|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
122-433 |
1.65e-138 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 401.99 E-value: 1.65e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 122 EEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQFYQNRKCCE-SNLEPLFGGYIEALRREAECVEADSGRLAAELNHV 200
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 201 QEAMEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLKRLYEEEVCVLQAHISDTSVIVKM 280
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 281 DNSRDLNMDCVVAEIKAQYDDVASRSRAEAESWYRTKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQR 360
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980832 361 AKLEAAVAEAEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLALDIEIATYRRLLEGEEQR 433
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
17-119 |
1.10e-18 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 82.78 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 17 NFSSCSAVAP-----KTGNRCCISAAPFRGVSCYRGLTGFSSRSLCN---PSPCGPRMAVGGFRSGS---------CGRS 79
Cdd:pfam16208 1 GFSSCSAVVPsrsrrSYSSVSSSRRGGGGGGGGGGGGGGFGSRSLYNlggSKSISISVAGGGSRPGSgfgfgggggGGFG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980832 80 FGYRSGGVCGP--------------------------------SPPC----ITTVSVNESLLTPLNLEIDPNAQCV 119
Cdd:pfam16208 81 GGFGGGGGGGFgggggfgggfggggyggggfggggfggrggfgGPPCppggIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
176-452 |
3.24e-11 |
|
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: 66.24 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 176 IEALRREAECVEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATA--------ENEFVVLKKDVDCAYLRKSDLEANVE 247
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 248 AL---VEESSFLKRLYEEEVCVLQAHISDTSVIVKMDNSRDLNMDCVVAEIKAQYDDVASRSRAEAESWYRTKCEEMKAT 324
Cdd:TIGR02169 312 EKereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 325 virhgETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQ---QGEAALADARCKLAELEGALQKAKQDMAC 401
Cdd:TIGR02169 392 -----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 402 LLKEYQEVMN---------SKLALDIEIATYRRLLEGEEQRlceGVGSVNVCVSSSRGGV 452
Cdd:TIGR02169 467 YEQELYDLKEeydrvekelSKLQRELAEAEAQARASEERVR---GGRAVEEVLKASIQGV 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-434 |
1.41e-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: 57.76 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 142 RFLEQQNKLLETKWQFYQNRkccesnleplfggyIEALRREAECVEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATA 221
Cdd:TIGR02168 214 RYKELKAELRELELALLVLR--------------LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 222 ENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLKRLYEEEVCVLQAHISDtsvivKMDNSRDLN-MDCVVAEIKAQYD 300
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK-----LDELAEELAeLEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 301 DVASRSRAEAESWyrtkcEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALAD 380
Cdd:TIGR02168 355 SLEAELEELEAEL-----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 31980832 381 A-RCKLAELEGALQKAKQDMACLLKEYQEVMNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:TIGR02168 430 LeEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-434 |
2.69e-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: 56.60 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 111 EIDPNAQCVKyEEKEQIKCLNSKFAAFIDKVRFLEQQNKLLETKWQfYQNRKCCESNLEplfggyIEALRREAECVEADS 190
Cdd:TIGR02168 678 EIEELEEKIE-ELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKD------LARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 191 GRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVDCAylrKSDLEANVEALVEESSFLKRLYEEevcvlqah 270
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL---KEELKALREALDELRAELTLLNEE-------- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 271 isdtsvivkmdnsrdlnmdcvvaeikaqYDDVASRsraeaeswyRTKCEEMKATVIRHGETLRRTKEEINELnrmIQRLT 350
Cdd:TIGR02168 819 ----------------------------AANLRER---------LESLERRIAATERRLEDLEEQIEELSED---IESLA 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 351 AEIENAKCQRAKLEAAVAEAEQ---QGEAALADARCKLAELEGALQKAKQDMACLLKEYQEvmnsklaLDIEIATYRRLL 427
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNeraSLEEALALLRSELEELSEELRELESKRSELRRELEE-------LREKLAQLELRL 931
|
....*..
gi 31980832 428 EGEEQRL 434
Cdd:TIGR02168 932 EGLEVRI 938
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
176-505 |
2.23e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 176 IEALRREAECVEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVDcaylrksDLEANVEALVEE-SS 254
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREElGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 255 FLKRLYEEevcvlQAHISDTSVIVkmdNSRDLnmdcvvaeikaqyDDVASRSRAeaeswyrtkceeMKATVIRHGETLRR 334
Cdd:COG3883 91 RARALYRS-----GGSVSYLDVLL---GSESF-------------SDFLDRLSA------------LSKIADADADLLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 335 TKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaLADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKL 414
Cdd:COG3883 138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ----QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 415 ALDIEIATYRRLLEGEEQRLCEGVGSVNVCVSSSRGGVTCGGLTYGTTPGRQIVSGPSVTGGSITVMAPDSCSPCQPRAS 494
Cdd:COG3883 214 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGG 293
|
330
....*....|.
gi 31980832 495 SFTCGSSRSVR 505
Cdd:COG3883 294 GGGGAASGGSG 304
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
332-434 |
3.64e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 332 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ---GEAALADARCKLAELEGALQKAKQDMACLLKEYQE 408
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 31980832 409 VMNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
186-424 |
6.32e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 186 VEADSGRLAAELNHVQEAMEGYKKKYEE-EVALRA-TAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLKRLYEEe 263
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 264 vcvLQAHISDTSvivkmDNSRDLNMDCVVAEIKAQYDDVASRsRAEAESWYRTKCEEMKATVirhgETLRRTKEEIN-EL 342
Cdd:COG3206 245 ---LRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVIALR----AQIAALRAQLQqEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 343 NRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGeAALADARCKLAELEGALQKAKQDMACLLKEYQEVmnsKLALDIEIAT 422
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLEREVEVARELYESLLQRLEEA---RLAEALTVGN 387
|
..
gi 31980832 423 YR 424
Cdd:COG3206 388 VR 389
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
178-433 |
7.35e-06 |
|
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: 49.02 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 178 ALRREAECVEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALveessflk 257
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 258 rlyEEEVCVLQAHISDtsVIVKMDNSRDL--NM-------DCVVAE---IKAQYDDvaSRSRAEAESwyRTKceEMKA-T 324
Cdd:pfam01576 572 ---EKTKNRLQQELDD--LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 325 VIRHGETLRRTKEEINELNRMiqrltaeienakcQRAKLEAAVAEAEQQGEAALADARCKLAeLEGALQKAKQDMACLLK 404
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ-------------LRAEMEDLVSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELED 706
|
250 260 270
....*....|....*....|....*....|....*...
gi 31980832 405 EYQEVMNSKLALDIEI----ATYRRLLE-----GEEQR 433
Cdd:pfam01576 707 ELQATEDAKLRLEVNMqalkAQFERDLQardeqGEEKR 744
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
320-434 |
9.25e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 320 EMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAA---LADARCKLAELEGALQKAK 396
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAELAEAEEALLEAE 371
|
90 100 110
....*....|....*....|....*....|....*...
gi 31980832 397 QDMACLLKEYQEVMNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
292-410 |
1.77e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 292 VAEIKAQYDDVASRSRAEAESWYRTKCEEMKATVIRHGETLRRTKE-EINELNRM--IQRLTAEIEnakcQRAKLEAAVA 368
Cdd:COG2268 246 LAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREiELQEKEAEreEAELEADVR----KPAEAEKQAA 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 31980832 369 EAEQQGEA--------ALADARCKLAELEGAL-QKAKQDMacLLKEYQEVM 410
Cdd:COG2268 322 EAEAEAEAeairakglAEAEGKRALAEAWNKLgDAAILLM--LIEKLPEIA 370
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
326-434 |
1.87e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 326 IRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaLADARCKLAELEGALQKAKQDMACLLKE 405
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100
....*....|....*....|....*....
gi 31980832 406 YQEVMNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERL 416
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
332-407 |
3.58e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 332 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ----------GEAALADARCKLAELEGALQKAKQDMAC 401
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleqelaaLEAELAELEKEIAELRAELEAQKEELAE 108
|
....*.
gi 31980832 402 LLKEYQ 407
Cdd:COG4942 109 LLRALY 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
291-434 |
4.02e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 291 VVAEIKAQYD------DVASRSRAeaeswYRTKCEEMKATVI-----RHGETLRRTKEEINELNRMIQRLTAEIENAKCQ 359
Cdd:COG1196 194 ILGELERQLEplerqaEKAERYRE-----LKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980832 360 RAKLEAAVAEAEQQGEAALADarckLAELEGALQKAKQDMACLLKEYQEVMNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:COG1196 269 LEELRLELEELELELEEAQAE----EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
178-429 |
4.43e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 46.47 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 178 ALRREAeCVEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLK 257
Cdd:PLN03188 875 AIRREM-ALEEFCTKQASEITQLNRLVQQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFLEEELASLMHEHKLLK 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 258 RLYEEEVCVLQAHISDTSVIVKMDNSR---DLNMDCVVAE----IKAQ---YDDVASRSRAEAESWYRT--KCEEMKATV 325
Cdd:PLN03188 954 EKYENHPEVLRTKIELKRVQDELEHYRnfyDMGEREVLLEeiqdLRSQlqyYIDSSLPSARKRNSLLKLtySCEPSQAPP 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 326 IrhgETLRRTKEEINELNRMIQRL---TAE---IENAKCQRAKLEAAVAEAEQQGEAALADARCKlAELEGALQKAKQDM 399
Cdd:PLN03188 1034 L---NTIPESTDESPEKKLEQERLrwtEAEskwISLAEELRTELDASRALAEKQKHELDTEKRCA-EELKEAMQMAMEGH 1109
|
250 260 270
....*....|....*....|....*....|
gi 31980832 400 ACLLKEYQEVMNSKLALdieIATYRRLLEG 429
Cdd:PLN03188 1110 ARMLEQYADLEEKHIQL---LARHRRIQEG 1136
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-434 |
4.96e-05 |
|
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: 46.20 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 207 YKKKYEE-EVALRATAENefvvLKKDVDCAylrkSDLEANVEALVEESSFLKRL--YEEEVCVLQAHISDTSVIVKMDNS 283
Cdd:TIGR02168 170 YKERRKEtERKLERTREN----LDRLEDIL----NELERQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 284 RDLNMDcvVAEIKAQYDDVASRSRAEAESWYRTKCE--EMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKCQRA 361
Cdd:TIGR02168 242 EELQEE--LKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980832 362 KLEAAVAEAEQQGE---AALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:TIGR02168 320 ELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
320-410 |
8.63e-05 |
|
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: 44.89 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 320 EMKATVIRHGETLRRT----KEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALADARCKLAELEGALQKA 395
Cdd:pfam07888 297 EGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVA 376
|
90
....*....|....*
gi 31980832 396 KQDMACLLKEYQEVM 410
Cdd:pfam07888 377 QKEKEQLQAEKQELL 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
215-425 |
8.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 215 VALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEESSFLKRLYEEevcvLQAHISDTSVivKMDNSRDlNMDCVVAE 294
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQA--EIDKLQA-EIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 295 IKAQYDDVASRSRAEAESWYRTKCEEM------KATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKcqrAKLEAAVA 368
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVllgsesFSDFLDRLSALSKIADADADLLEELKADKAELEAKK---AELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 31980832 369 EAEQQgeaaLADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLALDIEIATYRR 425
Cdd:COG3883 158 ELEAL----KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-398 |
9.52e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 176 IEALRREAECVEADSGRLAAELNHVQEAmegykKKYEEEvalRATAEnefvvlkkdvdcayLRKSDLEANVEAL--VEES 253
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAA-----RKAEEE---RKAEE--------------ARKAEDAKKAEAVkkAEEA 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 254 sflkRLYEEEVCVLQaHISDTSVIVKMDNSRDLNMDCVVAEIKAQYDDVASRSRAEAEswyRTKCEEM-KATVIRHGETL 332
Cdd:PTZ00121 1236 ----KKDAEEAKKAE-EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEA 1307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980832 333 RRTKEEinelNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALADARCKLAELEGALQKAKQD 398
Cdd:PTZ00121 1308 KKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-414 |
1.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALAdarcKLAELEGALQKAKQDMACLLKEYQEV 409
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE----ELKELEEQLESLQEELAALEQELQAL 176
|
....*
gi 31980832 410 MNSKL 414
Cdd:COG4372 177 SEAEA 181
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
177-428 |
1.20e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 177 EALRREAECVEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEEssfl 256
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE---- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 257 KRLYEEEVCVLQAHISDtsvivkmdnsrdlnMDCVVAEIKAQYDDVASRSRAEAESWYRTKCEEMKATVIRHGETLRRTK 336
Cdd:TIGR02169 753 IENVKSELKELEARIEE--------------LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 337 EEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGE----------AALADARCKLAELEGALQKAKQDMACLLKEY 406
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeeleEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260
....*....|....*....|..
gi 31980832 407 QEVMNSKLALDIEIATYRRLLE 428
Cdd:TIGR02169 899 RELERKIEELEAQIEKKRKRLS 920
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
338-436 |
1.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 338 EINELNRMIQRLTAEIENAKCQRAKLEAAVAEAeqqgEAALADARCKLAELEGALQKAKQdmacLLKEYQE----VMNSK 413
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAA----KTELEDLEKEIKRLELEIEEVEA----RIKKYEEqlgnVRNNK 89
|
90 100
....*....|....*....|....*
gi 31980832 414 --LALDIEIATYRRLLEGEEQRLCE 436
Cdd:COG1579 90 eyEALQKEIESLKRRISDLEDEILE 114
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
330-434 |
1.79e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaLADARCKLAELEGALQKAKQDMAcllkeyqev 409
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA--------- 86
|
90 100
....*....|....*....|....*
gi 31980832 410 mnsklALDIEIATYRRLLEGEEQRL 434
Cdd:COG4942 87 -----ELEKEIAELRAELEAQKEEL 106
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-398 |
2.38e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 176 IEALRREAECVEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVdcaylrkSDLEANVEALVEESSF 255
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 256 LKRLYEEEVCVLQAH--ISDTSVIVKMDNSRDlnmdcvvAEIKAQYDDVASRSRAEaeswyrtkceemkatvirHGETLR 333
Cdd:COG4942 102 QKEELAELLRALYRLgrQPPLALLLSPEDFLD-------AVRRLQYLKYLAPARRE------------------QAEELR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980832 334 RTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALADARCKLAELEGALQKAKQD 398
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-428 |
2.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 176 IEALRREAEcveadsgRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRK--SDLEANVEALVEES 253
Cdd:COG4913 612 LAALEAELA-------ELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEReiAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 254 SFLKRLYEEevcvlqahisdtsvivkmdnsrdlnmdcvVAEIKAQYDDVASRSraeaeswyrtkcEEMKATVIRHGETLR 333
Cdd:COG4913 685 DDLAALEEQ-----------------------------LEELEAELEELEEEL------------DELKGEIGRLEKELE 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 334 RTKEEINELNRMIQRLTAEIENAkcQRAKLEAAVAEA--EQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMN 411
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLE--LRALLEERFAAAlgDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWP 801
|
250 260
....*....|....*....|.
gi 31980832 412 SKLA-LDIEIAT---YRRLLE 428
Cdd:COG4913 802 AETAdLDADLESlpeYLALLD 822
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
332-428 |
4.31e-04 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 40.76 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 332 LRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ---GEAALADARCKLAELEGALQKAKQDMACLLKEYQE 408
Cdd:pfam11559 47 RDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERElalLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQ 126
|
90 100
....*....|....*....|....*
gi 31980832 409 V----MNSKLALDIEIATYR-RLLE 428
Cdd:pfam11559 127 IktqfAHEVKKRDREIEKLKeRLAQ 151
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-434 |
5.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 292 VAEIKAQYDDVASRSRA----EAESWYRTKCEEMKATVIRHGETLRR---TKEEINELNRMIQRLTAEIENAKCQRAKLE 364
Cdd:COG4913 633 LEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELK 712
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980832 365 AAVAEAEQQGEAALADARCKLAELEGALQKAKQDM-ACLLKEYQEVMNSKL------ALDIEIATYRRLLEGEEQRL 434
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVerelreNLEERIDALRARLNRAEEEL 789
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
294-408 |
9.91e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 294 EIKAQYDDVASRSRAEAESWYRTKCEEMKA---TVIRHGETLRRTKEEI----NELNRMIQRLTAEIENAKCQRAKLEAA 366
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFEKELRERRNELQKlekRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEELEEL 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 31980832 367 VAEAEQQGE--AAL--ADARCKLaeLEGALQKAKQDMACLLKEYQE 408
Cdd:PRK12704 137 IEEQLQELEriSGLtaEEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
336-413 |
1.09e-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: 40.68 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 336 KEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALADARCKLAELEGALQKAKQDMAC--------LLKEYQ 407
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREElaakippeLLALYE 181
|
....*.
gi 31980832 408 EVMNSK 413
Cdd:COG1579 182 RIRKRK 187
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
293-400 |
1.18e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 293 AEIKAQYDDVASRSRAEAESwyrtkceemKATVIRHGETLR------RTKEEINELNRMIQRLTAEIENAKCQRAKLEAA 366
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAED---------KLVQQDLEQTLAlldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 31980832 367 VAEAEQQ--GEAALADARCKLAELEGALQKAKQDMA 400
Cdd:PRK11281 110 NDEETREtlSTLSLRQLESRLAQTLDQLQNAQNDLA 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
284-407 |
1.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 284 RDLNMDCVVAEIKAQYDDVASRSRAEAESWY---------RTKCEEMKATVIRHGETLR---------RTKEEINELNRM 345
Cdd:COG4717 361 EELQLEELEQEIAALLAEAGVEDEEELRAALeqaeeyqelKEELEELEEQLEELLGELEellealdeeELEEELEELEEE 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980832 346 IQRLTAEIENAKCQRAKLEAAVAEAEQQGEaaladarckLAELEGALQKAKQDMACLLKEYQ 407
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGE---------LAELLQELEELKAELRELAEEWA 493
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
319-434 |
1.48e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 319 EEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIEnakcqraKLEAAVAEAEQQgeaaladarckLAELEGALQKAKQd 398
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELEEKDER-----------IERLERELSEARS- 455
|
90 100 110
....*....|....*....|....*....|....*...
gi 31980832 399 macllKEYQEVMNSK--LALDIEIATYRRLLEGEEQRL 434
Cdd:COG2433 456 -----EERREIRKDReiSRLDREIERLERELEEERERI 488
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
330-418 |
1.53e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.57 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAK-LEAAVAEAEQQGEAALADARcklAELEGALQKAKQDMAcllKEYQE 408
Cdd:cd06503 37 ESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEiIEEARKEAEKIKEEILAEAK---EEAERILEQAKAEIE---QEKEK 110
|
90
....*....|....*.
gi 31980832 409 VMN------SKLALDI 418
Cdd:cd06503 111 ALAelrkevADLAVEA 126
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
330-433 |
1.57e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 330 ETLRRTKEEINELNRM--------------IQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALADARCKLAELEGALQKA 395
Cdd:PRK09039 53 SALDRLNSQIAELADLlslerqgnqdlqdsVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110
....*....|....*....|....*....|....*....
gi 31980832 396 KQDMACLlkeyqEVMNSKL-ALDIEIATYRRLLEGEEQR 433
Cdd:PRK09039 133 ARALAQV-----ELLNQQIaALRRQLAALEAALDASEKR 166
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
178-434 |
2.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 178 ALRREAEcvEADSGRLAAELNHVQEAMEGYKKKYEEEVALRATAENEFVVLKKDVDCAYLRKSDLEANVEALVEEssflk 257
Cdd:COG1196 217 ELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE----- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 258 rlyeeevcvLQAHISDtsvivkmdnsrdlnmdcvVAEIKAQYDDVASRSRAEAESWyrtkcEEMKATVIRHGETLRRTKE 337
Cdd:COG1196 290 ---------EYELLAE------------------LARLEQDIARLEERRRELEERL-----EELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 338 EINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQGEAALADarckLAELEGALQKAKQDMACLLKEYQEVMNSKLALD 417
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250
....*....|....*..
gi 31980832 418 IEIATYRRLLEGEEQRL 434
Cdd:COG1196 414 ERLERLEEELEELEEAL 430
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
305-430 |
2.54e-03 |
|
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.
Pssm-ID: 464427 [Multi-domain] Cd Length: 278 Bit Score: 39.70 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 305 RSRAEAESWyrtkcEEMKATVIRHGETLRRTKEE--------------INELNRMIQRltAEIENAKCQRAKLEAAVAEA 370
Cdd:pfam14992 44 RSLAEDEER-----EELNFTIMEKEDALQELELEtaklekkneilvksVMELQRKLSR--KSDKNTGLEQETLKQMLEEL 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980832 371 E---QQGEAALADARCKLAELEGALQKAKQ---DMACLLKEYQEVMNSklaldIEIATYRRLLEGE 430
Cdd:pfam14992 117 KvklQQSEESCADQEKELAKVESDYQSVHQlceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
|
|
| Metal_resist |
pfam13801 |
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to ... |
341-422 |
2.54e-03 |
|
Heavy-metal resistance; This is a metal-binding protein which is involved in resistance to heavy-metal ions. The protein forms a four-helix hooked hairpin, consisting of two long alpha helices each flanked by a shorter alpha helix. It binds a metal ion in a type-2 like centre. It contains two copies of an LTXXQ motif.
Pssm-ID: 433488 [Multi-domain] Cd Length: 119 Bit Score: 38.04 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 341 ELNRMIQRLTAEienakcQRAKLEAAVAEAEQQGEAALADARCKLAELEGALQKAKQDMACLLKEYQEVMNSKLALDIEI 420
Cdd:pfam13801 31 MLLRAALGLPAE------QRERLRAALRDHARELRALRRELRAARRELAALLAAPPFDPAAIEAALAEARQARAALQAQI 104
|
..
gi 31980832 421 AT 422
Cdd:pfam13801 105 EE 106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
176-434 |
2.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 176 IEALRREAECVEADSGRLAAELNHVQEAMEGYKKKYEEevaLRATAEnEFVVLKKDVDcAYLRKSDLEanVEALVEESSF 255
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVK-ELKELKEKAE-EYIKLSEFY--EEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 256 LKRL--YEEEVCVLQAHISDTSvivkmdnsrdlNMDCVVAEIKAQYDDVaSRSRAEAESWYRtKCEEMKATVIRhgetLR 333
Cdd:PRK03918 313 EKRLsrLEEEINGIEERIKELE-----------EKEERLEELKKKLKEL-EKRLEELEERHE-LYEEAKAKKEE----LE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 334 RTKEEINELNrmIQRLTAEIENAKcqRAKLEaaVAEAEQQGEAALADARCKLAELEGA---LQKAK------------QD 398
Cdd:PRK03918 376 RLKKRLTGLT--PEKLEKELEELE--KAKEE--IEEEISKITARIGELKKEIKELKKAieeLKKAKgkcpvcgrelteEH 449
|
250 260 270
....*....|....*....|....*....|....*.
gi 31980832 399 MACLLKEYQEVMNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
317-389 |
3.52e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 37.56 E-value: 3.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980832 317 KCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEIENAKcqrAKLEAavaeAEQQGEAALADARCKLAELE 389
Cdd:pfam18595 51 KLEEAKKKLKELRDALEEKEIELRELERREERLQRQLENAQ---EKLER----LREQAEEKREAAQARLEELR 116
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
330-434 |
3.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgeaaladarckLAELEGALQKAKQDMACLLKEYQEV 409
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE-----------AEELQEELEELQKERQDLEQQRKQL 134
|
90 100
....*....|....*....|....*
gi 31980832 410 MNSKLALDIEIATYRRLLEGEEQRL 434
Cdd:COG4372 135 EAQIAELQSEIAEREEELKELEEQL 159
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-427 |
4.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 330 ETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLE----AAVAEAEQQGEAALADARCKLAELEGALQKAKQDMACLLKE 405
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
90 100
....*....|....*....|....
gi 31980832 406 YQEVMNSKLALDIE--IATYRRLL 427
Cdd:COG4717 229 LEQLENELEAAALEerLKEARLLL 252
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
316-428 |
4.94e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 39.62 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 316 TKCEEMKAtviRHGeTLRRTKEEINELNRmiQRLTAEIENAKCQRAKLEA------------AVAEA---------EQQG 374
Cdd:PTZ00491 661 TKSQEAAA---RHQ-AELLEQEARGRLER--QKMHDKAKAEEQRTKLLELqaesaavessgqSRAEAlaeaearliEAEA 734
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31980832 375 EAALADARCK----LAELEGALQKAKQDmacLLKEYQEVMNS------KLALDIEIATYRRLLE 428
Cdd:PTZ00491 735 EVEQAELRAKalriEAEAELEKLRKRQE---LELEYEQAQNEleiakaKELADIEATKFERIVE 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-434 |
6.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 237 LRKSDLEANVEALVEESSFLKRLYEEevcvlqahisdtsvIVKMDNSRDLnmdcvVAEIKAQYDDVAsRSRAEAEswyrt 316
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLERAHEA--------------LEDAREQIEL-----LEPIRELAERYA-AARERLA----- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 317 KCEEMKATVI--RHGETLRRTKEEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQ----GEAALADARCKLAELEG 390
Cdd:COG4913 273 ELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnGGDRLEQLEREIERLER 352
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 31980832 391 ALQKAKQDmaclLKEYQEVMNS-KLALDIEIATYRRLLEGEEQRL 434
Cdd:COG4913 353 ELEERERR----RARLEALLAAlGLPLPASAEEFAALRAEAAALL 393
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
337-430 |
6.75e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980832 337 EEINELNRMIQRLTAEIENAKCQRAKLEAAVAEAEQQgEAALADarcKLAELEGALQKAKQDmacLLKEYQEVMNS-KLA 415
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKEAEKL-KEELEE---KKEKLQEEEDKLLEE---AEKEAQQAIKEaKKE 585
|
90
....*....|....*
gi 31980832 416 LDIEIATYRRLLEGE 430
Cdd:PRK00409 586 ADEIIKELRQLQKGG 600
|
|
| |
