|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
114-425 |
2.44e-155 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 445.13 E-value: 2.44e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 114 QEKEQIKTLNNRFASFIDKVRFLEQQNKMLETKWSLLQNQT-ATRSNIDAMFEAYIANLRRQLDSLGNDKMKLEADLHNM 192
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 193 QGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEAYMNKVELEAKLESLTDEINFLRQIFEEEIRELQSQIKDTSVVVEM 272
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 273 DNSRNLDMDAIVAEVRAQYEDIANRSRAEAEMWYKSKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQR 352
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41056085 353 ANLENQIAEAEERGEMAVRDAKGRIKDLEDALQRAKQDMARQIREYQDLMNVKLALDIEIATYRKLLEGEEDR 425
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-433 |
1.45e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 119 IKTLNNRFASFIDKVRFLEQQNKMLETKWSLLQNQTATRSNIDAMFEAYIANLRRQLDSLGNDKMKLEADLHNMQGLVED 198
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 199 FKNKYEDEINKRTECENEFVlikkdvdEAYMNKVELEAKLESLTDEInflrQIFEEEIRELQSQIKDTSVVVEMDNSRNL 278
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELA-------EAEAEIEELEAQIEQLKEEL----KALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 279 DMDAIVAEVRAQYEDIANRSRAEAE--MWYKSKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLE 356
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 357 NQIAEAEErgemAVRDAKGRIKDLEDALQRAKQDMARQIR----EYQDLMNVKLALDIEIATYRKLLEGEEDRLATGIKA 432
Cdd:TIGR02168 908 SKRSELRR----ELEELREKLAQLELRLEGLEVRIDNLQErlseEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
.
gi 41056085 433 I 433
Cdd:TIGR02168 984 L 984
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
87-111 |
3.12e-10 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 58.90 E-value: 3.12e-10
10 20
....*....|....*....|....*
gi 41056085 87 IQAVTVNKSLLAPLNLEIDPNIQIV 111
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-401 |
6.23e-10 |
|
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: 62.01 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 103 EIDPNIQIVRTQEKEQIKTLNNRFASFIDKVRFLEQQNKMLETKWSLLQNQtatrsnIDAMfEAYIANLRRQLDSLGNDK 182
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE------KEAL-ERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 183 MKLEADLHNMQGLVEDfKNKYEDEINKRTE--CENEFVLIKKDVDEAYMNKVELEAKLESLTDEINFL---RQIFEEEIR 257
Cdd:TIGR02169 254 EKLTEEISELEKRLEE-IEQLLEELNKKIKdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeerLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 258 ELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDIANRSRAEAEMWYKSKYEEMQtsankYGDDLRSTKTEIADLNRM 337
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD-----YREKLEKLKREINELKRE 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41056085 338 IQRLQSEIDAVKGQRANLENQIAEAEERG---EMAVRDAKGRIKDLEDALQRAKQDMARQIREYQDL 401
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
171-427 |
3.23e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 171 LRRQLDSLGNDK------MKLEADLHNMQGLV-----EDFKNKYEDEINKRTECENEFVLIKKDVDEAYMNKVELEAKLE 239
Cdd:COG1196 198 LERQLEPLERQAekaeryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 240 SLTDEINFLRQIFEEEIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDIANRSRAEAEMwykskyEEMQTSANK 319
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL------EEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 320 ygdDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEErgemAVRDAKGRIKDLEDALQRAKQDMARQIREYQ 399
Cdd:COG1196 352 ---ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260
....*....|....*....|....*...
gi 41056085 400 DLMNVKLALDIEIATYRKLLEGEEDRLA 427
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
233-434 |
8.28e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 233 ELEAKLESLTDEINFLRQIFE--EEIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDIAnrsRAEAEMwyksky 310
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELE---RLDASS------ 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 311 eemqtsankygDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGEmAVRDAKGRIKDLEDALQRAK-Q 389
Cdd:COG4913 685 -----------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELRALlE 752
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41056085 390 DMARQIREYQDLMNVKLALDIEIATYRKLLEGEEDRLATGIKAIN 434
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-386 |
4.14e-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: 49.67 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 102 LEIDPNIQIVRTqeKEQIKTLNNRFASFIDKVRFLEQQNKMLETKWSLLQNQTATRSNIDAMFEAYIANLRRQLDSLGND 181
Cdd:TIGR02168 720 ELEELSRQISAL--RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 182 KMKLEADLHNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEAYMNKVELEAKLESLTDEINFLRQIFEEEIRELQS 261
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 262 QIKDTSVVVEMDNSRNLDMDAIVAEVRaqyedianrsraeaemwykskyeEMQTSANKYGDDLRSTKTEIADLNRMIQRL 341
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELR-----------------------ELESKRSELRRELEELREKLAQLELRLEGL 934
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41056085 342 QSEIDAVKGQ---RANLENQIAEAEERG-EMAVRDAKGRIKDLEDALQR 386
Cdd:TIGR02168 935 EVRIDNLQERlseEYSLTLEEAEALENKiEDDEEEARRRLKRLENKIKE 983
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
110-434 |
1.31e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 110 IVRTQE-KEQIKTLNNRFASFIDKVRFLEQQNKMLETKwslLQNQTATRSNIDAMFEAyIANLRRQLDSLGNDKMKLEAD 188
Cdd:PRK03918 185 IKRTENiEELIKEKEKELEEVLREINEISSELPELREE---LEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 189 LHNMQGLVEDFKNKYED------EINKRTECENEFVLIKKDVDEAYMNKVELEAKLESLTDEINFLRQIFEE-------- 254
Cdd:PRK03918 261 IRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleekeerl 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 255 -EIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDIANRSRAEAEMWYKS---KYEEMQTSANKYGDDLRSTKTE 330
Cdd:PRK03918 341 eELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEElekAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 331 IADLNRMIQRLQSE-------------------IDAVKGQRANLENQIAEAEERgemaVRDAKGRIKDLEDALQRAKQ-- 389
Cdd:PRK03918 421 IKELKKAIEELKKAkgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEK----ERKLRKELRELEKVLKKESEli 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 41056085 390 ---DMARQIREYQDLMNVKLALDIEIAT--YRKL------LEGEEDRLATGIKAIN 434
Cdd:PRK03918 497 klkELAEQLKELEEKLKKYNLEELEKKAeeYEKLkeklikLKGEIKSLKKELEKLE 552
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
226-436 |
2.83e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 226 EAYMNKVeLEAKLESLTDEINFLRQ---IFEEEIRELQSQIKD---TSVVVEMDNSRNLDMDAIvAEVRAQYEDiANRSR 299
Cdd:COG3206 159 EAYLEQN-LELRREEARKALEFLEEqlpELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQQL-SELESQLAE-ARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 300 AEAEMWYKSKYEEMQTSANKYGDDLRST-----KTEIADLNRMIQRLQS-------EIDAVKGQRANLENQIAEAEERG- 366
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPviqqlRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRIl 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41056085 367 ---EMAVRDAKGRIKDLEDALQRAKQDMARQIREYQDLMNVKLALDIEIATYRKLLEG-EEDRLATGIKAINIS 436
Cdd:COG3206 316 aslEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRlEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-397 |
5.92e-05 |
|
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: 45.53 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 174 QLDSLGNDKMKLEADLHNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEAYMNKVELEAKLESLTDEINFLRQIFE 253
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 254 EEIRELQSQIKdtsVVVEMDNSRNLDM-----DAIVAEVRAQYEDIANRSRAEAEMWYKSKYEEMQTSAnkygDDLRSTK 328
Cdd:COG4942 101 AQKEELAELLR---ALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR----AELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056085 329 TEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGEMAVRDAKGRIKDLEDALQRAKQDMARQIRE 397
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
253-393 |
6.25e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 253 EEEIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDI-ANRSRAEAemWYKSKYEEMQTSANKYGD---DLRSTK 328
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAeAERSRLQA--LLAELAGAGAAAEGRAGElaqELDSEK 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056085 329 TEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGemavRDAKGRIKD----LEDALQRAKQDMAR 393
Cdd:PRK09039 130 QVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
114-422 |
7.31e-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: 45.49 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 114 QEKEQ-IKTLNNRFASFIDKVRFLEQQNKMLETKWSLLQN-QTATRSNIDAMFEA--YIANLRRQLDSLgndkMKLEADL 189
Cdd:pfam15921 506 QEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvQTECEALKLQMAEKdkVIEILRQQIENM----TQLVGQH 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 190 HNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEAYMnkvELEAKLESLTDEINFLRQIFEEEIRELQ--SQIKDtS 267
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAVKdiKQERD-Q 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 268 VVVEMDNSRNlDMDAIVAEvraqYEdIANRSraeaemwYKSKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDA 347
Cdd:pfam15921 658 LLNEVKTSRN-ELNSLSED----YE-VLKRN-------FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41056085 348 VKGQRANLENQIaeAEERGEMAVRDAKgrIKDLEDALQRAKQDmARQIREYQDLMNVKLAldiEIATYRKLLEGE 422
Cdd:pfam15921 725 AMKVAMGMQKQI--TAKRGQIDALQSK--IQFLEEAMTNANKE-KHFLKEEKNKLSQELS---TVATEKNKMAGE 791
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
162-393 |
8.10e-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: 45.49 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 162 AMFEAYIANLRRQLDSLGNDKMKLEADLHNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEaYMNKVEL-EAKLES 240
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ-LLNEVKTsRNELNS 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 241 LTDEINFLRQIFEEEIRELQS-----QIKDTSVVVEMDNSRNL-------DMDAIVAEVRAQYEDIANRSRAEAEMWYKS 308
Cdd:pfam15921 672 LSEDYEVLKRNFRNKSEEMETttnklKMQLKSAQSELEQTRNTlksmegsDGHAMKVAMGMQKQITAKRGQIDALQSKIQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 309 KYEEMQTSANKYGDDLRSTKT----EIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEergeMAVRDAKGRIKDLEDAL 384
Cdd:pfam15921 752 FLEEAMTNANKEKHFLKEEKNklsqELSTVATEKNKMAGELEVLRSQERRLKEKVANME----VALDKASLQFAECQDII 827
|
....*....
gi 41056085 385 QRAKQDMAR 393
Cdd:pfam15921 828 QRQEQESVR 836
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
322-433 |
1.08e-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: 44.37 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 322 DDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERgemaVRDAKGRIKDLEDALQRAKQDMARqireyqdl 401
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAE-------- 87
|
90 100 110
....*....|....*....|....*....|..
gi 41056085 402 mnvklaLDIEIATYRKLLEGEEDRLATGIKAI 433
Cdd:COG4942 88 ------LEKEIAELRAELEAQKEELAELLRAL 113
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
236-432 |
1.62e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 236 AKLESLTDEINFLRQIFEEEIRELQSQIKDtsvvvemdnsrnldMDAIVAEVRAQYEDIaNRSRAEAEmwykSKYEEMQT 315
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAA--------------LEARLEAAKTELEDL-EKEIKRLE----LEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 316 SANKYGDDLRSTKTeiadlNRMIQRLQSEIDAVKGQRANLENQIAEAEERgemaVRDAKGRIKDLEDALQRAKQDMARQI 395
Cdd:COG1579 74 RIKKYEEQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKK 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 41056085 396 REYQDLMNvklALDIEIATyrklLEGEEDRLATGIKA 432
Cdd:COG1579 145 AELDEELA---ELEAELEE----LEAEREELAAKIPP 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
165-397 |
1.68e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 165 EAYIANLRRQLDSLGNDKMKLEADLHNMQGLVEdfKNKYEDEINKRTECEN--EFVLIKKDVDEAYMNKVELEAKLESLT 242
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERVE--EAEALLEAGKCPECGQpvEGSPHVETIEEDRERVEELEAELEDLE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 243 DEINFLRQIFE--EEIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDIanRSRAEAemwYKSKYEEMQTSANKY 320
Cdd:PRK02224 489 EEVEEVEERLEraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL--RERAAE---LEAEAEEKREAAAEA 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 321 GDDLRSTKTEIADLNRMIQRLQSEIDAVK------GQRANLENQIAEAEER----GEM------AVRDAKGRIKDLEDAL 384
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKrealAELnderreRLAEKRERKRELEAEF 643
|
250
....*....|...
gi 41056085 385 QRAKQDMARQIRE 397
Cdd:PRK02224 644 DEARIEEAREDKE 656
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-428 |
1.86e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 235 EAKLESLTDEINFLRqifeEEIRELQSQIKDTsvvvemdnsrNLDMDAIVAEVRAQYEDIanrSRAEAEMwykskyEEMQ 314
Cdd:TIGR02168 224 ELELALLVLRLEELR----EELEELQEELKEA----------EEELEELTAELQELEEKL---EELRLEV------SELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 315 TSANKYGDDLRSTKTEIADLNRMIQRLQSeidavkgQRANLENQIAEAEErgemavrdakgRIKDLEDALQRAKQDMARQ 394
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRE-------RLANLERQLEELEA-----------QLEELESKLDELAEELAEL 342
|
170 180 190
....*....|....*....|....*....|....
gi 41056085 395 IREYQDLMNVKLALDIEIATYRKLLEGEEDRLAT 428
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
248-438 |
1.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 248 LRQIFEE---------EIRELQSQIKDTSvvvemdnsRNLD-MDAIVAEVRAQYE------DIANRSRA--------EAE 303
Cdd:COG1196 157 RRAIIEEaagiskykeRKEEAERKLEATE--------ENLErLEDILGELERQLEplerqaEKAERYRElkeelkelEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 304 MWYKsKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEA---EERGEMAVRDAKGRIKDL 380
Cdd:COG1196 229 LLLL-KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIARL 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 41056085 381 EDALQRAKQDMARQIREYQDLMNVKLALDIEIATYRKLLEGEEDRLATGIKAINISKQ 438
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-399 |
3.51e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 174 QLDSLGNDKMKLEADLHNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEAYMNKVELEAKLESLTDEINFL---RQ 250
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 251 IFEEEIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDIANRSRAEAEM---------WYKSKYEEMQTSANKYG 321
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEleeleaeleELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 322 DDLRSTKTEIADLN----RM----------IQRLQSEI------------DAVKGQRANLENQIAEAEERGEmAVRDAKG 375
Cdd:TIGR02168 386 SKVAQLELQIASLNneieRLearlerledrRERLQQEIeellkkleeaelKELQAELEELEEELEELQEELE-RLEEALE 464
|
250 260
....*....|....*....|....
gi 41056085 376 RIKDLEDALQRAKQDMARQIREYQ 399
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQ 488
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
220-402 |
4.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 220 IKKDVDEAYMNKVELEAKLESLTDEINFLRQIFEE---EIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEVRAQYEDI-- 294
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrv 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 295 -ANRSRAEAEMWYK------SKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGE 367
Cdd:PRK02224 336 aAQAHNEEAESLREdaddleERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
170 180 190
....*....|....*....|....*....|....*...
gi 41056085 368 MAVR---DAKGRIKDLEDALQRAKQDmarqIREYQDLM 402
Cdd:PRK02224 416 ELREerdELREREAELEATLRTARER----VEEAEALL 449
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
276-426 |
7.37e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 276 RNLDMDAIVAEVRAQY------EDIANRSRAEAEmwykskyEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAvk 349
Cdd:COG2433 361 PDVDRDEVKARVIRGLsieealEELIEKELPEEE-------PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE-- 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41056085 350 gqranLENQIAEAEErgemavrdakgRIKDLEDALQRAKQDMARQIREYQDLMnvklALDIEIATYRKLLEGEEDRL 426
Cdd:COG2433 432 -----LEAELEEKDE-----------RIERLERELSEARSEERREIRKDREIS----RLDREIERLERELEEERERI 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-386 |
1.09e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 116 KEQIKTLNNRFASFIDKVRFLEQQNKMLETKWSLLQNQTATRSNIDAMFEAYI--ANLRRQLDSLGNDKMKLEADLHNMQ 193
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 194 GLvedfknkyEDEINkrtECENEFVLIKKDVDEAYMNKVELEAKLESLTDEINFLRQIFEEeirelQSQIKDTSVVVEMD 273
Cdd:COG4913 689 AL--------EEQLE---ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA-----AEDLARLELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 274 N-SRNLDMDAIVAEVRAQYEDiaNRSRAEAEMWYKSK--YEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQS-EIDAVK 349
Cdd:COG4913 753 ErFAAALGDAVERELRENLEE--RIDALRARLNRAEEelERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLP 830
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 41056085 350 GQRANLENQIAEAEERG--------EMAVRDAKGRIKDLEDALQR 386
Cdd:COG4913 831 EYEERFKELLNENSIEFvadllsklRRAIREIKERIDPLNDSLKR 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-394 |
1.41e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 148 SLLQNQTATRSNIDAMFEAyIANLRRQLDSLGNDKMKLEADLHNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEa 227
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE- 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 228 ymnkveLEAKLESLTDEINFL-RQIFEEEIRELQSQIKDTSVVVEMDNSRNLDMDAIVAEvRAQYEDIANRSRAEAEmwy 306
Cdd:TIGR02169 770 ------LEEDLHKLEEALNDLeARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQ--- 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 307 kSKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGemavRDAKGRIKDLEDALQR 386
Cdd:TIGR02169 840 -EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL----RELERKIEELEAQIEK 914
|
....*...
gi 41056085 387 AKQDMARQ 394
Cdd:TIGR02169 915 KRKRLSEL 922
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
326-394 |
1.50e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.22 E-value: 1.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056085 326 STKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERgemaVRDAKGRIKDLEDALQRAKQDMARQ 394
Cdd:pfam11559 56 SLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
174-409 |
2.10e-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: 40.87 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 174 QLDSLGNDKM-KLEADLHNMQGLVEDFKNKYEDEINKRTE-----------CENEFVLIK---KDVDEAYMNKV-ELEAK 237
Cdd:pfam15921 246 QLEALKSESQnKIELLLQQHQDRIEQLISEHEVEITGLTEkassarsqansIQSQLEIIQeqaRNQNSMYMRQLsDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 238 LESLTDEINFLRQIFEEEIRELQSQI-----KDTSVVVEMDN----SRNLD--MDAIVAEVRAQYEDIANRSRAEAEMWy 306
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLvlansELTEARTERDQfsqeSGNLDdqLQKLLADLHKREKELSLEKEQNKRLW- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 307 kskyeEMQTSANKYGDDLRStktEIADLNRMIQRLQSEIDAVKGQ-RANLENQIAEAEERGEmavrdAKGRIKDLEDALQ 385
Cdd:pfam15921 405 -----DRDTGNSITIDHLRR---ELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNE-----SLEKVSSLTAQLE 471
|
250 260
....*....|....*....|....
gi 41056085 386 RAKQdMARQIREyqDLMNVKLALD 409
Cdd:pfam15921 472 STKE-MLRKVVE--ELTAKKMTLE 492
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
178-401 |
2.10e-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: 40.93 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 178 LGNDKMKLEADLHNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDEA-------YMNKVELEAKLESLTDEINFL-- 248
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklQLEKVTTEAKIKKLEEDILLLed 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 249 --------RQIFEEEIRELQSQIKDTSVVVEMDNSRNLDMDAIVAevraqyeDIANRSRAEAEMWykskyeeMQTSANKy 320
Cdd:pfam01576 146 qnsklskeRKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMIS-------DLEERLKKEEKGR-------QELEKAK- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 321 gddlRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGE----------MAVRDAKGRIKDLEDALQRAKQD 390
Cdd:pfam01576 211 ----RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeetaqknnalKKIRELEAQISELQEDLESERAA 286
|
250
....*....|.
gi 41056085 391 MARQIREYQDL 401
Cdd:pfam01576 287 RNKAEKQRRDL 297
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
314-399 |
2.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 314 QTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERgemaVRDAKGRIKDLEDALQRAKQDMAR 393
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEERREELGE 90
|
....*.
gi 41056085 394 QIREYQ 399
Cdd:COG3883 91 RARALY 96
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
226-359 |
2.59e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 40.43 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 226 EAYMNKVELEAKLESLTDEINFLRQIFEEEIRELQSQIKDTSVVVEMDNSrNLDMDAIVAEVRAQYEDIAN----RSRAE 301
Cdd:pfam13166 318 AFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKSIELDSVDAKIESI-NDLVASINELIAKHNEITDNfeeeKNKAK 396
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41056085 302 AEMWYkSKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQI 359
Cdd:pfam13166 397 KKLRL-HLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQL 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-393 |
4.74e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 196 VEDFKNKYED------EINKRTECENEFVLIKKDVDEAymnKVELEAKLESLTDEINFLRQI---FEEEIRELQSQIKDT 266
Cdd:PRK03918 157 LDDYENAYKNlgevikEIKRRIERLEKFIKRTENIEEL---IKEKEKELEEVLREINEISSElpeLREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 267 SVVVEMDNSRNLDMDAIVAEVRAQYEDIANRSRAEAEM------------------WYKSKYEEMQTSANKYGDDLRSTK 328
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELkkeieeleekvkelkelkEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41056085 329 TEIADLNRMIQRLQSEIDavkgQRANLENQIAEAEERGEmAVRDAKGRIKDLEDALQRAKQDMAR 393
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKKEE 373
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
332-425 |
4.90e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 332 ADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGEmavrDAKGRIKDLEDALQRAKQDMARQIREYQDLMNVKLALDIE 411
Cdd:PRK09039 77 QDLQDSVANLRASLSAAEAERSRLQALLAELAGAGA----AAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQ 152
|
90
....*....|....
gi 41056085 412 IATYRKLLEGEEDR 425
Cdd:PRK09039 153 LAALEAALDASEKR 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
233-425 |
5.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 233 ELEAKLESLTDEINFLRQIFEEEIRELQSQIKDTSVVVEmdnsRNLDMDAIVAEVRAQYEDI-ANRSRAEAEMWYKSKYE 311
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELeAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 312 EMQTSANKygddLRSTKTEIADLNRMIQRLQSEIDAVKG---QRANLENQIAEAEERGEMAVRD----AKGRIKDLEDAL 384
Cdd:COG4717 126 QLLPLYQE----LEALEAELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQlslaTEEELQDLAEEL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41056085 385 QRAKQDMARQIREYQDLMNVKLALDIEIATYRKLLEGEEDR 425
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
150-428 |
5.20e-03 |
|
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: 39.82 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 150 LQNQTATRSNIDAMFEAYIA--NLRRQLDS-LGNDKMKLEADLHNMQGLVEDFKNKYEDEINKRTECENEFVLIKKDVDE 226
Cdd:pfam12128 596 AASEEELRERLDKAEEALQSarEKQAAAEEqLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 227 AYMNKVE----LEAKLESLTDEINFLRQIFEEEIRELQSQIKDTSVVVEMDNSRNLdmDAIVAEVRAQYEDIANRSRAeA 302
Cdd:pfam12128 676 RKDSANErlnsLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL--ALLKAAIAARRSGAKAELKA-L 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 303 EMWYKSKYEEMQTSankyGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERGEMAVRDAKGRIKDLED 382
Cdd:pfam12128 753 ETWYKRDLASLGVD----PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ 828
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41056085 383 ALQRAKQDMARQIREYQDLMNVKLALDIEIATYRKLLEGEEDRLAT 428
Cdd:pfam12128 829 QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
307-438 |
7.68e-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: 38.59 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 307 KSKYEEMQTSANKYGDDLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLENQIAEAEERgemaVRDAKGRIKDLEDALQR 386
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE----LEAQKEELAELLRALYR 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41056085 387 AKQ--------------DMARQIREYQDLMNVKLALDIEIATYRKLLEGEEDRLATGIKAINISKQ 438
Cdd:COG4942 116 LGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
170-357 |
8.90e-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: 38.85 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 170 NLRRQLDSLGNDKMKLEADLHNMQGLVEDFKNKY------------EDEINKR-----TECENEFVLIKKDVDEAYMNKV 232
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlkkKIQKNKSlesqiSELKKQNNQLKDNIEKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056085 233 ELEAKLESLTDEINFLRQIFEEEIRELQSQIKDtsvvVEMDNSRNLDMDAIVAEVRAQYEDIANRSRAEaemWYKSKYEE 312
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSE 315
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41056085 313 MQTSANKygddLRSTKTEIADLNRMIQRLQSEIDAVKGQRANLEN 357
Cdd:TIGR04523 316 LKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
|
| |
