|
Name |
Accession |
Description |
Interval |
E-value |
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
31-374 |
8.89e-08 |
|
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: 55.60 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 31 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPGRGPDfvRTLAEKKPDTGWVITGLKQRIF 110
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 111 RLEQQCKEKDSTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLasseatgkKPILEKKMGVKRQKKMS 181
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQL--------KKAHNAEEAVRTNPEIN 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 182 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDwskprllRRIAELEKKVSSSESPKNSASELVKPNPVVP 261
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 262 SPSNISvqkQLKGDQSKEDQPKVDPSEDQ-EHLQGTVKTLREELSALQEQLLgkdlEMKQMLQSK--------IDLEKEL 332
Cdd:pfam10174 631 KKKGAQ---LLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLS----STQQSLAEKdghltnlrAERRKQL 703
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 333 ETAREGEKE------------------SQEREQALREEVEALTKKCQELEEAKRQETQER 374
Cdd:pfam10174 704 EEILEMKQEallaaisekdaniallelSSSKKKKTQEEVMALKREKDRLVHQLKQQTQNR 763
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-376 |
9.62e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 105 LKQRIFRLEQQCKEKDSTINKLQTDM--KTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMSS 182
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 183 ALLNLTRSVQELTEENQSLKEDLDRMLSnsptvskikgyvdwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvps 262
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEE--------------ELEEAEEELEEAEAELAEAEEALLEAEAELA------- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 263 pSNISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKES 342
Cdd:COG1196 376 -EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|....
gi 2778098833 343 QEREQALREEVEALTKKCQELEEAKRQETQERQD 376
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
84-392 |
3.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 84 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDSTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEATG 163
Cdd:TIGR02168 656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELSRQI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 164 KKPILEKKMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSS 243
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 244 ESPKNSASELV--KPNPVVPSPSNISVQKQLKGDQSKEdqpKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQM 321
Cdd:TIGR02168 809 RAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778098833 322 LQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIAMTHEAHPEVHAP 392
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleglEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
28-375 |
3.56e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 28 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPGRGPDFVRTLAEKKPDTGW-VITGL 105
Cdd:pfam15921 331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 106 KQRIFRLEQQCKEKDSTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPILEKKMGVKRQKK 179
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 180 MSsaLLNLTRSVQELTeenQSLKEDLDRMLSNSPTVSKIKGYVDWskprllrRIAELEKKVSSSESPKNSASE------- 252
Cdd:pfam15921 489 MT--LESSERTVSDLT---ASLQEKERAIEATNAEITKLRSRVDL-------KLQELQHLKNEGDHLRNVQTEcealklq 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 253 LVKPNPVVPS-PSNISVQKQLKGDQSKEDQPKvdpSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKE 331
Cdd:pfam15921 557 MAEKDKVIEIlRQQIENMTQLVGQHGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2778098833 332 --------LETAREGEKESQEREQAL------REEVEALTKKCQELEEAKRQETQERQ 375
Cdd:pfam15921 634 kvklvnagSERLRAVKDIKQERDQLLnevktsRNELNSLSEDYEVLKRNFRNKSEEME 691
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-380 |
4.90e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 24 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEEN---------SRKDRQIEQLLDPGRgpdfVRTLAE 93
Cdd:TIGR02169 162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryqalLKEKREYEGYELLKE----KEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 94 KKPDTGWVITGLKQRIFRLEQQCKEKDSTINKLQTDMKTTNLEEMRIAMETYY---EEIHRLQTLLASSEATGKKPILEK 170
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 171 KMGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDrmlsnsptvsKIKGYVDWSKPR---LLRRIAELEKKvsSSESPK 247
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD----------KLTEEYAELKEEledLRAELEEVDKE--FAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 248 NSASELVKPNPVvpspsnISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQmlqskid 327
Cdd:TIGR02169 386 ELKDYREKLEKL------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK------- 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2778098833 328 LEKELETAREGEKESQEREQALREEVEALTKKCQELE------EAKRQETQERQDSFIA 380
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelaeaEAQARASEERVRGGRA 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-388 |
1.05e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 288 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAregEKESQEREQALREEVEALTKKCQELEEAK 367
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEELEELA 385
|
90 100
....*....|....*....|.
gi 2778098833 368 RQETQERQDSFIAMTHEAHPE 388
Cdd:COG1196 386 EELLEALRAAAELAAQLEELE 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
287-378 |
1.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 287 SEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKcQELEEA 366
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEA 372
|
90
....*....|..
gi 2778098833 367 KRQETQERQDSF 378
Cdd:COG1196 373 ELAEAEEELEEL 384
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-369 |
2.07e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 37 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 116
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 117 KEKDSTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEAtgkkpilEKKMGVKRQKKMSSALLNLTRSVQEL 194
Cdd:TIGR02168 305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELKE-------ELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 195 TEENQSLKEDLDRmlsnsptvskikgyvdwskprLLRRIAELEKKVSSSESPKNSASElvkpnpvvpspsniSVQKQlkg 274
Cdd:TIGR02168 378 EEQLETLRSKVAQ---------------------LELQIASLNNEIERLEARLERLED--------------RRERL--- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 275 DQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLlgkdlemkqmlqskIDLEKELETAREGEKESQEREQALREEVE 354
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL--------------ERLEEALEELREELEEAEQALDAAERELA 485
|
330
....*....|....*
gi 2778098833 355 ALTKKCQELEEAKRQ 369
Cdd:TIGR02168 486 QLQARLDSLERLQEN 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-375 |
2.24e-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: 44.63 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 102 ITGLKQRIFRLEQQCKEKDSTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMS 181
Cdd:TIGR04523 77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 182 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptVSKIKGYVDWSKPRLLR---RIAELEKKVSSSESPKNSASELVKPNp 258
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLKlelLLSNLKKKIQKNKSLESQISELKKQN- 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 259 vvpspSNISVQKQLKGDQSKEDQPKVDPSEDQehlqgtVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAR-E 337
Cdd:TIGR04523 228 -----NQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsE 296
|
250 260 270
....*....|....*....|....*....|....*....
gi 2778098833 338 GEKESQEREQALREEV-EALTKKCQELEEAKRQETQERQ 375
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQNNK 335
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
31-376 |
3.92e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 31 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQI-EQLLDPGRGPDFVRTLAEKkpdtgwvITGLKQRI 109
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsALRKDLARLEAEVEQLEER-------IAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 110 FRLEQQCKEKDSTINKLQtdmktTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpilekkmgvkrqkkmsSALLNLTR 189
Cdd:TIGR02168 757 TELEAEIEELEERLEEAE-----EELAEAEAEIEELEAQIEQLKEELKALR---------------------EALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 190 SVQELTEENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvvpSPSNISVQ 269
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE------ALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 270 KQLKGDQSKEDQPKVdpSEDQEHLQGTVKTLREELSALQEQL--LGKDLE-MKQMLQSKID-----LEKELETAREGEKE 341
Cdd:TIGR02168 885 LEEALALLRSELEEL--SEELRELESKRSELRRELEELREKLaqLELRLEgLEVRIDNLQErlseeYSLTLEEAEALENK 962
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2778098833 342 SQEREQALREEVEALTKKCQEL--------EEAkrQETQERQD 376
Cdd:TIGR02168 963 IEDDEEEARRRLKRLENKIKELgpvnlaaiEEY--EELKERYD 1003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-385 |
4.23e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 107 QRIFRLEQQCKEKDSTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEAtgKKPILEKKMGVKRQKKMS--SAL 184
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEE--KLEELRLEVSELEEEIEElqKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 185 LNLTRSVQELTEENQSLKEDLDRmlsnsptvskikgyVDWSKPRLLRRIAELEKKvsssespKNSASElvkpnpvvpsps 264
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLAN--------------LERQLEELEAQLEELESK-------LDELAE------------ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 265 nisvQKQLKGDQSKEDQPKVDP-SEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQ 343
Cdd:TIGR02168 338 ----ELAELEEKLEELKEELESlEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2778098833 344 EREQALREEVEALTKKcqeLEEAKRQETQERQDSFIAMTHEA 385
Cdd:TIGR02168 414 DRRERLQQEIEELLKK---LEEAELKELQAELEELEEELEEL 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-378 |
7.49e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 32 EKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPGRGPDFVRTLAEKKPDTGWV-ITGLKQRIF 110
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 111 RLEQQCKEKDSTINKLQTDMKTTNleemriametyyEEIHRLQTLLASSEATGKKPILEKKMGVKRQKKMSSALLNLTRS 190
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLLN------------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 191 VQELTEENQSLKEDLDRmlsnsptVSKIKGYVDWSKPRLLRRIAELEKKVSSSESpknsaselvkpnpvvpspsnisVQK 270
Cdd:TIGR02168 861 IEELEELIEELESELEA-------LLNERASLEEALALLRSELEELSEELRELES----------------------KRS 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 271 QLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSK--------IDLEKELE-------TA 335
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDeeearrrlKRLENKIKelgpvnlAA 991
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2778098833 336 REGEKESQEREQALREEVEALTKKCQELEEAKRQ---ETQER-QDSF 378
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEidrEARERfKDTF 1038
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
32-375 |
9.24e-04 |
|
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: 42.25 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 32 EKEDMYDEIIELKKSLhmQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgrgpdfvrTLAE--KKPDTGWVITGLKQRI 109
Cdd:COG5185 250 QTSDKLEKLVEQNTDL--RLEKLGENAESSKRLNENANNLIKQFENTKE---------KIAEytKSIDIKKATESLEEQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 110 FRLEqqcKEKDSTINKLQTDMKTTNLEemriametyyEEIHRLQTLLASSEATGKKPILEKKMGV---KRQKKMSSALLN 186
Cdd:COG5185 319 AAAE---AEQELEESKRETETGIQNLT----------AEIEQGQESLTENLEAIKEEIENIVGEVelsKSSEELDSFKDT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 187 LTRSVQELTEENQSLKEDLDRMLSnspTVSKIKGYVDWSKPRLLRRIAELEKKVS-SSESPKNSASELVKPNPVVPSPSN 265
Cdd:COG5185 386 IESTKESLDEIPQNQRGYAQEILA---TLEDTLKAADRQIEELQRQIEQATSSNEeVSKLLNELISELNKVMREADEESQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 266 ISVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELsalqEQLLGKDLEMKQMLQSKIDLEKELETAREGEkESQER 345
Cdd:COG5185 463 SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL----EKLRAKLERQLEGVRSKLDQVAESLKDFMRA-RGYAH 537
|
330 340 350
....*....|....*....|....*....|
gi 2778098833 346 EQALREEVEALTKKCQELEEAKRQETQERQ 375
Cdd:COG5185 538 ILALENLIPASELIQASNAKTDGQAANLRT 567
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
31-365 |
9.50e-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: 42.31 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 31 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPgrgpdfVRTLAEKKPDTGWVITGLKQRIF 110
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 111 RLEQQCKEKDSTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKpiLEKKMGVKRQKkmssallnltrs 190
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELI------------ 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 191 VQELTEENQSLKEDLDrMLSNSptVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKPNPvvpspSNISVQK 270
Cdd:TIGR04523 456 IKNLDNTRESLETQLK-VLSRS--INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-----SLKEKIE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 271 QLKGDQSKEDQpKVDPSEDQehlqgtVKTLREEL--SALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQA 348
Cdd:TIGR04523 528 KLESEKKEKES-KISDLEDE------LNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
330
....*....|....*..
gi 2778098833 349 LREEVEALTKKCQELEE 365
Cdd:TIGR04523 601 LIKEIEEKEKKISSLEK 617
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
31-379 |
1.00e-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: 42.31 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 31 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpgrgpdfVRTLAEKkpdtgwvITGLKQRIF 110
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQK----------NKSLESQ-------ISELKKQNN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 111 RLEQQCKEKDSTINKLQTDMKTTNlEEMRIAMETYYEEIHRLQTLLASSEATGKKpILEKKMGVKRQKKMSSALLN---- 186
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQ-TQLNQLKDEQNKIKKQLSEKQKELEQNNKK-IKELEKQLNQLKSEISDLNNqkeq 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 187 -LTRSVQELTEENQSLKEDLDRMLSNS--------PTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASELVKPN 257
Cdd:TIGR04523 307 dWNKELKSELKNQEKKLEEIQNQISQNnkiisqlnEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 258 PVVPSPSNI---SVQKQLKGDQSKEDQPKVDPSE------DQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDL 328
Cdd:TIGR04523 387 KNLESQINDlesKIQNQEKLNQQKDEQIKKLQQEkellekEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2778098833 329 EKELET-AREGEKESQEREQALRE------EVEALTKKCQELEEaKRQETQERQDSFI 379
Cdd:TIGR04523 467 ETQLKVlSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE-KVKDLTKKISSLK 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
288-374 |
1.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 288 EDQEHLQGTVKTLREELSALQEQL-LGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEA 366
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
....*...
gi 2778098833 367 KRQETQER 374
Cdd:COG4717 243 ERLKEARL 250
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
298-376 |
1.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2778098833 298 KTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQETQERQD 376
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
186-384 |
1.14e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 186 NLTRSVQELTEENQSLKEDLDrmlsnspTVSKIKGYVDWSKPRLLRRIAELEKKVSSSESPKNSASE-LVKPNPVVPSPS 264
Cdd:pfam01576 374 NLEKAKQALESENAELQAELR-------TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEkLSKLQSELESVS 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 265 NISVQKQLKGDQSKEDQPKVDPS--EDQEHLQ----------GTVKTLREELSALQEQL---------LGKDLEM--KQM 321
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQlqDTQELLQeetrqklnlsTRLRQLEDERNSLQEQLeeeeeakrnVERQLSTlqAQL 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2778098833 322 LQSKIDLEKE---LETAREGEKESQEREQALREEVEALTKKCQELEEAKRQETQERQDSFIAMTHE 384
Cdd:pfam01576 527 SDMKKKLEEDagtLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ 592
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-376 |
1.28e-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: 41.93 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 102 ITGLKQRIFRLEQQCKEKDSTINKLQTDM--KTTNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPILEKKMGVKRQKK 179
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELeeKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKK 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 180 MSSALLNLTRSVQELTEENQSLKEDLDRmLSNSPTVSKIKgyvdwsKPRLLRRIAELEKKVSS-SESPKNSASELVKpnp 258
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELI------IKNLDNTRESLETQLKVlSRSINKIKQNLEQ--- 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 259 vvpspsnisVQKQLKgdqSKEDQPKVDPSEDQEhLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREG 338
Cdd:TIGR04523 487 ---------KQKELK---SKEKELKKLNEEKKE-LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2778098833 339 ------EKESQEREQ---ALREEVEALTKKCQELEEAKRQETQERQD 376
Cdd:TIGR04523 554 lkkenlEKEIDEKNKeieELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
181-334 |
1.56e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 181 SSALLNLtrSVQELTEENQSLKEDLdRMLSnsptvSKIKGYVDwSKPRLLRRIAELEKKVSSSESPKNSASELVKpnpvv 260
Cdd:pfam15294 127 GSALLHM--EIERLKEENEKLKERL-KTLE-----SQATQALD-EKSKLEKALKDLQKEQGAKKDVKSNLKEISD----- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 261 pspsnisVQKQLKGDQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQL--LGKDLE-----------MKQMLQSKID 327
Cdd:pfam15294 193 -------LEEKMAALKSDLEKTLNASTALQKSLEEDLASTKHELLKVQEQLemAEKELEkkfqqtaayrnMKEMLTKKNE 265
|
....*..
gi 2778098833 328 LEKELET 334
Cdd:pfam15294 266 QIKELRK 272
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
288-376 |
2.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 288 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 367
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
....*....
gi 2778098833 368 RQETQERQD 376
Cdd:COG4372 125 QDLEQQRKQ 133
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-366 |
2.47e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 105 LKQRIFRLEQQCKEKDSTINKL-----QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEatGKKPILEKKMG--VKRQ 177
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEIsselpELREELEKLEKEVKELEELKEEIEELEKELESLE--GSKRKLEEKIRelEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 178 KKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGyvdwskpRLLRRIAELEKKVSSSESPKNSAS 251
Cdd:PRK03918 269 EELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLS-------RLEEEINGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 252 ELVKpnpvvpspsnisvqkqlkgdQSKEDQPKVDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEmkqmlqskiDLEKE 331
Cdd:PRK03918 342 ELKK--------------------KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE---------KLEKE 392
|
250 260 270
....*....|....*....|....*....|....*
gi 2778098833 332 LETAREGEKESQEREQALREEVEALTKKCQELEEA 366
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKA 427
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
451-471 |
2.49e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 2.49e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
297-468 |
3.32e-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: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 297 VKTLREELSALQEQLlgkdlemKQMLQSKIDLEkELETAREgekESQEREQALREEVEALTKKCQELEEaKRQETQERQD 376
Cdd:COG4913 663 VASAEREIAELEAEL-------ERLDASSDDLA-ALEEQLE---ELEAELEELEEELDELKGEIGRLEK-ELEQAEEELD 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 377 SFIAMTHEAhpevhapspcsrhsepdsdnnadnnagEDGGSQPPALCSEERREAAI-----RTLQAQWKAHRcKKRKAAL 451
Cdd:COG4913 731 ELQDRLEAA---------------------------EDLARLELRALLEERFAAALgdaveRELRENLEERI-DALRARL 782
|
170
....*....|....*..
gi 2778098833 452 DEAATVLQAAFRGHLAR 468
Cdd:COG4913 783 NRAEEELERAMRAFNRE 799
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
288-377 |
3.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 288 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 367
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
90
....*....|
gi 2778098833 368 RQETQERQDS 377
Cdd:COG1196 354 EEAEAELAEA 363
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
296-369 |
4.12e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 4.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2778098833 296 TVKTLREELSALQEQLLgkdlemKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQ 369
Cdd:COG3206 292 DVIALRAQIAALRAQLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
288-376 |
4.24e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 288 EDQEHLQGTVKTLREELSALQEQLLGKDLEMKQMLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAK 367
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138
|
....*....
gi 2778098833 368 RQETQERQD 376
Cdd:COG4372 139 AELQSEIAE 147
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
453-471 |
4.75e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 4.75e-03
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
168-370 |
6.64e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 168 LEKKMGVK-RQKKMSSALLNLTRSVQELTE------ENQSLKEDLDRMLSNSPTVSKIKGYVDWSKPRLLRRIAELEKKV 240
Cdd:pfam02463 175 LKKLIEETeNLAELIIDLEELKLQELKLKEqakkalEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 241 SSSESPKNSASELVKpnpvvpSPSNISVQKQLKGDQSKEDqpkvDPSEDQEHLQGTVKTLREELSALQEQLLGKDLEMKQ 320
Cdd:pfam02463 255 SSKQEIEKEEEKLAQ------VLKENKEEEKEKKLQEEEL----KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2778098833 321 MLQSKIDLEKELETAREGEKESQEREQALREEVEALTKKCQELEEAKRQE 370
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
288-376 |
8.10e-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: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 288 EDQEHLQGTVKTLREELSALQEQLL-GKDLEMKQMLQSKID-LEKELETAREGEKESQEREQALREEVEALTKKCQELEE 365
Cdd:COG1579 59 KEIKRLELEIEEVEARIKKYEEQLGnVRNNKEYEALQKEIEsLKRRISDLEDEILELMERIEELEEELAELEAELAELEA 138
|
90
....*....|.
gi 2778098833 366 AKRQETQERQD 376
Cdd:COG1579 139 ELEEKKAELDE 149
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
31-376 |
8.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 31 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpgRGPDFVRTLAEKKPDTGWV---ITGLKQ 107
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 108 RIFRLEQQCKEKDSTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpilekkmgvkrqkkmssALLNL 187
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 188 TRSVQELTEENQSLKEDLDRmlsnsptvskikgyvdwskprLLRRIAELEKKVSSSESPKNSASELVKPNpvvpspsnis 267
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778098833 268 vqKQLKGDQSKEDQPKVDPSEDQ----EHLQGTVKTLREELSALQEQL-LGKDL-----EMKQMLQSKIDLEKELETARE 337
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDrervEELEAELEDLEEEVEEVEERLeRAEDLveaedRIERLEERREDLEELIAERRE 530
|
330 340 350
....*....|....*....|....*....|....*....
gi 2778098833 338 GEKESQEREQALREEVEALTKKCQELEEAKRQETQERQD 376
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
|
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