREIDFLKLQIVEQQNL 338
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-313 |
1.08e-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: 60.84 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 16 ETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKsQELKQVREHEQRKHAVLVTELktkLHEEKMKELQAVREALL 95
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQL---EELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 96 RQHEAELLrvikikdNENQRLQALLNTLRdgapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMV 175
Cdd:TIGR02168 343 EEKLEELK-------EELESLEAELEELE-------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 176 IQADKikaaeirsvyhlHQEEITRIKKECEREIRRLEQQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRL 255
Cdd:TIGR02168 403 ERLEA------------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184491 256 REAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSSL 313
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-309 |
2.27e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 1 MSKKGAGSRAKGDKAETLAALQAANEELR-AKLTDIQIELQQEKSKVSKVEREKSQELK---QVREHEQRKHAVLVTELK 76
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKkadELKKAEELKKAEEKKKAE 1567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 77 TKLHEEKMKELQAVREALLRQHEAELLRVIKIKDNENQRLQAllNTLRDGAPDKVKTVLLCEAkEEAKKGFEVEKVKMQQ 156
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA--EEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAE 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 157 EISELKGAKKQVEEaltmviqaDKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDARRfqlKIAELsaiiRK 236
Cdd:PTZ00121 1645 EKKKAEELKKAEEE--------NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK---KAEEL----KK 1709
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184491 237 LEdrnallsEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRR 309
Cdd:PTZ00121 1710 KE-------AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
17-264 |
2.48e-08 |
|
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: 55.93 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 17 TLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRkhaVLVTELKTKLHEEKMKELqavrEALLR 96
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR---IAALARRIRALEQELAAL----EAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 97 QHEAELLRVIKIKDNENQRLQALLNTL-RDGAPDKVKTVLLCEAKEEAkkgfevekVKMQQEISELKGAKKQVEEALTMV 175
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDA--------VRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 176 IQADKIKAAEIRSvyhlHQEEITRIKKECEREIRRLEQQLDEKdarrfQLKIAELSAIIRKLEDRNALLSEERNELLKRL 255
Cdd:COG4942 159 LAELAALRAELEA----ERAELEALLAELEEERAALEALKAER-----QKLLARLEKELAELAAELAELQQEAEELEALI 229
|
....*....
gi 1907184491 256 REAESQYKP 264
Cdd:COG4942 230 ARLEAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-351 |
2.79e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQielQQEKSKVSKVEREKSQELKQVREhEQRKhavlVTELKTKLHEE 82
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK---KAEEAKKKAEEAKKADEAKKKAE-EAKK----ADEAKKKAEEA 1495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 83 KmKELQAVREALLRQHEAELLRvikiKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:PTZ00121 1496 K-KKADEAKKAAEAKKKADEAK----KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEIT------------RIKKE---CEREIRRLEQQLDEKDARrfQLKI 227
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeeakkaeeaKIKAEelkKAEEEKKKVEQLKKKEAE--EKKK 1648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 228 AELsaiIRKLEDRNALLSEErnelLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGII 307
Cdd:PTZ00121 1649 AEE---LKKAEEENKIKAAE----EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907184491 308 RRPSSLNDLDQSQDEREIDFLKLQIVEQQnlIDELSKVSMQHFR 351
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLK 1763
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-291 |
6.68e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 11 KGDKAETLAALQAANEELRAKLTDIQI-ELQQEKSKVSKVEREKSQELKQVREHEQRKHavlvteLKTKLHEEKMKELQA 89
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLT------LEKEYLEKEIQELQE 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 90 VREALlrqheaellrviKIKDNENQRLQALLNTlrdgapDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVE 169
Cdd:TIGR02169 841 QRIDL------------KEQIKSIEKEIENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 170 EA---LTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDarrFQLKIAELSAIIRKLEDRNALLSE 246
Cdd:TIGR02169 903 RKieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED---VQAELQRVEEEIRALEPVNMLAIQ 979
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907184491 247 ERNELLKRLREaesqykpLLDKNKRLTRKNEDLSHTLRRIESKLK 291
Cdd:TIGR02169 980 EYEEVLKRLDE-------LKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
6-360 |
1.21e-07 |
|
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: 54.21 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 6 AGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSkvSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMK 85
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 86 ELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAK 165
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 166 KQVE--EALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDArRFQLKIAELSAIIRKLEDRNAL 243
Cdd:pfam02463 321 KEKKkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA-KKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 244 LSEERNELLKRLREAESQykpLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAgiirrpSSLNDLDQSQDER 323
Cdd:pfam02463 400 KSEEEKEAQLLLELARQL---EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE------LKLLKDELELKKS 470
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907184491 324 EIDFLKLQIVEQQNLIDELSKVSMQHFRAVLSCVRRS 360
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
339-458 |
1.25e-07 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 52.94 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 339 IDELSKVSMQHFRAVLSCVRR-------SHAPCCPVPSGATPPTAlcPPEPRPLLPCAlrSHAPYCPvPSGATT--PTAL 409
Cdd:PHA02682 55 VKEAGRYYQSRLKANSACMQRpsgqsplAPSPACAAPAPACPACA--PAAPAPAVTCP--APAPACP-PATAPTcpPPAV 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907184491 410 CPPEPRPllpcalrghAPCCPVHSLK------LPSPDSLCPSRavPLLTAHSLLP 458
Cdd:PHA02682 130 CPAPARP---------APACPPSTRQcppappLPTPKPAPAAK--PIFLHNQLPP 173
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-349 |
1.36e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQV----------REHEQRKHAVLV 72
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAeekkkaeeakKAEEDKNMALRK 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 73 TELKTKLHEEKMKELQAVREAL-------LRQHEAELLRVIKIKDNENQRLQalLNTLRDGAPDKVKTVllceakEEAKK 145
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEkkmkaeeAKKAEEAKIKAEELKKAEEEKKK--VEQLKKKEAEEKKKA------EELKK 1654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 146 GFEVEKVKMQQEISELKGAKKQVEEALTMviQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDARRFQL 225
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKA--EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 226 KIAELSAIIRKLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNE-DLSHTLRRIESKLKFV-TQENIEMRQR 303
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKdIFDNFANIIE 1812
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907184491 304 AGIIRRPsSLNDLDQSQDErEIDflklQIVEQQNLIDELSKVSMQH 349
Cdd:PTZ00121 1813 GGKEGNL-VINDSKEMEDS-AIK----EVADSKNMQLEEADAFEKH 1852
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-324 |
1.74e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 7 GSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREkSQELKQVREHEQRKHAVLVTELKT-KLHEEKMK 85
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR-LDELSQELSDASRKIGEIEKEIEQlEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 86 ELQAVREALLRQHEAELLRVI-KIKDNEN--QRLQALLNTLRDgAPDKVKTVLLCEAKEEAKKgfevEKVKMQQEISELK 162
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKsELKELEAriEELEEDLHKLEE-ALNDLEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 163 GAKKQVEEALTMVIQADKIKAAEIrsvyhlhqEEITRIKKECEREIRRLEQQLDE--KDARRFQLKIAELSAIIRKLEDR 240
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEI--------QELQEQRIDLKEQIKSIEKEIENlnGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 241 NALLSEERNELLKRLREAESQYkplldknKRLTRKNEDLSHTLRRIESKLKFVTQENIEM-RQRAGIIRRPSSLNDLDQS 319
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKI-------EELEAQIEKKRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDV 956
|
....*
gi 1907184491 320 QDERE 324
Cdd:TIGR02169 957 QAELQ 961
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-258 |
1.96e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 13 DKAETLAALQAANEELRAKLTDIQiELQQEKSKVSKVERE-KSQELKQVREHEQRKHAVLvtelktklhEEKMKELQAVR 91
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLA-ELEYLRAALRLWFAQrRLELLEAELEELRAELARL---------EAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 92 EALlRQHEAELLRviKIKDNENQRLQALLNTLRDgapdkvktvllceakeeakkgfevekvkMQQEISELKGAKKQVEEA 171
Cdd:COG4913 319 DAL-REELDELEA--QIRGNGGDRLEQLEREIER----------------------------LERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 172 LTMViqadKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDARRFQLK--IAELSAIIRKLEDRNALLSEERN 249
Cdd:COG4913 368 LAAL----GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRreLRELEAEIASLERRKSNIPARLL 443
|
....*....
gi 1907184491 250 ELLKRLREA 258
Cdd:COG4913 444 ALRDALAEA 452
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-344 |
3.17e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 48 KVEREKS-QELKQVREHEQRKHAVLvTELKTKLHE--------EKMKELQAvrEALLRQHEAELLRvIKIKDNENQRLQA 118
Cdd:COG1196 171 KERKEEAeRKLEATEENLERLEDIL-GELERQLEPlerqaekaERYRELKE--ELKELEAELLLLK-LRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 119 LLntlrdgapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTmviqadkikaaEIRSVYHLHQEEIT 198
Cdd:COG1196 247 EL-----------------EELEAELEELEAELAELEAELEELRLELEELELELE-----------EAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 199 RIKKECEREIRRLEQQLDEKDarRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQykpLLDKNKRLTRKNED 278
Cdd:COG1196 299 RLEQDIARLEERRRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAE 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184491 279 LSHTLRRIESKLKfvtQENIEMRQRAGIIRRPSSLNDLDQSQDEREIDFLKLQIVEQQNLIDELSK 344
Cdd:COG1196 374 LAEAEEELEELAE---ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
25-350 |
4.58e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.28 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 25 NEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREAlLRQHEAELLR 104
Cdd:TIGR01612 691 NTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILED-FKNKEKELSN 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 105 VIKIKDNENQRL---QALLNTLRDGAPDKVKTVLLCEakEEAKKGFE----------VEKVKMQQEISELKGAKKQVEEA 171
Cdd:TIGR01612 770 KINDYAKEKDELnkyKSKISEIKNHYNDQINIDNIKD--EDAKQNYDkskeyiktisIKEDEIFKIINEMKFMKDDFLNK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 172 LTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREirrleqqldekdarrfQLKIAElsaiiRKLEDRNALLSEERNEL 251
Cdd:TIGR01612 848 VDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDD----------------KLNDYE-----KKFNDSKSLINEINKSI 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 252 LKRLREAESQYKplLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSS---LNDLDQSQDEREIDFL 328
Cdd:TIGR01612 907 EEEYQNINTLKK--VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKdkfDNTLIDKINELDKAFK 984
|
330 340
....*....|....*....|..
gi 1907184491 329 KLQIVEQQNLIDELskvsMQHF 350
Cdd:TIGR01612 985 DASLNDYEAKNNEL----IKYF 1002
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
25-344 |
4.96e-06 |
|
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: 48.86 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 25 NEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKelqavrealLRQHEAELLR 104
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKK---------LEEIQNQISQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 105 VIKIKDNENQRLQALLNTLRDGAPDKVKtvllcEAKEEAKKGFEVEKVKMQ-----QEISELKGAKKQVEEALTMVIQAD 179
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSE-----KQRELEEKQNEIEKLKKEnqsykQEIKNLESQINDLESKIQNQEKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 180 KIKAAEIRSV---YHLHQEEITRIKKECER---EIRRLEQQLDEK-------DARRFQLK--IAELSAIIRK----LEDR 240
Cdd:TIGR04523 408 QQKDEQIKKLqqeKELLEKEIERLKETIIKnnsEIKDLTNQDSVKeliiknlDNTRESLEtqLKVLSRSINKikqnLEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 241 NALLSEERNELLK---RLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQragiirrpsslnDLD 317
Cdd:TIGR04523 488 QKELKSKEKELKKlneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF------------ELK 555
|
330 340
....*....|....*....|....*..
gi 1907184491 318 QSQDEREIDFLKLQIVEQQNLIDELSK 344
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKK 582
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-233 |
9.50e-06 |
|
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: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKskvsKVEREKSQELKQVREHEQRKHAVLVTELKTKlhEE 82
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEEAEEELEEA--EA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 83 KMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDgapdkvktvllCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-----------LEELEEAEEALLERLERLEEELEELE 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184491 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKEcEREIRRLEQQLDEKDARRFQLKIAELSAI 233
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-324 |
1.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 3 KKGAGSRAKGDKAETLAALQAANE----ELRAKLTDIQIELQQEKSKVSKV---EREKSQELKQVREHEQRK-HAVLVTE 74
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEaeaaEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEEDKKKaDELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 75 LKTKLHEEKMKELQAVREALLRQHEAELLRV---IKIKDNENQRLQallnTLRDGAPDKVKTVLLCEAKEEAKKGFEVEK 151
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 152 -----VKMQQEISELKGAKKQVEEALTM--VIQADKI-KAAEIRSVYHLHQEEITRIKKECER--------EIRRLEQQL 215
Cdd:PTZ00121 1491 kaeeaKKKADEAKKAAEAKKKADEAKKAeeAKKADEAkKAEEAKKADEAKKAEEKKKADELKKaeelkkaeEKKKAEEAK 1570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 216 DEKDARRFQLKIAElsaIIRKLEdrnallsEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQ 295
Cdd:PTZ00121 1571 KAEEDKNMALRKAE---EAKKAE-------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
330 340
....*....|....*....|....*....
gi 1907184491 296 ENIEMRQRAGIIRRPSSLNDLDQSQDERE 324
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
4-296 |
1.08e-05 |
|
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: 48.19 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 4 KGAGSRAKGDKAETLAALQAANEELRaKLTDIQIELQQEKSKVSKVEREKSQElKQVREHEQRKhavlVTELKTKLHEEK 83
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERT----VSDLTASLQEKE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 84 mkelqavreallRQHEAELLRVIKIKDNENQRLQALLNTLRDGapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKG 163
Cdd:pfam15921 510 ------------RAIEATNAEITKLRSRVDLKLQELQHLKNEG-----------DHLRNVQTECEALKLQMAEKDKVIEI 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 164 AKKQVEEALTMVIQADKIKAAEIRSVYHLHQE---------EITRIKKECEREIRRLEQQLDEKDARRFQLKIAElSAII 234
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrrlelqEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG-SERL 645
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184491 235 RKLEDrnalLSEERNELLKRLREAESQYKPLLDKNKRLTR----KNEDLSHTLRRIESKLKFVTQE 296
Cdd:pfam15921 646 RAVKD----IKQERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSE 707
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-344 |
2.54e-05 |
|
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: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 15 AETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREAL 94
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 95 LRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKK-------- 166
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpl 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 167 ---------------QVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDARRFQLKIAEL- 230
Cdd:COG1196 580 dkiraraalaaalarGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAg 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 231 -SAIIRKLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRR 309
Cdd:COG1196 660 gSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
330 340 350
....*....|....*....|....*....|....*
gi 1907184491 310 PSSLNDLDQSQDEREIDFLKLQIVEQQNLIDELSK 344
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
35-296 |
2.56e-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: 46.94 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 35 IQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAvLVTELK-----TKLHEEKMKELQAVREALLRQHEAELLRVIK-- 107
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQnqeklNQQKDEQIKKLQQEKELLEKEIERLKETIIKnn 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 108 --IKDNENQRLQ-----ALLNTLRDGAPDKVKTVLLCEAKEEAK-KGFEVEKVKMQQEISELKGAKKQVEE--------- 170
Cdd:TIGR04523 440 seIKDLTNQDSVkeliiKNLDNTRESLETQLKVLSRSINKIKQNlEQKQKELKSKEKELKKLNEEKKELEEkvkdltkki 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 171 -ALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREirRLEQQLDEKDARRFQLK--IAELSAIIRKLEDRNALLSEE 247
Cdd:TIGR04523 520 sSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE--NLEKEIDEKNKEIEELKqtQKSLKKKQEEKQELIDQKEKE 597
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907184491 248 RNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQE 296
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-258 |
2.82e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 18 LAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVlvtelktklhEEKMKELQAVREALlRQ 97
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL----------SEDIESLAAEIEEL-EE 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 98 HEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVllceakeeakKGFEVEKVKMQQEISELKGAKKQVEEALT-MVI 176
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEEL----------RELESKRSELRRELEELREKLAQLELRLEgLEV 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 177 QADKIKAAeIRSVYHL-------HQEEITRIKKECEREIRRLEQQLDEkdarrfqLKIAELSAI--IRKLEDRNALLSEE 247
Cdd:TIGR02168 937 RIDNLQER-LSEEYSLtleeaeaLENKIEDDEEEARRRLKRLENKIKE-------LGPVNLAAIeeYEELKERYDFLTAQ 1008
|
250
....*....|....
gi 1907184491 248 RNEL---LKRLREA 258
Cdd:TIGR02168 1009 KEDLteaKETLEEA 1022
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-303 |
3.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 84 MKELQAVREALLRQHE-AELLRVIKIKDNENQRLQALLNTLRDgapdkVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:COG4913 234 FDDLERAHEALEDAREqIELLEPIRELAERYAAARERLAELEY-----LRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 163 GAKKQVEEALTmviQADkikaAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDARRFQLK-------------IAE 229
Cdd:COG4913 309 AELERLEARLD---ALR----EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEallaalglplpasAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184491 230 LSAIIRKLEDRNALLSEERNELLKRLREAESQYkplldknKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQR 303
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAAL-------RDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
339-449 |
3.59e-05 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 45.62 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 339 IDELSKVSMQHFRAVLSCVRRSHAPCCPVPSGATP--PTALCPPePRPLLPcalrSHAPYCPVPsgattptALCPPEPRP 416
Cdd:PHA02682 47 VDPLDKYSVKEAGRYYQSRLKANSACMQRPSGQSPlaPSPACAA-PAPACP----ACAPAAPAP-------AVTCPAPAP 114
|
90 100 110
....*....|....*....|....*....|...
gi 1907184491 417 LLPCALrghAPCCPvhslklpsPDSLCPSRAVP 449
Cdd:PHA02682 115 ACPPAT---APTCP--------PPAVCPAPARP 136
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
143-291 |
4.56e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 143 AKKGFEVEKVKmqqeISELKGakKQVEEALTMVIQADKikaAEIRSVYHLHQEEITRIKKECEREIRRLEQQLD--EKDA 220
Cdd:COG2433 359 VPPDVDRDEVK----ARVIRG--LSIEEALEELIEKEL---PEEEPEAEREKEHEERELTEEEEEIRRLEEQVErlEAEV 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184491 221 RRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESqykplLDK-NKRLTRKNEDLSHTLRRIESKLK 291
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEARSEERREIRKDREISR-----LDReIERLERELEEERERIEELKRKLE 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-296 |
5.51e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 14 KAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEReksqELKQVREHEQRkhavlVTELKTKLhEEKMKELQAVREa 93
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE----RIKELEEKEER-----LEELKKKL-KELEKRLEELEE- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 94 llrqhEAELLRVIKIKDNENQRLQALLNTLrdgAPDKVKTVLlcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALT 173
Cdd:PRK03918 360 -----RHELYEEAKAKKEELERLKKRLTGL---TPEKLEKEL--EELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 174 MVIQADKIKAAEIRSVYHLHQEEitrIKKECEREIRRLEQQLDEKDARRFQLKiAELSAIIRKLEDRNALLSEErnELLK 253
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKE---LLEEYTAELKRIEKELKEIEEKERKLR-KELRELEKVLKKESELIKLK--ELAE 503
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907184491 254 RLREAESQYKPL-LDKNKRLTRKNEDLSHTLRRIESKLKFVTQE 296
Cdd:PRK03918 504 QLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
13-222 |
6.06e-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: 45.83 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 13 DKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVErEKSQELKQVREHEQRKHAVLVTELKTKlhEEKMKELQAVRE 92
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-EEYAELKEELEDLRAELEEVDKEFAET--RDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 93 ALLRQHEaELLRVIKIKDNENQRLQALLNTLRDGAPDKvktvllceakEEAKKGFEVEKVKMQQEISELKGAKKQveeal 172
Cdd:TIGR02169 396 KLKREIN-ELKRELDRLQEELQRLSEELADLNAAIAGI----------EAKINELEEEKEDKALEIKKQEWKLEQ----- 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907184491 173 tmvIQADKIKAaeiRSVYHLHQEEITRIkkecEREIRRLEQQLDEKDARR 222
Cdd:TIGR02169 460 ---LAADLSKY---EQELYDLKEEYDRV----EKELSKLQRELAEAEAQA 499
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-342 |
6.68e-05 |
|
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: 45.48 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 16 ETLAALQAANEELRAKLTDIQIELQQEKSkvskvEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVRealL 95
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSS-----ELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE---L 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 96 RQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVllceakEEAKKGFEVEKVKMQQEISE----LKGAKKQVEEA 171
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEV------EDLKTELEKEKLKNIELTAHcdklLLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 172 LTMVIQADKikaaeirsvyhlHQEEITRIKKECEREIRRLEqQLDEKDArrfQLKiAELSAIIRKLEDRNallSEERNEL 251
Cdd:pfam05483 509 SDMTLELKK------------HQEDIINCKKQEERMLKQIE-NLEEKEM---NLR-DELESVREEFIQKG---DEVKCKL 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 252 LKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTqeniEMRQRAGIIRRPSSLNDLDQSQDEREIDFLKLQ 331
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE----ELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
330
....*....|.
gi 1907184491 332 IVEQQNLIDEL 342
Cdd:pfam05483 645 LASAKQKFEEI 655
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
39-342 |
8.43e-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: 45.11 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 39 LQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHE-EKMKELQAVREALLRqheAELLRVIKIKDNENQRLQ 117
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaEKARQAEMDRQAAIY---AEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 118 allntlRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEI------SELKGAKKQ--VEEALTMVIQADKIKAAEIRSV 189
Cdd:pfam17380 355 ------QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervrQELEAARKVkiLEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 190 Y-HLHQEEITRIKKECEREIRRLEQQLDEKDARRFQLKIAELSAIIRKLE-----DRNALLSEERNELLKRLREAESQyK 263
Cdd:pfam17380 429 QeEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLElekekRDRKRAEEQRRKILEKELEERKQ-A 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 264 PLLDKNKR--LTRKNEDLSHTL----RRIESKLKFVTQENIEMRQR--AGIIRRPSSLNDLDQSQDEREidfLKLQIVEQ 335
Cdd:pfam17380 508 MIEEERKRklLEKEMEERQKAIyeeeRRREAEEERRKQQEMEERRRiqEQMRKATEERSRLEAMERERE---MMRQIVES 584
|
....*..
gi 1907184491 336 QNLIDEL 342
Cdd:pfam17380 585 EKARAEY 591
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
9-263 |
8.61e-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: 45.42 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 9 RAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQ--ELKQVREHEQRKHAVLVTELKTKLHEEKMKE 86
Cdd:TIGR00606 829 QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQigTNLQRRQQFEEQLVELSTEVQSLIREIKDAK 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 87 LQAV-REALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKV---KTVL--LCEAKEEAKKGFEVEKVKMQQEISE 160
Cdd:TIGR00606 909 EQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymKDIEnkIQDGKDDYLKQKETELNTVNAQLEE 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 161 LKGAKKQVEEALTMVIQAdkIKAAEIRSvyHLHQEEITRIKKEceREIRRLEQQLDEKDARRFQLKIAELSAIIRKLEDR 240
Cdd:TIGR00606 989 CEKHQEKINEDMRLMRQD--IDTQKIQE--RWLQDNLTLRKRE--NELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEEN 1062
|
250 260
....*....|....*....|...
gi 1907184491 241 NALLSEERNELLKRLREAESQYK 263
Cdd:TIGR00606 1063 IDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
26-261 |
8.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 26 EELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRkhavlVTELKTKLhEEKMKELQAVREALLRQHE--AELL 103
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-----LEALQAEI-DKLQAEIAEAEAEIEERREelGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 104 RVIKIKDNENQRLQALLNTlrDGAPDKVKTVLLceakeeakkgfeVEKV--KMQQEISELKGAKKQVEEALTMVIQAdki 181
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGS--ESFSDFLDRLSA------------LSKIadADADLLEELKADKAELEAKKAELEAK--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 182 kaaeirsvyhlhQEEITRIKKECEREIRRLEQQLDEKDArrfqlKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQ 261
Cdd:COG3883 156 ------------LAELEALKAELEAAKAELEAQQAEQEA-----LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
11-298 |
9.90e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 11 KGDKAETLAALQAAN----EELRAKLTDIQI-ELQQEKSKVSkverEKSQELKQVREHEQrkhavLVTELKTKLHEEKMK 85
Cdd:PRK05771 15 KSYKDEVLEALHELGvvhiEDLKEELSNERLrKLRSLLTKLS----EALDKLRSYLPKLN-----PLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 86 ELQAVREALLRQHEAELLRVI-KIK--DNENQRLQALLNTLrdgapDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEeEISelENEIKELEQEIERL-----EPWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 163 GAKKQVEEALTmviqadkIKAAEIRSVYhlhqeeITRIKKECEREIRRLeqqLDEKDARRFQLK-IAELSAIIRKLEDRN 241
Cdd:PRK05771 161 KLESDVENVEY-------ISTDKGYVYV------VVVVLKELSDEVEEE---LKKLGFERLELEeEGTPSELIREIKEEL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184491 242 ALLSEERNELLKRLREAESQYKPLLDKNKrltrknEDLSHTLRRIESKLKFVTQENI 298
Cdd:PRK05771 225 EEIEKERESLLEELKELAKKYLEELLALY------EYLEIELERAEALSKFLKTDKT 275
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
12-287 |
1.33e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 12 GDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEqrkhaVLVTELKTKLHEEKMKELQAVR 91
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE-----AQISELQEDLESERAARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 92 EallRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKtvLLCEAKEEAKKGFEVEKVKMQQE-ISELKGAKKQVEE 170
Cdd:pfam01576 293 Q---RRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVT--ELKKALEEETRSHEAQLQEMRQKhTQALEELTEQLEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 171 ALTMVIQADKIKAAEIRSVYHLHQE--EITRIKKECEREIRRLEQQLDE-----KDARRFQLKIAE-LSAIIRKLEDRNA 242
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAElrTLQQAKQDSEHKRKKLEGQLQElqarlSESERQRAELAEkLSKLQSELESVSS 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907184491 243 LLSEERNELLKRLREAESQYKPLLDKNKRL---TRKNEDLSHTLRRIE 287
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTRLRQLE 495
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
11-331 |
1.50e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 44.35 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 11 KGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVS------KVEREKSQELKQVREHEQRKHAVLvtelktKLHEEKM 84
Cdd:pfam05557 99 LADAREVISCLKNELSELRRQIQRAELELQSTNSELEelqerlDLLKAKASEAEQLRQNLEKQQSSL------AEAEQRI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 85 KEL------QAVREALLRQHEAELLRVIKIkDNENQRLQALLNTLRDGAPDKvktVLLCEAKEEAKKGFEVEKvKMQQEI 158
Cdd:pfam05557 173 KELefeiqsQEQDSEIVKNSKSELARIPEL-EKELERLREHNKHLNENIENK---LLLKEEVEDLKRKLEREE-KYREEA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 159 SELKGAKKQVEEALTMVIQADKIKAAEIRS-------VYHLHQEEITRIK---------KECEREIRRLEQQLDE--KDA 220
Cdd:pfam05557 248 ATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlsrrIEQLQQREIVLKEenssltssaRQLEKARRELEQELAQylKKI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 221 RRFQLKIAELSAIIRKLEDRNALLSEERNeLLKRLREAesqykplLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEM 300
Cdd:pfam05557 328 EDLNKKLKRHKALVRRLQRRVLLLTKERD-GYRAILES-------YDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEM 399
|
330 340 350
....*....|....*....|....*....|.
gi 1907184491 301 RQRAGIIRRPSSLNDLDQSQDEREIDFLKLQ 331
Cdd:pfam05557 400 EAQLSVAEEELGGYKQQAQTLERELQALRQQ 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-344 |
1.56e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 26 EELRAKLTDIQIELQQEKSKVSKVEREKS---QELKQVReHEQRKHAVLVTELKTKlhEEKMKELQAVREALLRQHEaEL 102
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLniqKNIDKIK-NKLLKLELLLSNLKKK--IQKNKSLESQISELKKQNN-QL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 103 LRVIKIKDNENQRLQALLNTlrdgAPDKVKTVllceaKEEAKKgfevEKVKMQQEISELKGAKKQVEEaLTMVIQadKIK 182
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISN----TQTQLNQL-----KDEQNK----IKKQLSEKQKELEQNNKKIKE-LEKQLN--QLK 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 183 AaEIRSVYHLHQEEITRIKKE----CEREIRRLEQQLDEKdarrfQLKIAELSAIIRKLEDRNALLSEERNELLKRLREA 258
Cdd:TIGR04523 295 S-EISDLNNQKEQDWNKELKSelknQEKKLEEIQNQISQN-----NKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 259 ESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslndLDQSQDEREIDFLKLQIVEQQNL 338
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ-------QEKELLEKEIERLKETIIKNNSE 441
|
....*.
gi 1907184491 339 IDELSK 344
Cdd:TIGR04523 442 IKDLTN 447
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
191-342 |
2.42e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 191 HLHQEeitriKKECEREIRRLEQQLDEKDARRFQL---------KIAELSAIIRKLEDRNALLSEERNELLKRLREAESQ 261
Cdd:pfam01576 93 QLQNE-----KKKMQQHIQDLEEQLDEEEAARQKLqlekvtteaKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 262 YKPLLDKNKRLTRKNEDLSHTLRRIESKLKfvtqENIEMRQRAGIIRRpsslndldqsQDEREIDFLKLQIVEQQNLIDE 341
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLK----KEEKGRQELEKAKR----------KLEGESTDLQEQIAELQAQIAE 233
|
.
gi 1907184491 342 L 342
Cdd:pfam01576 234 L 234
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
21-297 |
3.00e-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: 43.56 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 21 LQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVrEHEQRKHAVLVTELKTkLHEEKMKELQAVREALLRQHEA 100
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI-ENLEEKEMNLRDELES-VREEFIQKGDEVKCKLDKSEEN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 101 ELLRVIKIKDNENQR--LQALLNTLRDGAPDKVKTV--LLCEAKEEAKKG------FEVEKVKMQQEISELKGAKKQVEE 170
Cdd:pfam05483 575 ARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIeeLHQENKALKKKGsaenkqLNAYEIKVNKLELELASAKQKFEE 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 171 altmvIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDekdaRRFQLKIAELSAIIRKLEDRNALLSEERNE 250
Cdd:pfam05483 655 -----IIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID----KRCQHKIAEMVALMEKHKHQYDKIIEERDS 725
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184491 251 ---LLKRLREAESQYKPLLD------KNKRLTRKNEdlSHTLRRIESKLKFVTQEN 297
Cdd:pfam05483 726 elgLYKNKEQEQSSAKAALEielsniKAELLSLKKQ--LEIEKEEKEKLKMEAKEN 779
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-291 |
3.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 154 MQQEISELKGAKKQVEEAltmviqADKIKA-AEIRSVYHLHQEEITRIkKECEREIRRLEQQLDEKDARRFQLKIAELSA 232
Cdd:COG4913 230 LVEHFDDLERAHEALEDA------REQIELlEPIRELAERYAAARERL-AELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 233 IIRKLEDRNALLSEERNELLKRLREAESQYKPL-LDKNKRLTRKNEDLSHTLRRIESKLK 291
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRA 362
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
23-304 |
3.38e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 23 AANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVrEHEQRKHAVLVTELKTKlhEEKMKELQAVREALLRQHEAEL 102
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL-EKASREETFARTALKNA--RLDLRRLFDEKQSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 103 LRVIKIKDNENQRLQALLNTLRDGAPDkvktvllceAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTmviqadkik 182
Cdd:pfam12128 674 AERKDSANERLNSLEAQLKQLDKKHQA---------WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLK--------- 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 183 aAEIRSVYHLHQEEITRIKKECEREIRRLEqqLDEKDARRFQLKIAELSAIIRKLE-DRNALLSEERnellkRLREAESQ 261
Cdd:pfam12128 736 -AAIAARRSGAKAELKALETWYKRDLASLG--VDPDVIAKLKREIRTLERKIERIAvRRQEVLRYFD-----WYQETWLQ 807
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907184491 262 YKPLLDKNKRLT-RKNEDLSHTLRRIESKLKFVTQeNIEMRQRA 304
Cdd:pfam12128 808 RRPRLATQLSNIeRAISELQQQLARLIADTKLRRA-KLEMERKA 850
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
146-286 |
4.49e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 146 GFEVEKVKMQQEISELKG-AKKQVEEAltmVIQADKIKAAEIRSVyhlhQEEITRIKKECEREIRRLEQQLDEKDARrfq 224
Cdd:PRK12704 21 GYFVRKKIAEAKIKEAEEeAKRILEEA---KKEAEAIKKEALLEA----KEEIHKLRNEFEKELRERRNELQKLEKR--- 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184491 225 LKIAElsaiiRKLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRI 286
Cdd:PRK12704 91 LLQKE-----ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-265 |
7.44e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 37 IELQQEKSKVSKVEREKSQELKQVREHEQR--KHAVLVTELKTKLH--EEKMKELqavrEALLRQHEaELLRVIKIKDNE 112
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKEleELKEEIEELEKELEslEGSKRKL----EEKIRELE-ERIEELKKEIEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 113 NQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEaltmviqaDKIKAAEIRSVYHL 192
Cdd:PRK03918 278 LEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE--------KEERLEELKKKLKE 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907184491 193 HQEEITRIKKECE--REIRRLEQQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQYKPL 265
Cdd:PRK03918 350 LEKRLEELEERHElyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-352 |
7.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 7.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEE 82
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 83 KMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEkvKMQQEISELK 162
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 163 GAKKQVEEALTMviQADKIKAAEIRSVYHLhqeeitriKKECErEIRRLEQQldEKDARRFQLKIAELSAIIRKLEDRNA 242
Cdd:PTZ00121 1448 EAKKKAEEAKKA--EEAKKKAEEAKKADEA--------KKKAE-EAKKADEA--KKKAEEAKKKADEAKKAAEAKKKADE 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 243 LLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDL--SHTLRRIESKLKfVTQENIEMRQRAGIIRRPSslnDLDQSQ 320
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKAEEKKK-AEEAKKAEEDKNMALRKAE---EAKKAE 1590
|
330 340 350
....*....|....*....|....*....|..
gi 1907184491 321 DEREIDFLKLQIVEQQNLIDELSKVSMQHFRA 352
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
351-466 |
8.69e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 351 RAVLSCVRRSHAPCCPVPSGATPPTALCPPEPRPLLPCALRSHAPYCP-------VPSGATTPTALCPPEPRPLLPCALR 423
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPaapappaVPAGPATPGGPARPARPPTTAGPPA 2768
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907184491 424 GHAPCCPVHSlklpspdslcPSRAVPLLTAHSLLPYLLSTPHP 466
Cdd:PHA03247 2769 PAPPAAPAAG----------PPRRLTRPAVASLSESRESLPSP 2801
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
81-183 |
1.06e-03 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 40.75 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 81 EEKMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKtvllCEAKEEAKKgFEVEKVKMQQEISE 160
Cdd:pfam03961 140 GTKTEIEVGVDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLP----PEKREQLEK-LLETKNKLSEELEE 214
|
90 100
....*....|....*....|...
gi 1907184491 161 LKGAKKQVEEALTMVIQADKIKA 183
Cdd:pfam03961 215 LEEELKELKEELESLLGEGKISV 237
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
22-185 |
1.22e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 22 QAANEELRAKLTDIQIELQQEKsKVSKVEREKSQELKQVREHEQRKHAVlvtelktklheekmkelQAVREALLRQHEAE 101
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAE-----------------EAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 102 llrvikikdnENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEiselkGAKKQVEEALTMVIQADKI 181
Cdd:PRK09510 136 ----------EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAA-----EAKKKAEAEAAAKAAAEAK 200
|
....
gi 1907184491 182 KAAE 185
Cdd:PRK09510 201 KKAE 204
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
138-340 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 138 EAKEEAKKGFEVEKVKMQQEISELKGAKKQVEE---ALTMVIQA--DKIKAAEIRSVYHLHQEEITRIK----------- 201
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQErreALQRLAEYswDEIDVASAEREIAELEAELERLDassddlaalee 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 202 --KECEREIRRLEQQLDEKDARRFQL--KIAELSAIIRKLEDR----NALLSEERNELLKRLREAESQYKPLLDKNKRLT 273
Cdd:COG4913 693 qlEELEAELEELEEELDELKGEIGRLekELEQAEEELDELQDRleaaEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184491 274 RKNEDLSHTLRRIESKLkfvtqenieMRQRAGIIRR-PSSLNDLDQSQDEREiDFLK-LQIVEQQNLID 340
Cdd:COG4913 773 ERIDALRARLNRAEEEL---------ERAMRAFNREwPAETADLDADLESLP-EYLAlLDRLEEDGLPE 831
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
26-291 |
1.73e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.04 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 26 EELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVRE--HEQRKHAVLVT----ELKTKLHEEKMKELQAVREalLRQHE 99
Cdd:pfam15964 399 EELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEaqKQLASQEMDVTkvcgEMRYQLNQTKMKKDEAEKE--HREYR 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 100 AELLRVIKIKDNENQRL--------QALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEV---EKVKMQQEISELKGAK--- 165
Cdd:pfam15964 477 TKTGRQLEIKDQEIEKLglelseskQRLEQAQQDAARAREECLKLTELLGESEHQLHLtrlEKESIQQSFSNEAKAQalq 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 166 -KQVEEALT-----MVIQADKiKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDARRFQLKIAE--LSAIIRKL 237
Cdd:pfam15964 557 aQQREQELTqkmqqMEAQHDK-TVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKeyLQDRLEKL 635
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184491 238 EDRNALLSEE--------------RNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLK 291
Cdd:pfam15964 636 QKRNEELEEQcvqhgrmhermkqrLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQVP 703
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
168-292 |
1.96e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 168 VEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLEQQLDEKDARRFQLKIAE--LSAIIRKLEDRNALLS 245
Cdd:PRK12705 43 QKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEnqLEEREKALSARELELE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907184491 246 EERNELLKRLREA-----ESQYKPLLdknKRLTRK-NEDLSHTLRRIESKLKF 292
Cdd:PRK12705 123 ELEKQLDNELYRVagltpEQARKLLL---KLLDAElEEEKAQRVKKIEEEADL 172
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
8-213 |
2.16e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 8 SRAKGDKAETLAA--LQAANEELRAKLTDIQIELQQE----KSKVSKVEREKSQELKQVREHEQRKHAVLvtELKTKLHE 81
Cdd:PRK12704 29 AEAKIKEAEEEAKriLEEAKKEAEAIKKEALLEAKEEihklRNEFEKELRERRNELQKLEKRLLQKEENL--DRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 82 EKMKELQAVREALLRQHE-AELLR--VIKIKDNENQRLQALLNTLRDGApdkvKTVLLCEAKEEAKKgfevEKVKMQQEI 158
Cdd:PRK12704 107 KREEELEKKEKELEQKQQeLEKKEeeLEELIEEQLQELERISGLTAEEA----KEILLEKVEEEARH----EAAVLIKEI 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184491 159 SEL--KGAKKQVEEALTMVIQ---ADkiKAAEIR-SVYHLHQEEIT-R-IKKEcEREIRRLEQ 213
Cdd:PRK12704 179 EEEakEEADKKAKEILAQAIQrcaAD--HVAETTvSVVNLPNDEMKgRiIGRE-GRNIRALET 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
21-268 |
2.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 21 LQAANEELRAKLTDIQIELQQEKSKVSKVEreksQELKQVREheqrKHAVLVTELKTKLHEEKMKELQAVREALLRQHEA 100
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQ----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 101 ELLRVikikdnenQRLQALLNTLRDGAPDKVKTVLLceakeeakkgfevekVKMQQEISELKGAKKQVEEALTmvIQADK 180
Cdd:COG3206 238 AEARL--------AALRAQLGSGPDALPELLQSPVI---------------QQLRAQLAELEAELAELSARYT--PNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 181 IKAAeirsvyhlhQEEITRIKKECEREIRRLEQQLdEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAE- 259
Cdd:COG3206 293 VIAL---------RAQIAALRAQLQQEAQRILASL-EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEv 362
|
250
....*....|.
gi 1907184491 260 --SQYKPLLDK 268
Cdd:COG3206 363 arELYESLLQR 373
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
24-279 |
2.75e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 24 ANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVRE-----HEQRKHAVLVTELKTKLHEEKMKELQAVREALLRQH 98
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEearmaHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 99 EAELLRVIKIKDNENQRLQALLNTLRDGapdKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEealtmviqA 178
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEA---KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE--------A 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 179 DKIKAAEIRSvyhlhQEEITRIKKECEREIRRLEQQLDEKDARRFQLKIAElsAIIRKLEDRNALLSEER--NELLKRLR 256
Cdd:PTZ00121 1369 AEKKKEEAKK-----KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA--AAKKKADEAKKKAEEKKkaDEAKKKAE 1441
|
250 260
....*....|....*....|...
gi 1907184491 257 EAESQYKplLDKNKRLTRKNEDL 279
Cdd:PTZ00121 1442 EAKKADE--AKKKAEEAKKAEEA 1462
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
16-344 |
2.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 16 ETLAALQAANEELRAKLT--DIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREA 93
Cdd:COG4717 102 EELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 94 LLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVllcEAKEEAKKGFEVEKV--KMQQEISELK--------- 162
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEELEQLENELEaaALEERLKEARlllliaaal 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 163 -----------GAKKQVEEALTMVI-----------------QADKIKAAEIRSVYHLHQEEITRIKKECE--------- 205
Cdd:COG4717 259 lallglggsllSLILTIAGVLFLVLgllallflllarekaslGKEAEELQALPALEELEEEELEELLAALGlppdlspee 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 206 -----REIRRLEQQLDEKDARRFQLKIAELSAIIRKL------EDRNALLS-----EERNELLKRLREAESQYKPLLDKN 269
Cdd:COG4717 339 llellDRIEELQELLREAEELEEELQLEELEQEIAALlaeagvEDEEELRAaleqaEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184491 270 KRLTRKN--EDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslNDLDQSQDEREIDFLKLQIVEQQNLIDELSK 344
Cdd:COG4717 419 EELLEALdeEELEEELEELEEELEELEEELEELREELAELE-----AELEQLEEDGELAELLQELEELKAELRELAE 490
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
11-162 |
3.92e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.10 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 11 KGDKAETLAALQAANEELRAKLtdiqieLQQEKskvsKVEREKSQELKQVREHEQRkhavlvtelktkLHEEKMKELQAV 90
Cdd:cd16269 188 QADQALTEKEKEIEAERAKAEA------AEQER----KLLEEQQRELEQKLEDQER------------SYEEHLRQLKEK 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184491 91 REALLRQHEAELLRVIKIKDNENQRLQallntlrdgapdkvktvllceakeeaKKGFEVEKVKMQQEISELK 162
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALL--------------------------EEGFKEQAELLQEEIRSLK 291
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
13-295 |
3.96e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 13 DKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREK--SQELKQVREHEQ------------------------- 65
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLllliaaallallglggsllslilti 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 66 -------------------RKHAVLVTELKTKLHEEKMKELQA-----------VREALLRQHEAELLRVIKIKDNENQR 115
Cdd:COG4717 276 agvlflvlgllallflllaREKASLGKEAEELQALPALEELEEeeleellaalgLPPDLSPEELLELLDRIEELQELLRE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 116 LQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEvEKVKMQQEISELKGAKKQVEEALtmviqadkikaAEIRSVYHLHQE 195
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQL-----------EELLGELEELLE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 196 EITriKKECEREIRRLEQQLDEKDARRFQL--KIAELSAIIRKLEDRNAL--LSEERNELLKRLREAESQY------KPL 265
Cdd:COG4717 424 ALD--EEELEEELEELEEELEELEEELEELreELAELEAELEQLEEDGELaeLLQELEELKAELRELAEEWaalklaLEL 501
|
330 340 350
....*....|....*....|....*....|
gi 1907184491 266 LDKNKRLTRKnEDLSHTLRRIESKLKFVTQ 295
Cdd:COG4717 502 LEEAREEYRE-ERLPPVLERASEYFSRLTD 530
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
138-275 |
4.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 138 EAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMV---IQADKIKAAEIRSV--YHLHQEEITRIKKE---CEREIR 209
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLGNVRNNkeYEALQKEIESLKRRisdLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184491 210 RLEQQLDEKDArrfqlkiaELSAIIRKLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRK 275
Cdd:COG1579 114 ELMERIEELEE--------ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-291 |
4.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 16 ETLAALQAANEELRAKLTDIQIElqQEKSKVSKVEREKSQELKQVREHEQRKhavlvTELKTKLhEEKMKELQAVREA-- 93
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARI-----GELKKEI-KELKKAIEELKKAkg 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 94 ----------------LLRQHEAELLRVIKIKDNENQRLQALLNTLRdgapdKVKTVLLCEAK--EEAKKGFEVEKVKMQ 155
Cdd:PRK03918 437 kcpvcgrelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELR-----ELEKVLKKESEliKLKELAEQLKELEEK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 156 QEISELKGAKKQVEEALTMVIQADKIKAaEIRSVyhlhQEEITRIKkECEREIRRLEQQLDEKDArrfqlkiaELSAIIR 235
Cdd:PRK03918 512 LKKYNLEELEKKAEEYEKLKEKLIKLKG-EIKSL----KKELEKLE-ELKKKLAELEKKLDELEE--------ELAELLK 577
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184491 236 KLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLK 291
Cdd:PRK03918 578 ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
148-296 |
6.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 148 EVEKVKMQQEISELKGAKKQVEEALTmviqADKIKAAEIRSVYHLHQEEItrikKECEREIRRLEQQLDE----KDARRF 223
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLE----AAKTELEDLEKEIKRLELEI----EEVEARIKKYEEQLGNvrnnKEYEAL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184491 224 QLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQYKpllDKNKRLTRKNEDLSHTLRRIESKLKFVTQE 296
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
358-464 |
9.05e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 38.77 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184491 358 RRSHAPCCPvPSGATPPTALCPPEPRPLLPCALRSHAPYCPVPSGATTPTALCPPEPRPLLPCALRGHAPCCPVHSLKLP 437
Cdd:PHA03247 2665 RRARRLGRA-AQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
90 100
....*....|....*....|....*..
gi 1907184491 438 SPDslcpSRAVPLLTAHSLLPYLLSTP 464
Cdd:PHA03247 2744 VPA----GPATPGGPARPARPPTTAGP 2766
|
|
| |
