|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-337 |
1.76e-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: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 13 DKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKmKELQAVRE 92
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE-LELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 93 AlLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEAL 172
Cdd:COG1196 289 E-EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 173 tmviQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKR 252
Cdd:COG1196 368 ----LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 253 LREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAgiirrpSSLNDLDQSQDEREIDFLKLQIVE 332
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL------LLLLEAEADYEGFLEGVKAALLLA 517
|
....*
gi 1907184497 333 QQNLI 337
Cdd:COG1196 518 GLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-336 |
4.76e-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: 62.00 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 7 GSRAKGDKAETLAALQAANE--ELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHavlvtELKTKLHEEKM 84
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 85 KELQAVREALLRQHEAELLRVikikdnENQRLQALLNTLRDGApdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGA 164
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSK------ELTELEAEIEELEERL----------EEAEEELAEAEAEIEELEAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 165 KKQVEEALTmviqadkikaaEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALLSE 244
Cdd:TIGR02168 798 LKALREALD-----------ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 245 ERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslndLDQSQDEREID 324
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE-------LRLEGLEVRID 939
|
330
....*....|..
gi 1907184497 325 FLKLQIVEQQNL 336
Cdd:TIGR02168 940 NLQERLSEEYSL 951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-311 |
5.88e-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: 58.53 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 16 ETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKsQELKQVREHEQRKHAVLVTELktkLHEEKMKELQAVREALL 95
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQL---EELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 96 RQHEAELLrvikikdNENQRLQALLNTLRdgapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMV 175
Cdd:TIGR02168 343 EEKLEELK-------EELESLEAELEELE-------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 176 IQADKikaaeirsvyHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLRE 255
Cdd:TIGR02168 403 ERLEA----------RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907184497 256 AESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSSL 311
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
17-240 |
1.11e-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: 56.70 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 17 TLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQR----KHAVLVTELKTKLHEEKMKELQAVRE 92
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 93 ALLRQHE------AELLRVIkIKDNENQRLQALLNtlRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKK 166
Cdd:COG4942 94 ELRAELEaqkeelAELLRAL-YRLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184497 167 QVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNA 240
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-349 |
2.01e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQielQQEKSKVSKVEREKSQELKQVREhEQRKhavlVTELKTKLHEE 82
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK---KAEEAKKKAEEAKKADEAKKKAE-EAKK----ADEAKKKAEEA 1495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 83 KmKELQAVREALLRQHEAELLRvikiKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:PTZ00121 1496 K-KKADEAKKAAEAKKKADEAK----KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEIT----RIKKECEREIRRLQL---DEKDARRFQLKIAELSAI---- 231
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKkkae 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 232 -IRKLEDRNALLSEErnelLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSS 310
Cdd:PTZ00121 1651 eLKKAEEENKIKAAE----EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907184497 311 LNDLDQSQDEREIDFLKLQIVEQQnlIDELSKVSMQHFR 349
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLK 1763
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
337-456 |
1.30e-07 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 52.94 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 337 IDELSKVSMQHFRAVLSCVRR-------SHAPCCPVPSGATPPTAlcPPEPRPLLPCAlrSHAPYCPvPSGATT--PTAL 407
Cdd:PHA02682 55 VKEAGRYYQSRLKANSACMQRpsgqsplAPSPACAAPAPACPACA--PAAPAPAVTCP--APAPACP-PATAPTcpPPAV 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907184497 408 CPPEPRPllpcalrghAPCCPVHSLK------LPSPDSLCPSRavPLLTAHSLLP 456
Cdd:PHA02682 130 CPAPARP---------APACPPSTRQcppappLPTPKPAPAAK--PIFLHNQLPP 173
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
6-358 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 6 AGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSkvSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMK 85
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 86 ELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAK 165
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 166 KQV---EEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALL 242
Cdd:pfam02463 321 KEKkkaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 243 SEERNELLKRLREAESQykpLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAgiirrpSSLNDLDQSQDERE 322
Cdd:pfam02463 401 SEEEKEAQLLLELARQL---EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE------LKLLKDELELKKSE 471
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907184497 323 IDFLKLQIVEQQNLIDELSKVSMQHFRAVLSCVRRS 358
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-289 |
1.52e-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: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 11 KGDKAETLAALQAANEELRAKLTDIQI-ELQQEKSKVSKVEREKSQELKQVREHEQRKHavlvteLKTKLHEEKMKELQA 89
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLT------LEKEYLEKEIQELQE 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 90 VREALlrqheaellrviKIKDNENQRLQALLNTlrdgapDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVE 169
Cdd:TIGR02169 841 QRIDL------------KEQIKSIEKEIENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 170 EA---LTMVIQADKIKAAEIRSVYHLHQEEITRIKKEcEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEER 246
Cdd:TIGR02169 903 RKieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDP-KGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY 981
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907184497 247 NELLKRLREaesqykpLLDKNKRLTRKNEDLSHTLRRIESKLK 289
Cdd:TIGR02169 982 EEVLKRLDE-------LKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-322 |
3.99e-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: 52.76 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 7 GSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREkSQELKQVREHEQRKHAVLVTELKT-KLHEEKMK 85
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR-LDELSQELSDASRKIGEIEKEIEQlEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 86 ELQAVREALLRQHEAELLRVI-KIKDNEN--QRLQALLNTLRDgAPDKVKTVLLCEAKEEAKKgfevEKVKMQQEISELK 162
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKsELKELEAriEELEEDLHKLEE-ALNDLEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 163 GAKKQVEEALTMVIQADKIKAAEIRSVyhlhQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALL 242
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQEL----QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 243 SEERNELLKRLREAESQYkplldknKRLTRKNEDLSHTLRRIESKLKFVTQENIEM-RQRAGIIRRPSSLNDLDQSQDER 321
Cdd:TIGR02169 888 KKERDELEAQLRELERKI-------EELEAQIEKKRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAEL 960
|
.
gi 1907184497 322 E 322
Cdd:TIGR02169 961 Q 961
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-342 |
4.51e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 48 KVEREKS-QELKQVREHEQRKHAVLvTELKTKLHE--------EKMKELQAvrEALLRQHEAELLRvIKIKDNENQRLQA 118
Cdd:COG1196 171 KERKEEAeRKLEATEENLERLEDIL-GELERQLEPlerqaekaERYRELKE--ELKELEAELLLLK-LRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 119 LLntlrdgapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTmviqadkikaaEIRSVYHLHQEEIT 198
Cdd:COG1196 247 EL-----------------EELEAELEELEAELAELEAELEELRLELEELELELE-----------EAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 199 RIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQykpLLDKNKRLTRKNEDLS 278
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE---LAEAEEALLEAEAELA 375
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184497 279 HTLRRIESKLKfvtQENIEMRQRAGIIRRPSSLNDLDQSQDEREIDFLKLQIVEQQNLIDELSK 342
Cdd:COG1196 376 EAEEELEELAE---ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-265 |
1.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQ--QEKSKVSKVERE---------KSQELKQVREHEQRKHAVL 71
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAeedknmalrKAEEAKKAEEARIEEVMKL 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 72 VTELKTKLHEEKMKELQAVREA-LLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVE 150
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 151 KVKMQQEISELKGAKKQVEEA-----LTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRR---LQLDEKDARRF- 221
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaeeAKKDEEEKKKIa 1760
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907184497 222 QLKIAELSAIIRKLEDRNALLSEE-RNELLKRLREAESQYKPLLD 265
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKDIFD 1805
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-307 |
1.54e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 1 MSKKGAGSRAKGDKAETLAALQAANEELR-AKLTDIQIELQQEKSKVSKVEREKSQELK---QVREHEQRKHAvlvtELK 76
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKkadELKKAEELKKA----EEK 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 77 TKLHEEKMKE---LQAVREA-LLRQHEAELLRVIKIKDNENQRLQAllNTLRDGAPDKVKTVLLCEAkEEAKKGFEVEKV 152
Cdd:PTZ00121 1564 KKAEEAKKAEedkNMALRKAeEAKKAEEARIEEVMKLYEEEKKMKA--EEAKKAEEAKIKAEELKKA-EEEKKKVEQLKK 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 153 KMQQEISELKGAKKQVEEaltmviqaDKIKAAEIRsvyhlHQEEITRIKKEcerEIRRLQLDEKDARRFQLKIAELSaii 232
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEE--------NKIKAAEEA-----KKAEEDKKKAE---EAKKAEEDEKKAAEALKKEAEEA--- 1701
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907184497 233 RKLEDRNALLSEERNElLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRR 307
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKK-AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-297 |
2.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 26 EELRAKLTDIQ---IELQQEKSKVSKVEREKSQELKQVREHEQRKHAvlvTELKTKLHEEKMKELQAVREAL--LRQHEA 100
Cdd:PRK03918 217 PELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRE---LEERIEELKKEIEELEEKVKELkeLKEKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 101 ELLRVIKIKDNENQRLQAL---LNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMVIQ 177
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIekrLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 178 ADKIKAAE-IRSVYHLHQ--EEITRIKKECEREIRRL-----QLDEKDARR----FQLK--------------------- 224
Cdd:PRK03918 374 LERLKKRLtGLTPEKLEKelEELEKAKEEIEEEISKItarigELKKEIKELkkaiEELKkakgkcpvcgrelteehrkel 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184497 225 IAELSAIIRKLEDRNALLSEERNELLKRLREAESqykpLLDKNKRLtRKNEDLSHTLRRIESKLKFVTQENIE 297
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEK----VLKKESEL-IKLKELAEQLKELEEKLKKYNLEELE 521
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
25-348 |
2.52e-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: 50.44 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 25 NEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREAlLRQHEAELLR 104
Cdd:TIGR01612 691 NTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILED-FKNKEKELSN 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 105 VIKIKDNENQRL---QALLNTLRDGAPDKVKTVLLCEakEEAKKGFE----------VEKVKMQQEISELKGAKKQVEEA 171
Cdd:TIGR01612 770 KINDYAKEKDELnkyKSKISEIKNHYNDQINIDNIKD--EDAKQNYDkskeyiktisIKEDEIFKIINEMKFMKDDFLNK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 172 LTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREirrlqldekdarrfQLKIAElsaiiRKLEDRNALLSEERNELLK 251
Cdd:TIGR01612 848 VDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDD--------------KLNDYE-----KKFNDSKSLINEINKSIEE 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 252 RLREAESQYKplLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSS---LNDLDQSQDEREIDFLKL 328
Cdd:TIGR01612 909 EYQNINTLKK--VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKdkfDNTLIDKINELDKAFKDA 986
|
330 340
....*....|....*....|
gi 1907184497 329 QIVEQQNLIDELskvsMQHF 348
Cdd:TIGR01612 987 SLNDYEAKNNEL----IKYF 1002
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-329 |
5.54e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 26 EELRAKLTDIQiELQQEKSKVSKVEREKSQELKQVREheQRKHAVLVTELKTKLHEEKMKELQAVREALLRQHEAeLLRV 105
Cdd:TIGR02169 170 RKKEKALEELE-EVEENIERLDLIIDEKRQQLERLRR--EREKAERYQALLKEKREYEGYELLKEKEALERQKEA-IERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 106 IKIKDNENQRLQALLNTLRDGAPDKVKtvLLCEAKEEAKKGFEVEKVKMQQEISELKG----AKKQVEEALTMVIQADKi 181
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQ--LLEELNKKIKDLGEEEQLRVKEKIGELEAeiasLERSIAEKERELEDAEE- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 182 KAAEIRSVYHLHQEEITRIKKECEREIRRL-------------------QLDEKDARrFQLKIAELSAIIRKLEDrnalL 242
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRdklteeyaelkeeledlraELEEVDKE-FAETRDELKDYREKLEK----L 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 243 SEERNE-------LLKRLREAESQ-------YKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRagIIRRP 308
Cdd:TIGR02169 398 KREINElkreldrLQEELQRLSEEladlnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE--LYDLK 475
|
330 340
....*....|....*....|...
gi 1907184497 309 SSLNDLD--QSQDEREIDFLKLQ 329
Cdd:TIGR02169 476 EEYDRVEkeLSKLQRELAEAEAQ 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-256 |
7.48e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 13 DKAETLAALQAANEELRAKLTDIQiELQQEKSKVSKVERE-KSQELKQVREHEQRKHAVLVTELKTklHEEKMKELQAVR 91
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLA-ELEYLRAALRLWFAQrRLELLEAELEELRAELARLEAELER--LEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 92 EALLRQheaellrvikIKDNENQRLQALLNTLRDgapdkvktvllceakeeakkgfevekvkMQQEISELKGAKKQVEEA 171
Cdd:COG4913 326 DELEAQ----------IRGNGGDRLEQLEREIER----------------------------LERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 172 LTMV---IQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRfqlKIAELSAIIRKLEDRNALLSEERNE 248
Cdd:COG4913 368 LAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR---ELRELEAEIASLERRKSNIPARLLA 444
|
....*...
gi 1907184497 249 LLKRLREA 256
Cdd:COG4913 445 LRDALAEA 452
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
23-302 |
8.90e-06 |
|
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: 48.30 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 23 AANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVrEHEQRKHAVLVTELKTKlhEEKMKELQAVREALLRQHEAEL 102
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL-EKASREETFARTALKNA--RLDLRRLFDEKQSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 103 LRVIKIKDNENQRLQALLNTLRDGAPDkvktvllceAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTmviqadkik 182
Cdd:pfam12128 674 AERKDSANERLNSLEAQLKQLDKKHQA---------WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLK--------- 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 183 aAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLE-DRNALLSEERnellkRLREAESQYK 261
Cdd:pfam12128 736 -AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAvRRQEVLRYFD-----WYQETWLQRR 809
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907184497 262 PLLDKNKRLT-RKNEDLSHTLRRIESKLKFVTQeNIEMRQRA 302
Cdd:pfam12128 810 PRLATQLSNIeRAISELQQQLARLIADTKLRRA-KLEMERKA 850
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-244 |
1.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKskvsKVEREKSQELKQVREHEQRKHAVLVTELKTKlhEE 82
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEEAEEELEEA--EA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 83 KMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDgapdkvktvllCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-----------LEELEEAEEALLERLERLEEELEELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKEcEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALL 242
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
..
gi 1907184497 243 SE 244
Cdd:COG1196 507 LE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-342 |
1.24e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 15 AETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREAL 94
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 95 LRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKK-------- 166
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflpl 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 167 ---------------QVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAI 231
Cdd:COG1196 580 dkiraraalaaalarGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 232 IRKLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSSL 311
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
330 340 350
....*....|....*....|....*....|....*
gi 1907184497 312 NDLDQSQDEREIDFLKLQIV----EQQNLIDELSK 342
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPpdleELERELERLER 774
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
4-294 |
2.75e-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: 46.65 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 4 KGAGSRAKGDKAETLAALQAANEELRaKLTDIQIELQQEKSKVSKVEREKSQElKQVREHEQRKhavlVTELKTKLHEEK 83
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERT----VSDLTASLQEKE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 84 mkelqavreallRQHEAELLRVIKIKDNENQRLQALLNTLRDGapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKG 163
Cdd:pfam15921 510 ------------RAIEATNAEITKLRSRVDLKLQELQHLKNEG-----------DHLRNVQTECEALKLQMAEKDKVIEI 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 164 AKKQVEEALTMVIQADKIKAAeirsvyhlhqeeITRIKKECEREI--RRLQL-------DEKDArrfqlKIAELSAIIRK 234
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGA------------MQVEKAQLEKEIndRRLELqefkilkDKKDA-----KIRELEARVSD 629
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184497 235 LEDRNALL--------------SEERNELLKRLREAESQYKPLLDKNKRLTR----KNEDLSHTLRRIESKLKFVTQE 294
Cdd:pfam15921 630 LELEKVKLvnagserlravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSE 707
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
25-342 |
3.22e-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: 46.55 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 25 NEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKelqavrealLRQHEAELLR 104
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKK---------LEEIQNQISQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 105 VIKIKDNENQRLQALLNTLRDGAPDKVKtvllcEAKEEAKKGFEVEKVKMQ-----QEISELKGAKKQVEEALTMVIQAD 179
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSE-----KQRELEEKQNEIEKLKKEnqsykQEIKNLESQINDLESKIQNQEKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 180 KIKAAEIRSV---YHLHQEEITRIKKECER---EIRRL---------QLDEKDARRFQLK--IAELSAIIRK----LEDR 238
Cdd:TIGR04523 408 QQKDEQIKKLqqeKELLEKEIERLKETIIKnnsEIKDLtnqdsvkelIIKNLDNTRESLEtqLKVLSRSINKikqnLEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 239 NALLSEERNELLK---RLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQragiirrpsslnDLD 315
Cdd:TIGR04523 488 QKELKSKEKELKKlneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF------------ELK 555
|
330 340
....*....|....*....|....*..
gi 1907184497 316 QSQDEREIDFLKLQIVEQQNLIDELSK 342
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKK 582
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
337-447 |
3.67e-05 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 45.24 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 337 IDELSKVSMQHFRAVLSCVRRSHAPCCPVPSGATP--PTALCPPePRPLLPcalrSHAPYCPVPsgattptALCPPEPRP 414
Cdd:PHA02682 47 VDPLDKYSVKEAGRYYQSRLKANSACMQRPSGQSPlaPSPACAA-PAPACP----ACAPAAPAP-------AVTCPAPAP 114
|
90 100 110
....*....|....*....|....*....|...
gi 1907184497 415 LLPCALrghAPCCPvhslklpsPDSLCPSRAVP 447
Cdd:PHA02682 115 ACPPAT---APTCP--------PPAVCPAPARP 136
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
35-294 |
4.06e-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: 46.17 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 35 IQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAvLVTELK-----TKLHEEKMKELQAVREALLRQHEAELLRVIK-- 107
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQnqeklNQQKDEQIKKLQQEKELLEKEIERLKETIIKnn 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 108 --IKDNENQRLQ-----ALLNTLRDGAPDKVKTVLLCEAKEEAK-KGFEVEKVKMQQEISELKGAKKQVEE--------- 170
Cdd:TIGR04523 440 seIKDLTNQDSVkeliiKNLDNTRESLETQLKVLSRSINKIKQNlEQKQKELKSKEKELKKLNEEKKELEEkvkdltkki 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 171 -ALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARRFQLK--IAELSAIIRKLEDRNALLSEERN 247
Cdd:TIGR04523 520 sSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKqtQKSLKKKQEEKQELIDQKEKEKK 599
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907184497 248 ELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQE 294
Cdd:TIGR04523 600 DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
11-296 |
4.59e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 11 KGDKAETLAALQAAN----EELRAKLTDIQI-ELQQEKSKVSkverEKSQELKQVREHEQrkhavLVTELKTKLHEEKMK 85
Cdd:PRK05771 15 KSYKDEVLEALHELGvvhiEDLKEELSNERLrKLRSLLTKLS----EALDKLRSYLPKLN-----PLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 86 ELQAVREALLRQHEAELLRVI-KIK--DNENQRLQALLNTLrdgapDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEeEISelENEIKELEQEIERL-----EPWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 163 GAKKQVEEALtmVIQADKIKAAEIRSVYHLHQEEITRIKKECEreIRRLQLDEKdarrfqlkiAELSAIIRKLEDRNALL 242
Cdd:PRK05771 161 KLESDVENVE--YISTDKGYVYVVVVVLKELSDEVEEELKKLG--FERLELEEE---------GTPSELIREIKEELEEI 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907184497 243 SEERNELLKRLREAESQYKPLLDKNKrltrknEDLSHTLRRIESKLKFVTQENI 296
Cdd:PRK05771 228 EKERESLLEELKELAKKYLEELLALY------EYLEIELERAEALSKFLKTDKT 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-294 |
1.61e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 14 KAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEReksqELKQVREHEQRkhavlVTELKTKLhEEKMKELQAVREa 93
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE----RIKELEEKEER-----LEELKKKL-KELEKRLEELEE- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 94 llrqhEAELLRVIKIKDNENQRLQALLNTLrdgAPDKVKTVLlcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALT 173
Cdd:PRK03918 360 -----RHELYEEAKAKKEELERLKKRLTGL---TPEKLEKEL--EELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 174 MVIQADKIKAAEIRSVYHLHQEEitrIKKECEREIRRLqldEKDARRFQLKIAELSAIIRKLEdrNALLSEER----NEL 249
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKE---LLEEYTAELKRI---EKELKEIEEKERKLRKELRELE--KVLKKESEliklKEL 501
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907184497 250 LKRLREAESQYKPL-LDKNKRLTRKNEDLSHTLRRIESKLKFVTQE 294
Cdd:PRK03918 502 AEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
39-340 |
2.28e-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: 43.57 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 39 LQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHE-EKMKELQAVREALLRqheAELLRVIKIKDNENQRLQ 117
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaEKARQAEMDRQAAIY---AEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 118 allntlRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEI------SELKGAKKQ--VEEALTMVIQADKIKAAEIRSV 189
Cdd:pfam17380 355 ------QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervrQELEAARKVkiLEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 190 Y-HLHQEEITRIKKECEREIRRLQLDEKDaRRFQLKIAELSAIIRKL-------EDRNALLSEERNELLKRLREAESQYK 261
Cdd:pfam17380 429 QeEARQREVRRLEEERAREMERVRLEEQE-RQQQVERLRQQEEERKRkklelekEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 262 PLLDKNKR--LTRKNEDLSHTL----RRIESKLKFVTQENIEMRQR--AGIIRRPSSLNDLDQSQDEREidfLKLQIVEQ 333
Cdd:pfam17380 508 MIEEERKRklLEKEMEERQKAIyeeeRRREAEEERRKQQEMEERRRiqEQMRKATEERSRLEAMERERE---MMRQIVES 584
|
....*..
gi 1907184497 334 QNLIDEL 340
Cdd:pfam17380 585 EKARAEY 591
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-350 |
2.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEE 82
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 83 KMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEkvKMQQEISELK 162
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 163 GAKKQVEEALTMviQADKIKAAEIRSVYHLhqeeitriKKECErEIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALL 242
Cdd:PTZ00121 1448 EAKKKAEEAKKA--EEAKKKAEEAKKADEA--------KKKAE-EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 243 SEERNELLKRLREAESQYKPLLDKNKRLTRKNEDL--SHTLRRIESKLKfVTQENIEMRQRAGIIRRPSslnDLDQSQDE 320
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKAEEKKK-AEEAKKAEEDKNMALRKAE---EAKKAEEA 1592
|
330 340 350
....*....|....*....|....*....|
gi 1907184497 321 REIDFLKLQIVEQQNLIDELSKVSMQHFRA 350
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-342 |
3.58e-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: 43.09 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 26 EELRAKLTDIQIELQQEKSKVSKVEREKS---QELKQVReHEQRKHAVLVTELKTKlhEEKMKELQAVREALLRQHEaEL 102
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLniqKNIDKIK-NKLLKLELLLSNLKKK--IQKNKSLESQISELKKQNN-QL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 103 LRVIKIKDNENQRLQALLNtlrdgapdKVKTVLLcEAKEEAKKgfevEKVKMQQEISELKGAKKQVEEaLTMVIQADKIK 182
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEIS--------NTQTQLN-QLKDEQNK----IKKQLSEKQKELEQNNKKIKE-LEKQLNQLKSE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 183 AAEIRSVYHlhQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQYKP 262
Cdd:TIGR04523 297 ISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 263 LLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslndLDQSQDEREIDFLKLQIVEQQNLIDELSK 342
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ-------QEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-322 |
4.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 3 KKGAGSRAKGDKAETLAALQAANE----ELRAKLTDIQIELQQEKSKVSKV---EREKSQELKQVREHEQRK-HAVLVTE 74
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEaeaaEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEEDKKKaDELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 75 LKTKLHEEKMKELQAVREALLRQHEAELLRV---IKIKDNENQRLQallnTLRDGAPDKVKTVLLCEAKEEAKKGFEVEK 151
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 152 -----VKMQQEISELKGAKKQVEEALTmviQADKIKAAEIRSVYHLHQEEITRiKKECEREIRRLQLDEKDARRFQLKIA 226
Cdd:PTZ00121 1491 kaeeaKKKADEAKKAAEAKKKADEAKK---AEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELKKAEEKKKA 1566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 227 ELSAiiRKLEDRNALL---SEERNELLKRLREAESQYKPLLDKNKRLTRKNEDL---SHTLRRIESKLKFVTQ---ENIE 297
Cdd:PTZ00121 1567 EEAK--KAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikAEELKKAEEEKKKVEQlkkKEAE 1644
|
330 340
....*....|....*....|....*
gi 1907184497 298 MRQRAGIIRRPSSLNDLDQSQDERE 322
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKK 1669
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
11-329 |
4.35e-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: 42.81 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 11 KGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVS------KVEREKSQELKQVREHEQRKHAVLvtelktKLHEEKM 84
Cdd:pfam05557 99 LADAREVISCLKNELSELRRQIQRAELELQSTNSELEelqerlDLLKAKASEAEQLRQNLEKQQSSL------AEAEQRI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 85 KEL------QAVREALLRQHEAELLRVIKIkDNENQRLQALLNTLRDGAPDKvktVLLCEAKEEAKKGFEVEKvKMQQEI 158
Cdd:pfam05557 173 KELefeiqsQEQDSEIVKNSKSELARIPEL-EKELERLREHNKHLNENIENK---LLLKEEVEDLKRKLEREE-KYREEA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 159 SELKGAKKQVEEALTMVIQADKIKAAEIRS-------VYHLHQEEITRIKKEC--------EREIRRLQLDEKDARRFQL 223
Cdd:pfam05557 248 ATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlsrrIEQLQQREIVLKEENSsltssarqLEKARRELEQELAQYLKKI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 224 -----KIAELSAIIRKLEDRNALLSEERNeLLKRLREAesqykplLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEM 298
Cdd:pfam05557 328 edlnkKLKRHKALVRRLQRRVLLLTKERD-GYRAILES-------YDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEM 399
|
330 340 350
....*....|....*....|....*....|.
gi 1907184497 299 RQRAGIIRRPSSLNDLDQSQDEREIDFLKLQ 329
Cdd:pfam05557 400 EAQLSVAEEELGGYKQQAQTLERELQALRQQ 430
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-280 |
5.42e-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: 42.73 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 16 ETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVreheqrkhavlvtELKTKLHEEKMKELQAVREAlL 95
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA-------------PGRQSIIDLKEKEIPELRNK-L 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 96 RQHEAELLRvIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKgfEVEKvKMQQEISELKGAkkQVEEALTMV 175
Cdd:TIGR00606 754 QKVNRDIQR-LKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELK--DVER-KIAQQAAKLQGS--DLDRTVQQV 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 176 IQADKIKAAEIRSVYHlHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLRE 255
Cdd:TIGR00606 828 NQEKQEKQHELDTVVS-KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
250 260
....*....|....*....|....*
gi 1907184497 256 AESQYKPLLDKNKRLTRKNEDLSHT 280
Cdd:TIGR00606 907 AKEQDSPLETFLEKDQQEKEELISS 931
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
21-295 |
6.26e-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: 42.40 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 21 LQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVrEHEQRKHAVLVTELKTkLHEEKMKELQAVREALLRQHEA 100
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI-ENLEEKEMNLRDELES-VREEFIQKGDEVKCKLDKSEEN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 101 ELLRVIKIKDNENQR--LQALLNTLRDGAPDKVKTV--LLCEAKEEAKKG------FEVEKVKMQQEISELKGAKKQVEE 170
Cdd:pfam05483 575 ARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIeeLHQENKALKKKGsaenkqLNAYEIKVNKLELELASAKQKFEE 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 171 ALTMVIQADKIKAAEIRSVYhlhqEEITRIKKECEREIRrlqLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNE-- 248
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKLL----EEVEKAKAIADEAVK---LQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSel 727
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907184497 249 -LLKRLREAESQYKPLLD------KNKRLTRKNEdlSHTLRRIESKLKFVTQEN 295
Cdd:pfam05483 728 gLYKNKEQEQSSAKAALEielsniKAELLSLKKQ--LEIEKEEKEKLKMEAKEN 779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
12-285 |
8.36e-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: 42.08 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 12 GDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEqrkhaVLVTELKTKLHEEKMKELQAVR 91
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE-----AQISELQEDLESERAARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 92 EallRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKtvLLCEAKEEAKKGFEVEKVKMQQ-----------EISE 160
Cdd:pfam01576 293 Q---RRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVT--ELKKALEEETRSHEAQLQEMRQkhtqaleelteQLEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 161 LKGAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEITRiKKECEREIRRLQLDEKDARRFQLKIAE-LSAIIRKLEDRN 239
Cdd:pfam01576 368 AKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK-RKKLEGQLQELQARLSESERQRAELAEkLSKLQSELESVS 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907184497 240 ALLSEERNELLKRLREAESQYKPLLDKNKRL---TRKNEDLSHTLRRIE 285
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTRLRQLE 495
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
349-464 |
9.17e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 349 RAVLSCVRRSHAPCCPVPSGATPPTALCPPEPRPLLPCALRSHAPYCP-------VPSGATTPTALCPPEPRPLLPCALR 421
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPaapappaVPAGPATPGGPARPARPPTTAGPPA 2768
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907184497 422 GHAPCCPVHSlklpspdslcPSRAVPLLTAHSLLPYLLSTPHP 464
Cdd:PHA03247 2769 PAPPAAPAAG----------PPRRLTRPAVASLSESRESLPSP 2801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-289 |
9.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 154 MQQEISELKGAKKQVEEAltmviqADKIKA-AEIRSVYHLHQEEITRI-KKECEREIRRLQLDEKDARRFQLKIAELSAI 231
Cdd:COG4913 230 LVEHFDDLERAHEALEDA------REQIELlEPIRELAERYAAARERLaELEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184497 232 IRKLEDRNALLSEERNELLKRLREAESQYKPL-LDKNKRLTRKNEDLSHTLRRIESKLK 289
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRA 362
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
22-185 |
9.78e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 22 QAANEELRAKLTDIQIELQQEKsKVSKVEREKSQELKQVREHEQRKHAVlvtelktklheekmkelQAVREALLRQHEAE 101
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAE-----------------EAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 102 llrvikikdnENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEiselkGAKKQVEEALTMVIQADKI 181
Cdd:PRK09510 136 ----------EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAA-----EAKKKAEAEAAAKAAAEAK 200
|
....
gi 1907184497 182 KAAE 185
Cdd:PRK09510 201 KKAE 204
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
81-183 |
9.96e-04 |
|
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: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 81 EEKMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKtvllCEAKEEAKKgFEVEKVKMQQEISE 160
Cdd:pfam03961 140 GTKTEIEVGVDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLP----PEKREQLEK-LLETKNKLSEELEE 214
|
90 100
....*....|....*....|...
gi 1907184497 161 LKGAKKQVEEALTMVIQADKIKA 183
Cdd:pfam03961 215 LEEELKELKEELESLLGEGKISV 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
9-261 |
1.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 9 RAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQ--ELKQVREHEQRKHAVLVTELKTKLHEEKMKE 86
Cdd:TIGR00606 829 QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQigTNLQRRQQFEEQLVELSTEVQSLIREIKDAK 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 87 LQAV-REALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKV---KTVL--LCEAKEEAKKGFEVEKVKMQQEISE 160
Cdd:TIGR00606 909 EQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymKDIEnkIQDGKDDYLKQKETELNTVNAQLEE 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 161 LKGAKKQVEEALTMVIQAdkIKAAEIRSvyHLHQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDRNA 240
Cdd:TIGR00606 989 CEKHQEKINEDMRLMRQD--IDTQKIQE--RWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID 1064
|
250 260
....*....|....*....|.
gi 1907184497 241 LLSEERNELLKRLREAESQYK 261
Cdd:TIGR00606 1065 LIKRNHVLALGRQKGYEKEIK 1085
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
138-361 |
1.67e-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: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 138 EAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMVIQADKIKAAEIRSVYHlhQEEITRIkkecEREIRRLQLDEKD 217
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA--EREIAEL----EAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 218 ARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQYKPLLDknkRLTRKNEDLSHTLR-RIESKLKFVTQENI 296
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRaLLEERFAAALGDAV 763
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 297 EMRQRAGIIRRPSSLNDlDQSQDEREI-----DFLKLQIVEQQNLIDELSkvSMQHFRAVLSCVRRSHAP 361
Cdd:COG4913 764 ERELRENLEERIDALRA-RLNRAEEELeramrAFNREWPAETADLDADLE--SLPEYLALLDRLEEDGLP 830
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
146-284 |
1.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 146 GFEVEKVKMQQEISELKG-AKKQVEEAltmVIQADKIKAAEIRSVyhlhQEEITRIKKECEREIRRlqldekdaRRFQLK 224
Cdd:PRK12704 21 GYFVRKKIAEAKIKEAEEeAKRILEEA---KKEAEAIKKEALLEA----KEEIHKLRNEFEKELRE--------RRNELQ 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184497 225 IAELSAIIRK--LEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRI 284
Cdd:PRK12704 86 KLEKRLLQKEenLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-289 |
2.32e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 26 EELRAKLTDIQIELQQEKSKVSKVEREKsQELKQVREHE-----QRKHAVLVTELKTKLHEEKMKELQAVREAL--LRQH 98
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKEselikLKELAEQLKELEEKLKKYNLEELEKKAEEYekLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 99 EAELLRVIKIKDNENQRLQALLNTLRdgapdkvktvllceAKEEAKKGFEVEKVKMQQEISELK-GAKKQVEEaltmviq 177
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLA--------------ELEKKLDELEEELAELLKELEELGfESVEELEE------- 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 178 adkikaaEIRSVYHLHQE--EITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRKLEDR-NALLS----EERNELL 250
Cdd:PRK03918 593 -------RLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKElEELEKkyseEEYEELR 665
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907184497 251 KRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLK 289
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
8-177 |
2.51e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 8 SRAKGDKAETLAA--LQAANEELRAKLTDIQIELQQE----KSKVSKVEREKSQELKQVREHEQRKHAVLvtELKTKLHE 81
Cdd:PRK12704 29 AEAKIKEAEEEAKriLEEAKKEAEAIKKEALLEAKEEihklRNEFEKELRERRNELQKLEKRLLQKEENL--DRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 82 EKMKELQAVREALLRQHE-AELLR--VIKIKDNENQRLQALLNTLRDGApdkvKTVLLCEAKEEAKKgfevEKVKMQQEI 158
Cdd:PRK12704 107 KREEELEKKEKELEQKQQeLEKKEeeLEELIEEQLQELERISGLTAEEA----KEILLEKVEEEARH----EAAVLIKEI 178
|
170 180
....*....|....*....|.
gi 1907184497 159 SEL--KGAKKQVEEALTMVIQ 177
Cdd:PRK12704 179 EEEakEEADKKAKEILAQAIQ 199
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
13-220 |
2.93e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 13 DKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEreksQELKQVREHEQrkhavlvtELKTKLhEEKMKELQAVRE 92
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----AELEALQAEID--------KLQAEI-AEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 93 ALlrqheAELLRVIKIKDNENQRLQALL---------------NTLRDGAPDKVKTVL-LCEAKEEAKKGFEVEKVKMQQ 156
Cdd:COG3883 87 EL-----GERARALYRSGGSVSYLDVLLgsesfsdfldrlsalSKIADADADLLEELKaDKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184497 157 EISELKGAKKQVEEALTmVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLQLDEKDARR 220
Cdd:COG3883 162 LKAELEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
11-162 |
2.96e-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: 39.48 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 11 KGDKAETLAALQAANEELRAKLtdiqieLQQEKskvsKVEREKSQELKQVREHEQRkhavlvtelktkLHEEKMKELQAV 90
Cdd:cd16269 188 QADQALTEKEKEIEAERAKAEA------AEQER----KLLEEQQRELEQKLEDQER------------SYEEHLRQLKEK 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184497 91 REALLRQHEAELLRVIKIKDNENQRLQallntlrdgapdkvktvllceakeeaKKGFEVEKVKMQQEISELK 162
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALL--------------------------EEGFKEQAELLQEEIRSLK 291
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
24-277 |
3.57e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 24 ANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVRE-----HEQRKHAVLVTELKTKLHEEKMKELQAVREALLRQH 98
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEearmaHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 99 EAELLRVIKIKDNENQRLQALLNTLRDGapdKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMVIQA 178
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEA---KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 179 D------KIKAAEIRSVYHLhQEEITRIKKECErEIRRLQLDEKDARRFQLKIAElsaiIRKLEDRNALLSEER--NELL 250
Cdd:PTZ00121 1377 KkkadaaKKKAEEKKKADEA-KKKAEEDKKKAD-ELKKAAAAKKKADEAKKKAEE----KKKADEAKKKAEEAKkaDEAK 1450
|
250 260
....*....|....*....|....*..
gi 1907184497 251 KRLREAESQYKplLDKNKRLTRKNEDL 277
Cdd:PTZ00121 1451 KKAEEAKKAEE--AKKKAEEAKKADEA 1475
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-301 |
4.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 84 MKELQAVREALLRQHE-AELLRVIKIKDNENQRLQALLNTLRDgapdkVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:COG4913 234 FDDLERAHEALEDAREqIELLEPIRELAERYAAARERLAELEY-----LRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 163 GAKKQVEEALTmviQADkikaAEIRSVYHLHQEEITRIKKECEREIRRLQ--LDEKDARRFQLK-------------IAE 227
Cdd:COG4913 309 AELERLEARLD---ALR----EELDELEAQIRGNGGDRLEQLEREIERLEreLEERERRRARLEallaalglplpasAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184497 228 LSAIIRKLEDRNALLSEERNELLKRLREAESQYkplldknKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQR 301
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAAL-------RDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
132-266 |
4.46e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 39.47 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 132 KTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRL 211
Cdd:PRK00106 70 KKELLLEAKEEARKYREEIEQEFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVE 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907184497 212 QLDEKDARRFQlKIAELSaiirKLEDRNALLSEERNELLK----RLREAESQYKPLLDK 266
Cdd:PRK00106 150 KLEEQKKAELE-RVAALS----QAEAREIILAETENKLTHeiatRIREAEREVKDRSDK 203
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-261 |
4.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 1 MSKKGAGSRAKGDKAETLAA--LQAANeelRAKLTDIQIELQQEKSKVSKVEREKsQELKQVREHEQRKHAVLvtelktk 78
Cdd:COG4913 582 QVKGNGTRHEKDDRRRIRSRyvLGFDN---RAKLAALEAELAELEEELAEAEERL-EALEAELDALQERREAL------- 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 79 lheekmKELQAVREALL--RQHEAELlrvikikdnenQRLQALLNTLRDGAPDkvktvlLCEAKEEAKKgFEVEKVKMQQ 156
Cdd:COG4913 651 ------QRLAEYSWDEIdvASAEREI-----------AELEAELERLDASSDD------LAALEEQLEE-LEAELEELEE 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 157 EISELKGAKKQVEEaltmviqadKIKAAEIRsvyhlhQEEITRIKKECEREIRRLQLDEKDARRFQLKIAELSAIIRK-L 235
Cdd:COG4913 707 ELDELKGEIGRLEK---------ELEQAEEE------LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREnL 771
|
250 260
....*....|....*....|....*.
gi 1907184497 236 EDRNALLSEERNELLKRLREAESQYK 261
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAFN 797
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
21-266 |
5.29e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 21 LQAANEELRAKLTDIQIELQQEKSKVSKVEreksQELKQVREheqrKHAVLVTELKTKLHEEKMKELQAVREALLRQHEA 100
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQ----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 101 ELLRVikikdnenQRLQALLNTLRDGAPDKVKTVLLceakeeakkgfevekVKMQQEISELKGAKKQVEEALTmvIQADK 180
Cdd:COG3206 238 AEARL--------AALRAQLGSGPDALPELLQSPVI---------------QQLRAQLAELEAELAELSARYT--PNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 181 IKAAeirsvyhlhQEEITRIKKECEREIRRLQLD-EKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAE-- 257
Cdd:COG3206 293 VIAL---------RAQIAALRAQLQQEAQRILASlEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEva 363
|
250
....*....|
gi 1907184497 258 -SQYKPLLDK 266
Cdd:COG3206 364 rELYESLLQR 373
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-289 |
5.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 16 ETLAALQAANEELRAKLTDIQIElqQEKSKVSKVEREKSQELKQVREHEQRKhavlvTELKTKLhEEKMKELQAVREA-- 93
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARI-----GELKKEI-KELKKAIEELKKAkg 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 94 --------LLRQHEAELLR--VIKIKDNENqRLQALLNTLRdgapdkvktvllcEAKEEAKkgfEVEKV-KMQQEISELK 162
Cdd:PRK03918 437 kcpvcgreLTEEHRKELLEeyTAELKRIEK-ELKEIEEKER-------------KLRKELR---ELEKVlKKESELIKLK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKE---CEREIRRLQLDEKDARRFQLKI----AELSAIIRKL 235
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLdeleEELAELLKEL 579
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907184497 236 EDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLK 289
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-171 |
7.81e-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: 38.88 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 8 SRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKskvskVEREKSQELKQVREHEQRKhavLVTELKTklHEEKMKEL 87
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALL-----NERASLEEALALLRSELEE---LSEELRE--LESKRSEL 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 88 QAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGF-------------------- 147
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlkrlenkikelgpvnlaaie 993
|
170 180
....*....|....*....|....*....
gi 1907184497 148 EVEKVK-----MQQEISELKGAKKQVEEA 171
Cdd:TIGR02168 994 EYEELKerydfLTAQKEDLTEAKETLEEA 1022
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
138-261 |
8.36e-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: 37.98 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 138 EAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMV---IQADKIKAAEIRSvyhlhQEEITRIKKECEREIRRLQLD 214
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLGNVRN-----NKEYEALQKEIESLKRRISDL 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907184497 215 EKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQYK 261
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
26-289 |
8.91e-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: 38.73 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 26 EELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVRE--HEQRKHAVLVT----ELKTKLHEEKMKELQAVREalLRQHE 99
Cdd:pfam15964 399 EELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEaqKQLASQEMDVTkvcgEMRYQLNQTKMKKDEAEKE--HREYR 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 100 AELLRVIKIKDNENQRL--------QALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEV---EKVKMQQEISELKGAK--- 165
Cdd:pfam15964 477 TKTGRQLEIKDQEIEKLglelseskQRLEQAQQDAARAREECLKLTELLGESEHQLHLtrlEKESIQQSFSNEAKAQalq 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 166 -KQVEEALT-----MVIQADKiKAAEIRSVYHLHQEEITRIKKECEREIRRLqldEKDARRFQLKIAELSAIIR------ 233
Cdd:pfam15964 557 aQQREQELTqkmqqMEAQHDK-TVNEQYSLLTSQNTFIAKLKEECCTLAKKL---EEITQKSRSEVEQLSQEKEylqdrl 632
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184497 234 -KLEDRNALLSEE--------------RNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLK 289
Cdd:pfam15964 633 eKLQKRNEELEEQcvqhgrmhermkqrLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQVP 703
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
356-462 |
9.23e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 38.77 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184497 356 RRSHAPCCPvPSGATPPTALCPPEPRPLLPCALRSHAPYCPVPSGATTPTALCPPEPRPLLPCALRGHAPCCPVHSLKLP 435
Cdd:PHA03247 2665 RRARRLGRA-AQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
90 100
....*....|....*....|....*..
gi 1907184497 436 SPDslcpSRAVPLLTAHSLLPYLLSTP 462
Cdd:PHA03247 2744 VPA----GPATPGGPARPARPPTTAGP 2766
|
|
| |
