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Conserved domains on  [gi|2010957999|emb|CAF0839615|]
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unnamed protein product [Rotaria sordida]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 24-164 2.92e-25

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


:

Pssm-ID: 366555  Cd Length: 136  Bit Score: 102.41  E-value: 2.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999   24 FIKKPQVILRVVAWVLSIIVFACIAQEGYAddqcRYNGSNACGYGIGIGVIAFILTMVFTGLDIYFpniSNVKTRKTVVL 103
Cdd:pfam01284    1 FLLTPLGILRILQLVFAIIVLGLIASLIAY----AGSYPSAVNFAVFVAVFSFLIALFFLLLYLFG---YSYFPSIAWPL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010957999  104 SELAISGFLVFLWFIGFCYMTDQWRKEPDKNKDGWDGR--NSVQSAIAFSFFSIFVWAGLTFF 164
Cdd:pfam01284   74 IDLIFDALAALFWLAAFIALAAALRGHSENQGSGDLTRrcRAAQAAIAFGFFAWLLFLASAVL 136
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 842-958 8.09e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 8.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  842 RLHDHIKQLRQSLKTSDEENNSLKR-------QLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLD 914
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAelqeleeKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2010957999  915 RQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 535-953 2.64e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  535 KLLSNQDKI----KENLNFSSKTKVDDssETDSVSENEFNLSKEKIKDNLKPQSDQSI-----DEDLDDLNNHLKQaLNH 605
Cdd:TIGR04523   90 KLKKNKDKInklnSDLSKINSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKFLTeikkkEKELEKLNNKYND-LKK 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  606 KDQPYRTATDILLQRLSNQQT--DNITNQYKNKSHHiqhddyiqskthdiwLSMLEKLEQEHKQrLEKQQKQYEEymfhl 683
Cdd:TIGR04523  167 QKEELENELNLLEKEKLNIQKniDKIKNKLLKLELL---------------LSNLKKKIQKNKS-LESQISELKK----- 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  684 eenmkrrldQYLSSTNSVQKSKSDISNQSFHEHDTHSSppidsnetihrsysnsnqyrpLVDQINKHNYPTNHLltSNTQ 763
Cdd:TIGR04523  226 ---------QNNQLKDNIEKKQQEINEKTTEISNTQTQ---------------------LNQLKDEQNKIKKQL--SEKQ 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  764 QQPIQTNISRSQSREDISNLRNELSTKHAKHVSDLKLYYEHEIDELKNQLNISRmghpnsSTTRQSIETIERINNEnirl 843
Cdd:TIGR04523  274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ------NQISQNNKIISQLNEQ---- 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  844 hdhIKQLRQSLKTSDEENNSLKRQLEE-------LRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQ 916
Cdd:TIGR04523  344 ---ISQLKKELTNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2010957999  917 SLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHK 953
Cdd:TIGR04523  421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
 
Name Accession Description Interval E-value
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 24-164 2.92e-25

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


Pssm-ID: 366555  Cd Length: 136  Bit Score: 102.41  E-value: 2.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999   24 FIKKPQVILRVVAWVLSIIVFACIAQEGYAddqcRYNGSNACGYGIGIGVIAFILTMVFTGLDIYFpniSNVKTRKTVVL 103
Cdd:pfam01284    1 FLLTPLGILRILQLVFAIIVLGLIASLIAY----AGSYPSAVNFAVFVAVFSFLIALFFLLLYLFG---YSYFPSIAWPL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010957999  104 SELAISGFLVFLWFIGFCYMTDQWRKEPDKNKDGWDGR--NSVQSAIAFSFFSIFVWAGLTFF 164
Cdd:pfam01284   74 IDLIFDALAALFWLAAFIALAAALRGHSENQGSGDLTRrcRAAQAAIAFGFFAWLLFLASAVL 136
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 842-958 8.09e-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: 8.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  842 RLHDHIKQLRQSLKTSDEENNSLKR-------QLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLD 914
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAelqeleeKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2010957999  915 RQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 535-953 2.64e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  535 KLLSNQDKI----KENLNFSSKTKVDDssETDSVSENEFNLSKEKIKDNLKPQSDQSI-----DEDLDDLNNHLKQaLNH 605
Cdd:TIGR04523   90 KLKKNKDKInklnSDLSKINSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKFLTeikkkEKELEKLNNKYND-LKK 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  606 KDQPYRTATDILLQRLSNQQT--DNITNQYKNKSHHiqhddyiqskthdiwLSMLEKLEQEHKQrLEKQQKQYEEymfhl 683
Cdd:TIGR04523  167 QKEELENELNLLEKEKLNIQKniDKIKNKLLKLELL---------------LSNLKKKIQKNKS-LESQISELKK----- 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  684 eenmkrrldQYLSSTNSVQKSKSDISNQSFHEHDTHSSppidsnetihrsysnsnqyrpLVDQINKHNYPTNHLltSNTQ 763
Cdd:TIGR04523  226 ---------QNNQLKDNIEKKQQEINEKTTEISNTQTQ---------------------LNQLKDEQNKIKKQL--SEKQ 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  764 QQPIQTNISRSQSREDISNLRNELSTKHAKHVSDLKLYYEHEIDELKNQLNISRmghpnsSTTRQSIETIERINNEnirl 843
Cdd:TIGR04523  274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ------NQISQNNKIISQLNEQ---- 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  844 hdhIKQLRQSLKTSDEENNSLKRQLEE-------LRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQ 916
Cdd:TIGR04523  344 ---ISQLKKELTNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2010957999  917 SLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHK 953
Cdd:TIGR04523  421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
805-976 1.30e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  805 EIDELKNQLNISRMGHPNSSTTRQSIET-IERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGqinnkdvEIK 883
Cdd:COG4372     39 ELDKLQEELEQLREELEQAREELEQLEEeLEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE-------EAE 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  884 NSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQTFTNE 963
Cdd:COG4372    112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191

                          170
                   ....*....|...
gi 2010957999  964 NNNQRINHDTNYN 976
Cdd:COG4372    192 ANRNAEKEEELAE 204
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 757-958 2.09e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.02  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  757 LLTSNTQQQpiqtniSRSQSREDISNLRNEL---STKHAKHVSDLKLYYEHEIDELKNQLNISRMGHPNSSTTRQSIEti 833
Cdd:pfam01576  312 LDTTAAQQE------LRSKREQEVTELKKALeeeTRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALE-- 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  834 erinNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYL 913
Cdd:pfam01576  384 ----SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL 459

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2010957999  914 ------------DRQSLFYQEEYQKV---TR------DLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:pfam01576  460 skdvsslesqlqDTQELLQEETRQKLnlsTRlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
830-951 3.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  830 IETIERINNENIRLHDHIKQLR------QSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNE----I 899
Cdd:PRK03918   203 EEVLREINEISSELPELREELEklekevKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEleekV 282

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2010957999  900 RHIKDQQNEKYVYLdRQSLFYqEEYQKVTRDLiltRERLARLEESYRQLENQ 951
Cdd:PRK03918   283 KELKELKEKAEEYI-KLSEFY-EEYLDELREI---EKRLSRLEEEINGIEER 329
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 659-968 1.09e-03

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: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  659 EKLEQEHKQRLEKQQKQYEEYMFHLEENMKRRLDQYLSSTNSVQKSkSDISNQSFHEHDTHSSPPIDSNETIHRSYSNSN 738
Cdd:COG5185    207 IKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-DKLEKLVEQNTDLRLEKLGENAESSKRLNENAN 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  739 QYRPLVdqinkhnyptnhlltSNTQQQpIQTNISRSQSREDISNLRNELSTKHA-KHVSDLKLYYEHEIDELKNQLNIS- 816
Cdd:COG5185    286 NLIKQF---------------ENTKEK-IAEYTKSIDIKKATESLEEQLAAAEAeQELEESKRETETGIQNLTAEIEQGq 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  817 -------------RMGHPNSSTTRQSIETIERINNENIRLHDHIKQLRQSLKTSDEENNS--------LKRQLEELRGQI 875
Cdd:COG5185    350 esltenleaikeeIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAtledtlkaADRQIEELQRQI 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  876 NNKDVEIKNSHKKLNEIEQELNEIRHIKDqqnekyvylDRQSLFYQEEYQKVTRDLiltRERLARLEESYRQLENQHKTC 955
Cdd:COG5185    430 EQATSSNEEVSKLLNELISELNKVMREAD---------EESQSRLEEAYDEINRSV---RSKKEDLNEELTQIESRVSTL 497

                          330
                   ....*....|...
gi 2010957999  956 RQQTFTNENNNQR 968
Cdd:COG5185    498 KATLEKLRAKLER 510
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 657-705 4.40e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 4.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2010957999  657 MLEKLEQEHKQRLEKQQKQYEEYMFHLEENMKRRLDQYLSSTNSVQKSK 705
Cdd:cd16269    216 LLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESK 264
 
Name Accession Description Interval E-value
MARVEL pfam01284
Membrane-associating domain; MARVEL domain-containing proteins are often found in ...
 24-164 2.92e-25

Membrane-associating domain; MARVEL domain-containing proteins are often found in lipid-associating proteins - such as Occludin and MAL family proteins. It may be part of the machinery of membrane apposition events, such as transport vesicle biogenesis.


Pssm-ID: 366555  Cd Length: 136  Bit Score: 102.41  E-value: 2.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999   24 FIKKPQVILRVVAWVLSIIVFACIAQEGYAddqcRYNGSNACGYGIGIGVIAFILTMVFTGLDIYFpniSNVKTRKTVVL 103
Cdd:pfam01284    1 FLLTPLGILRILQLVFAIIVLGLIASLIAY----AGSYPSAVNFAVFVAVFSFLIALFFLLLYLFG---YSYFPSIAWPL 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010957999  104 SELAISGFLVFLWFIGFCYMTDQWRKEPDKNKDGWDGR--NSVQSAIAFSFFSIFVWAGLTFF 164
Cdd:pfam01284   74 IDLIFDALAALFWLAAFIALAAALRGHSENQGSGDLTRrcRAAQAAIAFGFFAWLLFLASAVL 136
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 842-958 8.09e-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: 8.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  842 RLHDHIKQLRQSLKTSDEENNSLKR-------QLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLD 914
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAelqeleeKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2010957999  915 RQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 535-953 2.64e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  535 KLLSNQDKI----KENLNFSSKTKVDDssETDSVSENEFNLSKEKIKDNLKPQSDQSI-----DEDLDDLNNHLKQaLNH 605
Cdd:TIGR04523   90 KLKKNKDKInklnSDLSKINSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKFLTeikkkEKELEKLNNKYND-LKK 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  606 KDQPYRTATDILLQRLSNQQT--DNITNQYKNKSHHiqhddyiqskthdiwLSMLEKLEQEHKQrLEKQQKQYEEymfhl 683
Cdd:TIGR04523  167 QKEELENELNLLEKEKLNIQKniDKIKNKLLKLELL---------------LSNLKKKIQKNKS-LESQISELKK----- 225

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  684 eenmkrrldQYLSSTNSVQKSKSDISNQSFHEHDTHSSppidsnetihrsysnsnqyrpLVDQINKHNYPTNHLltSNTQ 763
Cdd:TIGR04523  226 ---------QNNQLKDNIEKKQQEINEKTTEISNTQTQ---------------------LNQLKDEQNKIKKQL--SEKQ 273

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  764 QQPIQTNISRSQSREDISNLRNELSTKHAKHVSDLKLYYEHEIDELKNQLNISRmghpnsSTTRQSIETIERINNEnirl 843
Cdd:TIGR04523  274 KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ------NQISQNNKIISQLNEQ---- 343

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  844 hdhIKQLRQSLKTSDEENNSLKRQLEE-------LRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQ 916
Cdd:TIGR04523  344 ---ISQLKKELTNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQE 420

                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 2010957999  917 SLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHK 953
Cdd:TIGR04523  421 KELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 841-958 1.08e-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: 50.06  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  841 IRLHDHIKQLRQSLKTSDEEnnSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVylDRQSLFY 920
Cdd:TIGR02168  216 KELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE--ELQKELY 291

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2010957999  921 --QEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:TIGR02168  292 alANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
805-976 1.30e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  805 EIDELKNQLNISRMGHPNSSTTRQSIET-IERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGqinnkdvEIK 883
Cdd:COG4372     39 ELDKLQEELEQLREELEQAREELEQLEEeLEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE-------EAE 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  884 NSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQTFTNE 963
Cdd:COG4372    112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191

                          170
                   ....*....|...
gi 2010957999  964 NNNQRINHDTNYN 976
Cdd:COG4372    192 ANRNAEKEEELAE 204
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
805-958 1.46e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  805 EIDELKNQLNISRmghpnsSTTRQSIETIERINneniRLHDHIKQLRQSLKTSDEENNSLKRQL---------EELRGQI 875
Cdd:COG4717     72 ELKELEEELKEAE------EKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAEL 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  876 NNKDVEIKNSHKKLNEIEQELNEIRHIKDQ----QNEKYVYLDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQ 951
Cdd:COG4717    142 AELPERLEELEERLEELRELEEELEELEAElaelQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221


                   ....*..
gi 2010957999  952 HKTCRQQ 958
Cdd:COG4717    222 LEELEEE 228
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 757-958 2.09e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 49.02  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  757 LLTSNTQQQpiqtniSRSQSREDISNLRNEL---STKHAKHVSDLKLYYEHEIDELKNQLNISRMGHPNSSTTRQSIEti 833
Cdd:pfam01576  312 LDTTAAQQE------LRSKREQEVTELKKALeeeTRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALE-- 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  834 erinNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYL 913
Cdd:pfam01576  384 ----SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL 459

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2010957999  914 ------------DRQSLFYQEEYQKV---TR------DLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:pfam01576  460 skdvsslesqlqDTQELLQEETRQKLnlsTRlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
803-952 2.85e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  803 EHEIDELKNQLnisrmghpnsSTTRQSIETIERINnENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINnkdvEI 882
Cdd:COG4717    101 EEELEELEAEL----------EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEELEERLEELRELEE----EL 165

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010957999  883 KNSHKKLNEIEQELNEIRHIKDQQNEKYVY---LDRQSLfyQEEYQKVTRDLILTRERLARLEESYRQLENQH 952
Cdd:COG4717    166 EELEAELAELQEELEELLEQLSLATEEELQdlaEELEEL--QQRLAELEEELEEAQEELEELEEELEQLENEL 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 833-958 3.25e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  833 IERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVY 912
Cdd:COG1196    234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2010957999  913 LDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 804-953 4.17e-05

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: 48.14  E-value: 4.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  804 HEIDELKNQLNisrmghpnssTTRQSIETIERinnenirlhdHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIK 883
Cdd:TIGR02169  681 ERLEGLKRELS----------SLQSELRRIEN----------RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  884 NSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQEEYQKVTRDliLTRERLARLEESYRQLENQHK 953
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVS 808
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 831-931 7.22e-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: 46.68  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  831 ETIERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKy 910
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98

                           90       100
                   ....*....|....*....|.
gi 2010957999  911 vyLDRQslfyQEEYQKVTRDL 931
Cdd:COG4942     99 --LEAQ----KEELAELLRAL 113
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 828-953 8.84e-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: 45.30  E-value: 8.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  828 QSIET-IERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQ 906
Cdd:COG1579     13 QELDSeLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2010957999  907 NekyvyLDRQsLFYQEEYQKVTRDLIL-TRERLARLEESYRQLENQHK 953
Cdd:COG1579     93 A-----LQKE-IESLKRRISDLEDEILeLMERIEELEEELAELEAELA 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 773-951 1.17e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  773 RSQSREDISNLRNELSTKHAKhvsdlklYYEH--EIDELKNQLNISRmghpnssttrqsiETIERINNENIRLHDHIKQL 850
Cdd:COG1196    269 LEELRLELEELELELEEAQAE-------EYELlaELARLEQDIARLE-------------ERRRELEERLEELEEELAEL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  851 RQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQEEYQKVTRD 930
Cdd:COG1196    329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                          170       180
                   ....*....|....*....|.
gi 2010957999  931 LILTRERLARLEESYRQLENQ 951
Cdd:COG1196    409 EEALLERLERLEEELEELEEA 429
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
847-958 1.25e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  847 IKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQEEYQK 926
Cdd:COG4372     26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2010957999  927 VTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:COG4372    106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
757-951 3.48e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  757 LLTSNTQQQPIQTNISRSQSREdiSNLRNEL----STKHAKHVSD-LKLY---------YEHEIDELKNQLNISRMGHPN 822
Cdd:COG3206     59 LLVEPQSSDVLLSGLSSLSASD--SPLETQIeilkSRPVLERVVDkLNLDedplgeeasREAAIERLRKNLTVEPVKGSN 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  823 ------SSTTRqsiETIERINNENIRLHdhikqLRQSLKTSDEENNS----LKRQLEELRgqinnkdveiknshKKLNEI 892
Cdd:COG3206    137 vieisyTSPDP---ELAAAVANALAEAY-----LEQNLELRREEARKalefLEEQLPELR--------------KELEEA 194

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2010957999  893 EQELNEIRhikdqQNEKYVYLDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQ 951
Cdd:COG3206    195 EAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
830-951 3.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 3.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  830 IETIERINNENIRLHDHIKQLR------QSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNE----I 899
Cdd:PRK03918   203 EEVLREINEISSELPELREELEklekevKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEleekV 282

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2010957999  900 RHIKDQQNEKYVYLdRQSLFYqEEYQKVTRDLiltRERLARLEESYRQLENQ 951
Cdd:PRK03918   283 KELKELKEKAEEYI-KLSEFY-EEYLDELREI---EKRLSRLEEEINGIEER 329
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 771-949 3.90e-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: 44.67  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  771 ISRSQSREDISNLRNELSTKHAKHVSDLKLYYEhEIDELKNQLNisrmghpnssttrqsietieRINNENIRLHDHIKQL 850
Cdd:TIGR02169  360 AELKEELEDLRAELEEVDKEFAETRDELKDYRE-KLEKLKREIN--------------------ELKRELDRLQEELQRL 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  851 RQSLKtsdeennSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLdrqslfyQEEYQKVTRD 930
Cdd:TIGR02169  419 SEELA-------DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKE 484

                          170
                   ....*....|....*....
gi 2010957999  931 LILTRERLARLEESYRQLE 949
Cdd:TIGR02169  485 LSKLQRELAEAEAQARASE 503
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
823-970 4.09e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  823 SSTTRQSIETIERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRH- 901
Cdd:COG4372     30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEe 109

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2010957999  902 -------IKDQQNEkYVYLDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQ--QTFTNENNNQRIN 970
Cdd:COG4372    110 aeelqeeLEELQKE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQALD 186
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
779-954 4.41e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  779 DISNLRNELstKHAKHVSDLKLYYEHEIDELKNQLN-----ISRMGHPNSSTTRQSIETIERINNENIRLHDHIKQLRQS 853
Cdd:PRK03918   540 EIKSLKKEL--EKLEELKKKLAELEKKLDELEEELAellkeLEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE 617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  854 LKtsdeENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEirhikdqqnekyvyldrqslfyqEEYQKVTRDLIL 933
Cdd:PRK03918   618 EK----ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-----------------------EEYEELREEYLE 670

                          170       180
                   ....*....|....*....|.
gi 2010957999  934 TRERLARLEESYRQLENQHKT 954
Cdd:PRK03918   671 LSRELAGLRAELEELEKRREE 691
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 846-951 4.65e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  846 HIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEirhikdQQNEKYVyldrqslfYQEEYQ 925
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE------AQAEEYE--------LLAELA 298

                           90       100
                   ....*....|....*....|....*.
gi 2010957999  926 KVTRDLILTRERLARLEESYRQLENQ 951
Cdd:COG1196    299 RLEQDIARLEERRRELEERLEELEEE 324
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 805-968 5.01e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 5.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  805 EIDELKNQLNisrmghpnssTTRQSIET----IERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDV 880
Cdd:COG4942     21 AAAEAEAELE----------QLQQEIAElekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  881 EIKNSHKKLNEIEQELNEiRHIKDQQNEKYVYLdrQSLFYQEEYQKVTRDLILT--------------RERLARLEESYR 946
Cdd:COG4942     91 EIAELRAELEAQKEELAE-LLRALYRLGRQPPL--ALLLSPEDFLDAVRRLQYLkylaparreqaeelRADLAELAALRA 167

                          170       180
                   ....*....|....*....|..
gi 2010957999  947 QLENQHKtcRQQTFTNENNNQR 968
Cdd:COG4942    168 ELEAERA--ELEALLAELEEER 187
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 775-954 6.37e-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: 43.90  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  775 QSREDISNLRNELSTKHA--KHVSDLKLYYEHEIDELKNQLN-----ISRMGHPNSSTTRQSIET--------IERINNE 839
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSelKELEARIEELEEDLHKLEEALNdlearLSHSRIPEIQAELSKLEEevsriearLREIEQK 820

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  840 NIRLHDHIKQLRQSLKTSDEEN-------NSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVY 912
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRidlkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2010957999  913 LdrqslfyQEEYQKVTRDLILTRERLARLEESYRQLENQHKT 954
Cdd:TIGR02169  901 L-------ERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 763-943 6.87e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 44.04  E-value: 6.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  763 QQQPIQTN--ISRSQSREDISNLrnELSTKHAKhvsdlklYYEHEIDELKNQLNisrmghpNSSTTRQSIET-IERINNE 839
Cdd:pfam10174  255 EVQMLKTNglLHTEDREEEIKQM--EVYKSHSK-------FMKNKIDQLKQELS-------KKESELLALQTkLETLTNQ 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  840 NIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQE----LNEIRHIKDQQNEKyvylDR 915
Cdd:pfam10174  319 NSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEkstlAGEIRDLKDMLDVK----ER 394

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2010957999  916 QSLFYQ---EEYQKVTRD----LILTRERLARLEE 943
Cdd:pfam10174  395 KINVLQkkiENLQEQLRDkdkqLAGLKERVKSLQT 429
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 777-913 7.53e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 42.79  E-value: 7.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  777 REDISNLRNELSTkHAKHVSDLKLYYEHEID---------ELKNQLnisrmghpnsstTRQSIETIERINnENIRLHDHI 847
Cdd:COG4026     72 RELAEKFFEELKG-MVGHVERMKLPLGHDVEyvdvelvrkEIKNAI------------IRAGLKSLQNIP-EYNELREEL 137

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2010957999  848 KQLRQSLKTSDEENNSLKRQLEELRGqinnkdvEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYL 913
Cdd:COG4026    138 LELKEKIDEIAKEKEKLTKENEELES-------ELEELREEYKKLREENSILEEEFDNIKSEYSDL 196
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
824-954 8.06e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 8.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  824 STTRQSIETIERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIK 903
Cdd:COG1340      1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2010957999  904 DQQNEKYvyldrQSLFYQ-EEYQKVTRDLILTRERLARLEESYRQLENQHKT 954
Cdd:COG1340     81 DELNEKL-----NELREElDELRKELAELNKAGGSIDKLRKEIERLEWRQQT 127
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
824-958 8.13e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 8.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  824 STTRQSIETI--ERINNENIRLH-----------DHIKQLRQSLKTSDEEN---NSLKRQLEELRGQINNKDVEIKnshk 887
Cdd:COG4717     37 STLLAFIRAMllERLEKEADELFkpqgrkpelnlKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELE---- 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010957999  888 klnEIEQELNEIRHIKDQQN--EKYVYLDRQSLFYQEEYQKVTRDLiltrERLARLEESYRQLENQHKTCRQQ 958
Cdd:COG4717    113 ---ELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEE 178
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 659-968 1.09e-03

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: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  659 EKLEQEHKQRLEKQQKQYEEYMFHLEENMKRRLDQYLSSTNSVQKSkSDISNQSFHEHDTHSSPPIDSNETIHRSYSNSN 738
Cdd:COG5185    207 IKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTS-DKLEKLVEQNTDLRLEKLGENAESSKRLNENAN 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  739 QYRPLVdqinkhnyptnhlltSNTQQQpIQTNISRSQSREDISNLRNELSTKHA-KHVSDLKLYYEHEIDELKNQLNIS- 816
Cdd:COG5185    286 NLIKQF---------------ENTKEK-IAEYTKSIDIKKATESLEEQLAAAEAeQELEESKRETETGIQNLTAEIEQGq 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  817 -------------RMGHPNSSTTRQSIETIERINNENIRLHDHIKQLRQSLKTSDEENNS--------LKRQLEELRGQI 875
Cdd:COG5185    350 esltenleaikeeIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAtledtlkaADRQIEELQRQI 429

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  876 NNKDVEIKNSHKKLNEIEQELNEIRHIKDqqnekyvylDRQSLFYQEEYQKVTRDLiltRERLARLEESYRQLENQHKTC 955
Cdd:COG5185    430 EQATSSNEEVSKLLNELISELNKVMREAD---------EESQSRLEEAYDEINRSV---RSKKEDLNEELTQIESRVSTL 497

                          330
                   ....*....|...
gi 2010957999  956 RQQTFTNENNNQR 968
Cdd:COG5185    498 KATLEKLRAKLER 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 728-968 1.11e-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: 43.12  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  728 ETIHRSYSNSNQYRPLVDQIN--KHNYPTNHLLTSNTQQQPIQTNISRSQSREDisNLRNELSTKHAKhVSDLKLYYeHE 805
Cdd:TIGR02168  203 KSLERQAEKAERYKELKAELRelELALLVLRLEELREELEELQEELKEAEEELE--ELTAELQELEEK-LEELRLEV-SE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  806 IDELKNQLNisrmghpnsSTTRQSIETIERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNS 885
Cdd:TIGR02168  279 LEEEIEELQ---------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  886 HKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQTFTNENN 965
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429


                   ...
gi 2010957999  966 NQR 968
Cdd:TIGR02168  430 LEE 432
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 775-970 1.14e-03

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: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  775 QSREDISNLRNELSTKHAKHVSDLKLYYEHEIDELKNQLNISRMGHPNSSTTRQSIET-----IERINNENIRLHDHIKQ 849
Cdd:TIGR00618  304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHevatsIREISCQQHTLTQHIHT 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  850 LRQSLKTSDEENNSLKRQLEELRGQINNKDVEiknsHKKLNEIEQELneiRHIKDQQNEKYVYLDRQSLFYQEEYQKVTR 929
Cdd:TIGR00618  384 LQQQKTTLTQKLQSLCKELDILQREQATIDTR----TSAFRDLQGQL---AHAKKQQELQQRYAELCAAAITCTAQCEKL 456

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2010957999  930 DLILTRERLARLEESYRQLENQHKTCRQQTFTNENNNQRIN 970
Cdd:TIGR00618  457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 859-958 1.41e-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: 42.44  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  859 EENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEirhikdqqnekyvyLDRQSLFYQEEYQKVTRDLILTRERL 938
Cdd:COG4942     20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--------------LERRIAALARRIRALEQELAALEAEL 85

                           90       100
                   ....*....|....*....|
gi 2010957999  939 ARLEESYRQLENQHKTCRQQ 958
Cdd:COG4942     86 AELEKEIAELRAELEAQKEE 105
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
755-949 1.67e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  755 NHLLTSNTQQQPIQTNISRSQSRedISNLRNELSTKHAKhvsdlklyyeheIDELKNQLNISRMGHPNSSTTRQSIETIE 834
Cdd:COG3206    205 NGLVDLSEEAKLLLQQLSELESQ--LAEARAELAEAEAR------------LAALRAQLGSGPDALPELLQSPVIQQLRA 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  835 RINNENIRLhdhiKQLRQSLKtsdeENN----SLKRQLEELRGQINNKDVEIKNS-HKKLNEIEQELNEIRHIKDQQNEK 909
Cdd:COG3206    271 QLAELEAEL----AELSARYT----PNHpdviALRAQIAALRAQLQQEAQRILASlEAELEALQAREASLQAQLAQLEAR 342

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2010957999  910 YVYLDRQslfyQEEYQKVTRDLILTRERLARLEESYRQLE 949
Cdd:COG3206    343 LAELPEL----EAELRRLEREVEVARELYESLLQRLEEAR 378
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
865-949 1.82e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  865 KRQLEELRGQINNKdvEIKNSHKKLNEIEQELNEIRHIKDQQNEkyvyldrqslfyQEEYQKVTRD---LIL-----TRE 936
Cdd:PRK02224   186 RGSLDQLKAQIEEK--EEKDLHERLNGLESELAELDEEIERYEE------------QREQARETRDeadEVLeeheeRRE 251

                           90
                   ....*....|...
gi 2010957999  937 RLARLEESYRQLE 949
Cdd:PRK02224   252 ELETLEAEIEDLR 264
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 659-958 2.06e-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: 42.36  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  659 EKLEQehKQRLEKQQKQYEEYMFHLEENMKRRLDQYLSSTNSVQKSKSDISNQ--SFHEHDTHSSPPIDSNEtihrsySN 736
Cdd:TIGR02169  195 EKRQQ--LERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQlaSLEEELEKLTEEISELE------KR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  737 SNQYRPLVDQINKHNYP--TNHLLTSNTQQQPIQTNISRSQSREDISNLRNE-LSTKHAKHVSDLKlYYEHEIDELKNQL 813
Cdd:TIGR02169  267 LEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEID-KLLAEIEELEREI 345

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  814 NISRMGHPNSSTTRQSIET--------IERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNS 885
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEeledlraeLEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010957999  886 HKKLNEIEQELNEIRHIKDQQNEKyVYLDRQSLfyqeeyQKVTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:TIGR02169  426 NAAIAGIEAKINELEEEKEDKALE-IKKQEWKL------EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 847-958 2.53e-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: 41.97  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  847 IKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNE-----IRHIKDQQN--EKYVYLDRQSLF 919
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlARLEAEVEQleERIAQLSKELTE 758

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2010957999  920 YQEEYQKVTRDLILTRERLAR-------LEESYRQLENQHKTCRQQ 958
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEaeaeieeLEAQIEQLKEELKALREA 804
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 763-958 2.69e-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: 41.97  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  763 QQQPIQTNISRSQSREDISNLRNElSTKHAKHVSDLklyyEHEIDELKNQLNISRmghpnssttrqsiETIERINNENIR 842
Cdd:TIGR02168  718 RKELEELSRQISALRKDLARLEAE-VEQLEERIAQL----SKELTELEAEIEELE-------------ERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  843 LHDHIKQLRQSLKTSDEENNSLKRQLEELRGQIN-------NKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYL-- 913
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaa 859

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2010957999  914 --------------DRQSLfyQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQ 958
Cdd:TIGR02168  860 eieeleelieelesELEAL--LNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 847-909 2.70e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 2.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2010957999  847 IKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEK 909
Cdd:COG3883     25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 760-948 2.85e-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: 41.97  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  760 SNTQQQPIQT-NISRSQSREDISNLRNELSTkHAKHVSDLKL----------YYEHEIDELKNQL-----NISRMGHPNS 823
Cdd:TIGR02168  784 IEELEAQIEQlKEELKALREALDELRAELTL-LNEEAANLRErleslerriaATERRLEDLEEQIeelseDIESLAAEIE 862

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  824 STT---RQSIETIERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQelnEIR 900
Cdd:TIGR02168  863 ELEeliEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV---RID 939

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2010957999  901 HIKDQQNEKYvyldrqSLFYQ---EEYQKVTRDLILTRERLARLEESYRQL 948
Cdd:TIGR02168  940 NLQERLSEEY------SLTLEeaeALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 793-970 3.13e-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: 41.97  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  793 KHVSDLKLYYEHEIDELKNQLNISRMGHPNSSTTRQSIET-IERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEEL 871
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeLESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  872 RGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLfyQEEYQKVTRDLILTRERLARLEESYRQLENQ 951
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL--QAELEELEEELEELQEELERLEEALEELREE 469

                          170
                   ....*....|....*....
gi 2010957999  952 HKTCRQQTFTNENNNQRIN 970
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQ 488
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 657-705 4.40e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.64  E-value: 4.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2010957999  657 MLEKLEQEHKQRLEKQQKQYEEYMFHLEENMKRRLDQYLSSTNSVQKSK 705
Cdd:cd16269    216 LLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESK 264
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 823-969 4.88e-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: 40.88  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  823 SSTTRQSIETIERinneNIRLHDHIKQLRqslKTSDEENNSLKRQLEELRGQINNKDVeiknSHKKLNEIEQELNEIRHI 902
Cdd:pfam05557   37 SALKRQLDRESDR----NQELQKRIRLLE---KREAEAEEALREQAELNRLKKKYLEA----LNKKLNEKESQLADAREV 105

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2010957999  903 KDQQNEKYVYLDRQSLFYQEEYQKVTRDLILTRERLARLEESYRQLENQHKTCRQQTFTNENNNQRI 969
Cdd:pfam05557  106 ISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI 172
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 518-909 5.34e-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: 40.77  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  518 ILSEIIDENHRTPNKQEKLLSNQDKIKENLNFSSKtkVDDSSETDSVSENEFNLSKEKIKD-NLKPQSDQSIDEDLDDLN 596
Cdd:TIGR04523  185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQ--ISELKKQNNQLKDNIEKKQQEINEkTTEISNTQTQLNQLKDEQ 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  597 NHLKQALNHKDQPYRTAtdillqrlsNQQTDNITNQYKNkshhiqhddyIQSKTHDIWLSMLEKLEQEHKQRLEKQQKQY 676
Cdd:TIGR04523  263 NKIKKQLSEKQKELEQN---------NKKIKELEKQLNQ----------LKSEISDLNNQKEQDWNKELKSELKNQEKKL 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  677 EEYMFHLEENMKR--RLDQYLSSTNSvQKSKSDISNQSFHEHDTHSSPPIDSNETIHRSYSNSNQyrPLVDQIN------ 748
Cdd:TIGR04523  324 EEIQNQISQNNKIisQLNEQISQLKK-ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK--NLESQINdleski 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  749 KHNYPTNHLLTSNTQQQPIQTNI----------SRSQSREDISNLRNELSTKHA--KHVSDLKLYYEHEIDELKNQLNIs 816
Cdd:TIGR04523  401 QNQEKLNQQKDEQIKKLQQEKELlekeierlkeTIIKNNSEIKDLTNQDSVKELiiKNLDNTRESLETQLKVLSRSINK- 479

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  817 rmghpNSSTTRQSIETIERINNENIRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQEL 896
Cdd:TIGR04523  480 -----IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL 554

                          410
                   ....*....|....*
gi 2010957999  897 N--EIRHIKDQQNEK 909
Cdd:TIGR04523  555 KkeNLEKEIDEKNKE 569
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
773-900 5.93e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  773 RSQSREDISNLRNELST--KHAKHVSDLKLYYEH--EIDELKNQLNIS----RMGHPNSSTTRQSIETIERINNENIRLH 844
Cdd:COG4717     97 LEELEEELEELEAELEElrEELEKLEKLLQLLPLyqELEALEAELAELperlEELEERLEELRELEEELEELEAELAELQ 176

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2010957999  845 DHIKQLRQSLKTSDEEN-NSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIR 900
Cdd:COG4717    177 EELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
766-872 6.04e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 6.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  766 PIQTNISRSQSREDISNLRNELSTKHAkHVSDLklyyEHEIDELKNQLNISRMghpNSSTTRQSIETIERINNENIRLHD 845
Cdd:COG2433    401 KEHEERELTEEEEEIRRLEEQVERLEA-EVEEL----EAELEEKDERIERLER---ELSEARSEERREIRKDREISRLDR 472

                           90       100
                   ....*....|....*....|....*..
gi 2010957999  846 HIKQLRQSLKTSDEENNSLKRQLEELR 872
Cdd:COG2433    473 EIERLERELEEERERIEELKRKLERLK 499
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
773-959 6.28e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 6.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  773 RSQSREDISNLRNELSTKHAKhvsdLKLYYEhEIDELKNQLNISRMGHPNSSTTRQSIETIER--------INNEN---- 840
Cdd:COG1340     66 RDELNEKVKELKEERDELNEK----LNELRE-ELDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlsPEEEKelve 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  841 ---------------IRLHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKdveiknsHKKLNEIEQELNEIRHIKDQ 905
Cdd:COG1340    141 kikelekelekakkaLEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQEL-------HEEMIELYKEADELRKEADE 213

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2010957999  906 QNEKYVyldrqslfyqeEYQKVTRDLiltRERLARLEESYRQLENQHKTCRQQT 959
Cdd:COG1340    214 LHKEIV-----------EAQEKADEL---HEEIIELQKELRELRKELKKLRKKQ 253
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 763-949 6.32e-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: 40.81  E-value: 6.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  763 QQQPIQTNISRSQSREDISNLRNELSTKHAkhvsdLKLYYEHEIDELKNQLNISRmghpnsSTTRQSIETIERINNENIR 842
Cdd:TIGR02168  690 EEKIAELEKALAELRKELEELEEELEQLRK-----ELEELSRQISALRKDLARLE------AEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  843 LHDHIKQLRQSLKTSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQE 922
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                          170       180
                   ....*....|....*....|....*..
gi 2010957999  923 EYQKVTRDLILTRERLARLEESYRQLE 949
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELE 865
mukB PRK04863
chromosome partition protein MukB;
773-971 7.21e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  773 RSQSREDISNLRNELSTKHAK---HVSDLKLYYEHEIDELKNQLNISRMGHPNSS--TTRQSIETIERinneniRLHDH- 846
Cdd:PRK04863   784 REKRIEQLRAEREELAERYATlsfDVQKLQRLHQAFSRFIGSHLAVAFEADPEAElrQLNRRRVELER------ALADHe 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  847 --IKQLRQSLKTSDEennsLKRQLEELRGQINNKDVEIKNshKKLNEIEQELNEIrhikdQQNEKYVyldRQslfYQEEY 924
Cdd:PRK04863   858 sqEQQQRSQLEQAKE----GLSALNRLLPRLNLLADETLA--DRVEEIREQLDEA-----EEAKRFV---QQ---HGNAL 920

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2010957999  925 QKVTRDLILTR---ERLARLEESYRQLENQHKTCRQQTFTNENNNQRINH 971
Cdd:PRK04863   921 AQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAH 970
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 778-958 8.93e-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: 40.43  E-value: 8.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  778 EDISNLRNELSTkhakhvsdlklyYEHEIDELKNQLNISRmghpnssttRQSIETIERINNENIRLhdhiKQLRQSLKTS 857
Cdd:TIGR02168  691 EKIAELEKALAE------------LRKELEELEEELEQLR---------KELEELSRQISALRKDL----ARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  858 DEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNEKYVYLDRQSLFYQEEYQkvtrdliLTRER 937
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT-------LLNEE 818

                          170       180
                   ....*....|....*....|.
gi 2010957999  938 LARLEESYRQLENQHKTCRQQ 958
Cdd:TIGR02168  819 AANLRERLESLERRIAATERR 839
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
792-949 9.25e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 9.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  792 AKHVSDL-KLYYEH---------EIDELKNQL-NISRMgHPNSSTTRQSIETIERIN------NENIRLHDHIKQLRQSL 854
Cdd:COG4913    203 FKPIGDLdDFVREYmleepdtfeAADALVEHFdDLERA-HEALEDAREQIELLEPIRelaeryAAARERLAELEYLRAAL 281

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2010957999  855 K--TSDEENNSLKRQLEELRGQINNKDVEIKNSHKKLNEIEQELNEIRHIKDQQNekyvyLDR-QSLfyQEEYQKVTRDL 931
Cdd:COG4913    282 RlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG-----GDRlEQL--EREIERLEREL 354

                          170
                   ....*....|....*...
gi 2010957999  932 ILTRERLARLEESYRQLE 949
Cdd:COG4913    355 EERERRRARLEALLAALG 372
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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