|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
55-366 |
2.72e-135 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 389.28 E-value: 2.72e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 55 NEKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAYFRTIEELQQKILCAKSENARLVVQIDNA 134
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 135 KLASDDFRTKYQTELSMRQLVEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKNHEEEVNTLRCQLGD-RLNVEV 213
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 214 DAAPTVDLNRVLNETRCQYEALVETNRREVEEWFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHCMR 293
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81905425 294 NSLENTLTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDVRARLECEINTYRSLLESEDCN 366
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-362 |
2.63e-11 |
|
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: 65.46 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 110 IEELQQKILCAKSENARLVVQIDNAKLASDDFRTKyqtelsmRQLVEADINSLRRILDELTLCKSDLEAQVESLREELLC 189
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLE-------VSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 190 LKKNhEEEVNTLRCQLGDRLnvEVDAAPTVDLNRVLNETRCQYEALVETNRREVEEWF---------TTQSEELNKQVVS 260
Cdd:TIGR02168 314 LERQ-LEELEAQLEELESKL--DELAEELAELEEKLEELKEELESLEAELEELEAELEelesrleelEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 261 SSEQLQSCQAEIIELRRTVNALEIELQAQHCMRNSLENTLTESE-ARYSSQLSQVQCLITNVESQLGEIRADLERQNQEY 339
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260
....*....|....*....|...
gi 81905425 340 QVLLDVRARLECEINTYRSLLES 362
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDS 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-363 |
6.93e-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: 57.76 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 63 LNDRLASYMEKVRQLERENAELECRIQERNQQQDpLVCPAYQAYFRTIEELQQKILCAKSENARLVVQIDNAKLASDDFR 142
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQIS-ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 143 TKYQTELSMRQLVEADINSLRRILDELTLCKSDLEAQVESLREELLclkknheeeVNTLRCQlgdrlNVEVDAAPTVDLN 222
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA---------NLRERLE-----SLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 223 RVLNETRCQYEALVETNRREVEEwFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELqaqhcmrNSLENTLTE 302
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEALLNERASLEEALALLRSELEELSEEL-------RELESKRSE 912
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81905425 303 SEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDVRARLECEINTYRSLLESE 363
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
65-360 |
1.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 65 DRLASYMEKVRQLERENAELECRIQERNQQQDplvcpAYQAYFRTIEELQQ------KILCAKSENARLVVQIDNAKLAS 138
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELD-----ALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 139 DDFRtkyqtELSmRQL--VEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKNHEEEVNTLRCQLGDRLnvevdaa 216
Cdd:COG4913 685 DDLA-----ALE-EQLeeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL------- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 217 ptvdlnrvlnETRCQyEALVETNRREVEEWFTTQSEELNKQVVSSSEQLQSCQAEII--------ELRRTVNALEiELQA 288
Cdd:COG4913 752 ----------EERFA-AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetaDLDADLESLP-EYLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 289 qhcMRNSLENT-LTESEARYSSQLSQ-----VQCLITNVESQLGEIRADLERQNQE-----------YQvlLDVRARLEC 351
Cdd:COG4913 820 ---LLDRLEEDgLPEYEERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDSlkripfgpgryLR--LEARPRPDP 894
|
....*....
gi 81905425 352 EINTYRSLL 360
Cdd:COG4913 895 EVREFRQEL 903
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
63-304 |
1.56e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 63 LNDRLASYMEKVRQLERENAELECRIQERNQqqdplvcpAYQAYFRTIEELQQKILCAKSENARLVVQIDNAKLASDDF- 141
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQK--------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELe 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 142 --RTKYQTELSMRQ----LVEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKN---HEEEVNTLRCQLGdRLNVE 212
Cdd:TIGR02168 330 skLDELAEELAELEekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqLELQIASLNNEIE-RLEAR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 213 VDAApTVDLNRVLNETRCQYEALVETNRREVEEWFTTQSEELNK---QVVSSSEQLQSCQAEIIELRRTVNALEIELQAQ 289
Cdd:TIGR02168 409 LERL-EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEElqeELERLEEALEELREELEEAEQALDAAERELAQL 487
|
250
....*....|....*
gi 81905425 290 HCMRNSLENTLTESE 304
Cdd:TIGR02168 488 QARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-361 |
2.13e-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: 53.15 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 77 LERENAELECRIQERNQQqdplvcpaYQAYFRTIEELQQKILcAKSENARLVVQIDNAKLASDDFRTKYQTELSMRQLVE 156
Cdd:TIGR02169 249 LEEELEKLTEEISELEKR--------LEEIEQLLEELNKKIK-DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 157 ADiNSLRRILDELtlckSDLEAQVESLREELlclkknheEEVNTLRCQLGDRLNvevdaaptvDLNRVLNETRCQYEALV 236
Cdd:TIGR02169 320 AE-ERLAKLEAEI----DKLLAEIEELEREI--------EEERKRRDKLTEEYA---------ELKEELEDLRAELEEVD 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 237 ETNRREVEEwfttqseelnkqVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHCMRNSLENTLTESEAR---YSSQLSQ 313
Cdd:TIGR02169 378 KEFAETRDE------------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineLEEEKED 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 81905425 314 VQCLITNVESQLGEIRADLERQNQEYQVLLDVRARLECEINTYRSLLE 361
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
98-353 |
2.80e-07 |
|
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: 52.07 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 98 LVCPAYQAYFRTIEELQQKIlcaksenARLVVQIDNAKLASDDFRTKYQTELSMRQLVEADINSLRRILDELTLCKSDLE 177
Cdd:COG4942 10 LLALAAAAQADAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 178 AQVESLREELLCLKKNHEEevntLRCQLGDRLNVEVDAAPTVDLNRVLNEtrcqyEALVETNRREveEWFTTQSEELNKQ 257
Cdd:COG4942 83 AELAELEKEIAELRAELEA----QKEELAELLRALYRLGRQPPLALLLSP-----EDFLDAVRRL--QYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 258 VvsssEQLQSCQAEIIELRRTVNALEIELQAqhcmrnsLENTLTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQ 337
Cdd:COG4942 152 A----EELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|....*.
gi 81905425 338 EYQVLLDVRARLECEI 353
Cdd:COG4942 221 EAEELEALIARLEAEA 236
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
57-350 |
4.04e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 57 KETMQFLNDRLASYMEKVRQLEREnaelecriqernqqqdplvcpayqayfrtIEELQQKilcaksenaRLVVQIDNakl 136
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAA-----------------------------LEEFRQK---------NGLVDLSE--- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 137 asddfrtkyQTELSMRQLveadinslrrildeltlckSDLEAQVESLREELlclkknheEEVNTLRCQLGDRLNVEVDAA 216
Cdd:COG3206 213 ---------EAKLLLQQL-------------------SELESQLAEARAEL--------AEAEARLAALRAQLGSGPDAL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 217 PTVDLNRVLNETRCQYEALvETNRREVEEWFTtqseELNKQVVSSSEQLQSCQAEI-IELRRTVNALEIELQAQhcmrNS 295
Cdd:COG3206 257 PELLQSPVIQQLRAQLAEL-EAELAELSARYT----PNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEAL----QA 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 81905425 296 LENTLTESEARYSSQLSQvqclITNVESQLGEIRADLERQNQEYQVLLdvrARLE 350
Cdd:COG3206 328 REASLQAQLAQLEARLAE----LPELEAELRRLEREVEVARELYESLL---QRLE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
143-361 |
1.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 143 TKYQT--ELSMRQLVEADINsLRRILDELtlckSDLEAQVESLREELLCLKKNHE--EEVNTLRCQL-GDRLNVEVDAAP 217
Cdd:TIGR02168 168 SKYKErrKETERKLERTREN-LDRLEDIL----NELERQLKSLERQAEKAERYKElkAELRELELALlVLRLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 218 TvdLNRVLNETRCQYEALvETNRREVEEwfttQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQhcmrnsle 297
Cdd:TIGR02168 243 E--LQEELKEAEEELEEL-TAELQELEE----KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL-------- 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81905425 298 ntlTESEARYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDVRARLECEINTYRSLLE 361
Cdd:TIGR02168 308 ---RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
152-350 |
2.92e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 152 RQLVEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKNHEEEVNTLRCQLGDRLNVEVDAAPTVDLNRVLNETRCQ 231
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 232 YEALVETNRREVEEwFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAqhcmRNSLENTLTESEARYSSQL 311
Cdd:COG1196 321 LEEELAELEEELEE-LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE----AEEELEELAEELLEALRAA 395
|
170 180 190
....*....|....*....|....*....|....*....
gi 81905425 312 SQVQCLITNVESQLGEIRADLERQNQEYQVLLDVRARLE 350
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-350 |
4.75e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 56 EKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQqdplvcpayqayfrtIEELQQKILCAKSENARLVVQIDNAK 135
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELE---------------LEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 136 LASDDFRTKYQTELSMRQLVEADINSLRRILDELTLCKSDLEAQVESLREELlclkKNHEEEVNTLRCQLGDRLNVEVDA 215
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL----AEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 216 AptvdlNRVLNETRcqyEALVETNRREVEEwftTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHCMRNS 295
Cdd:COG1196 385 A-----EELLEALR---AAAELAAQLEELE---EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 81905425 296 LENTLTESEARYSSQLSQvqclITNVESQLGEIRADLERQNQEYQVLLDVRARLE 350
Cdd:COG1196 454 LEEEEEALLELLAELLEE----AALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
63-358 |
1.29e-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: 47.42 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 63 LNDRLASYMEKVRQLERENAE---LECRIQERNQQQDPLvcPAYQAYFRTIEELQQKILCAKSENARLV----VQIDN-A 134
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEitkLRSRVDLKLQELQHL--KNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIENmT 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 135 KLASDDFRTKYQTELSMRQLvEADINSLRRILDELTLCKS-------DLEAQVESLREELLCLKKNHEEEVNTLR--CQL 205
Cdd:pfam15921 576 QLVGQHGRTAGAMQVEKAQL-EKEINDRRLELQEFKILKDkkdakirELEARVSDLELEKVKLVNAGSERLRAVKdiKQE 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 206 GDRLNVEVDAAPTvDLNRVLNEtrcqYEALVETnrreveewFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALeiE 285
Cdd:pfam15921 655 RDQLLNEVKTSRN-ELNSLSED----YEVLKRN--------FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM--E 719
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 81905425 286 LQAQHCMRNS--LENTLTESEARYSSQLSQVQCL---ITNVESQLGEIRADLERQNQEYQVLLDVRARLECEINTYRS 358
Cdd:pfam15921 720 GSDGHAMKVAmgMQKQITAKRGQIDALQSKIQFLeeaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
68-361 |
1.38e-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: 47.42 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 68 ASYMEKVRQLERENAELECRIQErnqqqdplvcpAYQAYFRTIEELQQKILCAKSENARLVVQIDNAKLASDDFRTKYQT 147
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELRE-----------AKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 148 ----------ELSM-----RQLVEAD------INSLRRILDELTLCKSDLEAQVESLREE--------LLCLKKNHE--E 196
Cdd:pfam15921 382 lladlhkrekELSLekeqnKRLWDRDtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqmerqMAAIQGKNEslE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 197 EVNTLRCQLgdrlnvevdaAPTVDLNRVLNETRCQYEALVETNRREVEEWFTTQSEElnkqvvssSEQLQSCQAEIIELR 276
Cdd:pfam15921 462 KVSSLTAQL----------ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--------ERAIEATNAEITKLR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 277 RTVNALEIELQAQHCMRNSLENTLTESEArYSSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDVRARLECEINTY 356
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR 602
|
....*
gi 81905425 357 RSLLE 361
Cdd:pfam15921 603 RLELQ 607
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
54-362 |
3.66e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.72 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 54 GNEKETMQFLNDRLASYMEKVRQLERENAELECRIQERNQQQDplvcpaYQAYFRTIE---ELQQKILCAKSENARLVVQ 130
Cdd:COG5185 271 GENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATES------LEEQLAAAEaeqELEESKRETETGIQNLTAE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 131 IDNAKLASDDFRTKYQTELSmrQLVEadINSLRRILDELtlckSDLEAQVESLREELLCLKKNHEEEVNTLRCQLGDRL- 209
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIE--NIVG--EVELSKSSEEL----DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLk 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 210 NVEVDAAptvDLNRVLNETRCQYEALVETNR---REVEEWFTTQSEELNKQVVSS-SEQLQSCQAEIIELRRTVNALEIE 285
Cdd:COG5185 417 AADRQIE---ELQRQIEQATSSNEEVSKLLNeliSELNKVMREADEESQSRLEEAyDEINRSVRSKKEDLNEELTQIESR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 286 LQAqhcMRNSLENTLTESEARYS---SQLSQVQCLITNVESQLG---------EIRADLERQNQEYQV---LLDVRARLE 350
Cdd:COG5185 494 VST---LKATLEKLRAKLERQLEgvrSKLDQVAESLKDFMRARGyahilalenLIPASELIQASNAKTdgqAANLRTAVI 570
|
330
....*....|..
gi 81905425 351 CEINTYRSLLES 362
Cdd:COG5185 571 DELTQYLSTIES 582
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
66-350 |
8.14e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 66 RLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAYfRTIEELQQKILCAKSENARLvvqidnaklasddfrtky 145
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENVKSELKEL------------------ 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 146 qtelsmrqlvEADINSLRRILDELTLCKSDLEAqveSLREELLCLKKNHEEEVNTLRCQLGDRLNvEVDAaptvDLNRVL 225
Cdd:TIGR02169 764 ----------EARIEELEEDLHKLEEALNDLEA---RLSHSRIPEIQAELSKLEEEVSRIEARLR-EIEQ----KLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 226 NEtRCQYEALVETNRREVEEWfTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHCMRNSLENTLTESEA 305
Cdd:TIGR02169 826 LE-KEYLEKEIQELQEQRIDL-KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 81905425 306 RYSSQLSQVQCLitnvESQLGEIRADLERQNQEYQVLLDVRARLE 350
Cdd:TIGR02169 904 KIEELEAQIEKK----RKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
155-337 |
8.77e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 155 VEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKN---HEEEVNTLRCQLGDRLNVE-VDAAPTVDLNRVLNET-- 228
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARALyRSGGSVSYLDVLLGSEsf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 229 -----RCQY-EALVETNRREVEEwFTTQSEELNKQvvssSEQLQSCQAEIIELRRTVNALEIELQAQHCMRNSLENTLTE 302
Cdd:COG3883 115 sdfldRLSAlSKIADADADLLEE-LKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190
....*....|....*....|....*....|....*
gi 81905425 303 SEARYSSQLSQVQCLITNVESQLGEIRADLERQNQ 337
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
56-361 |
9.52e-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: 44.78 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 56 EKETMQFLNDRLASYMEKVRQLERENAELECRIQ----ERNQQQDPLvcPAYQAYFRTIEELQQKiLCAKSENARLVVQI 131
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQqlceEKNALQEQL--QAETELCAEAEEMRAR-LAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 132 DNAKLASDDFRTkyQTELSMRQLVEADINSLRRILDE-------LTLCKSDLEAQVESLREELLCLkKNHEEEVNTLRCQ 204
Cdd:pfam01576 80 LESRLEEEEERS--QQLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDILLL-EDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 205 LGDRLN-VEVDAAPTVDLNRVLNETRCQYEALV----------ETNRREVEEWfttqSEELNKQVVSSSEQLQSCQAEII 273
Cdd:pfam01576 157 LEERISeFTSNLAEEEEKAKSLSKLKNKHEAMIsdleerlkkeEKGRQELEKA----KRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 274 ELRRTVNALEIELQAqhcmrnslenTLTESEARySSQLSQVQCLITNVESQLGEIRADLERQNQEYQVLLDVRARLECEI 353
Cdd:pfam01576 233 ELRAQLAKKEEELQA----------ALARLEEE-TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
....*...
gi 81905425 354 NTYRSLLE 361
Cdd:pfam01576 302 EALKTELE 309
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-362 |
4.22e-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: 42.75 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 163 RRILDELTLCkSDLEAQVESLREELLCLKKNHEE---EVNTLRCQLgDRLNVEVDAAPTVD-LNRVLNETRcQYEALVET 238
Cdd:TIGR02169 156 RKIIDEIAGV-AEFDRKKEKALEELEEVEENIERldlIIDEKRQQL-ERLRREREKAERYQaLLKEKREYE-GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 239 NRREveewftTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQhcmrNSLENTLTESEARyssqlsQVQCLI 318
Cdd:TIGR02169 233 EALE------RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEEQL------RVKEKI 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 81905425 319 TNVESQLGEIRADLERQNQEYQVLLDVRARLECEINTYRSLLES 362
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
58-347 |
4.76e-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: 42.36 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 58 ETMQFLNDRLASYMEKVRQL-ERENAELECRIQERNQQQDPLVcpayqayfRTIEELQQKILCAKSENARLVVQIDNAKL 136
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLE--------RSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 137 ASDDFRTKYQTELSMRQLVEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKNHE---EEVNTLRCQLgDRLNVEV 213
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklkREINELKREL-DRLQEEL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 214 DAAPT--VDLN---RVLNETRCQYEALVETNRREVEEwFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQA 288
Cdd:TIGR02169 416 QRLSEelADLNaaiAGIEAKINELEEEKEDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 81905425 289 qhcmrnsLENTLTESEARYSSQLSQVQCLITNVESQLGEIrADLERQNQEYQVLLDVRA 347
Cdd:TIGR02169 495 -------AEAQARASEERVRGGRAVEEVLKASIQGVHGTV-AQLGSVGERYATAIEVAA 545
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-364 |
6.17e-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: 41.67 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 252 EELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHCMRNSLENTLTESEARyssqlsqvqclITNVESQLGEIRAD 331
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE-----------LAELEKEIAELRAE 98
|
90 100 110
....*....|....*....|....*....|...
gi 81905425 332 LERQNQEYQVLLDVRARLEcEINTYRSLLESED 364
Cdd:COG4942 99 LEAQKEELAELLRALYRLG-RQPPLALLLSPED 130
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
83-385 |
6.37e-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: 41.96 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 83 ELECRIQERNQQQDPLVCPAYQAYFRTIEELQQKILCAKSENARlVVQIDNAKLASDDFRTKY------QTELSMRQLVE 156
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR-TIELKKEILEKKQEELKFvikelqQLEGSSDRILE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 157 ADiNSLRRILDELTlcKSDLEAQVESLREELLCLKKNHEEEVNTLRCQlgDRLNVEVDAApTVDLNRVLNETR---CQYE 233
Cdd:TIGR00606 476 LD-QELRKAERELS--KAEKNSLTETLKKEVKSLQNEKADLDRKLRKL--DQEMEQLNHH-TTTRTQMEMLTKdkmDKDE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 234 ALVETNRREVEEWFTTQSEELNKQVVSssEQLQSCQAEIIELRRTVNALEIELQAQHCMRNSLEN---TLTESEARYSSQ 310
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFPNKKQLE--DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNeleSKEEQLSSYEDK 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81905425 311 LSQVqCLITNVESQLGEIRADLERQNQEyqvlldvRARLECEINTYRSLLESedcnlpcnpcaTTNASGSCCGPC 385
Cdd:TIGR00606 628 LFDV-CGSQDEESDLERLKEEIEKSSKQ-------RAMLAGATAVYSQFITQ-----------LTDENQSCCPVC 683
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
70-342 |
1.03e-03 |
|
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: 41.26 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 70 YMEKVRQLERE----NAELECRIQERNQ--QQDPLVCPAYQAYFRTIEELQQKILCAKSENARL-------VVQIDNAKL 136
Cdd:pfam15921 340 YEDKIEELEKQlvlaNSELTEARTERDQfsQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnSITIDHLRR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 137 ASDD--------------FRTKYQTEL------------------SMRQLVEADINSLRRILDELTLCKSDLEAQVESLR 184
Cdd:pfam15921 420 ELDDrnmevqrleallkaMKSECQGQMerqmaaiqgkneslekvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 185 EELLCLKKNHE--EEVNTLRCQLGDRLNVEVDaaptvDLNRVLNE--------TRCQYEALVETNRREVEEWFTTQSEEL 254
Cdd:pfam15921 500 DLTASLQEKERaiEATNAEITKLRSRVDLKLQ-----ELQHLKNEgdhlrnvqTECEALKLQMAEKDKVIEILRQQIENM 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 255 NKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQHCMRNSLENTLTESEARYSS-QLSQVQclITNVESQ--------- 324
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlELEKVK--LVNAGSErlravkdik 652
|
330 340
....*....|....*....|....*..
gi 81905425 325 ------LGEI---RADLERQNQEYQVL 342
Cdd:pfam15921 653 qerdqlLNEVktsRNELNSLSEDYEVL 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
63-208 |
2.41e-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: 39.75 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 63 LNDRLASYMEKVRQLERENAELECRIQERNQQqdplvcpayqayfrtIEELQQKILCAKSENARLVVQI--------DNA 134
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKE---------------IAELRAELEAQKEELAELLRALyrlgrqppLAL 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 81905425 135 KLASDDFRTKYQTELSMRQLVEAD---INSLRRILDELTlcksDLEAQVESLREELLCLKKNHEEEVNTLRCQLGDR 208
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARreqAEELRADLAELA----ALRAELEAERAELEALLAELEEERAALEALKAER 197
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
159-290 |
2.62e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 159 INSLRRILDE-LTLCKSDLE------AQVESLREELLCLKKNHEEEVNTLRcqlgdRLNVEVDAAPTVDLNRVLNETRCQ 231
Cdd:smart00787 142 LEGLKEGLDEnLEGLKEDYKllmkelELLNSIKPKLRDRKDALEEELRQLK-----QLEDELEDCDPTELDRAKEKLKKL 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81905425 232 YEALVEtNRREVEEwFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVN------ALEIE-LQAQH 290
Cdd:smart00787 217 LQEIMI-KVKKLEE-LEEELQELESKIEDLTNKKSELNTEIAEAEKKLEqcrgftFKEIEkLKEQL 280
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-360 |
2.71e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 223 RVLNETrcqYEALVETNRREVEEWFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAQhcmrnSLENTLTE 302
Cdd:COG3206 152 AVANAL---AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAK-----LLLQQLSE 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81905425 303 SEARYS---SQLSQVQCLITNVESQLGEIRADLER--QNQEYQVLLDVRARLECEINTYRSLL 360
Cdd:COG3206 224 LESQLAearAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARY 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-364 |
3.31e-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: 39.65 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 252 EELNKQVVSSSEQLQSCQAEIIELRRTVNALEIEL-----------QAQHCMRNSLENTLTESEaRYSSQLSQVQCLITN 320
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleelsRQISALRKDLARLEAEVE-QLEERIAQLSKELTE 758
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 81905425 321 VESQLGEIRADLERQNQEYQVLLDVRARLECEINTYRSLLESED 364
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
63-363 |
3.70e-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: 39.39 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 63 LNDRLASYMEKVRQLERENAELECRIQERNQQQDPLVcpayqayfRTIEELQQKILCAKSENARLVVQI-DNAKLASDDF 141
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVS--------SLLNEAEGKNIKLSKDVSSLESQLqDTQELLQEET 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 142 RTKYQTELSMRQLvEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKNHEEEVNTLRCQLGDRLNVEVDAAptvDL 221
Cdd:pfam01576 482 RQKLNLSTRLRQL-EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELE---AL 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 222 NRVLNETRCQYEALVETNRREVEEWF-TTQSEELNKQVVSSSEQLQ-------------SCQ---------AEIIELRRT 278
Cdd:pfam01576 558 TQQLEEKAAAYDKLEKTKNRLQQELDdLLVDLDHQRQLVSNLEKKQkkfdqmlaeekaiSARyaeerdraeAEAREKETR 637
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 279 VNALEIELQAQHCMRNSLENTLTESEARYSSQLSQVQCLITNV----------ESQLGEIRADLERQNQEYQVLLDVRAR 348
Cdd:pfam01576 638 ALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhelerskralEQQVEEMKTQLEELEDELQATEDAKLR 717
|
330
....*....|....*
gi 81905425 349 LECEINTYRSLLESE 363
Cdd:pfam01576 718 LEVNMQALKAQFERD 732
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
81-262 |
4.16e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.97 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 81 NAELECRIQERNQQQDplvcpayqayfrTIEELQQKILCAKSE----NARLVVQIDNAKLASDDFRTKYQTELSMRQLVE 156
Cdd:pfam09787 46 TLELEELRQERDLLRE------------EIQKLRGQIQQLRTElqelEAQQQEEAESSREQLQELEEQLATERSARREAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 157 ADINSL----RRILDELTLCKSDLEAQVeslreellclkKNHEEEVNTLRCQLGDRLNVEVDAAPTVDLNRVLNETRCQY 232
Cdd:pfam09787 114 AELERLqeelRYLEEELRRSKATLQSRI-----------KDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLTETLIQK 182
|
170 180 190
....*....|....*....|....*....|
gi 81905425 233 EALVETNRREVEEwFTTQSEELNKQVVSSS 262
Cdd:pfam09787 183 QTMLEALSTEKNS-LVLQLERMEQQIKELQ 211
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
65-338 |
5.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 65 DRLASYMEKVRQLERENAELECRIQERNQQQDPLVCPAYQAyfRTIEELQQKILCAKS--ENARLVVQIDNAKLAS---- 138
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE--DRIERLEERREDLEEliAERRETIEEKRERAEElrer 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 139 -DDFRTKYQTELSMRQLVEADINSLRRILDELTLCKSDLEAQVESLR--EELLCLKKNHEEEVNTLRCQLGDRLNVEVDA 215
Cdd:PRK02224 546 aAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDEIERLREKREALAELNDER 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 216 APTVDLNRvlnETRCQYEALVETNRREVEEWFTTQSEELNKQVvssSEQLQSCQAEIIELRRTVNALEIELQAQHCMRN- 294
Cdd:PRK02224 626 RERLAEKR---ERKRELEAEFDEARIEEAREDKERAEEYLEQV---EEKLDELREERDDLQAEIGAVENELEELEELREr 699
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 81905425 295 --SLENTLTESEARYSSqlsqvqclITNVESQLGEIRADLERQNQE 338
Cdd:PRK02224 700 reALENRVEALEALYDE--------AEELESMYGDLRAELRQRNVE 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-335 |
6.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 152 RQLVEADINSLRRILDELTLCKSDLEAQVESLREELLCLKKNHEEevntlrcQLGDRLNV---EVDAApTVDLNRVlNET 228
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-------NGGDRLEQlerEIERL-ERELEER-ERR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 229 RCQYEALVET---NRREVEEWFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAqhcmrnsLENTLTESEA 305
Cdd:COG4913 361 RARLEALLAAlglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIASLER 433
|
170 180 190
....*....|....*....|....*....|
gi 81905425 306 RyssqlsqvqclITNVESQLGEIRADLERQ 335
Cdd:COG4913 434 R-----------KSNIPARLLALRDALAEA 452
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
176-362 |
6.56e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 176 LEAQVESLREELlclkKNHEEEVNTLRCQLGDrlnVEVDAAPTVDLNRvLNETRCQYEALvETNRREVEEWFTTQSEELN 255
Cdd:COG3206 180 LEEQLPELRKEL----EEAEAALEEFRQKNGL---VDLSEEAKLLLQQ-LSELESQLAEA-RAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 256 KQVVSSSEQLQScqAEIIELRRTVNALEIELQaqhcmrnslentltESEARYSSQLSQVQCL---ITNVESQL-GEIRAD 331
Cdd:COG3206 251 SGPDALPELLQS--PVIQQLRAQLAELEAELA--------------ELSARYTPNHPDVIALraqIAALRAQLqQEAQRI 314
|
170 180 190
....*....|....*....|....*....|.
gi 81905425 332 LERQNQEYQVLLDVRARLECEINTYRSLLES 362
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAE 345
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
239-350 |
7.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.38 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 239 NRREVEEWFTTQSEELNKQVVSSSEQLQSCQAEIIELRRTVNALEIELQAqhcmRNSLENTLTESEARYSSQLSQVQCLI 318
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE----AQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110
....*....|....*....|....*....|..
gi 81905425 319 TNVESQLGEIRADLERQNQEYQVLLDVRARLE 350
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELE 343
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
66-198 |
7.51e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 38.30 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 66 RLASYMEKVRQLER-------ENAELECRIQERNqqqdplvcpayqayfRTIEELQQKILCAKSEnARLVVQIDNaklas 138
Cdd:COG2433 407 ELTEEEEEIRRLEEqverleaEVEELEAELEEKD---------------ERIERLERELSEARSE-ERREIRKDR----- 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 139 ddfrtkyqtELSMRqlvEADINSLRRILDEltlcksdLEAQVESLREELLCLKKNHEEEV 198
Cdd:COG2433 466 ---------EISRL---DREIERLERELEE-------ERERIEELKRKLERLKELWKLEH 506
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
54-357 |
8.76e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 54 GNEKETMQFLNDRLASYMEKVRQLE------RENAELECRIQERNQQQDPLVC--PAYQAYFRTIEELQQKIlcaksENA 125
Cdd:PRK01156 308 ENKKQILSNIDAEINKYHAIIKKLSvlqkdyNDYIKKKSRYDDLNNQILELEGyeMDYNSYLKSIESLKKKI-----EEY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 126 RlvvqIDNAKLASDDFRTKYQTELSMRQLVeADINSLRRILDELTLCKSDLEAQVESLREELLCLKKNHEEEVNTLRC-- 203
Cdd:PRK01156 383 S----KNIERMSAFISEILKIQEIDPDAIK-KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpv 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 204 ---QLGDRLNVEVDAAPTVDLNRV---LNETRCQYEALVETNRREVEEWFTTQSEELNKqVVSSSEQLQSCQAEIIELRR 277
Cdd:PRK01156 458 cgtTLGEEKSNHIINHYNEKKSRLeekIREIEIEVKDIDEKIVDLKKRKEYLESEEINK-SINEYNKIESARADLEDIKI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81905425 278 TVNaleiELQAQHCMRNSLENT-----LTESEARYSSQL---SQVQCL-ITNVESQLGEIRA---DLERQNQEYQV-LLD 344
Cdd:PRK01156 537 KIN----ELKDKHDKYEEIKNRykslkLEDLDSKRTSWLnalAVISLIdIETNRSRSNEIKKqlnDLESRLQEIEIgFPD 612
|
330 340
....*....|....*....|
gi 81905425 345 VRA-------RLECEINTYR 357
Cdd:PRK01156 613 DKSyidksirEIENEANNLN 632
|
|
| |
