|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
32-388 |
1.25e-89 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 279.50 E-value: 1.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQIELGKI 111
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 112 KSEQEQLQHTYAKKdadltssqnrlkdveallnakeaalntaVSERKTLENTLSDLqirvqelegglisaKKQLSDETLL 191
Cdd:pfam00038 81 RLAAEDFRQKYEDE----------------------------LNLRTSAENDLVGL--------------RKDLDEATLA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 192 RVDLENRCQSLMEELEFRKNMFEEEIKDTRRRH--ETRLVEVDSGRQMEyefkLAQALTDMRQQHDEQVKLYKEEMEQTY 269
Cdd:pfam00038 119 RVDLEAKIESLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLD----LTSALAEIRAQYEEIAAKNREEAEEWY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 270 VSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAE 349
Cdd:pfam00038 195 QSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQE 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 528491712 350 IRAKMQQQLDEYEQLLDVKLALDMEINAYRKLLEGEEER 388
Cdd:pfam00038 275 TRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| LTD |
pfam00932 |
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is ... |
437-544 |
1.76e-20 |
|
Lamin Tail Domain; The lamin-tail domain (LTD), which has an immunoglobulin (Ig) fold, is found in Nuclear Lamins, Chlo1887 from Chloroflexus, and several bacterial proteins where it occurs with membrane associated hydrolases of the metallo-beta-lactamase,synaptojanin, and calcineurin-like phosphoesterase superfamilies.
Pssm-ID: 460003 [Multi-domain] Cd Length: 108 Bit Score: 86.71 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 437 ASATGNVSIDELDVDG-----KFIRLHNNSEQDQPMAGFQLTRTIGEvtaTYKFTAKYNLKAGQKVTIWASNAGIS---- 507
Cdd:pfam00932 1 SSATGDVVISEVVYDGsggndEFIELYNTGSKAVDLSGWKLQDASGG---TYTFPNGTTLAPGQTVVVWTGSGTNSatag 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 528491712 508 SNPPADLIWKNQpswgtgeNIKVALLSPAGEEVAVRS 544
Cdd:pfam00932 78 YWGPSNAVWNNG-------GDAVALYDANGELVDSVG 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-330 |
6.99e-13 |
|
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: 72.01 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDvRNRELtglrtlyETELADARKALDDTARERARLQIELGKI 111
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-EVSEL-------EEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 112 KSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLL 191
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 192 RVDLENRCQSLMEELEfrknMFEEEIKDTRRRHEtRLVEVDSGRQMEYEfKLAQALTDMRQQHDEQVKLYKEEMEQTYVS 271
Cdd:TIGR02168 388 VAQLELQIASLNNEIE----RLEARLERLEDRRE-RLQQEIEELLKKLE-EAELKELQAELEELEEELEELQEELERLEE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528491712 272 KLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARA------WQDRINELEGALS 330
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkallkNQSGLSGILGVLS 526
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-390 |
1.22e-12 |
|
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: 71.24 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 7 TPAGQQSLSRGTSSTPLSPARISRLQEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREredvrnreltglrtlYETE 86
Cdd:TIGR02168 649 TLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE---------------LEEE 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 87 LADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSD 166
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 167 LQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLmeelEFRKNMFEEEIKDTRRRHETRlvevdSGRQMEYEFKLAQA 246
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESL----ERRIAATERRLEDLEEQIEEL-----SEDIESLAAEIEEL 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 247 LTDMRQQHDEQVKLYKEEMEQtyvsklenirlssemnsssaSMAREELREstlrveslagQLANLQKEARAWQDRINELE 326
Cdd:TIGR02168 865 EELIEELESELEALLNERASL--------------------EEALALLRS----------ELEELSEELRELESKRSELR 914
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528491712 327 galsHEKDLSRRLLAEKEREIAEIRAKMQQQLD----EYEQLLDVKLALDMEINAYRKLLEGEEERLK 390
Cdd:TIGR02168 915 ----RELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-371 |
1.63e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 64 QIREREDVRNRELTGLR-TLYETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEAL 142
Cdd:COG1196 217 ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 143 LNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRR 222
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 223 RHETRLvevdsgrqmeyEFKLAQALTDMRQQHDEQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASMAREELRESTLRVE 302
Cdd:COG1196 377 AEEELE-----------ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528491712 303 SLAGQLANLQKEARAWQDRINELEGALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLAL 371
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-389 |
7.18e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 84 ETE--LADARKALD---DTARERARlQIELGKIKSEQEQLQHTY--AKKDADLTSSQNRLKDVEALLNAKEAALNTAVSE 156
Cdd:TIGR02168 176 ETErkLERTRENLDrleDILNELER-QLKSLERQAEKAERYKELkaELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 157 RKTLENTLSDLQIRVQELEggliSAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRR---RHETRLVEVDS 233
Cdd:TIGR02168 255 LEELTAELQELEEKLEELR----LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERqleELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 234 GRQmEYEFKLAQ---ALTDMRQQHDEQVKLYKEEME--QTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQL 308
Cdd:TIGR02168 331 KLD-ELAEELAEleeKLEELKEELESLEAELEELEAelEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 309 ANLQKEARAWQDRINELEGALS-HEKDLSRRLLAEKEREIAEIRA----------KMQQQLDEYEQLLDVKLALDMEINA 377
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEelerleealeELREELEEAEQALDAAERELAQLQA 489
|
330
....*....|..
gi 528491712 378 YRKLLEGEEERL 389
Cdd:TIGR02168 490 RLDSLERLQENL 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-186 |
1.03e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 26 ARISRLQEK-----EELQQLNDRLAAYIDTVRSLESENSVLQIQIRErEDVRNRELtglrtlyETELADARKALDDTARE 100
Cdd:TIGR02169 329 AEIDKLLAEieeleREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFAET-------RDELKDYREKLEKLKRE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 101 R-------ARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQE 173
Cdd:TIGR02169 401 InelkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
170
....*....|...
gi 528491712 174 LEGGLISAKKQLS 186
Cdd:TIGR02169 481 VEKELSKLQRELA 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-364 |
3.02e-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: 50.45 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 160 LENTLSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEfrknMFEEEIKDTRRRHETRLVEVDSGRQM-- 237
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE----KLKERLEELEEDLSSLEQEIENVKSElk 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 238 EYEFKLAQALTDMRQQHDEQVKLYKEEME---QTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKE 314
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLSHsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 528491712 315 ARAWQDRINELEgalsHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQL 364
Cdd:TIGR02169 842 RIDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-354 |
4.99e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 98 ARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGG 177
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 178 LISAKKQLSDetLLRVDLENRCQSLMEElefrknmfeeeikdtrrrhetrLVEVDSGRQMEYEFKLAQALTDMRQQHDEQ 257
Cdd:COG4942 99 LEAQKEELAE--LLRALYRLGRQPPLAL----------------------LLSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 258 VKLYKEEMEQTyVSKLENIRLSSEMNSSSASMAREELRESTLRVESLagqLANLQKEARAWQDRINELEGAlshEKDLsR 337
Cdd:COG4942 155 LRADLAELAAL-RAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQE---AEEL-E 226
|
250
....*....|....*..
gi 528491712 338 RLLAEKEREIAEIRAKM 354
Cdd:COG4942 227 ALIARLEAEAAAAAERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-362 |
8.14e-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: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 66 RERED-VRNRELtgLRTLYETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLN 144
Cdd:TIGR02169 205 REREKaERYQAL--LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 145 AKEAalntavSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEfrknMFEEEIKDTRRRH 224
Cdd:TIGR02169 283 DLGE------EEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 225 ETRLVEVDSGRQ--MEYEFKLAQALTDMRQQHDEQVKlYKEEMEQtYVSKLENIRLSSEMNSSSASMAREELRESTLRVE 302
Cdd:TIGR02169 353 DKLTEEYAELKEelEDLRAELEEVDKEFAETRDELKD-YREKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528491712 303 SLAGQLANLQKEARAWQDRINELEGALSHEK----DLSRRLLAEKE--REIAEIRAKMQQQLDEYE 362
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEeyDRVEKELSKLQRELAEAE 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
89-396 |
1.57e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 89 DARKALDDTARERARLQIELGKIKSEQEQLQhtyakkdADLTSSQNRLKDVEALLNAKEAALNTAvserkTLENTLSDLQ 168
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALE-------AELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 169 IRVQELE---GGLISAKKQLSDETLLRVDLENRCQSLMEE---LEFRKNMFEEEIKDTRRRHETRLVEVDSGRQMEYEFK 242
Cdd:COG4913 675 AELERLDassDDLAALEEQLEELEAELEELEEELDELKGEigrLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 243 LAQALTD-----MRQQHDEQVKLYKEEMEQTYvSKLENIRlssemnsssasmaREELRESTLRVESLAGQLANLQkEARA 317
Cdd:COG4913 755 FAAALGDavereLRENLEERIDALRARLNRAE-EELERAM-------------RAFNREWPAETADLDADLESLP-EYLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 318 WQDRINElEGALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDvklaldmEINAYRKLLE-GEEERLKLSPSPS 396
Cdd:COG4913 820 LLDRLEE-DGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERID-------PLNDSLKRIPfGPGRYLRLEARPR 891
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
91-398 |
4.88e-05 |
|
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: 46.50 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 91 RKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIR 170
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 171 VQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRRRHETRLVevdsgrqmEYEFKLAQALTDM 250
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV--------DDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 251 RqQHDEQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLanLQKEARAWQDRINELEGALS 330
Cdd:pfam02463 324 K-KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--LESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528491712 331 HEKDLSRRLLAEKEREIAEIRAKMQQQLD----EYEQLLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSR 398
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELeileEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
35-272 |
8.82e-05 |
|
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: 45.55 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 35 EELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDvRNRELTGLRTLYETELADarkaLDDTARERARLQIELGKIKSE 114
Cdd:pfam01576 138 EDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEE-KAKSLSKLKNKHEAMISD----LEERLKKEEKGRQELEKAKRK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 115 QEQLQHTYAKKDADLtssQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDETLLRVD 194
Cdd:pfam01576 213 LEGESTDLQEQIAEL---QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 195 LENRCQSLMEELEFRKNMFEEEIKDT------RRRHETRLVEVDsgRQMEYEFKLAQA-LTDMRQQHDEQVKLYKEEMEQ 267
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTaaqqelRSKREQEVTELK--KALEEETRSHEAqLQEMRQKHTQALEELTEQLEQ 367
|
....*
gi 528491712 268 TYVSK 272
Cdd:pfam01576 368 AKRNK 372
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
31-390 |
1.56e-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: 44.83 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 31 LQEKEELQQLNDRLAAYIDT-VRSLESENSVLQIQ---IREREDVRNRELTGLRTLYETELADARKALDD-TARERARLQ 105
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREArDRQLAVAEDDLQALeseLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 106 IE------------LGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLsdLQIRVQE 173
Cdd:pfam12128 466 LEnfderierareeQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL--LHFLRKE 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 174 LEGGLISAKKQLSDETLLRVDLEnrcqslmeelefrKNMFEEEIKDTRRRHETRL----VEVDSGRQMEYEFK--LAQAL 247
Cdd:pfam12128 544 APDWEQSIGKVISPELLHRTDLD-------------PEVWDGSVGGELNLYGVKLdlkrIDVPEWAASEEELRerLDKAE 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 248 TDMRQQHDEQVKLyKEEMEQTYVsKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARAW-QDRINELE 326
Cdd:pfam12128 611 EALQSAREKQAAA-EEQLVQANG-ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLE 688
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528491712 327 GALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLA-LDMEINAYRKLLEGEEERLK 390
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALE 753
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
107-187 |
1.82e-04 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 43.95 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 107 ELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSER--------KTLENTLSDLQIRVQELEGGL 178
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELanaqaqalQTAQNNLATAQAALANAEARL 334
|
....*....
gi 528491712 179 ISAKKQLSD 187
Cdd:TIGR04320 335 AKAKEALAN 343
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
20-226 |
2.48e-04 |
|
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: 43.60 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 20 STPLSPARISRLQEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDvRNRELTGLRTLYETELADARKALDDTAR 99
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 100 ERARLQIELGKIKSE-QEQLQHTYAKKDAD----LTSSQN------RLKDVEALLNAKEAALNTAVSERKTLENTLSDLQ 168
Cdd:COG4942 91 EIAELRAELEAQKEElAELLRALYRLGRQPplalLLSPEDfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 528491712 169 IRVQELEggliSAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRRRHET 226
Cdd:COG4942 171 AERAELE----ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
85-256 |
3.78e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 85 TELADARKALDDTARERARLQ-------------IELGKIKSEQEQLQHTYAKKDADLtsSQNRLKDVEALLNAKEAALN 151
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaeryaaarERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 152 TAVSERKTLENTLSDLQIRVQELEGGLI-SAKKQLSDETLLRVDLENRCQSLME---ELEFRKNMFEEEIKDTRRRHETR 227
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEAllaALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190
....*....|....*....|....*....|.
gi 528491712 228 LVEVDS--GRQMEYEFKLAQALTDMRQQHDE 256
Cdd:COG4913 393 LEALEEelEALEEALAEAEAALRDLRRELRE 423
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
84-382 |
4.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 84 ETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKkdadLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENT 163
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE----IEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 164 LSDLQIRVQELEGGLISAKKQLSDETLLR--VDLENRCQSLMEELEFRKNMFEEEIKD----TRRRHETRLVEVDSGRQM 237
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEeyLDELREIEKRLSRLEEEINGIEERIKEleekEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 238 EYEFKLAQALTDMRQQHDEQVKLYKEEMEQTyVSKLENirlssemNSSSASMAREELREstlRVESLAGQLANLQKEARA 317
Cdd:PRK03918 355 EELEERHELYEEAKAKKEELERLKKRLTGLT-PEKLEK-------ELEELEKAKEEIEE---EISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528491712 318 WQDRINELEGA----------LSHEKDLsrRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLALDMEINAYRKLL 382
Cdd:PRK03918 424 LKKAIEELKKAkgkcpvcgreLTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELI 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-326 |
4.26e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 11 QQSLSRGTSSTPLSPARISRLQEKEE------------LQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRN----- 73
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEklkerleeleedLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNdlear 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 74 ------RELTGLRTLYETELADARKALDDTARERARLQIELG----KIKSEQEQLQHTYAKKD---ADLTSSQNRLKDVE 140
Cdd:TIGR02169 788 lshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekEIQELQEQRIDLKEQIKsieKEIENLNGKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 141 ALLNAKEAALNTAVS-------ERKTLENTLSDLQIRVQELEGGLISAKKQLSdetllrvDLENRCQSLMEELefrknmf 213
Cdd:TIGR02169 868 EELEELEAALRDLESrlgdlkkERDELEAQLRELERKIEELEAQIEKKRKRLS-------ELKAKLEALEEEL------- 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 214 eEEIKDTRRRHETrlvevDSGRQMEYefklaqaltdmrqqhdEQVKLYKEEMEQTyVSKLENIRLSsemnsssasmAREE 293
Cdd:TIGR02169 934 -SEIEDPKGEDEE-----IPEEELSL----------------EDVQAELQRVEEE-IRALEPVNML----------AIQE 980
|
330 340 350
....*....|....*....|....*....|...
gi 528491712 294 LRESTLRVESLAGQLANLQKEARAWQDRINELE 326
Cdd:TIGR02169 981 YEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
19-366 |
5.08e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 19 SSTPLSPARISRLQEKEELQQLNDRLAAYIDTVRSLESENSVlqiqirerEDVRNRELTGLRTLYETELADARKALDDTA 98
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL--------EKEQNKRLWDRDTGNSITIDHLRRELDDRN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 99 RERARLQIELGKIKSE-----QEQLQHTYAKKD---------ADLTSSQNRLKDVEALLNAKEAALNTAvserktlENTL 164
Cdd:pfam15921 426 MEVQRLEALLKAMKSEcqgqmERQMAAIQGKNEslekvssltAQLESTKEMLRKVVEELTAKKMTLESS-------ERTV 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 165 SDLQIRVQELEGGLISAKKQLSdETLLRVDLEnrcqslMEELEFRKNMfEEEIKDTRRRHET-RLVEVDSGRQMEYEFKL 243
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEIT-KLRSRVDLK------LQELQHLKNE-GDHLRNVQTECEAlKLQMAEKDKVIEILRQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 244 AQALTDMRQQHD--------EQVKLYKEEMEQtyvsKLENIRLSSEMNSSSASMAREELRESTLRVESLagQLANLQKEA 315
Cdd:pfam15921 571 IENMTQLVGQHGrtagamqvEKAQLEKEINDR----RLELQEFKILKDKKDAKIRELEARVSDLELEKV--KLVNAGSER 644
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528491712 316 -RAWQD-------RINELE------GALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLD 366
Cdd:pfam15921 645 lRAVKDikqerdqLLNEVKtsrnelNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-390 |
5.95e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 29 SRLQEKEELQQLNDRLAAYIDTVRSLESENsvlqiqIREREDVRNReltglrtlyeteLADARKALDDTARERARLQIEL 108
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAET------EREREELAEE------------VRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 109 GKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKKQLSDE 188
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 189 TLLRVDLENRCQSLMEELEFRKNMFE------EEIKDTRRRHETRLVEVDSGRQMEYEF--------------------- 241
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGnaedflEELREERDELREREAELEATLRTARERveeaealleagkcpecgqpve 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 242 ----------------KLAQALTDMRQQHDE-QVKLYKEEMEQTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESL 304
Cdd:PRK02224 463 gsphvetieedrerveELEAELEDLEEEVEEvEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 305 AGQLANLQKEARAWQDRINELEGAlshekdlsrrllAEKERE-IAEIRAKMQQQLDEYEQLLDVKLALDmEINAYRKLLE 383
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEE------------AEEAREeVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIE 609
|
....*..
gi 528491712 384 GEEERLK 390
Cdd:PRK02224 610 RLREKRE 616
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
32-369 |
7.69e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 32 QEKEELQQLNDRLAAYIDTVRSLESENSVLQIQIRE--------REDVRNRELTglRTLYETELADARKALDDTARERAR 103
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAEleseleeaREAVEDRREE--IEELEEEIEELRERFGDAPVDLGN 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 104 LQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISAKK 183
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 184 QLSdetllrvDLENRCQSLME--ELEFRKNMFEEEIKDTRRRHETRLVEVDSGR-QMEYEFKLAQAL-TDMRQQHDEQVK 259
Cdd:PRK02224 490 EVE-------EVEERLERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKReRAEELRERAAELeAEAEEKREAAAE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 260 LYKE-EMEQTYVSKLENirlssemnsssasmAREELRESTLRVESLAGQLANLQkEARAWQDRINELEGALSHEKDLSRR 338
Cdd:PRK02224 563 AEEEaEEAREEVAELNS--------------KLAELKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDERRE 627
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 528491712 339 LLAEKEREIAEIRAKMQ-----------QQLDEYEQLLDVKL 369
Cdd:PRK02224 628 RLAEKRERKRELEAEFDearieearedkERAEEYLEQVEEKL 669
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
13-362 |
9.81e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 13 SLSRGTSSTPLSPARISRLQEK-----EELQQLNDRLaayiDTVRSLESENSVLQIQIREREDVRNRELTGLRTLYETEL 87
Cdd:pfam15921 504 SLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEG----DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 88 ADARKAlDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVE----ALLNAKEAALNTAVSERKTLENT 163
Cdd:pfam15921 580 QHGRTA-GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 164 LSDLQIRVQELegglisakKQLSDE-TLLRVDLENRCqslmEELEFRKNMFEEEIKDTRR-----RHETRLVEVDSGRQM 237
Cdd:pfam15921 659 LNEVKTSRNEL--------NSLSEDyEVLKRNFRNKS----EEMETTTNKLKMQLKSAQSeleqtRNTLKSMEGSDGHAM 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 238 EYEFKLAQALTDMRQQHDE-QVKLYKEEMEQTYVSKLENIrlssemNSSSASMAREELRESTLRVESLAGQLANLQKEAR 316
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDAlQSKIQFLEEAMTNANKEKHF------LKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 528491712 317 AWQDRINELEGALshekDLSRRLLAE-----KEREIAEIRAKMQQQLDEYE 362
Cdd:pfam15921 801 RLKEKVANMEVAL----DKASLQFAEcqdiiQRQEQESVRLKLQHTLDVKE 847
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-175 |
1.37e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 26 ARISRLQEKEELQQLNDRLAAYIDTVRSLeSENSVLQiQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQ 105
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPEL-LQSPVIQ-QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 106 IELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELE 175
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-383 |
1.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 33 EKEELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRtlyetELADARKALDDTaRERARLQIELGKIK 112
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-----ELEEKVKELKEL-KEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 113 SEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELE------GGLISAKKQLS 186
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEeakakkEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 187 DETLLRVDLEnrcqslMEELEFRKNMFEEEIKDTRRRHETRLVEVDSGRQMEYEFKLAQALTDM-RQQHDEQvklYKEEM 265
Cdd:PRK03918 383 GLTPEKLEKE------LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcGRELTEE---HRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 266 EQTYVSKLENIRLSSEMNSSSASMAREELRE---------STLRVESLAGQLANLQ---------------KEARAWQDR 321
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRElekvlkkesELIKLKELAEQLKELEeklkkynleelekkaEEYEKLKEK 533
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528491712 322 INELEGALSH-EKDLSR--------RLLAEKEREIAEIRAKMQQQLDE--YEQLLDVKLALDMEINAYRKLLE 383
Cdd:PRK03918 534 LIKLKGEIKSlKKELEKleelkkklAELEKKLDELEEELAELLKELEElgFESVEELEERLKELEPFYNEYLE 606
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-207 |
1.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 26 ARISRLQEkeELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLY-ETELA---DARKALDDTARER 101
Cdd:COG4913 610 AKLAALEA--ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaEREIAeleAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 102 ARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLISA 181
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180
....*....|....*....|....*.
gi 528491712 182 KKQLSDEtllRVDLENRCQSLMEELE 207
Cdd:COG4913 768 RENLEER---IDALRARLNRAEEELE 790
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-361 |
2.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 35 EELQQLNDRLAAYIDTVRSLESENSV---LQIQIREREDVRNRELTGLRTLYETELADARKALDDTARERARLQIELGKI 111
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 112 KSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEA-ALNTAVSERKTLENTLSDLQIRVQELEGGLISA--------- 181
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEArLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallfl 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 182 ----KKQLSDETLLRVDLENRCQSLMEE--------LEFRKNMFEEEIKDTRRRHETRLVEVDSGRQMEYEFKLAQALTD 249
Cdd:COG4717 292 llarEKASLGKEAEELQALPALEELEEEeleellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 250 MRQ--------------QHDEQVKLYKEEMEQtyVSKLENiRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEA 315
Cdd:COG4717 372 IAAllaeagvedeeelrAALEQAEEYQELKEE--LEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 528491712 316 RAWQDRINELEGALshEKDLSRRLLAEKEREIAEIRAKMQQQLDEY 361
Cdd:COG4717 449 EELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEW 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
34-211 |
2.78e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 34 KEELQQLNDRLAAYIDTVRSLESENSVLQIQIRE---REDVRNRELTGLRTLYETELADARKALD----------DTARE 100
Cdd:COG4942 54 LKQLAALERRIAALARRIRALEQELAALEAELAElekEIAELRAELEAQKEELAELLRALYRLGRqpplalllspEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 101 RARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLkdvEALLNAKEAALNTAVSERKTLENTLSDLQIRVQELEGGLIS 180
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
170 180 190
....*....|....*....|....*....|.
gi 528491712 181 AKKQLSDETLLRVDLENRCQSLMEELEFRKN 211
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
86-185 |
3.45e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.10 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 86 ELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEA-LLNAKEAALNTAVSERKTLENTL 164
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAqALQTAQNNLATAQAALANAEARL 334
|
90 100
....*....|....*....|.
gi 528491712 165 SDLQIRVQELEGGLISAKKQL 185
Cdd:TIGR04320 335 AKAKEALANLNADLAKKQAAL 355
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
34-390 |
3.54e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 34 KEELQQLNDRLAAYIDTVRSLESE----NSVLQIQIREREDVRNREltglrTLYETELADARKALDDTARERARLQIELG 109
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKEleklNNKYNDLKKQKEELENEL-----NLLEKEKLNIQKNIDKIKNKLLKLELLLS 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 110 KIKSeQEQLQHTYAKKDADLTSSQNRLKD-----------VEALLNAKEAALNTAVSERKTLENTLSDLQIRVQEleggl 178
Cdd:TIGR04523 205 NLKK-KIQKNKSLESQISELKKQNNQLKDniekkqqeineKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 179 isAKKQLSdetllrvDLENRCQSLMEELEFRKNMFEE----EIKDTRRRHETRLVEVDSgrqmeyefKLAQALTDMRQQH 254
Cdd:TIGR04523 279 --NNKKIK-------ELEKQLNQLKSEISDLNNQKEQdwnkELKSELKNQEKKLEEIQN--------QISQNNKIISQLN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 255 DEQVKLYKEEMEqtyvSKLENIRLssemnsssasmaREELRESTLRVESLAGQLANLQKEARAWQDRINELEGALSHEKD 334
Cdd:TIGR04523 342 EQISQLKKELTN----SESENSEK------------QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528491712 335 LSRRL----------LAEKEREIAEIRAKMQQQLDEYEQLLDVKLALDMEINAYRKLLEGEEERLK 390
Cdd:TIGR04523 406 LNQQKdeqikklqqeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK 471
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
81-252 |
3.64e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 39.71 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 81 TLYETELADARKALDDTARERARLQIELgkikSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALntavserKTL 160
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAEL----DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQL-------AQA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 161 ENTLSDLQIRVQElegGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNmFEEEIKDTRRRHETRLVEVDSGRQmEYE 240
Cdd:pfam00529 123 QIDLARRRVLAPI---GGISRESLVTAGALVAQAQANLLATVAQLDQIYVQ-ITQSAAENQAEVRSELSGAQLQIA-EAE 197
|
170
....*....|..
gi 528491712 241 FKLAQALTDMRQ 252
Cdd:pfam00529 198 AELKLAKLDLER 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
256-399 |
8.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 256 EQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASmAREELRESTLRVESLAGQLANLQKE-------ARAWQDRINELEGA 328
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELRE-ELEKLEKEVKELEELKEEIEELEKEleslegsKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528491712 329 LShEKDLSRRLLAEKEREIAEIRAKMQQQL---DEYEQLLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSRV 399
Cdd:PRK03918 268 IE-ELKKEIEELEEKVKELKELKEKAEEYIklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
35-389 |
9.52e-03 |
|
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: 39.00 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 35 EELQQLNDRLAAYIDTVRSLESENSVLQIQIREREDVRNRELTGLRTLyETELADARKALDDTARERARLQIELGKIKSE 114
Cdd:pfam01576 363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKL-EGQLQELQARLSESERQRAELAEKLSKLQSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 115 QEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNtavserktlENTLSDLQI--RVQELEGGLISAKKQLSDETLLR 192
Cdd:pfam01576 442 LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ---------EETRQKLNLstRLRQLEDERNSLQEQLEEEEEAK 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 193 VDLENRCQSLMEELEFRKNMFEEEIKDTRRRHETRLvevdsgrqmeyefKLAQALTDMRQQHDEQVKLYkEEMEQTyvsk 272
Cdd:pfam01576 513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK-------------RLQRELEALTQQLEEKAAAY-DKLEKT---- 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 273 leNIRLssemnsssasmaREELRESTLRVESLAGQLANLQKEARawqdrinELEGALSHEKDLSRRLLAEKEREIAEIRA 352
Cdd:pfam01576 575 --KNRL------------QQELDDLLVDLDHQRQLVSNLEKKQK-------KFDQMLAEEKAISARYAEERDRAEAEARE 633
|
330 340 350
....*....|....*....|....*....|....*..
gi 528491712 353 KMQQQLDEYEQLLDVKLALDmEINAYRKLLEGEEERL 389
Cdd:pfam01576 634 KETRALSLARALEEALEAKE-ELERTNKQLRAEMEDL 669
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
84-389 |
9.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 84 ETELADARKALDDTARERARLQIELGKIKSEQEQLQHTYAKKDADLTSSQNRLKDVEALLNAKEAALNTAVSERKTLENT 163
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 164 LSDLQIRVQELEGGLISAKKQLSDETLLRVDLENRCQSLMEELEFRKNMFEEEIKDTRRRHETRLVEvdsgRQMEYEFKL 243
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK----EANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528491712 244 AQALTDMRQQHDEQVKLYKEEMEQTYVSKLENIRLSSEMNSSSASMAREELRESTLRVESLAGQLANLQKEARAWQDRIN 323
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528491712 324 ELEGALSHEKDLSRRLLAEKEREIAEIRAKMQQQLDEYEQLLDVKLALDMEINAYRKLLEGEEERL 389
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
|