|
Name |
Accession |
Description |
Interval |
E-value |
| Cnn_1N |
pfam07989 |
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ... |
101-170 |
3.75e-19 |
|
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.
Pssm-ID: 462333 [Multi-domain] Cd Length: 69 Bit Score: 81.41 E-value: 3.75e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 101 RELEEQMSALRKENFNLKLRIYFLEEGQPGaRADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAAR 170
Cdd:pfam07989 1 REQEKQIDKLKKENFNLKLKIHFLEERLEK-LAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-430 |
7.47e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 138 ESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAISHHEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPVEN--IAK 215
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 216 TRKMLRLESEVQRLEEELVNIEARNVAARNELEfmlaERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDS 295
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 296 LKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNA 375
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 386767865 376 ELETMRQQNVYFRELSENLQQKEVRQLDRGVAIVQPMRMTADAGVGITSSLERSG 430
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-407 |
8.29e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 8.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 100 VRELEEQMSALRKE--------NFNLKLRIYfleegqpgaradsSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAARA 171
Cdd:COG1196 195 LGELERQLEPLERQaekaeryrELKEELKEL-------------EAELLLLKLRELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 172 ISHHEELQRKAdidsQAIIDELQEQIHAYQMAESggqpveniAKTRKMLRLESEVQRLEEELVNIEARNV---AARNELE 248
Cdd:COG1196 262 LAELEAELEEL----RLELEELELELEEAQAEEY--------ELLAELARLEQDIARLEERRRELEERLEeleEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 249 FMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSM 328
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386767865 329 KEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYfRELSENLQQKEVRQLDRGVA 407
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAALLEAALAELLEELA 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
87-400 |
9.01e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 87 GGGNSPLPSQGRSVRELEE-QMSALRKENFNLKLRIYFLEEgqpgARADSSTESLSKQLIDAKIEIATLRKTVDvkmELL 165
Cdd:TIGR02169 657 GGSRAPRGGILFSRSEPAElQRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIE---QLE 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 166 KDAARAISHHEELQRKADIDSQAI-------------IDELQEQIHAYQMAES------GGQPVENIaktrkmlrlESEV 226
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIenvkselkelearIEELEEDLHKLEEALNdlearlSHSRIPEI---------QAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 227 QRLEEELVNIEARnvaaRNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKE 306
Cdd:TIGR02169 801 SKLEEEVSRIEAR----LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 307 NQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIaklnAELETMRQQNVY 386
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELS 952
|
330
....*....|....
gi 386767865 387 FRELSENLQQKEVR 400
Cdd:TIGR02169 953 LEDVQAELQRVEEE 966
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
96-404 |
2.31e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 96 QGRSVRELEEQMSALRKENFNLKlriyfleegQPGARADSSTESLSKQLIDAKIEIATLRKTVdvkmellkdaaRAISHH 175
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELE---------EELEQLRKELEELSRQISALRKDLARLEAEV-----------EQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 176 EELQRKADIDSQAIIDELQEQIHAYQMAEsggqpvenIAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFM---LA 252
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEEL--------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 253 ERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAA 332
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386767865 333 NTMDVQRQSILLLEATIKRKEKSCGSMQKNV----LNYEALIAKLNAELETMRQ---QNVYFRELSENLQQKEVRQLDR 404
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLegleVRIDNLQERLSEEYSLTLEeaeALENKIEDDEEEARRRLKRLEN 979
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
164-378 |
5.20e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 164 LLKDAARAIshHEELQrkaDIDSQaiIDELQEQIHAYQ--MAESGGQPVENIAKTRKM--------LRLESEVQRLEEEL 233
Cdd:PHA02562 171 LNKDKIREL--NQQIQ---TLDMK--IDHIQQQIKTYNknIEEQRKKNGENIARKQNKydelveeaKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 234 VNIEarnvaarnelefmlaERLESLTACEGKIQELAIKNSELVERLEKE-------------TASAESSNEAIDSLKVEL 300
Cdd:PHA02562 244 LNLV---------------MDIEDPSAALNKLNTAAAKIKSKIEQFQKVikmyekggvcptcTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 301 EACRKENQDLVTSIRTLK---HDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAEL 377
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEeimDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
.
gi 386767865 378 E 378
Cdd:PHA02562 389 D 389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-404 |
1.05e-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: 51.61 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 131 ARADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAI---SHHEELQRKADIDS-QAIIDELQEQIHAYQmaesg 206
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlGEEEQLRVKEKIGElEAEIASLERSIAEKE----- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 207 gqpveniaktRKMLRLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLTAcegKIQELAIKNSELVERLEKETASA 286
Cdd:TIGR02169 315 ----------RELEDAEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTE---EYAELKEELEDLRAELEEVDKEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 287 ESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKscgSMQKNVLNY 366
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL---EIKKQEWKL 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 386767865 367 EALIAKLNAELETMRQQNVYFRELSENLQQKEvRQLDR 404
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQ-RELAE 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-400 |
6.34e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 122 YFLEEGQPGARADSSTESLsKQLIDAKIEIATLRKtvdvKMELLKDAARaisHHEELQRKADidSQAIIDELQEQIHAYQ 201
Cdd:COG4913 216 YMLEEPDTFEAADALVEHF-DDLERAHEALEDARE----QIELLEPIRE---LAERYAAARE--RLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 202 maesggqpveniaKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFMLAERLESLTACEG----KIQELAIKNSELVE 277
Cdd:COG4913 286 -------------AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 278 RLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQsILLLEATIKRKEKScg 357
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR-DLRRELRELEAEIA-- 429
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 386767865 358 SMQKNVLNYEaliaklnAELETMRqqnvyfRELSENLQQKEVR 400
Cdd:COG4913 430 SLERRKSNIP-------ARLLALR------DALAEALGLDEAE 459
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
98-400 |
1.01e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 98 RSVRELEEQMSALRKENFNLKLRIYFLEEGQPGAR-----ADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAA--- 169
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPvdl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 170 -RAISHHEELQ-RKADI-----DSQAIIDELQEQI-HAYQMAESG-----GQPVENIAKTRKMLRLESEVQRLEEELVNI 236
Cdd:PRK02224 408 gNAEDFLEELReERDELrereaELEATLRTARERVeEAEALLEAGkcpecGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 237 EARnvaaRNELEFMLaERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSL---KVELEACRKENQDLVTS 313
Cdd:PRK02224 488 EEE----VEEVEERL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELrerAAELEAEAEEKREAAAE 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 314 IRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEkscgsmqknvlNYEALIAKLNAELETMRQQNvyfRELSEN 393
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIA-----------DAEDEIERLREKREALAELN---DERRER 628
|
....*..
gi 386767865 394 LQQKEVR 400
Cdd:PRK02224 629 LAEKRER 635
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
91-332 |
1.69e-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: 47.07 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 91 SPLPSQGRSVRELEEQMSALRKENFNLKLRIyfleegqpgARADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAAR 170
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKEL---------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 171 AISHHEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPV-----ENIAKTRKMLRLESEVQRLEEELVNIEARNVAARN 245
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 246 ELEFMLAERLESLTAcegKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQV 325
Cdd:COG4942 164 ALRAELEAERAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*..
gi 386767865 326 RSMKEAA 332
Cdd:COG4942 241 ERTPAAG 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
45-398 |
1.97e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 45 DRRVLRKLAEALSKSIDDTSPGalqdvTMENSYASFDvprppgGGNSPLPSQGRSVRELEEQMSALRKENFNLKLRIYFL 124
Cdd:pfam15921 423 DRNMEVQRLEALLKAMKSECQG-----QMERQMAAIQ------GKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 125 EEGQPGARADSSTESLSKQLIDA-KIEIATLRKTVDVKMELLKDAARAISHHEELQRKAD------IDSQAIIDELQEQI 197
Cdd:pfam15921 492 ESSERTVSDLTASLQEKERAIEAtNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEalklqmAEKDKVIEILRQQI 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 198 HayQMAESGGQpveniaKTRKMLRLESEVQRLEEElvnIEARNVAARnELEFMLAERLESLTACEGKIQELAIKNSELVE 277
Cdd:pfam15921 572 E--NMTQLVGQ------HGRTAGAMQVEKAQLEKE---INDRRLELQ-EFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 278 RLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQS----ILLLEATIKRKE 353
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSaqseLEQTRNTLKSME 719
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 386767865 354 KSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQKE 398
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK 764
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
138-314 |
2.09e-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: 46.07 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 138 ESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAISHHEElqrkaDIDS-QAIIDELQEQIhayqmaesggqpvENIAKT 216
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL-----EIEEvEARIKKYEEQL-------------GNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 217 RKMLRLESEVQRLEEELVNIEARnvaarnELEFMlaERLESLtacEGKIQELAIKNSELVERLEKETASAEssnEAIDSL 296
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEDE------ILELM--ERIEEL---EEELAELEAELAELEAELEEKKAELD---EELAEL 154
|
170
....*....|....*...
gi 386767865 297 KVELEACRKENQDLVTSI 314
Cdd:COG1579 155 EAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-404 |
2.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 216 TRKMLRLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLTACEgKIQELAIKNSEL---VERLEKETASAESSNEA 292
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLA-EYSWDEIDVASAereIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 293 IDSLKVELEACRKENQDLVTSIRTLKHDMKRqvrsmkeaantmdvqrqsillLEATIKRKEKSCGSMQKNVLNYEALIAK 372
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGR---------------------LEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190
....*....|....*....|....*....|....*.
gi 386767865 373 -LNAELETMRQQNV---YFRELSENLQQkEVRQLDR 404
Cdd:COG4913 746 eLRALLEERFAAALgdaVERELRENLEE-RIDALRA 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
97-409 |
3.66e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 97 GRSVRELEEQMS------ALRKENFNLKLRIYFLEEGQPGARADSSTESLsKQLIDAKIEIATLRKTVDVKMELLKDAAR 170
Cdd:TIGR02168 199 ERQLKSLERQAEkaerykELKAELRELELALLVLRLEELREELEELQEEL-KEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 171 AISHHEELQRKADIDSQAIIDELQEQIHAYQmaESGGQPVENIAK-TRKMLRLESEVQRLEEELVNIEARNVAARNELEf 249
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILR--ERLANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELE- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 250 MLAERLESLtacEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMK 329
Cdd:TIGR02168 355 SLEAELEEL---EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 330 EAAntMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQ--NVYFRELSENLQQKEVRQLDRGVA 407
Cdd:TIGR02168 432 EAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARLDSLERLQENLEGFSEGVK 509
|
..
gi 386767865 408 IV 409
Cdd:TIGR02168 510 AL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-406 |
6.07e-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: 45.82 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 213 IAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFM-----------------LAERLESLTACEGKIQELAIKNSEL 275
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELeeeleqlrkeleelsrqISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 276 VERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMK---------------------RQVRSMKEAANT 334
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrealdelraeltllneeaaNLRERLESLERR 832
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386767865 335 MDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELET----MRQQNVYFRELSENLQQ--KEVRQLDRGV 406
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllneRASLEEALALLRSELEElsEELRELESKR 910
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
157-326 |
9.97e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 157 TVDVKMELLKD--------------AARAISHH----EELQRKA--DIDSQAIIDE----------LQEQIHAYQMAESG 206
Cdd:COG2433 316 SVEEKLHLAREygydndherdalaaALKAYDAYknkfERVEKKVppDVDRDEVKARvirglsieeaLEELIEKELPEEEP 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 207 GQPVENIA-------KTRKMLRLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLtaceGKIQELAIKNSELVERL 279
Cdd:COG2433 396 EAEREKEHeerelteEEEEIRRLEEQVERLEAEVEELEAELEEKDERIE-RLERELSEA----RSEERREIRKDREISRL 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 386767865 280 EKEtasaessneaIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVR 326
Cdd:COG2433 471 DRE----------IERLERELEEERERIEELKRKLERLKELWKLEHS 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
100-398 |
3.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 100 VRELEEQMSALRKENFNLKLRIYFLEEGQPGARADSSTESLSKQLIDAKIEI----ATLRKTVDVKMELLKDAARAISHH 175
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIekrlSRLEEEINGIEERIKELEEKEERL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 176 EELQRKADiDSQAIIDELQEQIHAYQMA------------ESGGQPVENIAKtrKMLRLESEVQRLEEELVNIEARnvaa 243
Cdd:PRK03918 341 EELKKKLK-ELEKRLEELEERHELYEEAkakkeelerlkkRLTGLTPEKLEK--ELEELEKAKEEIEEEISKITAR---- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 244 RNELEFMLAER---LESLTACEGKI------------QELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQ 308
Cdd:PRK03918 414 IGELKKEIKELkkaIEELKKAKGKCpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 309 DLVTsirtlKHDMKRQVRSMKEAANTMDVQRqsillleatIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFR 388
Cdd:PRK03918 494 ELIK-----LKELAEQLKELEEKLKKYNLEE---------LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
330
....*....|
gi 386767865 389 ELSENLQQKE 398
Cdd:PRK03918 560 ELEKKLDELE 569
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
86-408 |
3.44e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 86 PGGGNSPLPSQGRSVRELEEQMSALRKENFNLKLRIYFLEEGQpgARADSSTESLSKQLIDAKIEIATLRKTVDVKMELL 165
Cdd:TIGR00618 523 PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM--QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLT 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 166 KDAAraishheELQRKADIDSQAIIDELQEQIHAYQMAESGGQPVENIAKtrKMLRLESEVQRLEEELVNIEARnvAARN 245
Cdd:TIGR00618 601 EKLS-------EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL--KLTALHALQLTLTQERVREHAL--SIRV 669
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 246 ELEFMLAERLESLTACEGKIQELAIKNSELVERLEK----ETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDM 321
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLlrelETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 322 KRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEA---LIAKLNAELETMRQQNVYFRELSENLQQKE 398
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEdthLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
330
....*....|
gi 386767865 399 VRQLDRGVAI 408
Cdd:TIGR00618 830 EEQFLSRLEE 839
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
130-324 |
4.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 130 GARADSSTESLSKQLIDAKIEIATLRKTV---DVKMELLKDAARAISHHEELQRkADIDSQAIIDELQEQIHAYQMAESG 206
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLealEAELDALQERREALQRLAEYSW-DEIDVASAEREIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 207 GQPVENIAKTRKmlRLESEVQRLEEELVNIEARNVAARNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASA 286
Cdd:COG4913 684 SDDLAALEEQLE--ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190
....*....|....*....|....*....|....*...
gi 386767865 287 ESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQ 324
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
91-383 |
4.17e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 91 SPLPSQGRSVRELEEQMSALRKENFNLKLRIyflEEGQPGARADSSTESLSKQLidakieiatlrktvdvkmellkDAAR 170
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKI---AEYTKSIDIKKATESLEEQL----------------------AAAE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 171 AISHHEELQRKADIDsqaiIDELQEQIHayQMAESGGQPVENIAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEfm 250
Cdd:COG5185 323 AEQELEESKRETETG----IQNLTAEIE--QGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLD-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 251 laerlESLTACEGKIQELAIK-------NSELVERLEKETASAESSNEAIDSLKVELEAC----RKENQDLVTSIRTLKH 319
Cdd:COG5185 395 -----EIPQNQRGYAQEILATledtlkaADRQIEELQRQIEQATSSNEEVSKLLNELISElnkvMREADEESQSRLEEAY 469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386767865 320 D-MKRQVRSMKEAANTMDVQRQSILlleATIKRKEkscgsmqknvlnyEALIAKLNAELETMRQQ 383
Cdd:COG5185 470 DeINRSVRSKKEDLNEELTQIESRV---STLKATL-------------EKLRAKLERQLEGVRSK 518
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
190-376 |
4.75e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 190 IDELQEQIHAYQmaesggqpveniAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFMlaERLESLTACEGKIQELA 269
Cdd:COG4717 73 LKELEEELKEAE------------EKEEEYAELQEELEELEEELEELEAELEELREELEKL--EKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 270 IKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSillLEATI 349
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE---LEEEL 215
|
170 180
....*....|....*....|....*..
gi 386767865 350 KRKEKSCGSMQKNVLNYEALIAKLNAE 376
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
93-306 |
7.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 93 LPSQGRSVRELEEQMSALRKENFNLKLriyfLEEGQpgARADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAArai 172
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA----LEEQL--EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ--- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 173 shhEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPVENIAKTRKmlRLESEVQRLEEELVNIEArnvAARNELEFMLA 252
Cdd:COG4913 734 ---DRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID--ALRARLNRAEEELERAMR---AFNREWPAETA 805
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386767865 253 ERLESLTACEGKIQELA-IKNSELVERLEK-ETASAESSNEAIDSLKVELEACRKE 306
Cdd:COG4913 806 DLDADLESLPEYLALLDrLEEDGLPEYEERfKELLNENSIEFVADLLSKLRRAIRE 861
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
211-400 |
8.52e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 211 ENIAKTRKMLRLESEvqRLEEELvniearnvAARNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKetasAESSN 290
Cdd:PRK03918 165 KNLGEVIKEIKRRIE--RLEKFI--------KRTENIEELIKEKEKELEEVLREINEISSELPELREELEK----LEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 291 EAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEaTIKRKEKSCGSMQKNVLNYEALI 370
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190
....*....|....*....|....*....|
gi 386767865 371 AKLNAELETMRQQNVYFRELSENLQQKEVR 400
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEER 339
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-308 |
1.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 138 ESLSKQLIDAKIEIATLRKTVDvKMELLKDAARAISHHEELQRK-ADIDSQaiIDELQEQIHAYQmaesggqpveniakt 216
Cdd:COG4717 98 EELEEELEELEAELEELREELE-KLEKLLQLLPLYQELEALEAElAELPER--LEELEERLEELR--------------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 217 rkmlRLESEVQRLEEELVNIEARNVAARNELEFMLAERLESLTAcegKIQELAIKNSELVERLEKETASAESSNEAIDSL 296
Cdd:COG4717 160 ----ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE---ELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170
....*....|..
gi 386767865 297 KVELEACRKENQ 308
Cdd:COG4717 233 ENELEAAALEER 244
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
142-334 |
1.60e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 142 KQLIDAKIEIATLRKTVDVKMELLKDAAraisHHEELQRKADIDsqaiiDELqeqihayqmaesggqpVENIAKTRKMLR 221
Cdd:PLN03229 560 KAEINKKFKEVMDRPEIKEKMEALKAEV----ASSGASSGDELD-----DDL----------------KEKVEKMKKEIE 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 222 LE--SEVQRLEEELVNIEARNVAARNELEFM-LAERLESLTACEGKIQELAIKNSEL---VERLEKETASAESSNEAIDS 295
Cdd:PLN03229 615 LElaGVLKSMGLEVIGVTKKNKDTAEQTPPPnLQEKIESLNEEINKKIERVIRSSDLkskIELLKLEVAKASKTPDVTEK 694
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 386767865 296 LKVE-LEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANT 334
Cdd:PLN03229 695 EKIEaLEQQIKQKIAEALNSSELKEKFEELEAELAAARET 734
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
100-368 |
1.84e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 100 VRELEEQMSALRKENFNLKLRIYFLEEGQPGARADSSTESLSKQLIDAKIEiaTLRKTVDVKMELLKDAARAISHHEE-- 177
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE--ELEDRDEELRDRLEECRVAAQAHNEea 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 178 ---LQRKADIDSQAiiDELQEQIHAyqmAESGGQPVENIAKTRkmlrlESEVQRLEEELVNIEAR---NVAARNELEFML 251
Cdd:PRK02224 345 eslREDADDLEERA--EELREEAAE---LESELEEAREAVEDR-----REEIEELEEEIEELRERfgdAPVDLGNAEDFL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 252 AERLESLTACEGKIQELAIKNSELVERLEKETA---------------------SAESSNEAIDSLKVELEACRKENQDL 310
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEV 494
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 386767865 311 VTSIRTLKhDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEA 368
Cdd:PRK02224 495 EERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-397 |
2.60e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 101 RELEEQMSALR---KENFNLKLRIYFLEegqpgaradSSTESLSKQLIDAKieiaTLRKTVDVKMELLKDAARAISHHEE 177
Cdd:TIGR04523 363 RELEEKQNEIEklkKENQSYKQEIKNLE---------SQINDLESKIQNQE----KLNQQKDEQIKKLQQEKELLEKEIE 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 178 LQRKADIDSQAIIDELQEQIHAYQMAesggqpVENIAKTRKMLR-----LESEVQRLEEELVNIEARNVAARNELEFMLA 252
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELI------IKNLDNTRESLEtqlkvLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 253 ERLESltacEGKIQELAIKNSEL---VERLEKETASAESS----NEAIDSLKVEL--EACRKENQDLVTSIRTLKHDMKR 323
Cdd:TIGR04523 504 EKKEL----EEKVKDLTKKISSLkekIEKLESEKKEKESKisdlEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKS 579
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386767865 324 QVRSMKEaantmdvqrqsillLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQK 397
Cdd:TIGR04523 580 LKKKQEE--------------KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK 639
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
98-402 |
4.36e-03 |
|
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: 39.72 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 98 RSVRELEEQMSALRKENFNLKLRIYFLEegqpgaradSSTESLSKQLIDAKIEIATLRKTVdvkMELLKDAARAISHHEE 177
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREIVLKEENSSLT---------SSARQLEKARRELEQELAQYLKKI---EDLNKKLKRHKALVRR 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 178 LQRKADIDSQAIiDELQEQIHAYQ----MAESGGQpveniaKTRKMLRLESEVQRLEEELVNIEARnvaaRNELEFMLAE 253
Cdd:pfam05557 344 LQRRVLLLTKER-DGYRAILESYDkeltMSNYSPQ------LLERIEEAEDMTQKMQAHNEEMEAQ----LSVAEEELGG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 254 RLESLTACEGKIQELaiknselveRLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQ-VRSMKEAA 332
Cdd:pfam05557 413 YKQQAQTLERELQAL---------RQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRcLQGDYDPK 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 333 NTMDVQRQSILLLEATIKRKEKScGSMQKNVLNYEALIAKLNAELETMRQQNvyfrELSENLQQKEVRQL 402
Cdd:pfam05557 484 KTKVLHLSMNPAAEAYQQRKNQL-EKLQAEIERLKRLLKKLEDDLEQVLRLP----ETTSTMNFKEVLDL 548
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
216-346 |
5.39e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 216 TRKMLRLESEVQRLEEElvniearnvaaRNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDS 295
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDE-----------RNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR 549
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 386767865 296 LKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLE 346
Cdd:pfam01576 550 LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLE 600
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
219-330 |
5.90e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 219 MLRLE-----SEVQRLEEELVNIEARNVAARNELEFMLAERLESLtacEGKIQELAIKNSELVERLEKETASAessnEAI 293
Cdd:COG0542 401 RVRMEidskpEELDELERRLEQLEIEKEALKKEQDEASFERLAEL---RDELAELEEELEALKARWEAEKELI----EEI 473
|
90 100 110
....*....|....*....|....*....|....*..
gi 386767865 294 DSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKE 330
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
186-396 |
7.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 186 SQAIIDELQEQIHAYQmaesggqpvENIAKTRKML-RLESEVQRLEEELVNIEARNVAARNELEfMLAERLESLtacEGK 264
Cdd:COG4942 18 QADAAAEAEAELEQLQ---------QEIAELEKELaALKKEEKALLKQLAALERRIAALARRIR-ALEQELAAL---EAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 265 IQELAIKNSELVERLEK------ETASAESSNEAIDSLKVELEAcrKENQDLVTSIRTLKH---DMKRQVRSMKEAANTM 335
Cdd:COG4942 85 LAELEKEIAELRAELEAqkeelaELLRALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYlapARREQAEELRADLAEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386767865 336 DVQRQSIL----LLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQ 396
Cdd:COG4942 163 AALRAELEaeraELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
129-341 |
8.05e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 129 PGARADSSTESLSKQLIDAKIEIATLRKTVDvkmELLKDAARAISHHEELQRKADiDSQAIIDELQEQIHAYQmaesggq 208
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELD---ALQAELEELNEEYNELQAELE-ALQAEIDKLQAEIAEAE------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 209 pvENIAKTRKMLrlesevqrleEELVNIEARNVAARNELEFML--------AERLESLTACEGKIQELAIKNSELVERLE 280
Cdd:COG3883 79 --AEIEERREEL----------GERARALYRSGGSVSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386767865 281 KETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQS 341
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
133-354 |
8.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 133 ADSSTESLSKQLIDAKIEIATLRKTVDvkmELLKDAARAISHHEELQRKAdIDSQAIIDELQEQIHAYQmaesggqpvEN 212
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA---ALKKEEKALLKQLAALERRI-AALARRIRALEQELAALE---------AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386767865 213 IAKTRKML-RLESEVQRLEEELVN--IEARNVAARNELEFML--------AERLESLTACEGKIQELAIKNSELVERLEK 281
Cdd:COG4942 85 LAELEKEIaELRAELEAQKEELAEllRALYRLGRQPPLALLLspedfldaVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386767865 282 ETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSillLEATIKRKEK 354
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE---LEALIARLEA 234
|
|
| |
