|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
131-444 |
1.82e-148 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 428.57 E-value: 1.82e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 131 QEREQIKVLNNKFASFIDKVRFLEQQNQVLETKWELLQQLDLNNcKNNLEPILEGYISNLRKQLETLSGDRVRLDSELRS 210
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAE-PSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 211 VREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKFFKCLYEGETAQIQSHISDTSIILS 290
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 291 MDNNRNLDLDSIIAEVRAQYEEIARKSKAEAEALYQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQ 370
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28173564 371 CANLETAIADAEQRGDCALKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLEGEECR 444
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
16-128 |
2.85e-33 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 124.00 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 16 GFSGCSAVLSGGSSSSY------------RAGGKGLSGGFSSRSLYSLGGARSISFNVAS-------------------- 63
Cdd:pfam16208 1 GFSSCSAVVPSRSRRSYssvsssrrggggGGGGGGGGGGFGSRSLYNLGGSKSISISVAGggsrpgsgfgfgggggggfg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28173564 64 ---GSGWAGGYGFGRGRASGFAGSMFGSVALG--------SVCPSLCPPGGIHQVTINKSLLAPLNVELDPEIQKV 128
Cdd:pfam16208 81 ggfGGGGGGGFGGGGGFGGGFGGGGYGGGGFGgggfggrgGFGGPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-432 |
5.71e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 130 AQEREQ-IKVLNNKFASFIDKVRFLEQQNQVLETKWELLQQLdlnncknnlepilegyISNLRKQLETLSGDRVRLDSEL 208
Cdd:TIGR02168 672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEE----------------LEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 209 RSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKFFKCLYEGETAQI---QSHISDT 285
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 286 SIILSMDNNRNLDLDSIIAEVRAQYEEIARKSKAEAE--ALYQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSE 363
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdiESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28173564 364 IEsvkkqcaNLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELAR---MLREYQELLSVKLSLDIEIA 432
Cdd:TIGR02168 896 LE-------ELSEELRELESK----RSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSLTLEEA 956
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
104-438 |
1.20e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 104 IHQVTINKSLLAPLNVELDPEIQKVRAQ-EREQIKvlNNKFASFIDKVrFLEQQNQVLETKWELL----QQLDLNNCKNN 178
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTElEKEKLK--NIELTAHCDKL-LLENKELTQEASDMTLelkkHQEDIINCKKQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 179 LEPILegyisnlrKQLETLSGDRVRLDSELRSVRevvEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVD 258
Cdd:pfam05483 529 EERML--------KQIENLEEKEMNLRDELESVR---EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 259 ALDGEIKffkclyegetaqiqshisdtsiilsmDNNRNldldsiIAEVRAQYEEIARKSKAEAEAL--YQTKFQELQLaa 336
Cdd:pfam05483 598 NLKKQIE--------------------------NKNKN------IEELHQENKALKKKGSAENKQLnaYEIKVNKLEL-- 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 337 grhgdDLKHTKNEISELTRLIQRlrsEIESVKKQCANLETAIADAEQRGDCALK-----DARA--KLDELEGALQQAKEE 409
Cdd:pfam05483 644 -----ELASAKQKFEEIIDNYQK---EIEDKKISEEKLLEEVEKAKAIADEAVKlqkeiDKRCqhKIAEMVALMEKHKHQ 715
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 28173564 410 LARMLREY-----------QELLSVKLSLDIEIATYRKLL 438
Cdd:pfam05483 716 YDKIIEERdselglyknkeQEQSSAKAALEIELSNIKAEL 755
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
120-439 |
1.25e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 120 ELDPEIQKVRAQER-----EQIKVLNNKFASFIDKVRFLEQQNQVLETKWELLQQL---------DLNNCKNNLEPILEG 185
Cdd:COG4717 113 ELREELEKLEKLLQllplyQELEALEAELAELPERLEELEERLEELRELEEELEELeaelaelqeELEELLEQLSLATEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 186 YISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENE---------------FVVLKKDVDAAYTSK 250
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaaLLALLGLGGSLLSLI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 251 VEL---------------------QAKVDALDGEIKFFKCLYEGETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQ 309
Cdd:COG4717 273 LTIagvlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 310 YEEIARKSKAEAEALYQTKFQELQLAAG-----------RHGDDLKHTKNEISELTRLIQRLRSEI---------ESVKK 369
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEAGvedeeelraalEQAEEYQELKEELEELEEQLEELLGELeellealdeEELEE 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28173564 370 QCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKE--ELARMLREYQELLSVKLSLDIEIATYRKLLE 439
Cdd:COG4717 433 ELEELEEELEELEEE----LEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
131-410 |
1.34e-10 |
|
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: 63.89 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 131 QEREQIKVLNNKFASfidKVRFLEQQNQVLETKWELLQQL---------DLNNCKNNLEPI---LEGYISNLRKQLETLS 198
Cdd:TIGR04523 398 SKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETiiknnseikDLTNQDSVKELIiknLDNTRESLETQLKVLS 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 199 GDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDaaytskvELQAKVDALDGEIKffkclyegetaQI 278
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS-------SLKEKIEKLESEKK-----------EK 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 279 QSHISD-TSIILSMDNnrNLDLDSIIAEVRAQYEEIArKSKAEAEALY--QTKFQELqlaAGRHGDDLKHTKNEISELTR 355
Cdd:TIGR04523 537 ESKISDlEDELNKDDF--ELKKENLEKEIDEKNKEIE-ELKQTQKSLKkkQEEKQEL---IDQKEKEKKDLIKEIEEKEK 610
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 28173564 356 LIQRLRSEIESVKKQCANLETAIadaeqrgdcalKDARAKLDELEGALQQAKEEL 410
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSII-----------KNIKSKKNKLKQEVKQIKETI 654
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
148-434 |
2.18e-09 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 60.03 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 148 DKVRFLEQQNQVLETKWELL-QQLDLNNcknnlepileGYISNLRKQletlSGDRV-RLDSELRSVREVVEDYKkryeEE 225
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIqQQIKTYN----------KNIEEQRKK----NGENIaRKQNKYDELVEEAKTIK----AE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 226 INKRTTAENEFVVLKKDVDAAY----TSKVELQAKVDALDGEIKFFKclYEGETAQIQSHISDTsiilsmdnnrnldlDS 301
Cdd:PHA02562 236 IEELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE--KGGVCPTCTQQISEG--------------PD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 302 IIAEVRAQYEEIarkskaeaealyQTKFQELQlaagRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIada 381
Cdd:PHA02562 300 RITKIKDKLKEL------------QHSLEKLD----TAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA--- 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 28173564 382 eqrgdcalKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATY 434
Cdd:PHA02562 361 --------KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
218-436 |
4.65e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 218 YKKRYEEEINK-RTTAEN----EFVV--LKKDVDaaytsKVELQAKVdaldgEIKFfkclyegetAQIQSHISDTSIILS 290
Cdd:TIGR02168 170 YKERRKETERKlERTRENldrlEDILneLERQLK-----SLERQAEK-----AERY---------KELKAELRELELALL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 291 MDN----NRNLD-LDSIIAEVRAQYEEIARKSKAEAEALYQTK--FQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSE 363
Cdd:TIGR02168 231 VLRleelREELEeLQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28173564 364 IESVKKQCANLETAIADAEQRGDCA---LKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRK 436
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
132-439 |
4.84e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 132 EREQIKVLNNKFASFIDKVRFLEQQNQVLETK---WELLQQLDLNNCKNNLEPILEGYISNLRKQLETLSGDRVRL---- 204
Cdd:COG3206 62 EPQSSDVLLSGLSSLSASDSPLETQIEILKSRpvlERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVieis 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 205 ----DSEL--RSVREVVEDYKKRYEEEINKRTTAENEFvvLKKDVDaaytskvELQAKVDALDGEIKFFKclyegetaqi 278
Cdd:COG3206 142 ytspDPELaaAVANALAEAYLEQNLELRREEARKALEF--LEEQLP-------ELRKELEEAEAALEEFR---------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 279 QSHIsdtsiILSMDNNRNLDLDSIiAEVRAQYEEiARKSKAEAEALYQTKFQELQLAAGRHGDDLKHT-----KNEISEL 353
Cdd:COG3206 203 QKNG-----LVDLSEEAKLLLQQL-SELESQLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPviqqlRAQLAEL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 354 TRLIQRLRS-------EIESVKKQCANLETAIADAEQRGDCALKD----ARAKLDELEGALQQAKEELARMLREYQELLS 422
Cdd:COG3206 276 EAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASLEAeleaLQAREASLQAQLAQLEARLAELPELEAELRR 355
|
330
....*....|....*..
gi 28173564 423 VKLSLDIEIATYRKLLE 439
Cdd:COG3206 356 LEREVEVARELYESLLQ 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
183-439 |
6.45e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 183 LEGYISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDG 262
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 263 EIKffkcLYEGETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEIARKSKAEAEALyqtkfQELQLAAGRHGDD 342
Cdd:COG1196 317 RLE----ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 343 LKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQrgdcALKDARAKLDELEGALQQAKEELARMLREYQELLS 422
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250
....*....|....*..
gi 28173564 423 VKLSLDIEIATYRKLLE 439
Cdd:COG1196 464 LLAELLEEAALLEAALA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
190-433 |
1.84e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 190 LRKQLETLSGDRvrldselrsvrEVVEDYKKrYEEEINKRttaENEFVVLKKDvdaaytskvELQAKVDALDGEIKFFKC 269
Cdd:COG1196 198 LERQLEPLERQA-----------EKAERYRE-LKEELKEL---EAELLLLKLR---------ELEAELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 270 LYEGETAQIQshisdtsiilsmdnnrnlDLDSIIAEVRAQYEEIARKSKAEAEALYQTKFQELQLAAgrhgdDLKHTKNE 349
Cdd:COG1196 254 ELEELEAELA------------------ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-----DIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 350 ISELTRLIQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDI 429
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
....
gi 28173564 430 EIAT 433
Cdd:COG1196 387 ELLE 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
131-444 |
5.36e-08 |
|
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: 55.89 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 131 QEREQ-IKVLNNKFASFIDKVRFLEQQNQVLETKWELLQ--QLDLNNCKNNLEPiLEGYISNLRKQLETLS---GDRVRL 204
Cdd:pfam15921 506 QEKERaIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnvQTECEALKLQMAE-KDKVIEILRQQIENMTqlvGQHGRT 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 205 DSELRsvrevVEdyKKRYEEEINKRTTAENEFVVLKKDVDAAYTskvELQAKVDALDGE-IKFFKCLYEGETAQIQSHIS 283
Cdd:pfam15921 585 AGAMQ-----VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELEkVKLVNAGSERLRAVKDIKQE 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 284 DTSIILSMDNNRNlDLDSIIAEvraqYEEIARKSKAEAEALyQTKFQELQLAAGRHGDDLKHTKNEISE----------- 352
Cdd:pfam15921 655 RDQLLNEVKTSRN-ELNSLSED----YEVLKRNFRNKSEEM-ETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkv 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 353 ---LTRLIQRLRSEIESVKKQCANLETAIADAEQRGDcALKDARAKLDELEGALQQAKEELA---RMLREYQELLSVKLS 426
Cdd:pfam15921 729 amgMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKH-FLKEEKNKLSQELSTVATEKNKMAgelEVLRSQERRLKEKVA 807
|
330
....*....|....*...
gi 28173564 427 lDIEIATYRKLLEGEECR 444
Cdd:pfam15921 808 -NMEVALDKASLQFAECQ 824
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-439 |
7.93e-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: 55.45 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 151 RFLEQQNQVLETKWELLQqLDLNNCKNNLEPI------LEGYISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEE 224
Cdd:TIGR02168 214 RYKELKAELRELELALLV-LRLEELREELEELqeelkeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 225 EINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKffkcLYEGETAQIQSHISDTSIILSMDNNRNLDLDSIIA 304
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD----ELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 305 EVRAQYEEIARKSKAEAEALYQTKFQELQLAAgrhgdDLKHTKNEISELTRLIQRLRSEIESV--KKQCANLETAIADAE 382
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNN-----EIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELE 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 28173564 383 QRgDCALKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLE 439
Cdd:TIGR02168 444 EL-EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
190-439 |
1.15e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 190 LRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKFFKC 269
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 270 L---YEGETAQIQSHISdtSIILSMDNNRNLDLDSIIAEVRAQYEEIaRKSKAEAEAlyqtKFQELQLAAGRHGDDLKHT 346
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKL-EEEVSRIEA----RLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 347 KNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELARMLREYQELLSVKLS 426
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250
....*....|...
gi 28173564 427 LDIEIATYRKLLE 439
Cdd:TIGR02169 908 LEAQIEKKRKRLS 920
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
187-439 |
1.68e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 187 ISNLRKQLETLSGDRVRLDSELRSVR--EVVEDYKKRYEEeiNKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEI 264
Cdd:COG4913 227 ADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAA--ARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 265 KFFkclyEGETAQIQSHISDtsiilsmdnnrnldLDSIIAEVRAQYEEIARKSKAEAEalyqtkfQELQlaagRHGDDLK 344
Cdd:COG4913 305 ARL----EAELERLEARLDA--------------LREELDELEAQIRGNGGDRLEQLE-------REIE----RLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 345 HTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDCALKDARAKLDELEGALQQAKEELARMLREYQELLSVK 424
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
250
....*....|....*
gi 28173564 425 LSLDIEIATYRKLLE 439
Cdd:COG4913 436 SNIPARLLALRDALA 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-420 |
3.15e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 171 DLNNCKNNLEpILEGYISNLRKQLETLSGDRvrldselrsvrEVVEDYKKRYEEEInkrttaENEFVVLKKDVDAAYTSK 250
Cdd:TIGR02169 178 ELEEVEENIE-RLDLIIDEKRQQLERLRRER-----------EKAERYQALLKEKR------EYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 251 VELQAKVDALDGEIkffkclyegetAQIQSHISDtsiilsmdnnRNLDLDSIIAEVRAQYEEIARKSKAEAEALyQTKFQ 330
Cdd:TIGR02169 240 EAIERQLASLEEEL-----------EKLTEEISE----------LEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 331 ELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDC---ALKDARAKLDELEGALQQAK 407
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAELEEVD 377
|
250
....*....|...
gi 28173564 408 EELARMLREYQEL 420
Cdd:TIGR02169 378 KEFAETRDELKDY 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
298-436 |
6.98e-07 |
|
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: 50.31 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 298 DLDSIIAEVRAQYEEI-ARKSKAEAE-ALYQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRS------------- 362
Cdd:COG1579 14 ELDSELDRLEHRLKELpAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28173564 363 ---EIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELARMLREYQELLSvklSLDIEIATYRK 436
Cdd:COG1579 94 lqkEIESLKRRISDLEDEILELMER----IEELEEELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEA 163
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
120-442 |
1.19e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 120 ELDPE-IQKVRAQEREQIKVLNNKFASFIDKVRFLEQQNQVLETKWELLQ-QLDLNNCKNNL-EPILEGYISNLRKQLET 196
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgQSVCPVCGTTLgEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 197 LSGDRVRLDSELRSVREVVEDYKKRYE----EEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDAldgeikffkclYE 272
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEylesEEINKSINEYNKIESARADLEDIKIKINELKDKHDK-----------YE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 273 GETAQIQS-HISDTSIILSMDNNRNLDLDSI-IAEVRAQYEEIARKSK------AEAEALYQTKFQELQLAAGRHGDD-- 342
Cdd:PRK01156 550 EIKNRYKSlKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNdlesrlQEIEIGFPDDKSYIDKSIREIENEan 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 343 -LKHTKNEISELTRLIQRLRSEIESVKKQCANLEtAIADAEQRGDCALKDARAKLDELEGALQQAKEELARMLREYQELL 421
Cdd:PRK01156 630 nLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILR 708
|
330 340
....*....|....*....|.
gi 28173564 422 SVKLSLDIEIATYRKLLEGEE 442
Cdd:PRK01156 709 TRINELSDRINDINETLESMK 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
113-385 |
1.88e-06 |
|
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: 50.84 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 113 LLAPLNVELDPEIQKVRAQEREQIKVLNNKFASFIDKVRFLEQQNQVLEtkwELLQQLDLNNCKnnlepiLEGYISNLRK 192
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE---ERLAKLEAEIDK------LLAEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 193 QLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKFFkclyE 272
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL----S 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 273 GETAQIQSHISdtsiilsmdnnrnlDLDSIIAEVRAQYEEIARKSKAEAEALYQTKfqelqlaagrhgDDLKHTKNEISE 352
Cdd:TIGR02169 420 EELADLNAAIA--------------GIEAKINELEEEKEDKALEIKKQEWKLEQLA------------ADLSKYEQELYD 473
|
250 260 270
....*....|....*....|....*....|...
gi 28173564 353 LTRLIQRLRSEIESVKKQCANLETAIADAEQRG 385
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
296-442 |
2.00e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 296 NLD-LDSIIAEVRAQYE------EIARKSKAEAEALYQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVK 368
Cdd:COG1196 187 NLErLEDILGELERQLEplerqaEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28173564 369 KQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLEGEE 442
Cdd:COG1196 267 AELEELRLELEELELE----LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
342-418 |
2.49e-06 |
|
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: 49.76 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 342 DLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQR----------GDCALKDARAKLDELEGALQQAKEELA 411
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraleqelaaLEAELAELEKEIAELRAELEAQKEELA 107
|
....*..
gi 28173564 412 RMLREYQ 418
Cdd:COG4942 108 ELLRALY 114
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
109-420 |
3.02e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 109 INK--SLLAPLNVELDPEIQKVRAQERE------QIKVLNNKFASFIDKVRFLEQQNQVLETKWEllqqlDLNNCKNNLE 180
Cdd:TIGR04523 98 INKlnSDLSKINSEIKNDKEQKNKLEVElnklekQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-----DLKKQKEELE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 181 P---ILEGYISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKrYEEEINKrttAENEFVVLKKDVDAAYTSKVELQAKV 257
Cdd:TIGR04523 173 NelnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS-LESQISE---LKKQNNQLKDNIEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 258 DALDGEIKffkclyegETAQIQSHISDTSiilsmdNNRNLDLDSI---IAEVRAQYEEIarksKAEAEALYQTKFQEL-- 332
Cdd:TIGR04523 249 SNTQTQLN--------QLKDEQNKIKKQL------SEKQKELEQNnkkIKELEKQLNQL----KSEISDLNNQKEQDWnk 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 333 ----QLAAGRhgDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLET-------AIADAEQRGDCALKDARAKLDELEg 401
Cdd:TIGR04523 311 elksELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESensekqrELEEKQNEIEKLKKENQSYKQEIK- 387
|
330
....*....|....*....
gi 28173564 402 ALQQAKEELARMLREYQEL 420
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKL 406
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
272-412 |
3.45e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.19 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 272 EGETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEiARKSKAEAEALYQTKFQELQLAAGRHGD---DLKHTKN 348
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28173564 349 EISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGdcalKDARAKLD----ELEGALQQAKEELAR 412
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIAdlgrRLNVALAQRVQELNR 194
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
134-439 |
3.66e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 134 EQIKVLNNKFASFIDKVRFLEQQNQVLETKWELLQQLdlnncKNNLEPILEgYISNLRKQLETLSGDRVRLDSELRSVRE 213
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKE-----VKELEELKE-EIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 214 VVEDYKKRYE--EEINKRTTAenefvvLKKDVDaAYTSKVELQAKVDALDGEIKFFKCLYEGETAQIQSHISDtsiiLSM 291
Cdd:PRK03918 267 RIEELKKEIEelEEKVKELKE------LKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 292 DNNRNLDLDSIIAEVRAQYEEI---------ARKSKAEAEALyQTKFQELQLA-AGRHGDDLKHTKNE----ISELTRLI 357
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELeerhelyeeAKAKKEELERL-KKRLTGLTPEkLEKELEELEKAKEEieeeISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 358 QRLRSEIESVKKQCANLETAIA---------DAEQRGDCaLKDARAKLDELEGALQQAKEELARMLREYQELLSVkLSLD 428
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKV-LKKE 492
|
330
....*....|.
gi 28173564 429 IEIATYRKLLE 439
Cdd:PRK03918 493 SELIKLKELAE 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-423 |
6.67e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 182 ILEGYISNLRKQLETLSGDRVRLDS----ELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDaaytskvELQAKV 257
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLkelkELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-------ELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 258 DALDGEIKFFKCLYEGETAQIQshisdtsiilsmdnnrnldldsiIAEVRAQYEEIARKSKAEAEALYQTKFQELQLAag 337
Cdd:COG4717 119 EKLEKLLQLLPLYQELEALEAE-----------------------LAELPERLEELEERLEELRELEEELEELEAELA-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 338 RHGDDLKHTKNEISELTRL-IQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEElaRMLRE 416
Cdd:COG4717 174 ELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEE----LEELEEELEQLENELEAAALE--ERLKE 247
|
....*..
gi 28173564 417 YQELLSV 423
Cdd:COG4717 248 ARLLLLI 254
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
299-442 |
6.94e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 299 LDSIIAEVRAQYEEI-ARKSKAEAE-ALYQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLET 376
Cdd:COG1196 244 LEAELEELEAELEELeAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28173564 377 AIADAEQRgdcaLKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLEGEE 442
Cdd:COG1196 324 ELAELEEE----LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
250-442 |
7.06e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 250 KVELQAKVDALDGEIKFFKCLYEGETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEIARKSKAEAEALYQ-TK 328
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 329 FQELQLAAGRHGDDLKHT--------KNEISELTRLIQR-------LRSEIESVKKQCANLETAIADAEQR------GDC 387
Cdd:pfam05557 84 YLEALNKKLNEKESQLADarevisclKNELSELRRQIQRaelelqsTNSELEELQERLDLLKAKASEAEQLrqnlekQQS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28173564 388 ALKDARAKLDELEGALQQ----------AKEELARM---------LRE----YQELLSVKLSLDIEIATYRKLLEGEE 442
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSqeqdseivknSKSELARIpelekelerLREhnkhLNENIENKLLLKEEVEDLKRKLEREE 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
121-444 |
9.20e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 121 LDPEIQKVRAQ---EREQIKVLNNKFASFIDKVRFLEQQNQVLETKWELLQQLDlnnckNNLEPILEGYISNLRKQLETL 197
Cdd:TIGR00618 540 LETSEEDVYHQltsERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT-----VRLQDLTEKLSEAEDMLACEQ 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 198 SGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVEL--------QAKVDALDGEIKFFKC 269
Cdd:TIGR00618 615 HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLpkellasrQLALQKMQSEKEQLTY 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 270 LYEGeTAQIQSHI-SDTSIILSMDNNRN---LDLDSIIAEVRAQyEEIARKSKAEAEALYQTKFQELQLAAGRHGDDL-- 343
Cdd:TIGR00618 695 WKEM-LAQCQTLLrELETHIEEYDREFNeieNASSSLGSDLAAR-EDALNQSLKELMHQARTVLKARTEAHFNNNEEVta 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 344 -KHTKNEISELTRLIQRLRSEIESVKKQCANLETAIadaeqrgdcalkdaRAKLDELEGALQQAKEELARMLREYQELLS 422
Cdd:TIGR00618 773 aLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI--------------GQEIPSDEDILNLQCETLVQEEEQFLSRLE 838
|
330 340
....*....|....*....|..
gi 28173564 423 VKLSLDIEIAtyRKLLEGEECR 444
Cdd:TIGR00618 839 EKSATLGEIT--HQLLKYEECS 858
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-439 |
9.32e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 191 RKQLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAytskvELQAKVDALDGEIkffkcl 270
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAEREIAELEAEL------ 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 271 yegetaqiqshisdtsiilsmdnnRNLDLDSiiAEVRAQYEEIArkskaEAEALYQTKFQELQLAAGRHGDdlkhTKNEI 350
Cdd:COG4913 678 ------------------------ERLDASS--DDLAALEEQLE-----ELEAELEELEEELDELKGEIGR----LEKEL 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 351 SELTRLIQRLRSEIESVKKQCANLETAIAD---AEQRGDCALKDARAKL----DELEGALQQAKEELARMLREYQE---L 420
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEerfAAALGDAVERELRENLeeriDALRARLNRAEEELERAMRAFNRewpA 802
|
250 260
....*....|....*....|
gi 28173564 421 LSVKLSLDIE-IATYRKLLE 439
Cdd:COG4913 803 ETADLDADLEsLPEYLALLD 822
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
187-504 |
1.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 187 ISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAytsKVELQAKVDALDGEIKF 266
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 267 fkcLYEGETAqiqshISDTSIILSMDN-----NRNLDLDSIIAEVRAQYEEI--ARKSKAEAEALYQTKFQELQLAAGRH 339
Cdd:COG3883 95 ---LYRSGGS-----VSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 340 GDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRgdcALKDARAKLDELEGALQQAKEELARMLREYQE 419
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA---AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 420 LLSVKLSLDIEIATYRKLLEGEECRMSGEYTNSVSISVINSSMAGMAGTGAGFGFSNAGTYGYWPSSVSGGYSMLPGGCV 499
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVV 323
|
....*
gi 28173564 500 TGSGN 504
Cdd:COG3883 324 GGASA 328
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-426 |
1.31e-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: 48.13 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 169 QLDLNNCKNNLEPiLEGYISNLRKQLETLsgdrvrldselRSVREVVEDYKkRYEEEINKrttaenefvvlkKDVDAAYT 248
Cdd:TIGR02168 178 ERKLERTRENLDR-LEDILNELERQLKSL-----------ERQAEKAERYK-ELKAELRE------------LELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 249 SKVELQAKVDALDGEIKFFKCLYEGETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEIARKSK-----AEAEA 323
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqkqilRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 324 LYQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGAL 403
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR----LEELEEQLETLRSKV 388
|
250 260
....*....|....*....|...
gi 28173564 404 QQAKEELARmLREYQELLSVKLS 426
Cdd:TIGR02168 389 AQLELQIAS-LNNEIERLEARLE 410
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
298-439 |
1.33e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 298 DLDSIIAEVRAQYEEI------ARKSKAEAEALYQT------KFQElQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIE 365
Cdd:COG1579 35 ELEDELAALEARLEAAkteledLEKEIKRLELEIEEvearikKYEE-QLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28173564 366 SVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELAR---MLREYQELLSVKLSLDIeIATYRKLLE 439
Cdd:COG1579 114 ELMERIEELEEELAELEAE----LAELEAELEEKKAELDEELAELEAeleELEAEREELAAKIPPEL-LALYERIRK 185
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
183-422 |
1.45e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 183 LEGYISNLRKQLETLSGDRVRLDSELRSVREV-------VEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQA 255
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNEELKELAEKrdelnaqVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 256 KVDALDGEIKFFKcLYEGETAQIQSHISD------TSiILSMDNNRNLDLDsiIAEVRAQYEEI--ARKSKAEAEALYqT 327
Cdd:COG1340 93 ELDELRKELAELN-KAGGSIDKLRKEIERlewrqqTE-VLSPEEEKELVEK--IKELEKELEKAkkALEKNEKLKELR-A 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 328 KFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQcanletaiADAEQRgdcALKDARAKLDELEGALQQAK 407
Cdd:COG1340 168 ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE--------ADELHK---EIVEAQEKADELHEEIIELQ 236
|
250
....*....|....*
gi 28173564 408 EElarmLREYQELLS 422
Cdd:COG1340 237 KE----LRELRKELK 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
183-412 |
1.55e-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: 47.45 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 183 LEGYISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDG 262
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 263 EIKffKCLYegeTAQIQSHISDTSIILSMDnnrnldlDSIIAEVRAQY-EEIARKSKAEAEALYQTKfQELQLAAGRHGD 341
Cdd:COG4942 105 ELA--ELLR---ALYRLGRQPPLALLLSPE-------DFLDAVRRLQYlKYLAPARREQAEELRADL-AELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28173564 342 DLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDcALKDARAKLDELEGALQQAKEELAR 412
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-421 |
3.88e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 183 LEGYISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEE------EINK----RTTAENEFVVLKKDVDAAYTSKVE 252
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletleaEIEDlretIAETEREREELAEEVRDLRERLEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 253 LQAKVDALDGEIKffkcLYEGETAQIQSHISDTSiilsmdnNRNLDLDSIIAEVRAQ---YEEIARKSKAEAEALyQTKF 329
Cdd:PRK02224 291 LEEERDDLLAEAG----LDDADAEAVEARREELE-------DRDEELRDRLEECRVAaqaHNEEAESLREDADDL-EERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 330 QELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDCALK---DARAKLDELEGALQQA 406
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdELREREAELEATLRTA 438
|
250
....*....|....*
gi 28173564 407 KEElarmLREYQELL 421
Cdd:PRK02224 439 RER----VEEAEALL 449
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
149-378 |
6.82e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 149 KVRFL---EQQNQVLETkwelLQQLDL---NNCKnnlEPILEGYISNLRKQLETLSG--DRVRLDSELRSVR-EVVEDYK 219
Cdd:PRK05771 8 KVLIVtlkSYKDEVLEA----LHELGVvhiEDLK---EELSNERLRKLRSLLTKLSEalDKLRSYLPKLNPLrEEKKKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 220 KRYEEEINKRttAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKF----------FKCLYEGETaqiqshisdTSIIL 289
Cdd:PRK05771 81 VKSLEELIKD--VEEELEKIEKEIKELEEEISELENEIKELEQEIERlepwgnfdldLSLLLGFKY---------VSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 290 SMDNNRNLDLDSIIAEVRAQYEEIARK----------SKAEAEALYQTK---FQELQLAAGRHGDD-LKHTKNEISELTR 355
Cdd:PRK05771 150 GTVPEDKLEELKLESDVENVEYISTDKgyvyvvvvvlKELSDEVEEELKklgFERLELEEEGTPSElIREIKEELEEIEK 229
|
250 260
....*....|....*....|...
gi 28173564 356 LIQRLRSEIESVKKQCANLETAI 378
Cdd:PRK05771 230 ERESLLEELKELAKKYLEELLAL 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-416 |
6.98e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 147 IDKVRFLEQQNQVLETKWELLQQL--DLNNCKNNLEPILEGYisnlrKQLETLSGDRVRLDSELRSVREVvedykkryEE 224
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERleALEAELDALQERREAL-----QRLAEYSWDEIDVASAEREIAEL--------EA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 225 EINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIkffkclyegetAQIQSHISdtsiilsmdnnrnlDLDSIIA 304
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI-----------GRLEKELE--------------QAEEELD 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 305 EVRAQYEEIARKSKAEAEALYQTKFQELqLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQ--------CANLET 376
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAA-LGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDA 809
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 28173564 377 AIADAEqrgdcalkDARAKLDELEG-ALQQAKEELARMLRE 416
Cdd:COG4913 810 DLESLP--------EYLALLDRLEEdGLPEYEERFKELLNE 842
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
120-370 |
7.31e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 120 ELDPEIQKVRaQEREQIKVLNNKFASFIDKVRFL-EQQNQVLETKWELLQQLD-----LNNCKNNLEPI--LEGYISNLR 191
Cdd:COG1340 44 KRDELNAQVK-ELREEAQELREKRDELNEKVKELkEERDELNEKLNELREELDelrkeLAELNKAGGSIdkLRKEIERLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 192 KQLETLSgdrVRLDSElrsvREVVEDYKkRYEEEINKRTTAENEfvvlKKDVDAAYTSKVELQAKVDALDGEIKffkcly 271
Cdd:COG1340 123 WRQQTEV---LSPEEE----KELVEKIK-ELEKELEKAKKALEK----NEKLKELRAELKELRKEAEEIHKKIK------ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 272 egETAQIQSHISDtsiilsmdnnrnldldsIIAEVRAQYEEIarksKAEAEALYQtKFQELQLAAGRHGDDLKHTKNEIS 351
Cdd:COG1340 185 --ELAEEAQELHE-----------------EMIELYKEADEL----RKEADELHK-EIVEAQEKADELHEEIIELQKELR 240
|
250
....*....|....*....
gi 28173564 352 ELTRLIQRLRSEIESVKKQ 370
Cdd:COG1340 241 ELRKELKKLRKKQRALKRE 259
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
332-438 |
8.13e-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: 45.14 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 332 LQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELA 411
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELA 86
|
90 100
....*....|....*....|....*..
gi 28173564 412 RMLREYQELlsvKLSLDIEIATYRKLL 438
Cdd:COG4942 87 ELEKEIAEL---RAELEAQKEELAELL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-448 |
9.28e-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: 45.43 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 345 HTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQrgdcALKDARAKLDELEGALQQAKEELARMLREYQELLSVK 424
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE----ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100
....*....|....*....|....
gi 28173564 425 LSLDIEIATYRKLLEGEECRMSGE 448
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEA 773
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
299-430 |
1.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 299 LDSIIAEVRAQYEEIARKSKA-----EAEALYQTKFQ-ELQLAAGRHG-DDLKHTKNEISELTRLIQRLRSEIESVKKQC 371
Cdd:COG4717 100 LEEELEELEAELEELREELEKlekllQLLPLYQELEAlEAELAELPERlEELEERLEELRELEEELEELEAELAELQEEL 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28173564 372 ANL--ETAIADAEQRGDCA--LKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIE 430
Cdd:COG4717 180 EELleQLSLATEEELQDLAeeLEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
182-354 |
1.36e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.24 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 182 ILEGYISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRY---EEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKvd 258
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKdalEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQ-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 259 aldgEIKFFKclyeGETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEIaRKSKAEAEALYQTKFQELQLaagR 338
Cdd:smart00787 219 ----EIMIKV----KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC-RGFTFKEIEKLKEQLKLLQS---L 286
|
170
....*....|....*.
gi 28173564 339 HGddLKHTKNEISELT 354
Cdd:smart00787 287 TG--WKITKLSGNTLS 300
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
231-504 |
1.42e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 231 TAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKFFKCLYEGETAQIQshisdtsiilsmDNNRNLD-LDSIIAEVRAQ 309
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE------------ALQAEIDkLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 310 YEEIARKSKAEAEALYQTKFQ----ELQLAAGRHGDDL----------KHTKNEISELTRLIQRLRSEIESVKKQCANLE 375
Cdd:COG3883 81 IEERREELGERARALYRSGGSvsylDVLLGSESFSDFLdrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 376 TAIADAEQrgdcALKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLEGEECRMSGEYTNSVSI 455
Cdd:COG3883 161 ALKAELEA----AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 28173564 456 SVINSSMAGMAGTGAGFGFSNAGTYGYWPSSVSGGYSMLPGGCVTGSGN 504
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGG 285
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
298-442 |
1.46e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 298 DLDSIIAEVRAQYEEIARKSKAEAEAL--YQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQcanle 375
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER----- 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28173564 376 taIADAEQRgdcaLKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLEGEE 442
Cdd:COG1196 311 --RRELEER----LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
122-439 |
2.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 122 DPEIQKVRAQEREQIKVLNNKFASFIDKVRFLEQQNQVLETKWEllqqldlnncknnlepILEGYISNLRKQLETLSGDR 201
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA----------------ELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 202 VRLDSELRSVREVVEDYKKRYEEeinkrttAENEFVVLKKDVDAAYTSKVELQAKVDALDGEI-KFFKCLYEGETAQIQS 280
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGN-------AEDFLEELREERDELREREAELEATLRTARERVeEAEALLEAGKCPECGQ 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 281 HISDTSIILSMDNNRNL--DLDSIIAEVRAQYEEI-ARKSKAEAEALYQTKFQELQLAAGRHGDDLKHTKNEISELTRLI 357
Cdd:PRK02224 460 PVEGSPHVETIEEDRERveELEAELEDLEEEVEEVeERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERA 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 358 QRLRSEIESVKKQCANLETAIADAEQRGDcalkDARAKLDELEGALQQAKEELARmLREYQELLSvklsldiEIATYRKL 437
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAE----EAREEVAELNSKLAELKERIES-LERIRTLLA-------AIADAEDE 607
|
..
gi 28173564 438 LE 439
Cdd:PRK02224 608 IE 609
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
302-439 |
3.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 302 IIAEVRAQYEEIARKSKAEAEaLYQTKFQELQL---AAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAI 378
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPE-LNLKELKELEEelkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28173564 379 ADAEQRGDcaLKDARAKLDELEGALQQAKEELarmlREYQELLSVKLSLDIEIATYRKLLE 439
Cdd:COG4717 126 QLLPLYQE--LEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELE 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-442 |
3.41e-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: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 298 DLDSIIAEVRAQYEEIARKsKAEAEALYQTKFQELQLAAGRHG--------DDLKHTKNEISELTRLIQRLRSEIESVKK 369
Cdd:COG4913 628 EAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAEREiaeleaelERLDASSDDLAALEEQLEELEAELEELEE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 370 QCANLETAIADAEQRgdcaLKDARAKLDELEGALQQA--------KEELARMLREYQE---LLSVKLSLDIEIATYRKLL 438
Cdd:COG4913 707 ELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAedlarlelRALLEERFAAALGdavERELRENLEERIDALRARL 782
|
....
gi 28173564 439 EGEE 442
Cdd:COG4913 783 NRAE 786
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
357-413 |
3.43e-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: 41.15 E-value: 3.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 28173564 357 IQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELARM 413
Cdd:pfam11559 68 IERLQSKIERLKTQLEDLERELALLQAK----ERQLEKKLKTLEQKLKNEKEELQRL 120
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
127-410 |
3.54e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 127 KVRAQEREQIKVLNNKFASFIDKVRFLEQQNQVLETKWELLqqLDLNNCKNNLEPILEGYISNLRKQLETLSGDRVRLDS 206
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM--LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 207 ELRSVREVVEDY--KKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVelqAKVDALDGEIKFFKCLYEGETAQiqsHISD 284
Cdd:TIGR00606 766 DIEEQETLLGTImpEEESAKVCLTDVTIMERFQMELKDVERKIAQQA---AKLQGSDLDRTVQQVNQEKQEKQ---HELD 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 285 TsIILSMDNNRNL--DLDSIIAEVRAQYEEIARKSKAEAEALYQTKFQELQLAagrhgddlkhtkneisELTRLIQRLRS 362
Cdd:TIGR00606 840 T-VVSKIELNRKLiqDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV----------------ELSTEVQSLIR 902
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 28173564 363 EIESVKKQCANLETAIADAEQRGDCALKDARAKLDELEGALQQAKEEL 410
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKV 950
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
319-442 |
5.01e-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: 41.83 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 319 AEAEALYQ-----TKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDAR 393
Cdd:COG1579 4 EDLRALLDlqeldSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 28173564 394 AKLD------ELEgALQQAKEELARMLREYQELLsvkLSLDIEIATYRKLLEGEE 442
Cdd:COG1579 80 EQLGnvrnnkEYE-ALQKEIESLKRRISDLEDEI---LELMERIEELEEELAELE 130
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
146-410 |
6.20e-04 |
|
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: 42.50 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 146 FIDKVRFLEQQNQVLETKWELLQqldlnncknnlePIL---EGYISNLRKQLETLSGDRVRLDSELRSVREVVEdyKKRy 222
Cdd:pfam10174 466 RLEELESLKKENKDLKEKVSALQ------------PELtekESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE--QKK- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 223 eEEINKRTTaenefvVLKKDVDAAYTSKV--ELQAKVDALDGEIKFFKclyeGETAQIQSHISDTSIILSMDNNRNLDLD 300
Cdd:pfam10174 531 -EECSKLEN------QLKKAHNAEEAVRTnpEINDRIRLLEQEVARYK----EESGKAQAEVERLLGILREVENEKNDKD 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 301 SIIAEVRAQyeeIARKSKAEAEALYQTKF----------QELQLAAgRHGDDLK--HTKNEISELTRLIQRLRSEIESVK 368
Cdd:pfam10174 600 KKIAELESL---TLRQMKEQNKKVANIKHgqqemkkkgaQLLEEAR-RREDNLAdnSQQLQLEELMGALEKTRQELDATK 675
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 28173564 369 KQCANLETAIADAEqRGDCALKDARAKldELEGALQQAKEEL 410
Cdd:pfam10174 676 ARLSSTQQSLAEKD-GHLTNLRAERRK--QLEEILEMKQEAL 714
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
314-408 |
7.15e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.97 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 314 ARKSKAEAEALYQ------TKFQELQLaagrhgdDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDC 387
Cdd:pfam10473 47 AENSKAEVETLKAeieemaQNLRDLEL-------DLVTLRSEKENLTKELQKKQERVSELESLNSSLENLLEEKEQEKVQ 119
|
90 100
....*....|....*....|.
gi 28173564 388 ALKDARAKLDELEGALQQAKE 408
Cdd:pfam10473 120 MKEESKTAVEMLQTQLKELNE 140
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
124-422 |
7.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 124 EIQKVRAQEREQIKVLNNkfasfIDKVRFLEQQNQVLETKWELLQQLDLNNCKNNLEPILEGY--ISNLRKQLETLSGDR 201
Cdd:PRK03918 467 ELKEIEEKERKLRKELRE-----LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAeeYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 202 VRLDSELRSVrevvEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVElqakvdALDGEIKFFKCLY---------E 272
Cdd:PRK03918 542 KSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEELGFESVE------ELEERLKELEPFYneylelkdaE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 273 GETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEIARK-SKAEAEALYQtKFQELQLAAGRHGDDLKHTKNEIS 351
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELRE-EYLELSRELAGLRAELEELEKRRE 690
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28173564 352 ELTRLIQRLRSEIESVKKQCANLETaiadaeqrgdcaLKDARAKLDELEGALQQAKEELA-RMLREYQELLS 422
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEK------------LEKALERVEELREKVKKYKALLKeRALSKVGEIAS 750
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
187-448 |
8.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 187 ISNLRKQLETLSGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAYTSKVELQAKVDALDGEIKF 266
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 267 FkclyEGETAQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEIARKSKAEAEALYQTKFQELQLAAgrhgddlkht 346
Cdd:COG4372 127 L----EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA---------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 347 kNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDCALKDARAKLDELEGALQQAKEELARMLREYQELLSVKLS 426
Cdd:COG4372 193 -NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260
....*....|....*....|..
gi 28173564 427 LDIEIATYRKLLEGEECRMSGE 448
Cdd:COG4372 272 DTEEEELEIAALELEALEEAAL 293
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
124-265 |
8.79e-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: 41.06 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 124 EIQKVRAQEREQIKVLNNKFASFIDKVRFLEQQNQVLETKWELLQQL------DLNNCKNNLEpilegyISNLRKQLETL 197
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeQLGNVRNNKE------YEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28173564 198 SGDRVRLDSELRSVREVVEDYKKRYEEEINKRTTAENEFVVLKKDVDAAytsKVELQAKVDALDGEIK 265
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAERE 166
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
299-400 |
8.81e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 299 LDSIIAEVRAQYEEIARKSKAEAEALyQTKFQELQLaagrhgdDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAI 378
Cdd:smart00787 184 LEEELRQLKQLEDELEDCDPTELDRA-KEKLKKLLQ-------EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEI 255
|
90 100
....*....|....*....|....*....
gi 28173564 379 ADAE----QRGDCALKDA---RAKLDELE 400
Cdd:smart00787 256 AEAEkkleQCRGFTFKEIeklKEQLKLLQ 284
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
298-446 |
9.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 298 DLDSIIAEVRAQYEEIARKSKAEAEALYQTKfQELQLAAGRHgDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETA 377
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELR-EELEKLEKEV-KELEELKEEIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28173564 378 IADAEQRgdcaLKDARAKLDELEgALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLEGEECRMS 446
Cdd:PRK03918 268 IEELKKE----IEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
295-427 |
9.48e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.81 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 295 RNLDLDSIIAE---VRAQYEEIARKSKAEAEALYQTKFQELQLAAGrhgdDLKHTKNEISELTRLIQRLRSEI------- 364
Cdd:pfam05010 37 ENLEMRKIVAEfekTIAQMIEEKQKQKELEHAEIQKVLEEKDQALA----DLNSVEKSFSDLFKRYEKQKEVIsgykkne 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28173564 365 ESVKKQCANLETAIADAEQRGDcALKdARAkldelEGALQQAKEELARMLREYQ-ELLSVKLSL 427
Cdd:pfam05010 113 ESLKKCAQDYLARIKKEEQRYQ-ALK-AHA-----EEKLDQANEEIAQVRSKAKaETAALQASL 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
161-432 |
9.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 161 ETKWELLQQ--LDLNNCKNNLEPILEgYISNLRKQLETLSGDRVRlDSELRSVREVVEDYKKrYEEEINKrttaenefvV 238
Cdd:PRK03918 448 EHRKELLEEytAELKRIEKELKEIEE-KERKLRKELRELEKVLKK-ESELIKLKELAEQLKE-LEEKLKK---------Y 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 239 LKKDVDAAYTSKVELQAKVDALDGEIKFFKC------LYEGETAQIQSHISDTSIILSMDNNRNL--------DLDSIIA 304
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKelekleELKKKLAELEKKLDELEEELAELLKELEelgfesveELEERLK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 305 EVRAQYEEIARKSKAEaealyqtkfQELQlaagRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQR 384
Cdd:PRK03918 596 ELEPFYNEYLELKDAE---------KELE----REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE 662
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 28173564 385 G--------DCALKDARAKLDELEGALQQAKEELARMLREYQELLSVKLSL-DIEIA 432
Cdd:PRK03918 663 ElreeylelSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELeKLEKA 719
|
|
| FlgN |
pfam05130 |
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ... |
298-429 |
1.55e-03 |
|
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.
Pssm-ID: 428323 [Multi-domain] Cd Length: 140 Bit Score: 38.89 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 298 DLDSIIAEVRAQYEEIARKSKAEAEALYQTKFQELQlaagrhgdDLKHTKNE-ISELTRLIQRLRSEIESVKKQCANLET 376
Cdd:pfam05130 2 ELIELLEEELELLEELLELLEEEQEALKAGDIEALE--------ELTEEKQElLQKLAQLEKERRELLAELGLSPEEATL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 28173564 377 AIADAEQRGDCALKDARAKLDELEGALQQAKEELARMLReyQELLSVKLSLDI 429
Cdd:pfam05130 74 SELLAKEEEDPELRELWQELLELLERLKELNELNGELIE--QSLEFNNRSLNI 124
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
341-442 |
2.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 341 DDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAE---QRGDCALKDARAKLDELEGALQQAKEELARMLREY 417
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100
....*....|....*....|....*
gi 28173564 418 QELLSVKLSLDIEIATYRKLLEGEE 442
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAERE 149
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
111-442 |
2.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 111 KSLLAPLNVELDPEIQKVRAQErEQIKVLNNKFASFIDKVRFLEQQ-NQVLETKWELLQQLDLNNCKNNLEPILegyiSN 189
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLE-EKIRELEERIEELKKEIEELEEKvKELKELKEKAEEYIKLSEFYEEYLDEL----RE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 190 LRKQLETLSgdrvrldSELRSVREVV---EDYKKRYEEEINKRTTAENEFVVLKKDVDAaYTSKVELQAKVDALDGEI-- 264
Cdd:PRK03918 312 IEKRLSRLE-------EEINGIEERIkelEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEELERLKKRLtg 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 265 ----KFFKCLYEGETA--QIQSHISDtsiILSMDNNrnldLDSIIAEVRAQYEEIaRKSKAEAEALYQ--TKFQELQLAA 336
Cdd:PRK03918 384 ltpeKLEKELEELEKAkeEIEEEISK---ITARIGE----LKKEIKELKKAIEEL-KKAKGKCPVCGRelTEEHRKELLE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 337 gRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIAD---AEQrgdcaLKDARAKLDELEgalqqaKEELARM 413
Cdd:PRK03918 456 -EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkelAEQ-----LKELEEKLKKYN------LEELEKK 523
|
330 340
....*....|....*....|....*....
gi 28173564 414 LREYQELLSVKLSLDIEIATYRKLLEGEE 442
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
304-419 |
3.14e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 304 AEVRAQYEEIARKSKAEAEA-LYQTKFQELQLAAGRHGDDLKHTKNEI----SELTRLIQRLRSEIESVKKQCANLETAI 378
Cdd:PRK12704 58 ALLEAKEEIHKLRNEFEKELrERRNELQKLEKRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEELEELI 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 28173564 379 ADAEQRgdcaLK--------DARAKLdeLEGALQQAKEELARMLREYQE 419
Cdd:PRK12704 138 EEQLQE----LErisgltaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
298-430 |
5.46e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 38.01 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 298 DLDSIIAEVRAQYEEIARKSKA----EAEALYQTKFQELQLAAGR---HGDDLKHTKNEISELTRliQRLRSEIESVKKQ 370
Cdd:pfam01442 8 ELSTYAEELQEQLGPVAQELVDrlekETEALRERLQKDLEEVRAKlepYLEELQAKLGQNVEELR--QRLEPYTEELRKR 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28173564 371 CAN--------LETAIADAEQRGDCALKDARAKL----DELEGALQQAKEELARMLREYQELLSVKLSLDIE 430
Cdd:pfam01442 86 LNAdaeelqekLAPYGEELRERLEQNVDALRARLapyaEELRQKLAERLEELKESLAPYAEEVQAQLSQRLQ 157
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
153-440 |
6.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 153 LEQQNQVLETKWELLQQL--DLNNCKNNLEPiLEGYISNLRKQLETLSGDRVRLDSELRSVREvvedYKKRYEEEINKrt 230
Cdd:COG4372 47 LEQLREELEQAREELEQLeeELEQARSELEQ-LEEELEELNEQLQAAQAELAQAQEELESLQE----EAEELQEELEE-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 231 taenefvvLKKDVDAAYTSKVELQAKVDALDGEIKffkcLYEGETAQIQSHISDTSIILSMDNNRNLDLDsiIAEVRAQY 310
Cdd:COG4372 120 --------LQKERQDLEQQRKQLEAQIAELQSEIA----EREEELKELEEQLESLQEELAALEQELQALS--EAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 311 EEIARKSKAEAEALYQTKFQELQLAAGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDCALK 390
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 28173564 391 DARAKLDELEGALQQAKEELARMLREYQELLSVKLSLDIEIATYRKLLEG 440
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
342-420 |
6.33e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 6.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28173564 342 DLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRgdcaLKDARAKLDELEGALQQAKEELARMLREYQEL 420
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE----LEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
169-439 |
6.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 169 QLDLNNCKNNLEPiLEGYISNLRKQLETLS-------GDRVRLDSELRSVREVvEDYKKRYEEEINK---RTTAENEFVV 238
Cdd:PRK01156 196 NLELENIKKQIAD-DEKSHSITLKEIERLSieynnamDDYNNLKSALNELSSL-EDMKNRYESEIKTaesDLSMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 239 LKKDVDAAYtSKVELQAKVDALDGEIKFFKclYEGEtaqiqshISDTSIILSmdnnrNLDldsiiAEVRaQYEEIARKSk 318
Cdd:PRK01156 274 YYKELEERH-MKIINDPVYKNRNYINDYFK--YKND-------IENKKQILS-----NID-----AEIN-KYHAIIKKL- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 319 AEAEALYqTKFQELQlaagRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDCALKDARAKLDE 398
Cdd:PRK01156 332 SVLQKDY-NDYIKKK----SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA 406
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 28173564 399 LEGALqqakEELARMLREYQELLSvklSLDIEIATYRKLLE 439
Cdd:PRK01156 407 IKKEL----NEINVKLQDISSKVS---SLNQRIRALRENLD 440
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
239-419 |
6.68e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 38.89 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 239 LKKDVDaaytskvELQAKVDALDGEIKFFKCLYEGETAQIQSHISDTSIILSMDNNRNL--DLDSIIAEVRAQYEEIARK 316
Cdd:cd22656 126 LLKEAK-------KYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIArkEIKDLQKELEKLNEEYAAK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 317 SKA---EAEALYQTKFQELQLA------AGRHGDDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQRGDC 387
Cdd:cd22656 199 LKAkidELKALIADDEAKLAAAlrliadLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPA 278
|
170 180 190
....*....|....*....|....*....|..
gi 28173564 388 ALKdARAKLDElegaLQQAKEELARMLREYQE 419
Cdd:cd22656 279 AIL-AKLELEK----AIEKWNELAEKADKFRQ 305
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
181-437 |
7.17e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.26 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 181 PILEGYISNLRKQLETLSGDRVRLDSELRSVREVVEDYKK----------RYEEEINKRTTAENEFV---VLKKDVDAAY 247
Cdd:TIGR00606 573 KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNeleskeeqlsSYEDKLFDVCGSQDEESdleRLKEEIEKSS 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 248 TSKVELQAKVDALDGEIKFFK---------CLYEGET-AQIQSHISDTSIILSMDNNRNLDLDSIIAEVRAQYEEIARKS 317
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTdenqsccpvCQRVFQTeAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 318 KAEAEALyQTKFQElqlaagrhgddLKHTKNEISELTRLIQRLRSEIESVKKQcanLETAIADAEQRGDCaLKDArakld 397
Cdd:TIGR00606 733 PGRQSII-DLKEKE-----------IPELRNKLQKVNRDIQRLKNDIEEQETL---LGTIMPEEESAKVC-LTDV----- 791
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 28173564 398 eleGALQQAKEELARMLREYQELLSVKLSLDIEIaTYRKL 437
Cdd:TIGR00606 792 ---TIMERFQMELKDVERKIAQQAAKLQGSDLDR-TVQQV 827
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
341-411 |
7.80e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.55 E-value: 7.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28173564 341 DDLKHTKNEISELTRLIQRLRSEIESVKKQCANLETAIADAEQrgdcALKDARAKLDELEGALQQAKEELA 411
Cdd:TIGR04320 240 DGNKFDKTPIPNPPNSLAALQAKLATAQADLAAAQTALNTAQA----ALTSAQTAYAAAQAALATAQKELA 306
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
357-439 |
9.83e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 37.88 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28173564 357 IQRLRSEIESVKKQCAnleTAIAD---AEQRgdcaLKDARAKLDELEG----ALQQAKEELARmlreyqELLSVKLSLDI 429
Cdd:COG1842 32 IRDMEEDLVEARQALA---QVIANqkrLERQ----LEELEAEAEKWEEkarlALEKGREDLAR------EALERKAELEA 98
|
90
....*....|
gi 28173564 430 EIATYRKLLE 439
Cdd:COG1842 99 QAEALEAQLA 108
|
|
| |
