|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
404-602 |
1.73e-96 |
|
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: 293.51 E-value: 1.73e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 404 SESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDE-QRTSMTSQKSFQQLTMEKEQAL 482
Cdd:pfam05010 2 SQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEkQKQKELEHAEIQKVLEEKDQAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 483 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 562
Cdd:pfam05010 82 ADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKAE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1209185290 563 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELI 602
Cdd:pfam05010 162 TAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
407-605 |
4.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 407 DKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRK----IVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQAL 482
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 483 ADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAE 562
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1209185290 563 SAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 605
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
405-605 |
6.37e-07 |
|
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: 52.07 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 405 ESDKTAVLTLIREeiITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKTIAQM---IDEQRTSMTSQKSFQQLTMEKEQA 481
Cdd:COG4942 47 KKEEKALLKQLAA--LERRIAALA--RRIRALEQELAALEAELAELEKEIAELraeLEAQKEELAELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 482 LADLNSveRSLSDLFRRYENLKGVLEGFKKNEEALKKcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQvrtkAKA 561
Cdd:COG4942 123 ALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAELEALLAELEEERAALEA----LKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1209185290 562 ESAALHAGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 605
Cdd:COG4942 196 ERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
415-594 |
1.91e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 415 IREEIitKEIEANEWKKKYEETRQEVLEMRKIVAEYEktiaqmidEQRTSMTSQKSfqqltmEKEQALADLNS----VER 490
Cdd:TIGR02168 218 LKAEL--RELELALLVLRLEELREELEELQEELKEAE--------EELEELTAELQ------ELEEKLEELRLevseLEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 491 SLSDLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---AKAESAALH 567
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRE----RLANLERQLEELEAQLEELESKLDELAEELAELEEKleeLKEELESLE 357
|
170 180
....*....|....*....|....*..
gi 1209185290 568 AGLRKEQMKVESLERALQQKNQEIEEL 594
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETL 384
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
414-605 |
3.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 414 LIREEIITKEIEAN---------------EWKKKYEETRQE--VLEMRKIVAEYEKTIAQMideqrtsmtsqksfQQLTM 476
Cdd:COG1196 188 LERLEDILGELERQleplerqaekaeryrELKEELKELEAEllLLKLRELEAELEELEAEL--------------EELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 477 EKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCaqdyLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR 556
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE----LARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1209185290 557 TK---AKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 605
Cdd:COG1196 330 EEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-600 |
4.89e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 416 REEIITKEIEANEwkKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTsMTSQKSFQQltMEKEQALADLNSVERSLSDL 495
Cdd:TIGR02168 254 ELEELTAELQELE--EKLEELRLEVSELEEEIEELQKELYALANEISR-LEQQKQILR--ERLANLERQLEELEAQLEEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 496 FRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIH---AEEKLDKANEEIAQVRTKAKAESAALHAgLRK 572
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIASLNNEIER-LEA 407
|
170 180
....*....|....*....|....*...
gi 1209185290 573 EqmkVESLERALQQKNQEIEELTKICDE 600
Cdd:TIGR02168 408 R---LERLEDRRERLQQEIEELLKKLEE 432
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
422-600 |
5.61e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 422 KEIEANEWKKKYEETRQEvlEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADlnSVERSLSDLFRRYEN 501
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 502 LKGVLEGFKKNE-------EALKKCAQDYLARVKQEEQRYQALKIHAEE-KLDKANEEIAQVRTKAKAESAALHAGLRK- 572
Cdd:PTZ00121 1631 EKKKVEQLKKKEaeekkkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKk 1710
|
170 180 190
....*....|....*....|....*....|.
gi 1209185290 573 ---EQMKVESLERALQQKNQEIEELTKICDE 600
Cdd:PTZ00121 1711 eaeEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
405-605 |
6.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 405 ESDKTAVLTLIR---EEIITKEIEA--NEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKE 479
Cdd:COG4717 33 EAGKSTLLAFIRamlLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 480 QALADLNSVER--SLSDLFRRYENLKGVLEGFKKNEEALKKcaqdYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRT 557
Cdd:COG4717 113 ELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1209185290 558 KAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 605
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
416-594 |
9.67e-06 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 46.82 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 416 REEIITKEI-----EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM--IDEQRTSMtsQKSFQQLTMEKEQALADLNSV 488
Cdd:pfam13851 41 KEERNEKLMseiqqENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLknLKARLKVL--EKELKDLKWEHEVLEQRFEKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 489 ERSLSDLFRRYEnlkgvlegfkkneealkKCAQDYLARVKQE----EQRYQALkihaEEKLDKANEEIAQVRTKAKAESA 564
Cdd:pfam13851 119 ERERDELYDKFE-----------------AAIQDVQQKTGLKnlllEKKLQAL----GETLEKKEAQLNEVLAAANLDPD 177
|
170 180 190
....*....|....*....|....*....|
gi 1209185290 565 ALhaglrkeQMKVESLERALQQKNQEIEEL 594
Cdd:pfam13851 178 AL-------QAVTEKLEDVLESKNQLIKDL 200
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
412-601 |
3.83e-05 |
|
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: 46.89 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 412 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSfQQLTMEKEQALADLNSVERS 491
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH-QARTVLKARTEAHFNNNEEV 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 492 LSDLFR--RYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKaneEIAQVRTKAKAESAALHAg 569
Cdd:TIGR00618 771 TAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQ---EEEQFLSRLEEKSATLGE- 846
|
170 180 190
....*....|....*....|....*....|..
gi 1209185290 570 LRKEQMKVESLERALQQKNQEIEELTKICDEL 601
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
412-596 |
4.25e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 412 LTLIREEIITKEIEAnewkkkYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADLNSVE-- 489
Cdd:PRK04863 884 LNLLADETLADRVEE------IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqq 957
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 490 -RSLSDLFRR-----YENLKGVLEGFKKNEEALKKC---AQDYLARVKQE-----------EQRYQALK--IHA-EEKLD 546
Cdd:PRK04863 958 aFALTEVVQRrahfsYEDAAEMLAKNSDLNEKLRQRleqAEQERTRAREQlrqaqaqlaqyNQVLASLKssYDAkRQMLQ 1037
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1209185290 547 KANEEIAQ--VRTKAKAESAA------LHAGLRKEQMKVESLERALQQKNQEIEELTK 596
Cdd:PRK04863 1038 ELKQELQDlgVPADSGAEERArarrdeLHARLSANRSRRNQLEKQLTFCEAEMDNLTK 1095
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
425-601 |
4.56e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 425 EANEW-KKKYEETRQEVLEMRKIVAEY-EKTIAQMIDEQRTSMTSQKSfqQLTMEKEQALADLNSVERSLSDLFRRYENL 502
Cdd:COG3206 175 KALEFlEEQLPELRKELEEAEAALEEFrQKNGLVDLSEEAKLLLQQLS--ELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 503 KGVLEGFKKNEEAlkkcaQDYLARVKQEEQRYQALKIHAEEK---LDKANEEIAQVRTKAKAESAALHAGLRKE----QM 575
Cdd:COG3206 253 PDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAElealQA 327
|
170 180
....*....|....*....|....*.
gi 1209185290 576 KVESLERALQQKNQEIEELTKICDEL 601
Cdd:COG3206 328 REASLQAQLAQLEARLAELPELEAEL 353
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
415-596 |
4.64e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 415 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSmtsQKSFQQLTMEKEQALADLNSVERSLSD 494
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 495 LFR------RYENLKGVL--EGFKKNEEALKkcaqdYLARVKQEEQRyqalkihAEEKLDKANEEIAQVRTKAKAESAAL 566
Cdd:COG4942 109 LLRalyrlgRQPPLALLLspEDFLDAVRRLQ-----YLKYLAPARRE-------QAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 1209185290 567 HAGLRKEQMKVESLERALQQKNQEIEELTK 596
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
431-600 |
7.09e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 431 KKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFK 510
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 511 KNEEALKkcAQDYLARVKQEEQRYQALKIHAEEKldKANEEIAQVRTKAKAESAalhaglRKEQMKVESLERALQQKNQE 590
Cdd:PTZ00121 1310 KAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAEAEAAADEA------EAAEEKAEAAEKKKEEAKKK 1379
|
170
....*....|
gi 1209185290 591 IEELTKICDE 600
Cdd:PTZ00121 1380 ADAAKKKAEE 1389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
412-605 |
7.20e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 412 LTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEyektIAQMIDEQRTSM-TSQKSFQQLTMEKEQALADLNSVER 490
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEE----LSRQISALRKDLaRLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 491 SLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKAESAALHAGL 570
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190
....*....|....*....|....*....|....*...
gi 1209185290 571 RKEQMKVESLERA---LQQKNQEIEELTKICDELIAKL 605
Cdd:TIGR02168 838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESEL 875
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
415-572 |
7.76e-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: 44.53 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 415 IREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IDEQRTSM---TSQKSFQQLTMEKEQALADLNSV 488
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLgnvRNNKEYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 489 ERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHA 568
Cdd:COG1579 109 EDEILELMERIEELEEELAELEAELAELE-------AELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYE 181
|
....
gi 1209185290 569 GLRK 572
Cdd:COG1579 182 RIRK 185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
425-600 |
9.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 425 EANEWKKKYEETRQEVLEMRKIVAEYEKTiaqmidEQRTSMTSQKSFQQLTMEKEQALADlnsvERSLSDLFRRYENLKG 504
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKA------AEAAKAEAEAAADEAEAAEEKAEAA----EKKKEEAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 505 VLEGFKKNEEALKKCAQDylARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRK---EQMKVESLE 581
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEED--KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkaeEAKKAEEAK 1463
|
170
....*....|....*....
gi 1209185290 582 RALQQKnQEIEELTKICDE 600
Cdd:PTZ00121 1464 KKAEEA-KKADEAKKKAEE 1481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
435-596 |
3.74e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 435 ETRQEVLEMRKIVAEYEKTIAQmIDEQRTsmTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEgfkkNEE 514
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAE-LEKALA--ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 515 ALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVR---TKAKAESAALHAGLRKEQMKVESLERALQQKNQEI 591
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqiEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
....*
gi 1209185290 592 EELTK 596
Cdd:TIGR02168 827 ESLER 831
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
425-608 |
6.62e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 425 EANEWKKKYEETRQEVLEMRKIVAEY----------EKTIAQMIDEQRTSmtsqksfqQLTMEKEQALadlnsVERsLSD 494
Cdd:COG1340 79 ERDELNEKLNELREELDELRKELAELnkaggsidklRKEIERLEWRQQTE--------VLSPEEEKEL-----VEK-IKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 495 LFRRYENLKGVLEGFKKNEEALKKCAQdylARVKQEEQRyQALKIHAEEkLDKANEEIAQVRTKA---KAESAALHAGLR 571
Cdd:COG1340 145 LEKELEKAKKALEKNEKLKELRAELKE---LRKEAEEIH-KKIKELAEE-AQELHEEMIELYKEAdelRKEADELHKEIV 219
|
170 180 190
....*....|....*....|....*....|....*..
gi 1209185290 572 KEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 608
Cdd:COG1340 220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
430-596 |
7.47e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 430 KKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTS-QKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEG 508
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKlQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 509 FKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKN 588
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
....*...
gi 1209185290 589 QEIEELTK 596
Cdd:COG4372 164 EELAALEQ 171
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
425-581 |
8.11e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 425 EANEWKKKYEET----RQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTME-KEQALADLNSVERSLS-DLFRR 498
Cdd:pfam04012 12 NIHEGLDKAEDPekmlEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKlEEKAQAALTKGNEELArEALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 499 YENLKGVLEGFKKN-------EEALKKCAQDYLARVKQEEQRYQALKihAEEKLDKANEEIAQVRTKAKAESAAlhAGLR 571
Cdd:pfam04012 92 KKSLEKQAEALETQlaqqrsaVEQLRKQLAALETKIQQLKAKKNLLK--ARLKAAKAQEAVQTSLGSLSTSSAT--DSFE 167
|
170
....*....|
gi 1209185290 572 KEQMKVESLE 581
Cdd:pfam04012 168 RIEEKIEERE 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
406-593 |
8.48e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 406 SDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQM---IDEQRTSMTSQKSFQQLTMEKEQAL 482
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeIEERREELGERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 483 ADLNSVErSLSDLFRRYENLKGVLEGfkkneealkkcAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTK---- 558
Cdd:COG3883 106 DVLLGSE-SFSDFLDRLSALSKIADA-----------DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkael 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1209185290 559 --AKAESAALHAGLRKEQMKVESLERALQQKNQEIEE 593
Cdd:COG3883 174 eaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
500-604 |
1.47e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 500 ENLKGVLEGFKKNEEALKKcaqDYLARVKQEEQRyqaLKIHAEEKLDKANEEIAQVRTKAKAESAAL---HAGLRKEQMK 576
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK---EALLEAKEEIHK---LRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111
|
90 100
....*....|....*....|....*...
gi 1209185290 577 VESLERALQQKNQEIEELTKICDELIAK 604
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEE 139
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
406-574 |
2.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 406 SDKTAVLTLIREEIITKEI-EANEWKKKYEETRQEVLEMRKIVAEYEKTIAQmIDEQRTSMTSQKSFQQLTMEKEQALAD 484
Cdd:COG4717 62 QGRKPELNLKELKELEEELkEAEEKEEEYAELQEELEELEEELEELEAELEE-LREELEKLEKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 485 LNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQD-----------YLARVKQEEQRYQAL---KIHAEEKLDKANE 550
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEEleelleqlslaTEEELQDLAEELEELqqrLAELEEELEEAQE 220
|
170 180
....*....|....*....|....
gi 1209185290 551 EIAQVRTKAKAESAALHAGLRKEQ 574
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEER 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
417-607 |
2.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 417 EEIITKEIEANewKKKYEETRQEVLEMRKivaeyektiaqmidEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLF 496
Cdd:PRK03918 513 KKYNLEELEKK--AEEYEKLKEKLIKLKG--------------EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 497 RRYENLKgvLEGFKKNEEALKKCAQDY-----LARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAAL----- 566
Cdd:PRK03918 577 KELEELG--FESVEELEERLKELEPFYneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELeelek 654
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1209185290 567 ------HAGLRKEQMKvesLERALQQKNQEIEELTKICDELIAKLGK 607
Cdd:PRK03918 655 kyseeeYEELREEYLE---LSRELAGLRAELEELEKRREEIKKTLEK 698
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
472-605 |
2.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 472 QQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQR---------YQAL----- 537
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALqkeie 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1209185290 538 -----KIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKL 605
Cdd:COG1579 100 slkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
416-608 |
4.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 416 REEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQqltmEKEQALADLNSVERSLSD- 494
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELE----EVLREINEISSELPELREe 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 495 ------LFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEkLDKANEEIAQVRTKAKA--ESAAL 566
Cdd:PRK03918 223 leklekEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAEEyiKLSEF 301
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1209185290 567 HAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKT 608
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
422-566 |
4.46e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 422 KEIEAN-EWKKKYEETRQEVLEMRKIVAEYEKTIAQmideqrtsmtsqksfqqltmeKEQALadlnsvERSLSDLFRRYE 500
Cdd:PRK12704 58 ALLEAKeEIHKLRNEFEKELRERRNELQKLEKRLLQ---------------------KEENL------DRKLELLEKREE 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1209185290 501 NLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQAL-KIHAEEkldkANEEI-AQVRTKAKAESAAL 566
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsGLTAEE----AKEILlEKVEEEARHEAAVL 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-601 |
5.26e-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: 40.04 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 414 LIREEIITKEIEANewKKKYEETRQEVLEMRKIVAEYEKTiaqmideQRTSMTsqKSFQQLTMEKEQALADLNSVERSLS 493
Cdd:TIGR02168 188 LDRLEDILNELERQ--LKSLERQAEKAERYKELKAELREL-------ELALLV--LRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 494 DLFRRYENLKGVLEGFKKNEEALKKCAQDY----------LARVKQEEQRYQALKIHAEEKLDKANEEIAQV---RTKAK 560
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELqkelyalaneISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELA 336
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1209185290 561 AESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDEL 601
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
423-607 |
7.47e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 38.10 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 423 EIEANEWKKKYEETRQEVL-EMRKIVAEYEKTIAQMIDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFR---- 497
Cdd:pfam15665 13 EAEIQALKEAHEEEIQQILaETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEERELkaea 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 498 ----RYENL-KGVLEGFKKNEEALKKCAQdylARVKQEEQRYQALkihaEEKLDKANEEIAQVRTKAKaesaALHAGLRK 572
Cdd:pfam15665 93 ehrqRVVELsREVEEAKRAFEEKLESFEQ---LQAQFEQEKRKAL----EELRAKHRQEIQELLTTQR----AQSASSLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1209185290 573 EQMKVESLERA-LQQKNQEIEELT----KICDELIAKLGK 607
Cdd:pfam15665 162 EQEKLEELHKAeLESLRKEVEDLRkekkKLAEEYEQKLSK 201
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
395-607 |
7.65e-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: 39.28 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 395 ESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAqmideqrtsmtsqksfqql 474
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE------------------- 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 475 tmEKEQALADLnsvERSLSDLFRRYENLKGVLEGFKKNEEALKkcaqdylARVKQEEQRYQALKihaeEKLDKANEEIAQ 554
Cdd:TIGR02169 872 --ELEAALRDL---ESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELK----AKLEALEEELSE 935
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1209185290 555 VRTKAKA--ESAALHAGLRKEQMKVESLERALQQKN-------QEIEELTKICDELIAKLGK 607
Cdd:TIGR02169 936 IEDPKGEdeEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAK 997
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
475-605 |
7.94e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1209185290 475 TMEKEQ-ALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKI---HAEEKLDKANE 550
Cdd:COG1579 1 AMPEDLrALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELeieEVEARIKKYEE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1209185290 551 EIAQVRTkAKAESAALH--AGLRKEQmkvESLERALQQKNQEIEELTKICDELIAKL 605
Cdd:COG1579 81 QLGNVRN-NKEYEALQKeiESLKRRI---SDLEDEILELMERIEELEEELAELEAEL 133
|
|
|