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Conserved domains on  [gi|1958798241|ref|XP_038938158|]
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angiomotin-like protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Smc and Angiomotin_C domain-containing protein( domain architecture ID 10573751)

Smc and Angiomotin_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 658-864 1.22e-110

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


:

Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 340.59  E-value: 1.22e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  658 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 737
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  738 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 817
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798241  818 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 864
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 489-747 2.02e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  489 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 568
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  569 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 648
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  649 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 728
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                          250
                   ....*....|....*....
gi 1958798241  729 RILALEADMTKWEQKYLEE 747
Cdd:COG1196    457 EEEALLELLAELLEEAALL 475
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 658-864 1.22e-110

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 340.59  E-value: 1.22e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  658 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 737
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  738 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 817
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798241  818 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 864
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 489-747 2.02e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  489 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 568
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  569 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 648
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  649 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 728
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                          250
                   ....*....|....*....
gi 1958798241  729 RILALEADMTKWEQKYLEE 747
Cdd:COG1196    457 EEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 483-828 4.43e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 4.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  483 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMrNKL 557
Cdd:TIGR02168  133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  558 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeshhmsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 637
Cdd:TIGR02168  206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  638 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLpEYNAP 717
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-AEELA 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  718 ALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERD------TTISNH-SRNGSYGEsSLEAHIWPE 790
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlelqiASLNNEiERLEARLE-RLEDRRERL 419

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1958798241  791 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 828
Cdd:TIGR02168  420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
510-678 5.97e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 5.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  510 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 589
Cdd:PRK03918   595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  590 HEDkaaeshhmsqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 669
Cdd:PRK03918   664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720


                   ....*....
gi 1958798241  670 TQLQSACEK 678
Cdd:PRK03918   721 ERVEELREK 729
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 556-818 1.09e-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: 49.67  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  556 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGhEDKAAESHHMSQnkeflkEKEKLEMELAAVRTASEDHRRHIEILD 635
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  636 QALSNAQARVIKLEEELRE----KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLeRELDALRTQQKHGNGQPVNL 711
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  712 PEYNAPALMELVREKE---ERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSY 778
Cdd:TIGR02168  833 IAATERRLEDLEEQIEelsEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958798241  779 GESSLEAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 818
Cdd:TIGR02168  913 LRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 520-692 1.59e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 46.97  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  520 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSReyegHEDKAAESH- 598
Cdd:cd07596     11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  599 HMSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 672
Cdd:cd07596     83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161

                          170       180
                   ....*....|....*....|
gi 1958798241  673 QSACEKRGQMERRLRTWLER 692
Cdd:cd07596    162 EEARKRYEEISERLKEELKR 181
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 517-701 3.80e-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: 47.86  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  517 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 592
Cdd:pfam01576  145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  593 KAAESHHMSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 672
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300

                          170       180
                   ....*....|....*....|....*....
gi 1958798241  673 QSAcekrgqmerrLRTWLERELDALRTQQ 701
Cdd:pfam01576  301 LEA----------LKTELEDTLDTTAAQQ 319
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
636-697 1.35e-04

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 44.17  E-value: 1.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798241  636 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 697
Cdd:COG3167     46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 658-864 1.22e-110

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 340.59  E-value: 1.22e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  658 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 737
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  738 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 817
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798241  818 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 864
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 489-747 2.02e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  489 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 568
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  569 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 648
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  649 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 728
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                          250
                   ....*....|....*....
gi 1958798241  729 RILALEADMTKWEQKYLEE 747
Cdd:COG1196    457 EEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 483-828 4.43e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 4.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  483 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMrNKL 557
Cdd:TIGR02168  133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  558 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeshhmsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 637
Cdd:TIGR02168  206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  638 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLpEYNAP 717
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-AEELA 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  718 ALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERD------TTISNH-SRNGSYGEsSLEAHIWPE 790
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlelqiASLNNEiERLEARLE-RLEDRRERL 419

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1958798241  791 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 828
Cdd:TIGR02168  420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 490-735 1.71e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  490 IVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNR 569
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  570 DLRDRLETANRQLSSREYEGHEDKAAESHH--MSQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIK 647
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRerLQQEIEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  648 LEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTwlerELDALRTQQKHGNGQPVNLpeynaPALMELVREKE 727
Cdd:TIGR02168  466 LREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL-----GVLSELISVDE 533


                   ....*...
gi 1958798241  728 ERILALEA 735
Cdd:TIGR02168  534 GYEAAIEA 541
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 486-747 2.16e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.54  E-value: 2.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  486 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 564
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  565 HDFNRDLRDRLETANRQLSSREYEghEDKAAEShhmSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQAR 644
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLE--KEYLEKE---IQELQ--EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  645 VIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GNGQPVNLPEYNAPAL 719
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLEDV 956

                          250       260
                   ....*....|....*....|....*...
gi 1958798241  720 MELVREKEERILALEADMTKWEQKYLEE 747
Cdd:TIGR02169  957 QAELQRVEEEIRALEPVNMLAIQEYEEV 984
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
517-701 2.42e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 2.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  517 DNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDrLETANRQLSSREyeghedkaAE 596
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEID-VASAEREIAELE--------AE 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  597 SHHMSQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 676
Cdd:COG4913    677 LERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958798241  677 EKR------GQMERRLRTWLERELDALRTQQ 701
Cdd:COG4913    752 EERfaaalgDAVERELRENLEERIDALRARL 782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 492-748 3.36e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 3.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  492 ERAQQmveiLTEENRVLHQELQgcydnADKLHKFEKELQSISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 571
Cdd:COG1196    213 ERYRE----LKEELKELEAELL-----LLKLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  572 RDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 651
Cdd:COG1196    280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  652 LREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEERIL 731
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---------------ALLERLERLEEELE 424

                          250
                   ....*....|....*..
gi 1958798241  732 ALEADMTKWEQKYLEES 748
Cdd:COG1196    425 ELEEALAELEEEEEEEE 441
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
499-690 1.22e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  499 EILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLvksttkresldKAMRNKLEGEIRRLHDF--NRDLRDRLE 576
Cdd:COG4717     67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREELEKLEKLlqLLPLYQELE 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  577 TANRQLSS--REYEGHEDKAAESHHMSQNKEFLKEK-EKLEMELA-AVRTASEDHRRHIEILDQALSNAQARVIKLEEEL 652
Cdd:COG4717    136 ALEAELAElpERLEELEERLEELRELEEELEELEAElAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958798241  653 REKQayvEKVEKLQQALTQLQSACEkRGQMERRLRTWL 690
Cdd:COG4717    216 EEAQ---EELEELEEELEQLENELE-AAALEERLKEAR 249
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
486-714 1.41e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  486 DAFAIVERAQQMVEilteenrvlH-QELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDkAMRNKL-----EG 559
Cdd:COG4913    219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  560 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAESHH-MSQNKefLKEKEKLEMELAAVRTASEDHRRHIEILDQ 636
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELErlEARLDALREELDELEAqIRGNG--GDRLEQLEREIERLERELEERERRRARLEA 366

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798241  637 ALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAC-EKRGQMERRLRTwLERELDALRTQQKHGNGQPVNLPEY 714
Cdd:COG4913    367 LLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALeEALAEAEAALRD-LRRELRELEAEIASLERRKSNIPAR 441
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 511-709 5.15e-07

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.85  E-value: 5.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  511 ELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 586
Cdd:COG1579     11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  587 YEG--HEDKAAEshhmsqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 663
Cdd:COG1579     91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958798241  664 KLQQALTQLQSACEK-RGQMERRLRTWLEReldaLRtqqKHGNGQPV 709
Cdd:COG1579    153 ELEAELEELEAEREElAAKIPPELLALYER----IR---KRKNGLAV 192
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
510-678 5.97e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 5.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  510 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 589
Cdd:PRK03918   595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  590 HEDkaaeshhmsqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 669
Cdd:PRK03918   664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720


                   ....*....
gi 1958798241  670 TQLQSACEK 678
Cdd:PRK03918   721 ERVEELREK 729
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 506-702 7.90e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 7.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  506 RVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSTTKResldKAMRNKLEGEIRRLHDFNRDLRDRLE-------TA 578
Cdd:TIGR02169  311 AEKERELE---DAEERLAKLEAEIDKLLAEIEELEREIEEE----RKRRDKLTEEYAELKEELEDLRAELEevdkefaET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  579 NRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAY 658
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958798241  659 VEKVEKLQQALTQLQSACEKRgqmerrlRTWLERELDALRTQQK 702
Cdd:TIGR02169  464 LSKYEQELYDLKEEYDRVEKE-------LSKLQRELAEAEAQAR 500
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
520-728 8.63e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 8.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  520 DKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEShh 599
Cdd:PRK03918   214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKEL-- 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  600 msqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 679
Cdd:PRK03918   286 -----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958798241  680 GQMERRLRTwLERELDALRTQQKhgngqpVNLPEYNAPALMELVREKEE 728
Cdd:PRK03918   361 HELYEEAKA-KKEELERLKKRLT------GLTPEKLEKELEELEKAKEE 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 556-818 1.09e-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: 49.67  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  556 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGhEDKAAESHHMSQnkeflkEKEKLEMELAAVRTASEDHRRHIEILD 635
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  636 QALSNAQARVIKLEEELRE----KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLeRELDALRTQQKHGNGQPVNL 711
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  712 PEYNAPALMELVREKE---ERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSY 778
Cdd:TIGR02168  833 IAATERRLEDLEEQIEelsEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958798241  779 GESSLEAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 818
Cdd:TIGR02168  913 LRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
525-747 1.56e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  525 FEKELQsisEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAESHH 599
Cdd:COG4717     47 LLERLE---KEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  600 MSQNKEFLKEKEKLEMELAAVrtasedhrrhieildqalsnaQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEK- 678
Cdd:COG4717    124 LLQLLPLYQELEALEAELAEL---------------------PERLEELEERLEELRELEEELEELEAELAELQEELEEl 182

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798241  679 ----RGQMERRLRTWLErELDALRTQQKHgngqpvnlpeynapaLMELVREKEERILALEADMTKWEQKYLEE 747
Cdd:COG4717    183 leqlSLATEEELQDLAE-ELEELQQRLAE---------------LEEELEEAQEELEELEEELEQLENELEAA 239
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 520-692 1.59e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 46.97  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  520 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSReyegHEDKAAESH- 598
Cdd:cd07596     11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  599 HMSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 672
Cdd:cd07596     83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161

                          170       180
                   ....*....|....*....|
gi 1958798241  673 QSACEKRGQMERRLRTWLER 692
Cdd:cd07596    162 EEARKRYEEISERLKEELKR 181
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
492-729 1.70e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  492 ERAQQMVEILTEENRVLHQelqgcYDNADKLHKFEKELQSISeaYESLVKSTTKRESLdKAMRNKLEGEIRRLH-DFNR- 569
Cdd:PRK03918   480 KELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN--LEELEKKAEEYEKL-KEKLIKLKGEIKSLKkELEKl 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  570 -DLRDRLETANRQLSSREyegheDKAAESHHMSQNKEFLKEKEkLEMELAAVRTASE------DHRRHIEILDQALSNAQ 642
Cdd:PRK03918   552 eELKKKLAELEKKLDELE-----EELAELLKELEELGFESVEE-LEERLKELEPFYNeylelkDAEKELEREEKELKKLE 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  643 ARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRtwLERELDALRTQQKHGNgqpvNLPEYNAPALMEL 722
Cdd:PRK03918   626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELE----KRREEIKKTLEKL 699


                   ....*..
gi 1958798241  723 VREKEER 729
Cdd:PRK03918   700 KEELEER 706
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
492-700 2.72e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  492 ERAQQMVEILTEENRVLHQELQgcydnadklhKFEKELQSISEAYeSLVKSTTKRESLDKAMRNkLEGEIRRLHDFNRDL 571
Cdd:COG3206    171 EEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKN-GLVDLSEEAKLLLQQLSE-LESQLAEARAELAEA 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  572 RDRLETANRQLSSREyegheDKAAESHHMSQNKEFLKEKEKLEMELAAVR-TASEDHRRHIEI---LDQALSNAQARVIK 647
Cdd:COG3206    239 EARLAALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAELAELSaRYTPNHPDVIALraqIAALRAQLQQEAQR 313

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958798241  648 LEEELR-EKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQ 700
Cdd:COG3206    314 ILASLEaELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVAREL 366
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 517-701 3.80e-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: 47.86  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  517 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 592
Cdd:pfam01576  145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  593 KAAESHHMSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 672
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300

                          170       180
                   ....*....|....*....|....*....
gi 1958798241  673 QSAcekrgqmerrLRTWLERELDALRTQQ 701
Cdd:pfam01576  301 LEA----------LKTELEDTLDTTAAQQ 319
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
526-665 3.81e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.55  E-value: 3.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  526 EKELQSISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKaaeshhMSQNK 604
Cdd:COG2433    387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR------SEERR 459

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798241  605 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 665
Cdd:COG2433    460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
526-752 4.91e-05

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 46.99  E-value: 4.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  526 EKELQSISEAYESLVKSTTKRESLDKAMRnklegEIRRLHDFNRDLRDRLETANRQlssreyEGHEDKAAESHHMSQNKE 605
Cdd:COG0497    154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAALQ------PGEEEELEEERRRLSNAE 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  606 FLKEkeklemelaAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK-RG 680
Cdd:COG0497    223 KLRE---------ALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElRR 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  681 QMER------RLRTWLEReLDALRT-QQKHGnGQPVNLPEYNAPALMEL--VREKEERILALEADMTKWEQKYLEE---- 747
Cdd:COG0497    287 YLDSlefdpeRLEEVEER-LALLRRlARKYG-VTVEELLAYAEELRAELaeLENSDERLEELEAELAEAEAELLEAaekl 364


                   ....*
gi 1958798241  748 STIRH 752
Cdd:COG0497    365 SAARK 369
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
489-748 6.30e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 6.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  489 AIVERAQQMVEILTEE---NRVLHQELQ-GCYDNADK-LHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEG---E 560
Cdd:PRK03918   129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  561 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAESHhmsqnkeflKEKEKLEMELAAvrtasedhrrhieiLDQALSN 640
Cdd:PRK03918   209 INEISSELPELREELEKLEKEV--KELEELKEEIEELE---------KELESLEGSKRK--------------LEEKIRE 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  641 AQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgngqpvnlpeyNAPALM 720
Cdd:PRK03918   264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEEEIN------------GIEERI 330

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958798241  721 ELVREKEERILALEADMTKWEQKY--LEES 748
Cdd:PRK03918   331 KELEEKEERLEELKKKLKELEKRLeeLEER 360
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
503-738 9.80e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 9.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  503 EENRVLHQELQGcyDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKamRNKLEGEIRRLHDFNRDLRDRLETAnrq 581
Cdd:PRK02224   226 EEQREQARETRD--EADEVLEEHEERREELETLEAEIEDLReTIAETERE--REELAEEVRDLRERLEELEEERDDL--- 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  582 LSSREYEGHEDKAAESHHmsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEildqalsNAQARVIKLEEELREKQayvEK 661
Cdd:PRK02224   299 LAEAGLDDADAEAVEARR----EELEDRDEELRDRLEECRVAAQAHNEEAE-------SLREDADDLEERAEELR---EE 364

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798241  662 VEKLQQALTQLQSACEKRgqmeRRLRTWLERELDALRtqqKHGNGQPVNLPeyNAPALMELVREKEERILALEADMT 738
Cdd:PRK02224   365 AAELESELEEAREAVEDR----REEIEELEEEIEELR---ERFGDAPVDLG--NAEDFLEELREERDELREREAELE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 483-752 9.85e-05

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: 9.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  483 LGPDAFAIVEraQQMV-EILT---EENRVLhqelqgcydnadklhkFEkELQSISEAYEslvkstTKRESLDK--AMRNK 556
Cdd:COG1196    133 LGPESYSIIG--QGMIdRIIEakpEERRAI----------------IE-EAAGISKYKE------RKEEAERKleATEEN 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  557 LEgeirRLHDFNRDLRDRLETANRQlssREyeghedkAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQ 636
Cdd:COG1196    188 LE----RLEDILGELERQLEPLERQ---AE-------KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  637 ALSNAQARVIKLEEELREKQAYVE----KVEKLQQALTQLQS---ACEKRGQMERRLRTWLERELDALRTQQKHGNGQPV 709
Cdd:COG1196    254 ELEELEAELAELEAELEELRLELEelelELEEAQAEEYELLAelaRLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1958798241  710 NLPEyNAPALMELVREKEERILALEADMTKWEQKYLEESTIRH 752
Cdd:COG1196    334 ELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
636-697 1.35e-04

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 44.17  E-value: 1.35e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798241  636 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 697
Cdd:COG3167     46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 491-828 1.50e-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: 45.82  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  491 VERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLVkstTKRESLDKAMrNKLEGEIRRLHDFNRD 570
Cdd:TIGR02168  209 AEKAERYKELKAELRELELALL------VLRLEELREELEELQEELKEAE---EELEELTAEL-QELEEKLEELRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  571 LRDRLETANRQLssreyeghedkaaeshhmsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEE 650
Cdd:TIGR02168  279 LEEEIEELQKEL---------------------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  651 ELREKQAYVEKVEKLQQALT-QLQSACEKRGQMERRLRTwLERELDALRTQqkhgngqpVNLPEYNAPALMELVREKEER 729
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEaELEELEAELEELESRLEE-LEEQLETLRSK--------VAQLELQIASLNNEIERLEAR 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  730 ILALEADMTKWEQkyleesTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEE---EEVVQANRRCQDMEY 806
Cdd:TIGR02168  409 LERLEDRRERLQQ------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEelrEELEEAEQALDAAER 482

                          330       340
                   ....*....|....*....|..
gi 1958798241  807 TIKNLHAKIiekdAMIKVLQQR 828
Cdd:TIGR02168  483 ELAQLQARL----DSLERLQEN 500
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 492-748 1.97e-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: 45.58  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  492 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 568
Cdd:pfam10174  182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  569 RDLRDRLET--ANRQLSS--REYEGHEDKAAESHH--MSQNKEFLK-EKEKLEMELAAVRTASE-------DHRRHIEIL 634
Cdd:pfam10174  250 RDLEDEVQMlkTNGLLHTedREEEIKQMEVYKSHSkfMKNKIDQLKqELSKKESELLALQTKLEtltnqnsDCKQHIEVL 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  635 DQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQ----LQSACEKRGQM----ERRLRTwLERELDALRT 699
Cdd:pfam10174  330 KESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEekstLAGEIRDLKDMldvkERKINV-LQKKIENLQE 408

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798241  700 QQKHGNGQPVNLPEY------------NAPALME-LVREKEERILALEADMTKWEQKYLEES 748
Cdd:pfam10174  409 QLRDKDKQLAGLKERvkslqtdssntdTALTTLEeALSEKERIIERLKEQREREDRERLEEL 470
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 601-747 2.59e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.76  E-value: 2.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  601 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekrg 680
Cdd:COG1579     17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN----- 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798241  681 qmeRRLRTwLERELDALRTQQKHGngqpvnlpEYNAPALMELVREKEERILALEADMTKWEQKYLEE 747
Cdd:COG1579     89 ---KEYEA-LQKEIESLKRRISDL--------EDEILELMERIEELEEELAELEAELAELEAELEEK 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 519-702 2.65e-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: 44.37  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  519 ADKLHKFEKELQSISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 586
Cdd:COG4942     19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  587 YEGHEDKAAE---SHHMSQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 657
Cdd:COG4942     99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958798241  658 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 702
Cdd:COG4942    179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 498-682 3.40e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 43.20  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  498 VEILTEENRVLHQELQGCYDNADKLHKFEKEL---------------QSISEAYESLVKSTTKResldkamRNKLEgEIR 562
Cdd:cd00176     35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  563 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAAEshHMSQNKEFLKEKEKLEMELAAVRTASEDhrrhieiLDQALS 639
Cdd:cd00176    107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESVEE--LLKKHKELEEELEAHEPRLKSLNELAEE-------LLEEGH 177

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958798241  640 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKRGQM 682
Cdd:cd00176    178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 496-743 3.65e-04

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.65  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  496 QMVEILTEENrvlhqelQGCYDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKAMRNK-------------LEGEI 561
Cdd:TIGR00606  667 QFITQLTDEN-------QSCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  562 RRLHDFNRDLRDRLETANRQLSSR----------------EYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAvRTASE 625
Cdd:TIGR00606  740 DLKEKEIPELRNKLQKVNRDIQRLkndieeqetllgtimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAA-KLQGS 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  626 DHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAL-----------TQLQSACEKRGQMERRLRTwLEREL 694
Cdd:TIGR00606  819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLksktnelksekLQIGTNLQRRQQFEEQLVE-LSTEV 897

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958798241  695 DALRTQQKHGNGQpvNLPEynAPALMELVREKEERILALEADMTKWEQK 743
Cdd:TIGR00606  898 QSLIREIKDAKEQ--DSPL--ETFLEKDQQEKEELISSKETSNKKAQDK 942
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 507-747 6.29e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 6.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  507 VLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLEtanrqlssrE 586
Cdd:pfam05483  364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAE---------E 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  587 YEGHEDkaaESHHMSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 661
Cdd:pfam05483  434 LKGKEQ---ELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  662 VEKLQQALTQLQSACEKRGQMERRLR---------TWLERELDALRTQQKHGNGQ---PVNLPEYNAPALMELVREKEER 729
Cdd:pfam05483  509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQ 588

                          250       260
                   ....*....|....*....|....
gi 1958798241  730 ILALEADMTKWEQ------KYLEE 747
Cdd:pfam05483  589 MKILENKCNNLKKqienknKNIEE 612
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 491-678 7.62e-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: 43.51  E-value: 7.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  491 VERAQQMVEILTEENRVLHQELQGCYDNADKLhkfEKELQSISEAYESLvksTTKRESLDKAMRNkLEGEIRRLHDFNRD 570
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEEL---ESELEALLNERASL---EEALALLRSELEE-LSEELRELESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  571 LRDRLETANRQLSS--REYEGHEDKAAeshhmsQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIKL 648
Cdd:TIGR02168  913 LRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKRL 977

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798241  649 E-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 678
Cdd:TIGR02168  978 EnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 510-679 1.22e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  510 QELQGCYDN--------ADKLHKFEKELQSISEAYESLVKSTTK---------------RESLDKAMRNKLE--GEIRRL 564
Cdd:pfam01576  415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  565 HDFNRDLRDRLETanrqlssreyEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 644
Cdd:pfam01576  495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958798241  645 VIKLEEELREKQAYVEKVEK----LQQALT----------QLQSACEKR 679
Cdd:pfam01576  554 LEALTQQLEEKAAAYDKLEKtknrLQQELDdllvdldhqrQLVSNLEKK 602
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
516-725 1.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  516 YDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNR--DLRDRLETANRQLSSREYEGHEDK 593
Cdd:COG4717    343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELL 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  594 AAEshhmsqNKEFLKEK-EKLEMELAAvrtasedhrrhieiLDQALSNAQARVIKLEEELREkqayVEKVEKLQQALTQL 672
Cdd:COG4717    423 EAL------DEEELEEElEELEEELEE--------------LEEELEELREELAELEAELEQ----LEEDGELAELLQEL 478

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798241  673 QSACEKRGQMERR------LRTWLERELDALRtqqkhgngqpvnlpEYNAPALMELVRE 725
Cdd:COG4717    479 EELKAELRELAEEwaalklALELLEEAREEYR--------------EERLPPVLERASE 523
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 546-835 2.43e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  546 RESLDKAMRNklEGEIRRLHDFNRDLRDRL----ETANR----QLSSREYEGhedkaaeshhmsqnKEFLKEKEKLEMEL 617
Cdd:TIGR02169  176 LEELEEVEEN--IERLDLIIDEKRQQLERLrrerEKAERyqalLKEKREYEG--------------YELLKEKEALERQK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  618 AAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSACEK-RGQMERrlrtwLERELDA 696
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGElEAEIAS-----LERSIAE 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  697 LRTQQKHGNGQPVNL-PEYNapALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHS-- 773
Cdd:TIGR02169  313 KERELEDAEERLAKLeAEID--KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdy 390

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798241  774 --RNGSYGE--SSLEAHIWPEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGK 835
Cdd:TIGR02169  391 reKLEKLKReiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
PRK10361 PRK10361
DNA recombination protein RmuC; Provisional
 594-704 2.95e-03

DNA recombination protein RmuC; Provisional


Pssm-ID: 182409 [Multi-domain]  Cd Length: 475  Bit Score: 41.51  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  594 AAESHHMSQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 665
Cdd:PRK10361    22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958798241  666 QQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHG 704
Cdd:PRK10361   102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS 140
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
492-701 3.53e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  492 ERAQQMVEILTEENRVLHQELQGCY----DNADKLHKFEKELQSISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDF 567
Cdd:PRK02224   247 EERREELETLEAEIEDLRETIAETErereELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  568 NRDLRDRLETANRQLS--SREYEGHEDKAAEshHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL------- 638
Cdd:PRK02224   323 DEELRDRLEECRVAAQahNEEAESLREDADD--LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerf 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  639 ---------------------SNAQARVIKLEEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKRGQMERr 685
Cdd:PRK02224   401 gdapvdlgnaedfleelreerDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE- 479

                          250
                   ....*....|....*.
gi 1958798241  686 lrtwLERELDALRTQQ 701
Cdd:PRK02224   480 ----LEAELEDLEEEV 491
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
620-748 4.42e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  620 VRTASEDHRRHIEILDQALSNAQARVIKLEEEL---REKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDA 696
Cdd:COG3206    166 LELRREEARKALEFLEEQLPELRKELEEAEAALeefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE-AEARLAA 244

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958798241  697 LRTQQKHGNGQPVNLPeyNAPALMELvrekEERILALEADMTKWEQKYLEES 748
Cdd:COG3206    245 LRAQLGSGPDALPELL--QSPVIQQL----RAQLAELEAELAELSARYTPNH 290
Val_tRNA-synt_C pfam10458
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ...
 608-673 4.58e-03

Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA synthetases.


Pssm-ID: 431296 [Multi-domain]  Cd Length: 66  Bit Score: 36.48  E-value: 4.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798241  608 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 673
Cdd:pfam10458    4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
526-767 5.86e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  526 EKELQSISEAYESLVKSTTKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKE 605
Cdd:COG4372     34 RKALFELDKLQEELEQLREELEQAREEL-EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  606 FLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQlQSACEKRGQMERR 685
Cdd:COG4372    113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE-AEAEQALDELLKE 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  686 LRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAER 765
Cdd:COG4372    192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271


                   ..
gi 1958798241  766 DT 767
Cdd:COG4372    272 DT 273
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 504-842 6.76e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  504 ENRVLHQEL-----QGCYDNADKLHKFEK-ELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLET 577
Cdd:pfam17380  267 ENEFLNQLLhivqhQKAVSERQQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMER 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  578 aNRQLssrEYEGHEDKAAESHHMSQNK-----EFLKEKEKLEMELaavRTASEDHRRHIEildqalsnaQARVIKLEEEL 652
Cdd:pfam17380  347 -EREL---ERIRQEERKRELERIRQEEiameiSRMRELERLQMER---QQKNERVRQELE---------AARKVKILEEE 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  653 REKQAYVEKVEKLQQALTQLqsacEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAP---ALMELVREKEER 729
Cdd:pfam17380  411 RQRKIQQQKVEMEQIRAEQE----EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEErkrKKLELEKEKRDR 486

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  730 ILA-------LEADMTKWEQKYLEESTIRHFamsaAAAATAERDTTISnhsrngsygessleahiwpEEEEvvqaNRRCQ 802
Cdd:pfam17380  487 KRAeeqrrkiLEKELEERKQAMIEEERKRKL----LEKEMEERQKAIY-------------------EEER----RREAE 539

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1958798241  803 DMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGKTDSSSLR 842
Cdd:pfam17380  540 EERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 601-845 7.23e-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: 39.75  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  601 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACEKRG 680
Cdd:COG4942     27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  681 QMERRLrtwlereldaLRTQQKHGNGQPVNL---PEYNAPALM------ELVREKEERILALEADMTKWEQKYLEESTIR 751
Cdd:COG4942    104 EELAEL----------LRALYRLGRQPPLALllsPEDFLDAVRrlqylkYLAPARREQAEELRADLAELAALRAELEAER 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  752 HFAMSAAAAATAERDttisnhsrngsygesSLEAHIWPEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRK 831
Cdd:COG4942    174 AELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238

                          250
                   ....*....|....
gi 1958798241  832 DAGKTDSSSLRPAR 845
Cdd:COG4942    239 AAERTPAAGFAALK 252
PTZ00121 PTZ00121
MAEBL; Provisional
 503-747 7.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  503 EENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESldKAMRNKLEgEIRRLHDFNRDLRDRLETANRQL 582
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAE-EAKKAEEAKKKAEEAKKADEAKK 1477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  583 SSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEdhRRHIEILDQALSNAQARVIKLEEELReKQAYVEKV 662
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKK-KADELKKA 1554

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798241  663 EKLQQAlTQLQSACEKRGQMERRlRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADMTKWEQ 742
Cdd:PTZ00121  1555 EELKKA-EEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632


                   ....*
gi 1958798241  743 KYLEE 747
Cdd:PTZ00121  1633 KKVEQ 1637
PRK11020 PRK11020
YibL family ribosome-associated protein;
557-622 8.83e-03

YibL family ribosome-associated protein;


Pssm-ID: 182904 [Multi-domain]  Cd Length: 118  Bit Score: 37.31  E-value: 8.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798241  557 LEGEIRRLHDfnrdlrdRLETANRQLSSREYEGHEDKAAEshhmsqnkeFLKEKEKLEMELAAVRT 622
Cdd:PRK11020     3 EKNEIKRLSD-------RLDAIRHKLAAASLRGDAEKYAQ---------FEKEKATLEAEIARLKE 52
 
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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