|
Name |
Accession |
Description |
Interval |
E-value |
| HD_SAS6_N |
cd10142 |
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ... |
4-144 |
4.02e-58 |
|
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; Spindle assembly abnormal protein 6 (SAS6) is a central scaffolding component of the centrioles that ensures their 9-fold symmetry. It is required for centrosome biogenesis and duplication, and is required for both mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. It is also required for the recruitment of microcephaly protein STIL to the procentriole and for STIL-mediated centriole amplification. SAS6 is comprised of an N-terminal globular head domain, a centrally located coiled-coil domain, and a disordered C-terminus. These monomers homodimerize symmetrically, through two dimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These homodimers can self-assemble into a 9-fold symmetric cartwheel structure comprised of nine SAS6 homodimers associated via their head domains; the dimerized coiled-coil domains being the spokes, the central hub being the head domains. This model corresponds to the N-terminal head domain of SAS6, which is structurally related to other XRCC4-superfamily members, XRCC4, PAXX, XLF and CCDC61.
Pssm-ID: 408998 Cd Length: 137 Bit Score: 190.84 E-value: 4.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 4 LLFNKRLQVLVKSKDTDERRSVIRVSIELQlPSSPVHRKDLVVRLTDDTDLYFLYNLIISEEDFQSLKVQQGLLIDFTSF 83
Cdd:cd10142 1 VLYSRELPVEVKSQDREERLEVLRVKIEIL-SSGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688608304 84 PQKFIDLLEQCICEQDKENPRFLLQLSSSSsafDHSPSNLNIVETNAFKHLTHLSLKLLPG 144
Cdd:cd10142 80 PQKLIDLLELCIKEESKEPPKFLLVLVISS---DKGRATLEIVETNPFKHLTHLSLKFLPG 137
|
|
| SAS-6_N |
pfam16531 |
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar ... |
44-141 |
8.09e-28 |
|
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar protein, both in C.elegans and in humans. The N-terminal domain is the region through which the 9 rod-shaped homodimers that SAS-6 forms on oligomerization interact with each other. Proper functioning of the centriole requires this correct oligomerization.
Pssm-ID: 465163 Cd Length: 88 Bit Score: 106.89 E-value: 8.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 44 LVVRLTDDTDLYFLYNLIISEEDFQSLKVQQGLLIDFTSFPQKFIDLLEQCICEQDkenprfllqlSSSSSAFDHSPSNL 123
Cdd:pfam16531 1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKEPN----------LLVFLIQDDGTATL 70
|
90
....*....|....*...
gi 688608304 124 NIVETNAFKHLTHLSLKL 141
Cdd:pfam16531 71 VFIENNEFKNLEHLSLDF 88
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-475 |
2.11e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 161 KEEKQQLQQKLRKTEEDLTR----------QLN--YAQ-------QTLSEKSRELDK----LRSEWTSQTTSLSSRHMQD 217
Cdd:COG1196 171 KERKEEAERKLEATEENLERledilgelerQLEplERQaekaeryRELKEELKELEAelllLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 218 LTAEREKALETQSRLQQQNEQLRQELEsshhrstqQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSK 297
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELE--------ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 298 QQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTV 377
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 378 KSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEAT 457
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330
....*....|....*...
gi 688608304 458 VQKLDESREVLKTNENVI 475
Cdd:COG1196 483 LEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-498 |
2.79e-16 |
|
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: 82.80 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 161 KEEKQQLQQKLRKTEEDLTRqlnyAQQTLSEKSRELDKLRSewtsqttslssrhmQDLTAEREKALETQSRlQQQNEQLR 240
Cdd:TIGR02168 171 KERRKETERKLERTRENLDR----LEDILNELERQLKSLER--------------QAEKAERYKELKAELR-ELELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 241 QELESsHHRSTQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERL 320
Cdd:TIGR02168 232 LRLEE-LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 321 LNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISK-------LESTVKSLSEELIKANGIIKK 393
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaeleeLESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 394 LQADLKALLGKIKV----KNSVTVSQEKILQETSDKLQRQQR-ELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVL 468
Cdd:TIGR02168 391 LELQIASLNNEIERlearLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350
....*....|....*....|....*....|
gi 688608304 469 KTNENVITWLNKQLNENQlSRKQETVAMFE 498
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQ-ARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-464 |
6.45e-16 |
|
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: 81.64 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 162 EEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLSSRHMQDLTAEREkaletQSRLQQQNEQLRQ 241
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ-----ISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 242 ELESSHHRSTQQLQTkVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLL 321
Cdd:TIGR02168 741 EVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 322 NQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKANGIIKKLQADLKAL 401
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688608304 402 LGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRL-----------SLKEEEAAKLKEQLEATVQKLDES 464
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqerlseeySLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-447 |
1.91e-12 |
|
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: 70.48 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLRKTEEDLT---RQLNYAQQTLSEKSRELDKLRSEWTSQTTSLSSRHMQDLTAEREKALETQSRLQ 233
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIEnvkSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 234 QQNEQLRQELESSHHRStQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSE 313
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 314 CHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQlqisklESTVKSLSEELIKANgiIKK 393
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE------EIPEEELSLEDVQAE--LQR 962
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688608304 394 LQADLKALlGKIKVKN----SVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEA 447
Cdd:TIGR02169 963 VEEEIRAL-EPVNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
162-461 |
7.61e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 162 EEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLssrhmQDLTAEREKALETQSRLQQQNEQLRQ 241
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-----ARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 242 ELEsshhRSTQQLQTKVSELETANRELIDkkyksdstirdlkakltsLEEECQRSKQQVLSLRRENSALDSECHEKERLL 321
Cdd:COG1196 324 ELA----ELEEELEELEEELEELEEELEE------------------AEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 322 NQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKANGIIKKLQADLKAL 401
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 402 LGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKL 461
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-496 |
1.01e-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: 65.08 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 279 IRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKdkdqlvlRTKEVLEATQQQKNS 358
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-------RLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 359 VEGNAESKQLQISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQ 438
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688608304 439 RLSLKE---EEAAKLKEQLEATVQKLDESREVLKTNENVITwlnKQLNENQLSRKQETVAM 496
Cdd:TIGR02168 832 RIAATErrlEDLEEQIEELSEDIESLAAEIEELEELIEELE---SELEALLNERASLEEAL 889
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
212-463 |
8.21e-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: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 212 SRHMQDLTAEREKALETQSRLQQQNEQLRQELEsshhRSTQQLQTKVSELETANRElidkkyksdstIRDLKAKLTSLEE 291
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELS----DASRKIGEIEKEIEQLEQE-----------EEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 292 ECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLE-----QEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESK 366
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 367 QLQISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVT----------VSQEKILQETSDKLQRQQRELQDT 436
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELeeleaalrdlESRLGDLKKERDELEAQLRELERK 904
|
250 260
....*....|....*....|....*..
gi 688608304 437 QQRLSLKEEEAAKLKEQLEATVQKLDE 463
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-470 |
1.94e-09 |
|
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: 60.85 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 162 EEKQQLQQKLRKTEEDLTRqlnyAQQTLSEKSRELDKLRSEwtsqttslssrhmqDLTAEREKALETQSRLQQQNEQLR- 240
Cdd:TIGR02169 170 RKKEKALEELEEVEENIER----LDLIIDEKRQQLERLRRE--------------REKAERYQALLKEKREYEGYELLKe 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 241 -QELESSHHRSTQQLQTKVSELETANRELIDKKYKSDS---TIRDLKAKLTSL-EEECQRSKQQVLSLRRENSALDSECH 315
Cdd:TIGR02169 232 kEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEieqLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 316 EKERLLNQLQTRVAVLEQEIkdkdqlvlrtkevlEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELikangiikklq 395
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEI--------------DKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------- 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688608304 396 ADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSL----KEEEAAKLKEQLEATVQKLDESREVLKT 470
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEelqrLSEELADLNAAIAGIEAKINELEEEKED 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-506 |
3.17e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLRKTEEDLTRQLNYAQ--QTLSEKSRELDKLRSEWTSQTTSLSSRHMQDLTAEREKALETQSRLQQ 234
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 235 QNEQLRQELEsshhrstqQLQTKVSELETA-------NRELIDKKYKSdsTIRDLKAKLTSLEEECQRSKQQVLSLRREN 307
Cdd:PRK03918 413 RIGELKKEIK--------ELKKAIEELKKAkgkcpvcGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 308 SALDSECHEKERLLNQLQTrvavLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSE---EL 384
Cdd:PRK03918 483 RELEKVLKKESELIKLKEL----AEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 385 IKANGIIKKLQADLKALLGKIKVKNSVTVSQ-EKILQETsDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDE 463
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEElEERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 688608304 464 SREVLKTNENVITWLNKQLNENQLSRKQETVAMFETPAAALRS 506
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRA 680
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-387 |
5.85e-09 |
|
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: 59.31 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLrkteEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQ-----------------TTSLSSRHMQDLT 219
Cdd:TIGR02169 246 LASLEEELEKLTEEI----SELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigeleaeiaslerSIAEKERELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 220 AEREKALETQSRLQQQNEQLRQELESSHHRSTQqLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQ 299
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 300 VLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEI-------KDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISK 372
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKIneleeekEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
250
....*....|....*
gi 688608304 373 LESTVKSLSEELIKA 387
Cdd:TIGR02169 481 VEKELSKLQRELAEA 495
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
169-491 |
9.90e-09 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.38 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 169 QKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQT----TSLSSRHMQDLTAEREKAL-ETQSRLQQQNEQLrQEL 243
Cdd:PRK11281 76 DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETretlSTLSLRQLESRLAQTLDQLqNAQNDLAEYNSQL-VSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 244 ESSHHRSTQQLQTKVSELETANREL----IDKKYKSDSTIRDLKAKLTSLEeecQRSKQQVLSLrrENSALDSECHEKER 319
Cdd:PRK11281 155 QTQPERAQAALYANSQRLQQIRNLLkggkVGGKALRPSQRVLLQAEQALLN---AQNDLQRKSL--EGNTQLQDLLQKQR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 320 LL-----NQLQTRVAVLEQEIKDKdQLVLRTKEVLEATQQQK-NSVEGNAESKQ-----LQISK--LESTVK--SLSEEL 384
Cdd:PRK11281 230 DYltariQRLEHQLQLLQEAINSK-RLTLSEKTVQEAQSQDEaARIQANPLVAQeleinLQLSQrlLKATEKlnTLTQQN 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 385 IKANGI--------------IKKLQADLkaLLGKIKVKNSVTVSQEKILQETSDK---LQRQQRELqdTQQRLSL----- 442
Cdd:PRK11281 309 LRVKNWldrltqsernikeqISVLKGSL--LLSRILYQQQQALPSADLIEGLADRiadLRLEQFEI--NQQRDALfqpda 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688608304 443 ---------KEEEAAKLKEQLEatvQKLDESREVLktnENVITWLNKQLNEN---QLSRKQ 491
Cdd:PRK11281 385 yidkleaghKSEVTDEVRDALL---QLLDERRELL---DQLNKQLNNQLNLAinlQLNQQQ 439
|
|
| Sas6_CC |
pfam18594 |
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ... |
146-175 |
1.31e-08 |
|
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of spindle assembly abnormal protein 6 (Sas6). The highly conserved protein SAS-6 constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis.Structural analysis of Sas6 show that similar to XLF, and XRCC4 it forms a parallel coiled-coil dimer.
Pssm-ID: 408377 [Multi-domain] Cd Length: 30 Bit Score: 50.74 E-value: 1.31e-08
10 20 30
....*....|....*....|....*....|
gi 688608304 146 DTDIKKYLASCLSSVKEEKQQLQQKLRKTE 175
Cdd:pfam18594 1 DSEVKKYLADCLKSLKEEKQLLEQKLKKTE 30
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-388 |
1.45e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 153 LASCLSSVKEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSewTSQTTSLSSRHMQDLTAEREKALETQSRL 232
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--LERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 233 QQQNEQLRQELESSHHRSTQQLQTKVSELETANRELIDKKYKSDSTIRD---LKAKLTSLEEECQRSKQQVLSLRRENSA 309
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqyLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688608304 310 LDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKAN 388
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
153-484 |
1.83e-08 |
|
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: 57.34 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 153 LASCLSSVKEEKQQLQQKLRKTEE---DLTRQLNYAQQTLSEKSRELD---KLRSEWTSQTTSLSSRhMQDLTAEREKAL 226
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTqlnQLKDEQNKIKKQLSEKQKELEqnnKKIKELEKQLNQLKSE-ISDLNNQKEQDW 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 227 --ETQSRLQQQNEQLRQeLESSHHRSTQ---QLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVL 301
Cdd:TIGR04523 309 nkELKSELKNQEKKLEE-IQNQISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 302 SLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLS 381
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 382 EELIKANGIIKKLQADLKALLGKIKVKNS---VTVSQEKILQETSDKLQRQQRELQDTQQRLS----------------L 442
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLEsekkekeskisdledeL 547
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 688608304 443 KEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNE 484
Cdd:TIGR04523 548 NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQE 589
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-506 |
2.03e-08 |
|
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: 57.37 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 220 AEREKALETQSRLQQQNEQLRQELesshhrstQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQ 299
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKAL--------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 300 VLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEvleatqqqknsvegnaeskqlQISKLESTVKS 379
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE---------------------ELKALREALDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 380 LSEELIKANGIIKKLQADLKALLGKI---KVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLK-----------EE 445
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIaatERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallneraslEE 887
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688608304 446 EAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNENQLsRKQETVAMFETPAAALRS 506
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQERLSE 947
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
311-546 |
2.69e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 311 DSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKANGI 390
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 391 IKK-----------LQA-DLKALLGKIKVKNSVTVSQEKILQETS---DKLQRQQRELQDTQQRLSLKEEEAAKLKEQLE 455
Cdd:COG3883 95 LYRsggsvsyldvlLGSeSFSDFLDRLSALSKIADADADLLEELKadkAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 456 AtvqKLDESREVLKTNENVITWLNKQLNENQLSRKQETVAMFETPAAALRSAAVPHNMVQFNPMSVKPSAAEVSPAAFSQ 535
Cdd:COG3883 175 A---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250
....*....|.
gi 688608304 536 PANKENSEPVG 546
Cdd:COG3883 252 AGAAGAAAGSA 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
277-495 |
3.37e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 277 STIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQK 356
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 357 NSVEGNAES--KQLQISKLESTVKSL-----SEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQ 429
Cdd:COG4942 100 EAQKEELAEllRALYRLGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688608304 430 QRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNENQLSRKQETVA 495
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
157-480 |
7.94e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLRKTE---EDLTRQLNYAQQTLSEKSRELDKLRSEwtsqtTSLSSrhmqdltAEREKALETQSRLQ 233
Cdd:PRK02224 253 LETLEAEIEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAE-----AGLDD-------ADAEAVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 234 QQNEQLRQELES-----SHHRST--------QQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQV 300
Cdd:PRK02224 321 DRDEELRDRLEEcrvaaQAHNEEaeslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 301 LSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEA------TQQQKNS--VEGNAESKQlQISK 372
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecGQPVEGSphVETIEEDRE-RVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 373 LESTVKSLSEELIKANGII------KKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEE 446
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLeraedlVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
330 340 350
....*....|....*....|....*....|....
gi 688608304 447 AAKLKEQLEATVQKLDESREVLKTNENVITWLNK 480
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
185-383 |
2.22e-07 |
|
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: 52.84 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 185 AQQTLSEKSRELDKLRS---EWTSQTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLR---QELESSHHRSTQQLQTKV 258
Cdd:pfam09787 16 AARILQSKEKLIASLKEgsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRtelQELEAQQQEEAESSREQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 259 SELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSAldsechEKERLLNQLQTRV------AVLE 332
Cdd:pfam09787 96 QELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREA------EIEKLRNQLTSKSqssssqSELE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 688608304 333 QEIKDKDQLVLRTKEVLEATQQQKNSVegnaeskQLQISKLESTVKSLSEE 383
Cdd:pfam09787 170 NRLHQLTETLIQKQTMLEALSTEKNSL-------VLQLERMEQQIKELQGE 213
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
172-508 |
3.08e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 172 RKTEEDLTRQLNYAQQTLSEKSRELDKLRSEwtsQTTSLSSRHMQDLTAER-EKALETQSRLQQQNEQLRQELES----- 245
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQ---REQARETRDEADEVLEEhEERREELETLEAEIEDLRETIAEterer 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 246 -SHHRSTQQLQTKVSELETANRELIDK---KYKSDSTIRDLKAKLTSLEEECQRSKQQV-LSLRRENSALDSECHEKERL 320
Cdd:PRK02224 275 eELAEEVRDLRERLEELEEERDDLLAEaglDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 321 LNQ---LQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKANGIIKKLQAD 397
Cdd:PRK02224 355 EERaeeLREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 398 LKALLGKIK-----------------VKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEqLEATVQK 460
Cdd:PRK02224 435 LRTARERVEeaealleagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIER 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 688608304 461 LDESREVLktnENVITWLNKQLNEN--QLSRKQETVAMFETPAAALRSAA 508
Cdd:PRK02224 514 LEERREDL---EELIAERRETIEEKreRAEELRERAAELEAEAEEKREAA 560
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
321-496 |
5.71e-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: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 321 LNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKANGIIKKLQADLKA 400
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 401 LLGKIK------VKNS------VTVSQE---------KILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQ 459
Cdd:COG4942 102 QKEELAellralYRLGrqpplaLLLSPEdfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 688608304 460 KLDESREVLKTNENVITWLNKQLNENQLSRKQETVAM 496
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
150-469 |
6.53e-07 |
|
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: 52.43 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 150 KKYLASCLSSVKEEKQQLQQKLRkTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLS-----SRHMQDLTAEREK 224
Cdd:pfam15921 474 KEMLRKVVEELTAKKMTLESSER-TVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlkneGDHLRNVQTECEA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 225 ALETQSRLQQQNEQLRQELES------SHHRSTQQLQTKVSELEtanRELIDK----------KYKSDSTIRDLKAKLTS 288
Cdd:pfam15921 553 LKLQMAEKDKVIEILRQQIENmtqlvgQHGRTAGAMQVEKAQLE---KEINDRrlelqefkilKDKKDAKIRELEARVSD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 289 LEEEcqrsKQQVLSLRREN-SALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQ 367
Cdd:pfam15921 630 LELE----KVKLVNAGSERlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 368 LQISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNsvtvSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEA 447
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQ----SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
330 340
....*....|....*....|..
gi 688608304 448 AKLKEQLEATVQKLDESREVLK 469
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQERRLK 803
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
142-496 |
7.61e-07 |
|
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: 52.48 E-value: 7.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 142 LPGSDTDIKKYLASCLSSVKEEKQQLQQKlrktEEDLTRQLNYAQQTLSEKSRELDKLRsEWTSQTTSLssrhMQDLTAE 221
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKK----EEELQAALARLEEETAQKNNALKKIR-ELEAQISEL----QEDLESE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 222 ---REKALETQSRLQQQNEQLRQELESSHHRST--QQLQTK-VSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQr 295
Cdd:pfam01576 284 raaRNKAEKQRRDLGEELEALKTELEDTLDTTAaqQELRSKrEQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 296 skQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLES 375
Cdd:pfam01576 363 --EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 376 TVKSLSEELIKANGIIKKLQADLKALlgkikvknsvtvsqEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLE 455
Cdd:pfam01576 441 ELESVSSLLNEAEGKNIKLSKDVSSL--------------ESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE 506
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 688608304 456 atvqkldESREVLKTNENVITWLNKQLNEnqLSRKQETVAM 496
Cdd:pfam01576 507 -------EEEEAKRNVERQLSTLQAQLSD--MKKKLEEDAG 538
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
252-484 |
8.08e-07 |
|
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: 51.94 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 252 QQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVL 331
Cdd:TIGR04523 71 NNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 332 EQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIkangIIKKLQADLKALLGKIKVKNSV 411
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS----NLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688608304 412 TVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNE 484
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
161-460 |
8.52e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.05 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 161 KEEKQQLQQKLRKTEE-------DLTRQLN-YAQQ--TLSEKSRELDKLRSEwtSQTTSLSSRHMQDLTAEREKALET-- 228
Cdd:pfam17380 305 KEEKAREVERRRKLEEaekarqaEMDRQAAiYAEQerMAMERERELERIRQE--ERKRELERIRQEEIAMEISRMRELer 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 229 -QSRLQQQNEQLRQELESSHhrstqqlqtKVSELETANRELIDKKYKSDSTIRdlkakltSLEEECQRSKQQVLSLRREN 307
Cdd:pfam17380 383 lQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVEMEQIR-------AEQEEARQREVRRLEEERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 308 SALDSECHEKERllnqlQTRVAVLEQEIKDkdqlvlRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKA 387
Cdd:pfam17380 447 EMERVRLEEQER-----QQQVERLRQQEEE------RKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR 515
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688608304 388 NGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQK 460
Cdd:pfam17380 516 KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-492 |
1.14e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 150 KKYLASCLSSVKEEKQQLQQKLRKTEEDLTR--QLNYAQQTLSEKSRELDKLRSEWTSQTTSLSSrhmqDLTAEREKALE 227
Cdd:TIGR04523 168 KEELENELNLLEKEKLNIQKNIDKIKNKLLKleLLLSNLKKKIQKNKSLESQISELKKQNNQLKD----NIEKKQQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 228 TQSRLQQQNEQLRQeLESSHHRSTQQLQTKVSELETANRELIDKKyksdSTIRDLKAKLTSLEEECQRS-----KQQVLS 302
Cdd:TIGR04523 244 KTTEISNTQTQLNQ-LKDEQNKIKKQLSEKQKELEQNNKKIKELE----KQLNQLKSEISDLNNQKEQDwnkelKSELKN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 303 LRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSE 382
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 383 ELIKANGIIKKLQadlkallGKIKVKnsvtvSQEKILQETSDKLQRQQRELQDTQQRlSLKEEEAAKlkeqlEATVQKLD 462
Cdd:TIGR04523 399 KIQNQEKLNQQKD-------EQIKKL-----QQEKELLEKEIERLKETIIKNNSEIK-DLTNQDSVK-----ELIIKNLD 460
|
330 340 350
....*....|....*....|....*....|
gi 688608304 463 ESREVLKTNENVITWLNKQLNENQLSRKQE 492
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
216-465 |
2.90e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 216 QDLTAEREKALETQSRLQQQNEQLRQELEsshhrstqQLQTKVSELETANrelidkkyksdstirdlkaKLTSLEEECQR 295
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE--------EAEAALEEFRQKN-------------------GLVDLSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 296 SKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDkdqlvLRTKEVLEATQQQKNSVEGNAESKQLQISKLES 375
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEAELAELSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 376 TVKSLSEELikaNGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLE 455
Cdd:COG3206 292 DVIALRAQI---AALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
250
....*....|
gi 688608304 456 ATVQKLDESR 465
Cdd:COG3206 369 SLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-470 |
3.56e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 283 KAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKdkdqlVLRTKEVLEATQQQKNSVE-G 361
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELERLDaS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 362 NAESKQL--QISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKvknsvtvSQEKILQETSDKLQRQQRELQDTQQR 439
Cdd:COG4913 684 SDDLAALeeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD-------ELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190
....*....|....*....|....*....|.
gi 688608304 440 LSLKEEEAAKLKEQLEATVQKLDESREVLKT 470
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
309-469 |
4.09e-06 |
|
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: 48.38 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 309 ALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSlseelIKAN 388
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-----VRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 389 GIIKKLQADLKALLGKIKVKnsvtvsqEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVL 468
Cdd:COG1579 89 KEYEALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
.
gi 688608304 469 K 469
Cdd:COG1579 162 E 162
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-491 |
4.93e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLRKTEEDLtRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLSSRHMQDL----TAEREKALETQSRL 232
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARI-GELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELleeyTAELKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 233 QQQNEQLRQELE------------SSHHRSTQQLQTKVSELETANRELIDKKYKSDSTIRD----LKAKLTSLEEECQRS 296
Cdd:PRK03918 472 EEKERKLRKELRelekvlkkeselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEklikLKGEIKSLKKELEKL 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 297 KQqvlsLRRENSALDSECHEKERLLNQLQTRVavLEQEIKDKDQLVLRTKEVLEATQQ--QKNSVEGNAESKQLQISKLE 374
Cdd:PRK03918 552 EE----LKKKLAELEKKLDELEEELAELLKEL--EELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLE 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 375 STVKSLSEELIKANGIIKKLQADLKALlgkikvknsvtvsQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQL 454
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEEL-------------EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI 692
|
330 340 350
....*....|....*....|....*....|....*..
gi 688608304 455 EATVQKLDESREVLKTNENVITWLNKQLNENQLSRKQ 491
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
51-472 |
1.02e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 51 DTDLYFLYNLIISEED-FQSLKVQQGLLIDFtsFPQKFIDLLEQCICEQDKENPRFLLQLSSSSSAFDHSPSNLNIVETN 129
Cdd:pfam15921 230 DTEISYLKGRIFPVEDqLEALKSESQNKIEL--LLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 130 AFKHLTHLSLKLlpgsdTDIKKYLASCLSSVKEEKQQLQQKLrkteEDLTRQLNYAQQTLSEKSRELDKLRSE------- 202
Cdd:pfam15921 308 ARNQNSMYMRQL-----SDLESTVSQLRSELREAKRMYEDKI----EELEKQLVLANSELTEARTERDQFSQEsgnlddq 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 203 -------------------------WTSQT-TSLSSRHM------QDLTAEREKAL------ETQSRLQQQNEQLRQELE 244
Cdd:pfam15921 379 lqklladlhkrekelslekeqnkrlWDRDTgNSITIDHLrrelddRNMEVQRLEALlkamksECQGQMERQMAAIQGKNE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 245 SSHHRS--TQQLQTKVSELETANRELIDKKY---KSDSTIRDLKAKLTSLEEECQRSKQQVLSLRrenSALDSECHEKER 319
Cdd:pfam15921 459 SLEKVSslTAQLESTKEMLRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLR---SRVDLKLQELQH 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 320 LLNQ------LQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELI-------K 386
Cdd:pfam15921 536 LKNEgdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkilkdK 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 387 ANGIIKKLQADLKAL-LGKIKVKNS----------VTVSQEKILQE---TSDKLQRQQRELQDTQQRLSLKEEE----AA 448
Cdd:pfam15921 616 KDAKIRELEARVSDLeLEKVKLVNAgserlravkdIKQERDQLLNEvktSRNELNSLSEDYEVLKRNFRNKSEEmettTN 695
|
490 500
....*....|....*....|....
gi 688608304 449 KLKEQLEATVQKLDESREVLKTNE 472
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSME 719
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
173-492 |
1.34e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 173 KTEEDLTR-QLNYAQQTLSEKSRELDKLRSEWTSQTTSLssRHMQD-LTAEREKALETQSRLQQQNEQLRQELE--SSHH 248
Cdd:pfam10174 344 QTEVDALRlRLEEKESFLNKKTKQLQDLTEEKSTLAGEI--RDLKDmLDVKERKINVLQKKIENLQEQLRDKDKqlAGLK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 249 RSTQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLE----EECQRSKQQVLSLRRENSALDSECHEKERLLNQL 324
Cdd:pfam10174 422 ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerlEELESLKKENKDLKEKVSALQPELTEKESSLIDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 325 QT--------------RVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESkQLQISKLESTVKSLSEELIKANGI 390
Cdd:pfam10174 502 KEhasslassglkkdsKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-NDRIRLLEQEVARYKEESGKAQAE 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 391 IKKLQADLKAL--------------------------LGKIKVKNSVTVSQEKILQETSDKLqRQQRELQDTQQRLSLKE 444
Cdd:pfam10174 581 VERLLGILREVenekndkdkkiaelesltlrqmkeqnKKVANIKHGQQEMKKKGAQLLEEAR-RREDNLADNSQQLQLEE 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 688608304 445 --EEAAKLKEQLEATVQKLDESREVLKTNENVITWLN----KQLnENQLSRKQE 492
Cdd:pfam10174 660 lmGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRaerrKQL-EEILEMKQE 712
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
145-369 |
1.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 145 SDTDIKKyLASCLSSVKEEKQQLQQKLRKTE---EDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLssrhmqdltAE 221
Cdd:COG3883 14 ADPQIQA-KQKELSELQAELEAAQAELDALQaelEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---------EE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 222 REKALETQSRLQQQNEQLRQELE---SShhRSTQQL---QTKVSELETANRELIDKkYKSDstIRDLKAKLTSLEEECQR 295
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDvllGS--ESFSDFldrLSALSKIADADADLLEE-LKAD--KAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688608304 296 SKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQ 369
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
215-387 |
1.78e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 215 MQDLTAEREKALETQSRLQQQNEQLRQELESSHHRS--------TQQLQTKVSELETANRELIdkkyKSDSTIRDLKAKL 286
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidVASAEREIAELEAELERLD----ASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 287 TSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIkdKDQLVLRTKEVLEAtQQQKNSVEGNAESK 366
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAA-ALGDAVERELRENL 771
|
170 180
....*....|....*....|.
gi 688608304 367 QLQISKLESTVKSLSEELIKA 387
Cdd:COG4913 772 EERIDALRARLNRAEEELERA 792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
187-384 |
2.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 187 QTLSEKSRELDKLRSewtsQTTSLssRHMQDLTAEREKALETQSRLQQQNEQLRQELessHHRSTQQLQTKVSELETANR 266
Cdd:COG4913 235 DDLERAHEALEDARE----QIELL--EPIRELAERYAAARERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 267 ELIDKKYKSDSTIRDLKAKLTSLEEECQRSK-QQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQ----L 341
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaaL 385
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 688608304 342 VLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEEL 384
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
160-374 |
2.56e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 160 VKEEKQQLQQKLRKTEEDLtrqlnyaqQTLSEKSRELDklrsewTSQTTSLSSRHMQDLTAEREKALETQSRLQQQNEQL 239
Cdd:COG3206 180 LEEQLPELRKELEEAEAAL--------EEFRQKNGLVD------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 240 RQELESSH--------HRSTQQLQTKVSELEtANRELIDKKYKSDS-TIRDLKAKLTSLEEECQRSKQQVL-SLRRENSA 309
Cdd:COG3206 246 RAQLGSGPdalpellqSPVIQQLRAQLAELE-AELAELSARYTPNHpDVIALRAQIAALRAQLQQEAQRILaSLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688608304 310 LDSECHEKERLLNQLQTRVAVL---EQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLE 374
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
168-509 |
2.63e-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: 47.26 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 168 QQKLRKTEEDLTRQLNYAQQtLSEKSRELDKLRSEWTSQTTSLssrhMQDLTAEREKALETQSRLQQQNEQLRQELESSH 247
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDK-LEKLVEQNTDLRLEKLGENAES----SKRLNENANNLIKQFENTKEKIAEYTKSIDIKK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 248 HRSTQQLQTKVSELETanrELIDKKYKSDSTIRDLKAKLTsLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTR 327
Cdd:COG5185 310 ATESLEEQLAAAEAEQ---ELEESKRETETGIQNLTAEIE-QGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 328 VAVLEQEIKDKDQ-LVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELIKA----NGIIKKLQADLKALL 402
Cdd:COG5185 386 IESTKESLDEIPQnQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELiselNKVMREADEESQSRL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 403 GKIKVKNSVTVSQEKI-LQETSDKLQRQQRELQDTQQRLSlkeeeaAKLKEQLEATVQKLDESREVLKT-----NENVIT 476
Cdd:COG5185 466 EEAYDEINRSVRSKKEdLNEELTQIESRVSTLKATLEKLR------AKLERQLEGVRSKLDQVAESLKDfmrarGYAHIL 539
|
330 340 350
....*....|....*....|....*....|...
gi 688608304 477 WLNkqlNENQLSRKQETVAMFETPAAALRSAAV 509
Cdd:COG5185 540 ALE---NLIPASELIQASNAKTDGQAANLRTAV 569
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-398 |
2.82e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 216 QDLTAEREKALETQSRLQQQNEQLRQELesshhRSTQQLQTKVSELETANRELIDKKYkSDSTIRDLKAKLTSLEEecqr 295
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAEL-----DALQERREALQRLAEYSWDEIDVAS-AEREIAELEAELERLDA---- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 296 SKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSV---EGNAESKQLQISK 372
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElraLLEERFAAALGDA 762
|
170 180
....*....|....*....|....*..
gi 688608304 373 LESTV-KSLSEELIKANGIIKKLQADL 398
Cdd:COG4913 763 VERELrENLEERIDALRARLNRAEEEL 789
|
|
| HD_XRCC4-like_N |
cd22210 |
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ... |
52-144 |
2.86e-05 |
|
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily includes five families: XRCC4, XLF, PAXX, SAS6 and CCDC61. XRCC4 (X-ray repair cross-complementing protein 4), XLF (XRCC4-like factor) and PAXX (paralog of XRCC4 and XLF) play crucial roles in the non-homologous end-joining (NHEJ) DNA repair pathway. SAS6 (spindle assembly abnormal protein 6) and CCDC61 (coiled-coil domain-containing protein 61) have a centrosomal/centriolar function. Members of this superfamily have an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal low-complexity region. They form homodimers through two homodimerization domains: an N-terminal globular head domain and a parallel coiled-coil domain. In addition, some members such as XRCC4 and XLF form symmetric heterodimers that interact through their globular head domains at the opposite end of the homodimer interface, and may form XLF-XRCC4 filaments. This model corresponds to the N-terminal head domain of XRCC4 superfamily proteins.
Pssm-ID: 408999 Cd Length: 115 Bit Score: 43.68 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 52 TDLYFLYNLIISEEDFQSLKVQQGLLIDFTSFPQKFIDLLEQCIceqdKENPRFLLQLSSSSSAfdhspSNLNIVETNAF 131
Cdd:cd22210 33 SDDAFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKCI----LASDRFTFVLTIRGDE-----AYLKLVEILDE 103
|
90
....*....|...
gi 688608304 132 KhLTHLSLKLLPG 144
Cdd:cd22210 104 Q-LPHITFALRKV 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
214-456 |
3.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 214 HMQDLTAEREKALETQsrlqQQNEQLRQELEssHHRSTQQLQTKVSELETANRELidKKYKSDSTIRDLKAKLTSLEEEC 293
Cdd:COG4913 233 HFDDLERAHEALEDAR----EQIELLEPIRE--LAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 294 QRSKQQVLSLRRENSALDSECHEKERLLNQLQT-RVAVLEQEIKDKdqlvlrtkevleatQQQKNSVEGNAESKQLQISK 372
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERL--------------ERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 373 LESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELqdtQQRLSLKEEEAAKLKE 452
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL---ERRKSNIPARLLALRD 447
|
....
gi 688608304 453 QLEA 456
Cdd:COG4913 448 ALAE 451
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
189-325 |
3.47e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 44.54 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 189 LSEKSRELDKLRSEWTSQTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLRQELESSHhRSTQQLQTKVSELETANREL 268
Cdd:pfam08614 12 LLDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELY-RSRGELAQRLVDLNEELQEL 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 688608304 269 iDKKYKSDS-TIRDLKAKLTSLEEECQRskqqvlslrrensaLDSECHEKERLLNQLQ 325
Cdd:pfam08614 91 -EKKLREDErRLAALEAERAQLEEKLKD--------------REEELREKRKLNQDLQ 133
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
275-494 |
3.86e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 275 SDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERL--LNQLQTRVAVLEQEIKDKDQLVLRTKEVLEAT 352
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLqqLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 353 QQQKNSVEGNAESKQL--QISKLESTVKSLSEELIKANGIIKKLQADLKALlgkikvknsvtvsQEKILQETSDKLQRQQ 430
Cdd:COG3206 253 PDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAAL-------------RAQLQQEAQRILASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688608304 431 RELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREV---LKTNENVITWLNKQLNENQLSRKQETV 494
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLereVEVARELYESLLQRLEEARLAEALTVG 386
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
264-425 |
4.06e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 264 ANRELIDKKYKSDSTIRDLKAKLTSLEEECQR-SKQQVLSLRREnsaLDSECHEKERLLNQLQTRVAVLEQEIKDKDQLV 342
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 343 LRTKEVLEATQQqknsvegNAESKQLQISKLESTVKSLSEELIKANGIIKKLQAD------LKALLGKIKVKNSVTVSQ- 415
Cdd:PRK12704 106 EKREEELEKKEK-------ELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKEi 178
|
170
....*....|
gi 688608304 416 EKILQETSDK 425
Cdd:PRK12704 179 EEEAKEEADK 188
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
161-355 |
6.58e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 161 KEEKQQLQQKLRKTEEDLtRQLNYAQQTLSEKSRELDKLRS-EWTSQTTSLSSRHMQDLTAEREKALETQSRLqqqnEQL 239
Cdd:COG4913 616 EAELAELEEELAEAEERL-EALEAELDALQERREALQRLAEySWDEIDVASAEREIAELEAELERLDASSDDL----AAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 240 RQELEsshhrstqQLQTKVSELETANRELIDKkyksdstIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEkER 319
Cdd:COG4913 691 EEQLE--------ELEAELEELEEELDELKGE-------IGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-ER 754
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 688608304 320 LLNQLQTRV-----AVLEQEIKDKDQLVLRTKEVLEATQQQ 355
Cdd:COG4913 755 FAAALGDAVerelrENLEERIDALRARLNRAEEELERAMRA 795
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
318-505 |
6.64e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 318 ERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQL--QISKLESTVKSLSEELIKANGIIKKLQ 395
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLlqQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 396 ADLKALLGKIkvknsVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLD-ESREVLKTNENV 474
Cdd:COG3206 247 AQLGSGPDAL-----PELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEAE 321
|
170 180 190
....*....|....*....|....*....|.
gi 688608304 475 ITWLNKQLNENQLSRKQETVAMFETPAAALR 505
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-487 |
6.83e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 153 LASCLSSVKEEKQQLQQKLRKTEEDLTRQLnyaqQTLSEKSRELDKLRSEWTSQTTSLSS--RHMQDLTAEREKALETQS 230
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKEL----KELEEELKEAEEKEEEYAELQEELEEleEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 231 RLQQQNEQLRQELESSHHRstQQLQTKVSELETANRELidkkyksdSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSAl 310
Cdd:COG4717 120 KLEKLLQLLPLYQELEALE--AELAELPERLEELEERL--------EELRELEEELEELEAELAELQEELEELLEQLSL- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 311 dsechEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQ---------------ISKLES 375
Cdd:COG4717 189 -----ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaaLLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 376 TVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLE 455
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350
....*....|....*....|....*....|..
gi 688608304 456 ATVQKLDESREVLKTNENVITWLNKQLNENQL 487
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
276-449 |
7.16e-05 |
|
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: 44.53 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 276 DSTIRDLKAKLTSLEEECQRSKQQVLSLRREnsaldsechekerlLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQ 355
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEAR--------------LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 356 KNSVEGNAESKQLQ--ISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKvknsvtvSQEKILQETSDKLQRQQREL 433
Cdd:COG1579 82 LGNVRNNKEYEALQkeIESLKRRISDLEDEILELMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAEL 154
|
170
....*....|....*.
gi 688608304 434 QDTQQRLSLKEEEAAK 449
Cdd:COG1579 155 EAELEELEAEREELAA 170
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
269-473 |
7.37e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 269 IDKKYKS-DSTIRDLKAKLT------SLEEECQRSKQQVLSLRRENSALDSECHE---KERLLNQLQTRVAVLEQEIKDK 338
Cdd:COG5022 808 SRKEYRSyLACIIKLQKTIKrekklrETEEVEFSLKAEVLIQKFGRSLKAKKRFSllkKETIYLQSAQRVELAERQLQEL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 339 DQLVLRTKEVLEAtqqqknsvegnaeSKQLQiSKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKI 418
Cdd:COG5022 888 KIDVKSISSLKLV-------------NLELE-SEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 419 -----LQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNEN 473
Cdd:COG5022 954 pelnkLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQE 1013
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
153-326 |
7.39e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.79 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 153 LASCLSSVKEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEwTSQTTSlSSRHMQDLTAEREKALETQSR- 231
Cdd:pfam05667 315 ATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESS-IKQVEE-ELEELKEQNEELEKQYKVKKKt 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 232 ---LQQQNEQLRqELESSHHRSTQQLQTKVSELETANRELIDKkyksdstIRDLKAKLTSLEEECQRSKQQVLSLRRENS 308
Cdd:pfam05667 393 ldlLPDAEENIA-KLQALVDASAQRLVELAGQWEKHRVPLIEE-------YRALKEAKSNKEDESQRKLEEIKELREKIK 464
|
170
....*....|....*...
gi 688608304 309 ALDSECHEKERLLNQLQT 326
Cdd:pfam05667 465 EVAEEAKQKEELYKQLVA 482
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
144-426 |
8.88e-05 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 144 GSDTDIKKYLASCLSSVKE--------EKQQLQQKLRKTEEDLTRQ----------LNYAQQTLSEKSRELDK------- 198
Cdd:pfam07902 71 GESTGLFKSLEEMLSQLKElnleltdtKNSNLWSKIKLNNNGMLREyhndtikteiVESAEGIATRISEDTDKklaline 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 199 ----LRSEWTSQTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLRQELESSHHRSTQQLQTKVSELetanrelidkkyk 274
Cdd:pfam07902 151 tisgIRREYQDADRQLSSSYQAGIEGLKATMASDKIGLQAEIQASAQGLSQRYDNEIRKLSAKITTT------------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 275 SDSTIRDLKAKLTSLEEECQRSKQQV-LSLRRENSALDSechekerllnQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQ 353
Cdd:pfam07902 218 SSGTTEAYESKLDDLRAEFTRSNQGMrTELESKISGLQS----------TQQSTAYQISQEISNREGAVSRVQQDLDSYQ 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688608304 354 QQKNSVEGNAESKQLQISKLESTVKSLSEeliKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKL 426
Cdd:pfam07902 288 RRLQDAEKNYSSLTQTVKGLQSTVSDPNS---KLESRITQLAGLIEQKVTRGDVESIIRQSGDSIMLAIKAKL 357
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
143-476 |
1.63e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 143 PGSDTDIKKYLASCLSSVKEEKQQLQQklrkTEEDLTRQLNYAQQTLSeKSRELDKLRSEWTSQTTSLSSRHMQDLTAER 222
Cdd:TIGR00618 214 PDTYHERKQVLEKELKHLREALQQTQQ----SHAYLTQKREAQEEQLK-KQQLLKQLRARIEELRAQEAVLEETQERINR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 223 EKALETQSRLQQQNEQLRQELESSHhrstQQLQTKVSELETA--NRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQV 300
Cdd:TIGR00618 289 ARKAAPLAAHIKAVTQIEQQAQRIH----TELQSKMRSRAKLlmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 301 LSLRRENSALDSECH-------EKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEvLEATQQQKNSVEGNAESKQLQISKL 373
Cdd:TIGR00618 365 TSIREISCQQHTLTQhihtlqqQKTTLTQKLQSLCKELDILQREQATIDTRTSA-FRDLQGQLAHAKKQQELQQRYAELC 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 374 ESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRE--------------------L 433
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscihpnparqdidnP 523
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 688608304 434 QDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVIT 476
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
161-491 |
2.08e-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: 44.65 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 161 KEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEwtsqTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLR 240
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNE----IKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 241 qELESSHHRSTQQlqtKVSELETANRELidkkYKSDSTIRDLKAKLTSLEEEcqrskQQVLSLRRENSALDSECHEKERL 320
Cdd:TIGR00606 305 -DLYHNHQRTVRE---KERELVDCQREL----EKLNKERRLLNQEKTELLVE-----QGRLQLQADRHQEHIRARDSLIQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 321 LNQLQT------RVAVLEQEIKDKDQLVLRTKEVLEATQQQK-NSVEGNAESKQLQISKLESTVKSLSEELIKANGIIKK 393
Cdd:TIGR00606 372 SLATRLeldgfeRGPFSERQIKNFHTLVIERQEDEAKTAAQLcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 394 LQADLKALlgkikvknsvtVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEA---AKLKEQLEATVQKLDESREVLKT 470
Cdd:TIGR00606 452 KQEELKFV-----------IKELQQLEGSSDRILELDQELRKAERELSKAEKNSlteTLKKEVKSLQNEKADLDRKLRKL 520
|
330 340
....*....|....*....|.
gi 688608304 471 NENvitwlNKQLNENQLSRKQ 491
Cdd:TIGR00606 521 DQE-----MEQLNHHTTTRTQ 536
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
151-495 |
2.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 151 KYLASCLSSVKEEKQQLQqKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEwtsqttslssrhMQDLTAEREKALETQS 230
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLE-KFIKRTENIEELIKEKEKELEEVLREINEISSE------------LPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 231 RLqqqnEQLRQELEsshhrstqQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEE------ECQRSKQQVLSLR 304
Cdd:PRK03918 232 EL----EELKEEIE--------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 305 RENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEV---LEATQQQKNSVEGNAE------SKQLQISKLES 375
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkkLKELEKRLEELEERHElyeeakAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 376 TVKSLS-EELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQ-------RELqDTQQRLSLKEEEA 447
Cdd:PRK03918 380 RLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgREL-TEEHRKELLEEYT 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 688608304 448 AKLKEqLEATVQKLDESREVLKtneNVITWLNKQLNENQLSRKQETVA 495
Cdd:PRK03918 459 AELKR-IEKELKEIEEKERKLR---KELRELEKVLKKESELIKLKELA 502
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
159-486 |
3.05e-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: 43.88 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 159 SVKEEKQQLQQKLRKTEEDLTrQLNYAQQTLSEkSRELDKLRSEWTSQTTSLSSRHMQDLTAE----------------- 221
Cdd:TIGR00606 505 SLQNEKADLDRKLRKLDQEME-QLNHHTTTRTQ-MEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqledwlhsk 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 222 REKALETQSRLQQQNEQLrQELESSHHRSTQQLQTKVSELETANRELIDKkyksdSTIRDLKAKLTSLEEECQRSKQQVL 301
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKEL-ASLEQNKNHINNELESKEEQLSSYEDKLFDV-----CGSQDEESDLERLKEEIEKSSKQRA 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 302 SLRRENSALDSEChekERLLNQLQTRVAVLEQEIKDKDQLvlrtkevleatqqqknsvegnaeskQLQISKLESTVKSLS 381
Cdd:TIGR00606 657 MLAGATAVYSQFI---TQLTDENQSCCPVCQRVFQTEAEL-------------------------QEFISDLQSKLRLAP 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 382 EELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSlkeeeaakLKEQLEATVQKL 461
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE--------EQETLLGTIMPE 780
|
330 340
....*....|....*....|....*
gi 688608304 462 DESREVLKTNENVITWLNKQLNENQ 486
Cdd:TIGR00606 781 EESAKVCLTDVTIMERFQMELKDVE 805
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
161-485 |
4.65e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 161 KEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLSsrhmqDLTAEREKALETQSRLQQQNEQLR 240
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK-----VLSRSINKIKQNLEQKQKELKSKE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 241 QELeSSHHRSTQQLQTKVSELETANRELIDK-------KYKSDSTIRDLKAKLTS---------LEEECQRSKQQVLSLR 304
Cdd:TIGR04523 496 KEL-KKLNEEKKELEEKVKDLTKKISSLKEKiekleseKKEKESKISDLEDELNKddfelkkenLEKEIDEKNKEIEELK 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 305 RENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEgnaeskqLQISKLESTVKSLSEEL 384
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS-------SIIKNIKSKKNKLKQEV 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 385 IKANGIIKKLQADLKALLGKIKVK----NSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEaaklkEQLEATVQK 460
Cdd:TIGR04523 648 KQIKETIKEIRNKWPEIIKKIKESktkiDDIIELMKDWLKELSLHYKKYITRMIRIKDLPKLEEKY-----KEIEKELKK 722
|
330 340
....*....|....*....|....*
gi 688608304 461 LDESREVLktnENVITWLNKQLNEN 485
Cdd:TIGR04523 723 LDEFSKEL---ENIIKNFNKKFDDA 744
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
223-476 |
4.99e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 223 EKALETQSRLQQQNEQLRQELESSHHRsTQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQR---SKQQ 299
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 300 VLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQlQISKLESTVKS 379
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLD-ELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 380 LSEELikaNGIIKKLQ--ADLKALLGKIKVKnsvtvsqEKILQETSDKLQRQQRELQDTQQRL----SLKEEEAAKLKEQ 453
Cdd:PRK03918 319 LEEEI---NGIEERIKelEEKEERLEELKKK-------LKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEK 388
|
250 260
....*....|....*....|...
gi 688608304 454 LEATVQKLDESREVLKTNENVIT 476
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKIT 411
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-466 |
5.70e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 162 EEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEwtsqttslssrhmQDLTAEREkalETQSRLQQQneqlRQ 241
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAE-------------TELCAEAE---EMRARLAAR----KQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 242 ELESSHHrstqQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTslEEECQRSKQQVlslrrENSALDSECHEKERLL 321
Cdd:pfam01576 72 ELEEILH----ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQKLQL-----EKVTTEAKIKKLEEDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 322 NQLQtrvavleqeikDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKL----ESTVKSLSEELIKANGIIKKLQAD 397
Cdd:pfam01576 141 LLLE-----------DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLknkhEAMISDLEERLKKEEKGRQELEKA 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688608304 398 LKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRL---SLKEEEAAKLKEQLEATVQKLDESRE 466
Cdd:pfam01576 210 KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLeeeTAQKNNALKKIRELEAQISELQEDLE 281
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
410-491 |
7.03e-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: 42.06 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 410 SVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNENQLSR 489
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
..
gi 688608304 490 KQ 491
Cdd:COG4942 93 AE 94
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-499 |
7.64e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 169 QKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEwtsqttslssrhMQDLTAEREKALETQSRLQQQNEQLRQELESSHH 248
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEE------------IEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 249 RSTQqLQTKVSELETA---NRELID-----------KKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALdSEC 314
Cdd:PRK02224 427 REAE-LEATLRTARERveeAEALLEagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-EDL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 315 HEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELikangiikkl 394
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV---------- 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 395 qADLKALLGKIKvknsvtvsqekilqETSDKLQRqqreLQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENV 474
Cdd:PRK02224 575 -AELNSKLAELK--------------ERIESLER----IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER 635
|
330 340
....*....|....*....|....*
gi 688608304 475 ITWLNKQLNENQLSRKQETVAMFET 499
Cdd:PRK02224 636 KRELEAEFDEARIEEAREDKERAEE 660
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
161-274 |
8.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 161 KEEKQQLQQKLRKTEEDLTRQLnyaqQTLSEKSRELDKLRSEWTSQTTSLSSRH--MQDLTAEREKALETQSRLQQqnEQ 238
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKL----ELLEKREEELEKKEKELEQKQQELEKKEeeLEELIEEQLQELERISGLTA--EE 154
|
90 100 110
....*....|....*....|....*....|....*..
gi 688608304 239 LRQE-LESSHHRSTQQLQTKVSELETANRELIDKKYK 274
Cdd:PRK12704 155 AKEIlLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
173-481 |
9.93e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 173 KTEEDLTRQLNYAQQTL-SEKSRELDKLRSEWTSQTTSLSSRhMQDLTAEREKALETqsrLQQQNEQLRQElESSHHRST 251
Cdd:pfam01576 305 KTELEDTLDTTAAQQELrSKREQEVTELKKALEEETRSHEAQ-LQEMRQKHTQALEE---LTEQLEQAKRN-KANLEKAK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 252 QQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVL 331
Cdd:pfam01576 380 QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 332 EQEIKDKDQLVLRTKEVLEATQQQKNSVegnaESKQLQISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSV 411
Cdd:pfam01576 460 SKDVSSLESQLQDTQELLQEETRQKLNL----STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 412 TVSQEKILQETSDKLqrqQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQ 481
Cdd:pfam01576 536 DAGTLEALEEGKKRL---QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKK 602
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
157-469 |
1.55e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLRKTEE-----DLTRQLNYAQQTLSEKSRELDKLRSEWtsqttslssRHMQDLTAEREKALETQSR 231
Cdd:COG4717 104 LEELEAELEELREELEKLEKllqllPLYQELEALEAELAELPERLEELEERL---------EELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 232 LQQQNEQLRQELESSHHRSTQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQvlslrrensald 311
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE------------ 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 312 sECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEAtqqqknsVEGNAESKQLQISKLESTVKSLSEELIKANGII 391
Cdd:COG4717 243 -ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL-------VLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688608304 392 KKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLK 469
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
162-463 |
1.59e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 162 EEKQQLQQKLRKTEE-DLTRQLNYAQQTLSEKSRELDKLRSE----WTSQTTSLSSRHMQDLTAEREKALETQSRLQQQN 236
Cdd:TIGR00618 163 KEKKELLMNLFPLDQyTQLALMEFAKKKSLHGKAELLTLRSQlltlCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 237 EQLRQELESSHHRST--QQLQTKVSELETAnrelidkkyksdstiRDLKAKLTSLEEECQRSKqQVLSLRRENSALDSEC 314
Cdd:TIGR00618 243 AYLTQKREAQEEQLKkqQLLKQLRARIEEL---------------RAQEAVLEETQERINRAR-KAAPLAAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 315 HEKERLLNQLQTRVAVLEQEIKD-----KDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEElikang 389
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKraahvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQH------ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 390 iIKKLQADLKALLGKIKVKNSVTvSQEKILQETSDKLQRQQRELQ------DTQQRLSLKEEEAAKLKEQLEATVQKLDE 463
Cdd:TIGR00618 381 -IHTLQQQKTTLTQKLQSLCKEL-DILQREQATIDTRTSAFRDLQgqlahaKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
153-455 |
1.86e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 153 LASCLSSVKEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLSSRHMQDLTAEREKALEtqsrl 232
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH----- 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 233 qQQNEQLRQELESSHHRSTQQLQTKVSELETANRELIDKKYKSDSTIRDLKA----KLTSLEEECQRSKQQVLSLRRENS 308
Cdd:TIGR00618 650 -ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAqcqtLLRELETHIEEYDREFNEIENASS 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 309 ALDSECHEKERLLNQLQTRVAVLE----QEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEEL 384
Cdd:TIGR00618 729 SLGSDLAAREDALNQSLKELMHQArtvlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688608304 385 ---IKANGIIKKLQADlkallgKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLE 455
Cdd:TIGR00618 809 gqeIPSDEDILNLQCE------TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
165-335 |
2.41e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.09 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 165 QQLQQKLRKTEEDLTRQLNyAQQTLSEKSRELDKLRSEWTSQTtslssRHMQDLTAEREKALETQSRLQQQNEQLRQELE 244
Cdd:COG3096 515 QQLRAQLAELEQRLRQQQN-AERLLEEFCQRIGQQLDAAEELE-----ELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 245 sshhrstqQLQTKVSELEtanrelidkkyKSDSTIRDLKAKLTSLEEECQR---SKQQVLSLRREnsALDSEcHEKERLL 321
Cdd:COG3096 589 --------QLRARIKELA-----------ARAPAWLAAQDALERLREQSGEalaDSQEVTAAMQQ--LLERE-REATVER 646
|
170
....*....|....
gi 688608304 322 NQLQTRVAVLEQEI 335
Cdd:COG3096 647 DELAARKQALESQI 660
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
367-484 |
2.65e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 367 QLQISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIK-VKNSVTVSQEKILQETSDK-LQRQQRELQDTQQRLSLKE 444
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEeVEARIKKYEEQLGNVRNNKeYEALQKEIESLKRRISDLE 109
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 688608304 445 EEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNE 484
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-486 |
2.73e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 369 QISKLESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKI-----LQETSDKLQRQQRELQDTQQRLSLK 443
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasAEREIAELEAELERLDASSDDLAAL 690
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 688608304 444 EEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNENQ 486
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
224-484 |
2.89e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 224 KALETQSRLQ---QQNEQLRQELESSH---HRSTQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSK 297
Cdd:pfam07888 28 RAELLQNRLEeclQERAELLQAQEAANrqrEKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 298 QQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTV 377
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 378 KSLSEELIKAngiikklqadlkallgkikvKNSVTVSQEKILQetsdklqrqqreLQDTQQRLSLKEEEAAKLKEQLEAT 457
Cdd:pfam07888 188 RSLSKEFQEL--------------------RNSLAQRDTQVLQ------------LQDTITTLTQKLTTAHRKEAENEAL 235
|
250 260
....*....|....*....|....*..
gi 688608304 458 VQKLDESREVLKTNENVITWLNKQLNE 484
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEELSS 262
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
170-491 |
2.89e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 170 KLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTS--QTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLRQELESSH 247
Cdd:TIGR04523 79 ILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNdkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 248 HRStQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKqqvlSLRRENSALDSECHEKERLLNQLQTR 327
Cdd:TIGR04523 159 NKY-NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 328 VAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEEL------------IKANGIIKKLQ 395
Cdd:TIGR04523 234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlkseisdlnnQKEQDWNKELK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 396 ADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVI 475
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
330
....*....|....*.
gi 688608304 476 TWLNKQLNENQLSRKQ 491
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQ 409
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
157-444 |
2.96e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.66 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSReLDKLRSEWTSQTTSLSSRHMQDLTAEREKALETqSRLQQQN 236
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIH-VEILEEQLEKLRNELLIRGATEGLCVHSLSKEL-DVLKEEN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 237 EQLRQELESshhrstqqLQTKVSEL-ETANRELIDKKYKS--DSTIRDLKAKLTSLEEECQRSkqqvlslrrenSALDSE 313
Cdd:PLN02939 236 MLLKDDIQF--------LKAELIEVaETEERVFKLEKERSllDASLRELESKFIVAQEDVSKL-----------SPLQYD 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 314 ChekerLLNQLQTRVAVLEQEIKDKDQLVLrtkeVLEATQQQKNSVEgnaeskQLQISKLESTVKSLSEELIKAngiikk 393
Cdd:PLN02939 297 C-----WWEKVENLQDLLDRATNQVEKAAL----VLDQNQDLRDKVD------KLEASLKEANVSKFSSYKVEL------ 355
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 688608304 394 LQADLKALLGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKE 444
Cdd:PLN02939 356 LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLEH 406
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
219-510 |
2.96e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 219 TAEREKALETQSRLQQQNEQL-RQELESSHHRSTQQlqtkvsELETAnRELIDKKYKSDSTIRDLKAKLTSLEEECQRSK 297
Cdd:PRK11281 28 RAASNGDLPTEADVQAQLDALnKQKLLEAEDKLVQQ------DLEQT-LALLDKIDRQKEETEQLKQQLAQAPAKLRQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 298 QQVLSLRRENSALDSECHEKERLlNQLQTRVAvleqeikdkdqlvlrtkEVLEATQQ-QKNSVEGNAESKQLQiSKLEST 376
Cdd:PRK11281 101 AELEALKDDNDEETRETLSTLSL-RQLESRLA-----------------QTLDQLQNaQNDLAEYNSQLVSLQ-TQPERA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 377 VKSLSEELIKANGIIKKLqadlkallgkikvkNSVTVSQEKILQETSDKLQRQQR--ELQDTQQRLSLKEeeaaklKEQL 454
Cdd:PRK11281 162 QAALYANSQRLQQIRNLL--------------KGGKVGGKALRPSQRVLLQAEQAllNAQNDLQRKSLEG------NTQL 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 688608304 455 EATVQK-LDESREVLKTNENVITWLNKQLNENQLSRKQETVAMFETPAAALRSAAVP 510
Cdd:PRK11281 222 QDLLQKqRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANP 278
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
285-491 |
3.38e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.40 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 285 KLTSLEEECQRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTK---EVLEATQQQKNSVEG 361
Cdd:pfam05667 190 YLPPVTAQPSSRASVVPSLLERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRiaeQLRSAALAGTEATSG 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 362 NAESKQLQISKLESTVKSLSEELIKANGiikklqadlkallGKIKVKNSVTVSQEKILQETSDKLQRQQRELQDTQQrls 441
Cdd:pfam05667 270 ASRSAQDLAELLSSFSGSSTTDTGLTKG-------------SRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQR--- 333
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 688608304 442 lkEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNENQLSRKQ 491
Cdd:pfam05667 334 --EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEE 381
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
151-337 |
3.85e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 151 KYLASCLSSVKEEKQQLQQKLRKtEEDLTRQLNYAQQTLS---EKSRELDKLRSEWTSQttslssrhMQDLTAEREKALE 227
Cdd:PRK04863 509 RHLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGknlDDEDELEQLQEELEAR--------LESLSESVSEARE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 228 TQSRLQQQNEQLRQELESSHHRSTQ--QLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVLSLRR 305
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
170 180 190
....*....|....*....|....*....|....
gi 688608304 306 ENSALDS-ECHEKERlLNQLQTRV-AVLEQEIKD 337
Cdd:PRK04863 660 EIERLSQpGGSEDPR-LNALAERFgGVLLSEIYD 692
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
162-480 |
4.27e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 162 EEKQQLQQKLRkteeDLTRQLNYAQQTLSEKSRELDKLRSEWT------SQTTSLSSRHMQD----LTAEREKALETQSR 231
Cdd:COG3096 836 AELAALRQRRS----ELERELAQHRAQEQQLRQQLDQLKEQLQllnkllPQANLLADETLADrleeLREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 232 LQQQNEQLRqelesshhrstqQLQTKVSELetanrelidkkyKSDSTIRD-LKAKLTSLEEECQRSKQQVLSL-----RR 305
Cdd:COG3096 912 IQQHGKALA------------QLEPLVAVL------------QSDPEQFEqLQADYLQAKEQQRRLKQQIFALsevvqRR 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 306 ENSALDsechEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKN-------SVEGNAESKQlqiskleSTVK 378
Cdd:COG3096 968 PHFSYE----DAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSqynqvlaSLKSSRDAKQ-------QTLQ 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 379 SLSEELiKANGIIKKLQADLKALLGKIKVKNSVTVSQEKIlQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATV 458
Cdd:COG3096 1037 ELEQEL-EELGVQADAEAEERARIRRDELHEELSQNRSRR-SQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAK 1114
|
330 340
....*....|....*....|..
gi 688608304 459 QKLDESREVLKTNeNVITWLNK 480
Cdd:COG3096 1115 AGWCAVLRLARDN-DVERRLHR 1135
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
218-475 |
4.59e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 218 LTAEREKAlETQSRLQQQN----EQLRQELESSHHRSTQQLQTKVSELetanrelIDKkyksdstIRDLKAKLTSLEEEC 293
Cdd:PRK05771 12 VTLKSYKD-EVLEALHELGvvhiEDLKEELSNERLRKLRSLLTKLSEA-------LDK-------LRSYLPKLNPLREEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 294 -----QRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIK--------DKDQLVLRTKEVLEATqqqKNSVE 360
Cdd:PRK05771 77 kkvsvKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIErlepwgnfDLDLSLLLGFKYVSVF---VGTVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 361 GNAESKQLQISKlESTVKSLSEE-------LIKANGIIKKLQADLKAL-LGKIKVKNSVTVSQekILQETSDKLQRQQRE 432
Cdd:PRK05771 154 EDKLEELKLESD-VENVEYISTDkgyvyvvVVVLKELSDEVEEELKKLgFERLELEEEGTPSE--LIREIKEELEEIEKE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 688608304 433 LQDTQQRL-SLK---EEEAAKLKEQLEATVQKLDESREVLKTNENVI 475
Cdd:PRK05771 231 RESLLEELkELAkkyLEELLALYEYLEIELERAEALSKFLKTDKTFA 277
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
362-479 |
4.90e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.28 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 362 NAESKQLQISKLESTVKSLSEELIKAngiIKKLQADLKALLGKIKVKNSVTVSQEKILQETSDKLQ---------RQQRE 432
Cdd:cd22656 104 ADATDDEELEEAKKTIKALLDDLLKE---AKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKdlltdeggaIARKE 180
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 688608304 433 LQDTQQRL-SLKEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLN 479
Cdd:cd22656 181 IKDLQKELeKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
171-492 |
5.11e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 171 LRKTEEDLTRQLNYAQQTLSEKSRELDKLRSewTSQTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLRQ-ELESSHHR 249
Cdd:pfam10174 135 LRKTLEEMELRIETQKQTLGARDESIKKLLE--MLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQkEKENIHLR 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 250 STQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQVL--SLRRENSA------------------ 309
Cdd:pfam10174 213 EELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLlhTEDREEEIkqmevykshskfmknkid 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 310 -LDSECHEKERLLNQLQTRVAVLEQEIKDKDQLVLRTKEVLEATQQQKNSVEGNAESKQLQISKLESTVKSLSEELikan 388
Cdd:pfam10174 293 qLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQL---- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 389 giiKKLQADLKALLGKIK-VKNSVTVSQEKI--LQETSDKLQRQqreLQDTQQRLSLKEEEAAKLKEQLEATVQKLDESR 465
Cdd:pfam10174 369 ---QDLTEEKSTLAGEIRdLKDMLDVKERKInvLQKKIENLQEQ---LRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
330 340
....*....|....*....|....*..
gi 688608304 466 EVLKTNENVITWLNKQLNENQLSRKQE 492
Cdd:pfam10174 443 EALSEKERIIERLKEQREREDRERLEE 469
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
154-454 |
6.90e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.11 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 154 ASCLSSVKEEKQQLQQKLRKTEEDLTRQLNYAQQTLSEKSRELDKLRSEWTSQTTSLSS----------------RHMQD 217
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEelrqsrekheeleekyKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 218 LTAEREKALETQSRLQQQNEQLRQELESSHHRSTQQLQTKVSELE----TANRELIDKKyKSDSTIRDLKAKLTSLEEEC 293
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELErmkeRAKKAGAQRK-EEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 294 QRSKQQVLSLRRENSALDSECHEKERLLNQLQTRVAVLEQEIKDKDQLvlrtKEVLEATQQQKNSVEGNAESKQLQISKL 373
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL----LEELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 374 ESTVKSLSEELIKANGIIKKLQADLKALLGKIKVKNSVTVSQEKILQETS----DKLQRQQRELQDTQQRLSLKEEEAAK 449
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAeadkDRIEKLSAELQRLEERLQEERMEREK 343
|
....*
gi 688608304 450 LKEQL 454
Cdd:pfam07888 344 LEVEL 348
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
409-499 |
7.24e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 409 NSVTVSQEKILQETSDKLQRQQRELQDTQQRLSLKEEEAAKLKEQLEATVQKLDESREVLKTNENVITWLNKQLNENQLS 488
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90
....*....|.
gi 688608304 489 RKQETVAMFET 499
Cdd:COG3883 88 LGERARALYRS 98
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
157-300 |
7.69e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 157 LSSVKEEKQQLQQKLRKTE---EDLTRQLNYAQQTLSEKSRELDKLRSEwtsQTTSLSSRHMQDLTAErekaLETQSRLQ 233
Cdd:COG1579 33 LAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEYEALQKE----IESLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688608304 234 QQNEQLRQELESSHHRSTQQLQTKVSELETANRELIDKKYKSDSTIRDLKAKLTSLEEECQRSKQQV 300
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
205-401 |
8.59e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.84 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 205 SQTTSLSSRHMQDLTAEREKALETQSRLQQQNEQLRQELESSHHRSTQQLQTKVSELET--ANRELIDKKYKSD-STIRD 281
Cdd:PHA02562 183 IQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDelLNLVMDIEDPSAAlNKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688608304 282 LKAKLTSLEEECQRskqqVLSLRRENS---ALDSECHEKERLLNQLQTRVAVLEQEIKD----KDQLVLRTKEVLEAT-- 352
Cdd:PHA02562 263 AAAKIKSKIEQFQK----VIKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEKldtaIDELEEIMDEFNEQSkk 338
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 688608304 353 -QQQKNSVEGNAESKQL---QISKLESTVKSLSEELIKANGIIKKLQADLKAL 401
Cdd:PHA02562 339 lLELKNKISTNKQSLITlvdKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| |
