|
Name |
Accession |
Description |
Interval |
E-value |
| MAP70 |
pfam07058 |
Microtubule-associated protein 70; This family represents a family of plant ... |
71-611 |
0e+00 |
|
Microtubule-associated protein 70; This family represents a family of plant microtubule-associated proteins of size 70 kDa. The proteins contain four predicted coiled-coil domains, and truncation studies identify a central domain that targets the proteins to microtubules. It has no predicted trans-membrane domains, and the region between the coils from approximately residues 240-483 is the targetting region.
Pssm-ID: 399798 [Multi-domain] Cd Length: 544 Bit Score: 737.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 71 GSDPVKVELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKR 150
Cdd:pfam07058 1 GSDPVKVELNRLENEVRDKDRELGEALAEIKALRLSERLKEKAVEELTDELLKLDEKLKASENLLESKNLEIKKINDEKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 151 ASMAAQFAAEATLRRVHAAQKDDDMPPIEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSALAK 230
Cdd:pfam07058 81 AALAAQFAAEATLRRVHAAQKDEDMPPIEAILAPLEAELKLARQEINKLQDDNKALDRLTKSKEAALLEAERAVQIALAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 231 ASMVDDLQNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQRKFQEMNEERRIL 310
Cdd:pfam07058 161 ASLVDDLQNKNQELMKQIEICQEENKILDKAHRQKVAEVEKLSQTVRELEEAVLAGGAAANAVRDYQRKVKEMNEERRTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 311 DRELARAKVSASRVATVVANEWKDGSDKVMPVKQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFQLRLRVLEES 390
Cdd:pfam07058 241 ERELARAKVVANRVATVVANEWKDANDKVMPVKQWLEERRFLQGEMQQLRDKLAISERTAKAEAQLKEKVQLRLKVLEEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 391 LRGPSSSGNRSTPEGRSMSNGPSRRQSLGGADIIPKLTSNGFFSKRSPSSQFRSLNA-STSTILKHAKGTSRSFDGGSRS 469
Cdd:pfam07058 321 LRSSLSGSGRSFSEGRSRSNGPSRRQSLGGASNNGLLSSNGFSSRRRSSSSSSSSLSsSHAKGLKHAKGGSKSFDGGSKS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 470 LDRSKVLTNEPRSKFPLNQSSEGTSGGGSPNSTKQG----DSEKAAGTNNDSVPGVLHDLLQKEVITLRKAANDKDQSLR 545
Cdd:pfam07058 401 LGRGKHLLNGSTENSDAVRDCDTNDSWKGNADEGTIentnSNTDESNDETDNVSGQLYDMLQKEVIHLRKASHEKDQSLK 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334184100 546 DKDEAIEMLAKKVETLTKAMEVEAKKMRREVAAMEKEVSAMRVDnKGSDSRTRRHStNSKGASTTA 611
Cdd:pfam07058 481 DKDDAIEMLAKKVDTLTKAMEVEAKKMRREVAAMEKEVAAMRVD-KEHLGRSKRTG-SSKGAVSGR 544
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
78-376 |
1.32e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 78 ELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMAAQF 157
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 158 AAEATLRRVHAAQKDddmppIEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSALAKAsmvDDL 237
Cdd:COG1196 313 ELEERLEELEEELAE-----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL---EEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 238 QNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQRKFQEMNEERRILDRELARA 317
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 334184100 318 KVSASRVATVVANEWKDGSDKVMPVKQwleeRRFLQGEMQQLRDKLAIADRAAKSEAQL 376
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAA----RLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
74-392 |
1.46e-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: 58.14 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 74 PVKVELNRLEndvrdKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASM 153
Cdd:TIGR02168 665 SAKTNSSILE-----RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 154 AAQFAAEATLRRVHAAQKD--DDMPPIEAILAPLEAELKLARHEIVKLQDD-NRALDRLTKSKEAalLDAERTVQSALAK 230
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTEleAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREA--LDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 231 AsmVDDLQNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEavlaggtaanAVRDYQRKFQEMNEERRIL 310
Cdd:TIGR02168 818 E--AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE----------LIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 311 DRELARAKvsasrvatvvanewKDGSDKVMPVKQWLEERRFLQGEMQQLRDKLaiadraAKSEAQLkEKFQLRLRVLEES 390
Cdd:TIGR02168 886 EEALALLR--------------SELEELSEELRELESKRSELRRELEELREKL------AQLELRL-EGLEVRIDNLQER 944
|
..
gi 334184100 391 LR 392
Cdd:TIGR02168 945 LS 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-363 |
2.66e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 73 DPVKVELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSeklklteNLLDSKNLEIKKINEEKRAS 152
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-------NEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 153 MAAQFAAEATLRRVHAAQKDD--DMPPIEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSALAK 230
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELaeELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 231 asmVDDLQNKNQELMKQIEICQEENRIL--------DKLHRQKVAEV-EKFTQTVRELEEAVLAGGTAANAVRDYQRKFQ 301
Cdd:TIGR02168 395 ---IASLNNEIERLEARLERLEDRRERLqqeieellKKLEEAELKELqAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334184100 302 EMNEERRILDRELARAKVSASRVATVVANEwkdgSDKVMPVKQWLEERRFLQGEMQQLRDKL 363
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENL----EGFSEGVKALLKNQSGLSGILGVLSELI 529
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
78-320 |
1.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 78 ELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMAAQF 157
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 158 AAEATLRRVHAAQKDDdmppIEAILAPLEAELKLARHEIV---KLQDDNRALDRLTKSKEAALLDAERTVQSALAKASMV 234
Cdd:COG1196 362 EAEEALLEAEAELAEA----EEELEELAEELLEALRAAAElaaQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 235 DDLQNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQRKFQEMNEERRILDREL 314
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
....*.
gi 334184100 315 ARAKVS 320
Cdd:COG1196 518 GLRGLA 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
78-323 |
6.21e-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: 48.99 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 78 ELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMAAQF 157
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 158 AAEATL-RRVHAAQKDDDMPPIEAILAPLEAELKLARHEIVKLQDDNRAldrltkskeaALLDAERTVQSALAKASmvDD 236
Cdd:COG4942 101 AQKEELaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR----------EQAEELRADLAELAALR--AE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 237 LQNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLAggtAANAVRDYQRKFQEMNEERRILDRELAR 316
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE---LQQEAEELEALIARLEAEAAAAAERTPA 245
|
....*..
gi 334184100 317 AKVSASR 323
Cdd:COG4942 246 AGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
84-283 |
1.20e-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: 47.84 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 84 NDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMAAQFAAEATL 163
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 164 --------RRVHAAQKDDDMPPIEAILAPLEAELKLARHEIVK--LQDDNRALDRLTKSKEAALLDAERTVQSALAKASM 233
Cdd:COG4942 100 eaqkeelaELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 334184100 234 VDDLQNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAV 283
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
78-385 |
2.89e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 78 ELNRLENDVR-DKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEiKKINEEKRASMAAQ 156
Cdd:COG4717 178 ELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 157 FAAEATLRRVHAAQKDDDMPPI----EAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAAL--------LDAERTV 224
Cdd:COG4717 257 ALLALLGLGGSLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELeellaalgLPPDLSP 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 225 QSALAKASMVDDLQNKNQE---LMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQRKFQ 301
Cdd:COG4717 337 EELLELLDRIEELQELLREaeeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 302 EMNEERRILDRELARAKVSASRvatvvaNEWKDGSDKvmpVKQWLEERRFLQGEMQQLRDKLAIADRAAKsEAQLKEKFQ 381
Cdd:COG4717 417 ELEELLEALDEEELEEELEELE------EELEELEEE---LEELREELAELEAELEQLEEDGELAELLQE-LEELKAELR 486
|
....
gi 334184100 382 LRLR 385
Cdd:COG4717 487 ELAE 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
87-392 |
4.80e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 87 RDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEE-KRASMAAQFAAEATLRR 165
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 166 VHAAQKDddmppIEAILAPLEAELKLARHEIVKLQDDNRALDRltkskEAALLDAERTVQsALAKASMVDDLQNKNQELM 245
Cdd:TIGR02169 299 LEAEIAS-----LERSIAEKERELEDAEERLAKLEAEIDKLLA-----EIEELEREIEEE-RKRRDKLTEEYAELKEELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 246 KQieicqeenrildklhRQKVAEVEKFTQTVREleeavlaggtaanAVRDYQRKFQEMNEERRILDRELARAKVSASRVA 325
Cdd:TIGR02169 368 DL---------------RAELEEVDKEFAETRD-------------ELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334184100 326 TvvanewkDGSDKVMPVKQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFQLRLRVLEESLR 392
Cdd:TIGR02169 420 E-------ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
91-391 |
8.03e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.36 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 91 RELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRAsmaaqfaAEATLRRVHAAQ 170
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALRE-------AEAAKEELRIEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 171 KDDdmppiEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSALAKASMVDDlqnknqelmkqiei 250
Cdd:pfam19220 114 RDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQ-------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 251 cqeENRILDKLHRQKVAEVEKFTQTVRELEEAVLAggtAANAVRDYQRKFQEMNEERRILDRELARAKVSASRVATVVAN 330
Cdd:pfam19220 175 ---ENRRLQALSEEQAAELAELTRRLAELETQLDA---TRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRM 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334184100 331 EWKDGSDKVMPVKQWLEERRflqgemQQLRDKLA---IADRAAKSEAQLKEKFQLRLRVLEESL 391
Cdd:pfam19220 249 KLEALTARAAATEQLLAEAR------NQLRDRDEairAAERRLKEASIERDTLERRLAGLEADL 306
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-322 |
1.17e-03 |
|
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: 41.98 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 62 DNEFITLLHGSDPVKVELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSE--------------- 126
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvkekigelea 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 127 KLKLTENLLDSKNLEIKKINEEKRASMAAQFAAEATL----RRVHAAQKDDDmpPIEAILAPLEAELKLARHEIVKLQDD 202
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIeeleREIEEERKRRD--KLTEEYAELKEELEDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 203 NRALDRLTKSKEAALLDAERTVQSALAKasmVDDLQNKNQEL-MKQIEICQEENRILDKLH------RQKVAEVEKFTQt 275
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRE---LDRLQEELQRLsEELADLNAAIAGIEAKINeleeekEDKALEIKKQEW- 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 334184100 276 vrELEEAVLAGGTAANAVRDYQRKFQEMNEERRILDRELARAKVSAS 322
Cdd:TIGR02169 456 --KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-392 |
1.47e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 185 LEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSAL--AKASMVDDLQNKNQELMKQIEICQEENRILDK-- 260
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAElaELEAELEELRLELEELELELEEAQAEEYELLAel 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 261 --LHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQRKFQEMNEERRILDRELARAKVSASRVATVVANEWKDGSDK 338
Cdd:COG1196 298 arLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 334184100 339 VMPVKQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFQLRLRVLEESLR 392
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-395 |
1.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 79 LNRLENDVRDKDRELSESQAEIKALrlseRQREKAVEELTEELGKMSEklkLTENLLDSKNLeikkinEEKRAsmaaqfA 158
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEAL----EAELDALQERREALQRLAE---YSWDEIDVASA------EREIA------E 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 159 AEATLRRVHAAQKDddmppieaiLAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSALAKASMVDDLQ 238
Cdd:COG4913 673 LEAELERLDASSDD---------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 239 NKNQ-----ELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLA-----------GGTAANAVRDYQRKFQE 302
Cdd:COG4913 744 RLELralleERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadLDADLESLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 303 MNE------ERRILDRELARAKVSASRVATVVANEWKDGSDKVMPVKQWLEERRFLQG-------------EMQQLRDKL 363
Cdd:COG4913 824 LEEdglpeyEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPFGPGrylrlearprpdpEVREFRQEL 903
|
330 340 350
....*....|....*....|....*....|...
gi 334184100 364 -AIADRAAKSEAQLKEKFQLRLRVLEESLRGPS 395
Cdd:COG4913 904 rAVTSGASLFDEELSEARFAALKRLIERLRSEE 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
75-249 |
1.83e-03 |
|
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: 41.58 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 75 VKVELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMA 154
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 155 AQFAAEATLRRvhaaqkdddmppieailapLEAELKLARHEIVKLQDD-NRALDRLTKSKEAALLDAERTVQSALAKASM 233
Cdd:TIGR02168 902 ELRELESKRSE-------------------LRRELEELREKLAQLELRlEGLEVRIDNLQERLSEEYSLTLEEAEALENK 962
|
170
....*....|....*.
gi 334184100 234 VDDLQNKNQELMKQIE 249
Cdd:TIGR02168 963 IEDDEEEARRRLKRLE 978
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
82-318 |
2.24e-03 |
|
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: 41.26 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 82 LENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLK----LTENLLDSKNLEIKKINE---------E 148
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEaakcLKEDMLEDSNTQIEQLRKmmlshegvlQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 149 KRASMAAQFAaEATLRRVHAAQKDDDMP------PIEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALL---- 218
Cdd:pfam15921 188 EIRSILVDFE-EASGKKIYEHDSMSTMHfrslgsAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLqqhq 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 219 --------DAERTVQSALAKASMVDDLQNKNQElmkQIEICQEENRILDKLHRQKVAEVEKFTQTVR-ELEEavlaggta 289
Cdd:pfam15921 267 drieqlisEHEVEITGLTEKASSARSQANSIQS---QLEIIQEQARNQNSMYMRQLSDLESTVSQLRsELRE-------- 335
|
250 260
....*....|....*....|....*....
gi 334184100 290 anAVRDYQRKFQEMNEERRILDRELARAK 318
Cdd:pfam15921 336 --AKRMYEDKIEELEKQLVLANSELTEAR 362
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
76-389 |
3.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 76 KVELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMAA 155
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 156 QFAAEATLRRVHAAQKDDDMPPIEAilAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAAlLDAERTVQSALAKASMVD 235
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA-KKADEAKKKAEEAKKKAD 1500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 236 DLQNKNQELMKQIEICQ-EENRILDKLhrqKVAEVEKFTQTVRELEEAVLAggtaanavrDYQRKFQEMNEERRILDREL 314
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKaEEAKKADEA---KKAEEAKKADEAKKAEEKKKA---------DELKKAEELKKAEEKKKAEE 1568
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334184100 315 ARAKVSASRVATVVANEWKDGSDKVMP--VKQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFQLRLRVLEE 389
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
78-231 |
4.52e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 78 ELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKM-------SEKLKLTENLLDSKNLE--------I 142
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsGGSVSYLDVLLGSESFSdfldrlsaL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 143 KKINEEKRASMAAQFAAEATLRRVHAAQKDDdmppiEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAER 222
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAK-----LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
....*....
gi 334184100 223 TVQSALAKA 231
Cdd:COG3883 200 ELEAELAAA 208
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
85-378 |
4.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 85 DVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNL--EIKKINEEKRASMAAQFAAEAT 162
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 163 LRRVHAAQKDddmppieaiLAPLEAELKLARHEIvklqddNRALDRLTKSKEAALLDAERTVQSALAKASM----VDDLQ 238
Cdd:COG4717 155 LEELRELEEE---------LEELEAELAELQEEL------EELLEQLSLATEEELQDLAEELEELQQRLAEleeeLEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 239 NKNQELMKQIEICQEENRILDKLHRQKVAEV----------------EKFTQTVRELEEAVLAGGTAANAVRDYQRKFQE 302
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334184100 303 MNEERRILDRELARAKVSASRVATVVANEWKDGS---DKVMPVKQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKE 378
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDlspEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
147-316 |
6.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 147 EEKRASMAAQFAAEATLRRVHAAQKDDDmppieailapLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQS 226
Cdd:COG4913 265 AAARERLAELEYLRAALRLWFAQRRLEL----------LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184100 227 ALAKAsmVDDLQNKNQELMKQIEICQEE----NRILDKLHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQ----R 298
Cdd:COG4913 335 NGGDR--LEQLEREIERLERELEERERRrarlEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALaeaeA 412
|
170
....*....|....*...
gi 334184100 299 KFQEMNEERRILDRELAR 316
Cdd:COG4913 413 ALRDLRRELRELEAEIAS 430
|
|
| |
