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Conserved domains on  [gi|1958798245|ref|XP_038938160|]
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angiomotin-like protein 1 isoform X3 [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 ...
 650-856 1.14e-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: 1.14e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  650 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 729
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  730 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 809
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798245  810 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 856
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 481-739 1.96e-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: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  481 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 560
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  561 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 640
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  641 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 720
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                          250
                   ....*....|....*....
gi 1958798245  721 RILALEADMTKWEQKYLEE 739
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 ...
 650-856 1.14e-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: 1.14e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  650 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 729
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  730 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 809
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798245  810 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 856
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 481-739 1.96e-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: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  481 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 560
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  561 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 640
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  641 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 720
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                          250
                   ....*....|....*....
gi 1958798245  721 RILALEADMTKWEQKYLEE 739
Cdd:COG1196    457 EEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 475-820 4.61e-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: 4.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  475 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMrNKL 549
Cdd:TIGR02168  133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  550 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeshhmsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 629
Cdd:TIGR02168  206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  630 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLpEYNAP 709
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-AEELA 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  710 ALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERD------TTISNH-SRNGSYGEsSLEAHIWPE 782
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlelqiASLNNEiERLEARLE-RLEDRRERL 419

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1958798245  783 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 820
Cdd:TIGR02168  420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
502-670 6.89e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 6.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  502 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 581
Cdd:PRK03918   595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  582 HEDkaaeshhmsqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 661
Cdd:PRK03918   664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720


                   ....*....
gi 1958798245  662 TQLQSACEK 670
Cdd:PRK03918   721 ERVEELREK 729
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 548-810 1.14e-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: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  548 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGhEDKAAESHHMSQnkeflkEKEKLEMELAAVRTASEDHRRHIEILD 627
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  628 QALSNAQARVIKLEEELRE----KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLeRELDALRTQQKHGNGQPVNL 703
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  704 PEYNAPALMELVREKE---ERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSY 770
Cdd:TIGR02168  833 IAATERRLEDLEEQIEelsEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958798245  771 GESSLEAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 810
Cdd:TIGR02168  913 LRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 512-684 1.54e-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: 47.35  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  512 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSReyegHEDKAAESH- 590
Cdd:cd07596     11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  591 HMSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 664
Cdd:cd07596     83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161

                          170       180
                   ....*....|....*....|
gi 1958798245  665 QSACEKRGQMERRLRTWLER 684
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 ...
 509-693 3.77e-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: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  509 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 584
Cdd:pfam01576  145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  585 KAAESHHMSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 664
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300

                          170       180
                   ....*....|....*....|....*....
gi 1958798245  665 QSAcekrgqmerrLRTWLERELDALRTQQ 693
Cdd:pfam01576  301 LEA----------LKTELEDTLDTTAAQQ 319
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
628-689 1.38e-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: 1.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798245  628 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 689
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 ...
 650-856 1.14e-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: 1.14e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  650 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADM 729
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  730 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 809
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798245  810 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 856
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 481-739 1.96e-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: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  481 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 560
Cdd:COG1196    246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  561 RDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 640
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  641 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEE 720
Cdd:COG1196    392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                          250
                   ....*....|....*....
gi 1958798245  721 RILALEADMTKWEQKYLEE 739
Cdd:COG1196    457 EEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 475-820 4.61e-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: 4.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  475 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMrNKL 549
Cdd:TIGR02168  133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  550 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeshhmsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 629
Cdd:TIGR02168  206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  630 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLpEYNAP 709
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-AEELA 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  710 ALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERD------TTISNH-SRNGSYGEsSLEAHIWPE 782
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAqlelqiASLNNEiERLEARLE-RLEDRRERL 419

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1958798245  783 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 820
Cdd:TIGR02168  420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 482-727 1.76e-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: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  482 IVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNR 561
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  562 DLRDRLETANRQLSSREYEGHEDKAAESHH--MSQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIK 639
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRerLQQEIEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  640 LEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTwlerELDALRTQQKHGNGQPVNLpeynaPALMELVREKE 719
Cdd:TIGR02168  466 LREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL-----GVLSELISVDE 533


                   ....*...
gi 1958798245  720 ERILALEA 727
Cdd:TIGR02168  534 GYEAAIEA 541
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 478-739 2.25e-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: 2.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  478 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 556
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  557 HDFNRDLRDRLETANRQLSSREYEghEDKAAEShhmSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQAR 636
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLE--KEYLEKE---IQELQ--EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  637 VIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GNGQPVNLPEYNAPAL 711
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLEDV 956

                          250       260
                   ....*....|....*....|....*...
gi 1958798245  712 MELVREKEERILALEADMTKWEQKYLEE 739
Cdd:TIGR02169  957 QAELQRVEEEIRALEPVNMLAIQEYEEV 984
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
509-693 2.50e-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: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  509 DNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDrLETANRQLSSREyeghedkaAE 588
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEID-VASAEREIAELE--------AE 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  589 SHHMSQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 668
Cdd:COG4913    677 LERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958798245  669 EKR------GQMERRLRTWLERELDALRTQQ 693
Cdd:COG4913    752 EERfaaalgDAVERELRENLEERIDALRARL 782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 484-740 3.44e-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: 3.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  484 ERAQQmveiLTEENRVLHQELQgcydnADKLHKFEKELQSISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 563
Cdd:COG1196    213 ERYRE----LKEELKELEAELL-----LLKLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  564 RDRLETANRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 643
Cdd:COG1196    280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  644 LREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgngqpvnlpeynapALMELVREKEERIL 723
Cdd:COG1196    360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---------------ALLERLERLEEELE 424

                          250
                   ....*....|....*..
gi 1958798245  724 ALEADMTKWEQKYLEES 740
Cdd:COG1196    425 ELEEALAELEEEEEEEE 441
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
491-682 1.18e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  491 EILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLvksttkresldKAMRNKLEGEIRRLHDF--NRDLRDRLE 568
Cdd:COG4717     67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREELEKLEKLlqLLPLYQELE 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  569 TANRQLSS--REYEGHEDKAAESHHMSQNKEFLKEK-EKLEMELA-AVRTASEDHRRHIEILDQALSNAQARVIKLEEEL 644
Cdd:COG4717    136 ALEAELAElpERLEELEERLEELRELEEELEELEAElAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958798245  645 REKQayvEKVEKLQQALTQLQSACEkRGQMERRLRTWL 682
Cdd:COG4717    216 EEAQ---EELEELEEELEQLENELE-AAALEERLKEAR 249
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
478-706 1.47e-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: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  478 DAFAIVERAQQMVEilteenrvlH-QELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDkAMRNKL-----EG 551
Cdd:COG4913    219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  552 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAESHH-MSQNKefLKEKEKLEMELAAVRTASEDHRRHIEILDQ 628
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELErlEARLDALREELDELEAqIRGNG--GDRLEQLEREIERLERELEERERRRARLEA 366

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798245  629 ALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAC-EKRGQMERRLRTwLERELDALRTQQKHGNGQPVNLPEY 706
Cdd:COG4913    367 LLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALeEALAEAEAALRD-LRRELRELEAEIASLERRKSNIPAR 441
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 503-701 5.05e-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: 5.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  503 ELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 578
Cdd:COG1579     11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  579 YEG--HEDKAAEshhmsqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 655
Cdd:COG1579     91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958798245  656 KLQQALTQLQSACEK-RGQMERRLRTWLEReldaLRtqqKHGNGQPV 701
Cdd:COG1579    153 ELEAELEELEAEREElAAKIPPELLALYER----IR---KRKNGLAV 192
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
502-670 6.89e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 6.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  502 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 581
Cdd:PRK03918   595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  582 HEDkaaeshhmsqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 661
Cdd:PRK03918   664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720


                   ....*....
gi 1958798245  662 TQLQSACEK 670
Cdd:PRK03918   721 ERVEELREK 729
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 498-694 8.02e-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: 8.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  498 RVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSTTKResldKAMRNKLEGEIRRLHDFNRDLRDRLE-------TA 570
Cdd:TIGR02169  311 AEKERELE---DAEERLAKLEAEIDKLLAEIEELEREIEEE----RKRRDKLTEEYAELKEELEDLRAELEevdkefaET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  571 NRQLSSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAY 650
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958798245  651 VEKVEKLQQALTQLQSACEKRgqmerrlRTWLERELDALRTQQK 694
Cdd:TIGR02169  464 LSKYEQELYDLKEEYDRVEKE-------LSKLQRELAEAEAQAR 500
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
512-720 9.38e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 9.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  512 DKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEShh 591
Cdd:PRK03918   214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKEL-- 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  592 msqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 671
Cdd:PRK03918   286 -----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958798245  672 GQMERRLRTwLERELDALRTQQKhgngqpVNLPEYNAPALMELVREKEE 720
Cdd:PRK03918   361 HELYEEAKA-KKEELERLKKRLT------GLTPEKLEKELEELEKAKEE 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 548-810 1.14e-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: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  548 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGhEDKAAESHHMSQnkeflkEKEKLEMELAAVRTASEDHRRHIEILD 627
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEEL-EQLRKELEELSR------QISALRKDLARLEAEVEQLEERIAQLS 753

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  628 QALSNAQARVIKLEEELRE----KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLeRELDALRTQQKHGNGQPVNL 703
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEaeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAEL-TLLNEEAANLRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  704 PEYNAPALMELVREKE---ERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSY 770
Cdd:TIGR02168  833 IAATERRLEDLEEQIEelsEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958798245  771 GESSLEAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 810
Cdd:TIGR02168  913 LRRELEE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 512-684 1.54e-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: 47.35  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  512 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSReyegHEDKAAESH- 590
Cdd:cd07596     11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  591 HMSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 664
Cdd:cd07596     83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161

                          170       180
                   ....*....|....*....|
gi 1958798245  665 QSACEKRGQMERRLRTWLER 684
Cdd:cd07596    162 EEARKRYEEISERLKEELKR 181
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
517-739 1.60e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  517 FEKELQsisEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAESHH 591
Cdd:COG4717     47 LLERLE---KEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  592 MSQNKEFLKEKEKLEMELAAVrtasedhrrhieildqalsnaQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEK- 670
Cdd:COG4717    124 LLQLLPLYQELEALEAELAEL---------------------PERLEELEERLEELRELEEELEELEAELAELQEELEEl 182

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958798245  671 ----RGQMERRLRTWLErELDALRTQQKHgngqpvnlpeynapaLMELVREKEERILALEADMTKWEQKYLEE 739
Cdd:COG4717    183 leqlSLATEEELQDLAE-ELEELQQRLAE---------------LEEELEEAQEELEELEEELEQLENELEAA 239
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
484-721 2.02e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  484 ERAQQMVEILTEENRVLHQelqgcYDNADKLHKFEKELQSISeaYESLVKSTTKRESLdKAMRNKLEGEIRRLH-DFNR- 561
Cdd:PRK03918   480 KELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN--LEELEKKAEEYEKL-KEKLIKLKGEIKSLKkELEKl 551

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  562 -DLRDRLETANRQLSSREyegheDKAAESHHMSQNKEFLKEKEkLEMELAAVRTASE------DHRRHIEILDQALSNAQ 634
Cdd:PRK03918   552 eELKKKLAELEKKLDELE-----EELAELLKELEELGFESVEE-LEERLKELEPFYNeylelkDAEKELEREEKELKKLE 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  635 ARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRtwLERELDALRTQQKHGNgqpvNLPEYNAPALMEL 714
Cdd:PRK03918   626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELE----KRREEIKKTLEKL 699


                   ....*..
gi 1958798245  715 VREKEER 721
Cdd:PRK03918   700 KEELEER 706
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
484-692 3.28e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 3.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  484 ERAQQMVEILTEENRVLHQELQgcydnadklhKFEKELQSISEAYeSLVKSTTKRESLDKAMRNkLEGEIRRLHDFNRDL 563
Cdd:COG3206    171 EEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKN-GLVDLSEEAKLLLQQLSE-LESQLAEARAELAEA 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  564 RDRLETANRQLSSREyegheDKAAESHHMSQNKEFLKEKEKLEMELAAVR-TASEDHRRHIEI---LDQALSNAQARVIK 639
Cdd:COG3206    239 EARLAALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAELAELSaRYTPNHPDVIALraqIAALRAQLQQEAQR 313

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958798245  640 LEEELR-EKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQ 692
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 ...
 509-693 3.77e-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: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  509 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 584
Cdd:pfam01576  145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  585 KAAESHHMSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 664
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300

                          170       180
                   ....*....|....*....|....*....
gi 1958798245  665 QSAcekrgqmerrLRTWLERELDALRTQQ 693
Cdd:pfam01576  301 LEA----------LKTELEDTLDTTAAQQ 319
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
518-657 4.07e-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: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  518 EKELQSISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKaaeshhMSQNK 596
Cdd:COG2433    387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR------SEERR 459

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798245  597 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 657
Cdd:COG2433    460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
518-744 5.12e-05

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 46.99  E-value: 5.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  518 EKELQSISEAYESLVKSTTKRESLDKAMRnklegEIRRLHDFNRDLRDRLETANRQlssreyEGHEDKAAESHHMSQNKE 597
Cdd:COG0497    154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAALQ------PGEEEELEEERRRLSNAE 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  598 FLKEkeklemelaAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK-RG 672
Cdd:COG0497    223 KLRE---------ALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElRR 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  673 QMER------RLRTWLEReLDALRT-QQKHGnGQPVNLPEYNAPALMEL--VREKEERILALEADMTKWEQKYLEE---- 739
Cdd:COG0497    287 YLDSlefdpeRLEEVEER-LALLRRlARKYG-VTVEELLAYAEELRAELaeLENSDERLEELEAELAEAEAELLEAaekl 364


                   ....*
gi 1958798245  740 STIRH 744
Cdd:COG0497    365 SAARK 369
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
481-740 7.59e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 7.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  481 AIVERAQQMVEILTEE---NRVLHQELQ-GCYDNADK-LHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEG---E 552
Cdd:PRK03918   129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  553 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAESHhmsqnkeflKEKEKLEMELAAvrtasedhrrhieiLDQALSN 632
Cdd:PRK03918   209 INEISSELPELREELEKLEKEV--KELEELKEEIEELE---------KELESLEGSKRK--------------LEEKIRE 263

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  633 AQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgngqpvnlpeyNAPALM 712
Cdd:PRK03918   264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEEEIN------------GIEERI 330

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958798245  713 ELVREKEERILALEADMTKWEQKY--LEES 740
Cdd:PRK03918   331 KELEEKEERLEELKKKLKELEKRLeeLEER 360
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
495-730 9.62e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.57  E-value: 9.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  495 EENRVLHQELQGcyDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKamRNKLEGEIRRLHDFNRDLRDRLETAnrq 573
Cdd:PRK02224   226 EEQREQARETRD--EADEVLEEHEERREELETLEAEIEDLReTIAETERE--REELAEEVRDLRERLEELEEERDDL--- 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  574 LSSREYEGHEDKAAESHHmsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEildqalsNAQARVIKLEEELREKQayvEK 653
Cdd:PRK02224   299 LAEAGLDDADAEAVEARR----EELEDRDEELRDRLEECRVAAQAHNEEAE-------SLREDADDLEERAEELR---EE 364

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798245  654 VEKLQQALTQLQSACEKRgqmeRRLRTWLERELDALRtqqKHGNGQPVNLPeyNAPALMELVREKEERILALEADMT 730
Cdd:PRK02224   365 AAELESELEEAREAVEDR----REEIEELEEEIEELR---ERFGDAPVDLG--NAEDFLEELREERDELREREAELE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 475-744 1.03e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  475 LGPDAFAIVEraQQMV-EILT---EENRVLhqelqgcydnadklhkFEkELQSISEAYEslvkstTKRESLDK--AMRNK 548
Cdd:COG1196    133 LGPESYSIIG--QGMIdRIIEakpEERRAI----------------IE-EAAGISKYKE------RKEEAERKleATEEN 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  549 LEgeirRLHDFNRDLRDRLETANRQlssREyeghedkAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQ 628
Cdd:COG1196    188 LE----RLEDILGELERQLEPLERQ---AE-------KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  629 ALSNAQARVIKLEEELREKQAYVE----KVEKLQQALTQLQS---ACEKRGQMERRLRTWLERELDALRTQQKHGNGQPV 701
Cdd:COG1196    254 ELEELEAELAELEAELEELRLELEelelELEEAQAEEYELLAelaRLEQDIARLEERRRELEERLEELEEELAELEEELE 333

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1958798245  702 NLPEyNAPALMELVREKEERILALEADMTKWEQKYLEESTIRH 744
Cdd:COG1196    334 ELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
628-689 1.38e-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: 1.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798245  628 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 689
Cdd:COG3167     46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 483-820 1.63e-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: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  483 VERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLVkstTKRESLDKAMrNKLEGEIRRLHDFNRD 562
Cdd:TIGR02168  209 AEKAERYKELKAELRELELALL------VLRLEELREELEELQEELKEAE---EELEELTAEL-QELEEKLEELRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  563 LRDRLETANRQLssreyeghedkaaeshhmsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEE 642
Cdd:TIGR02168  279 LEEEIEELQKEL---------------------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  643 ELREKQAYVEKVEKLQQALT-QLQSACEKRGQMERRLRTwLERELDALRTQqkhgngqpVNLPEYNAPALMELVREKEER 721
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEaELEELEAELEELESRLEE-LEEQLETLRSK--------VAQLELQIASLNNEIERLEAR 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  722 ILALEADMTKWEQkyleesTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEE---EEVVQANRRCQDMEY 798
Cdd:TIGR02168  409 LERLEDRRERLQQ------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEelrEELEEAEQALDAAER 482

                          330       340
                   ....*....|....*....|..
gi 1958798245  799 TIKNLHAKIiekdAMIKVLQQR 820
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 ...
 484-740 1.98e-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: 45.20  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  484 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 560
Cdd:pfam10174  182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  561 RDLRDRLET--ANRQLSS--REYEGHEDKAAESHH--MSQNKEFLK-EKEKLEMELAAVRTASE-------DHRRHIEIL 626
Cdd:pfam10174  250 RDLEDEVQMlkTNGLLHTedREEEIKQMEVYKSHSkfMKNKIDQLKqELSKKESELLALQTKLEtltnqnsDCKQHIEVL 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  627 DQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQ----LQSACEKRGQM----ERRLRTwLERELDALRT 691
Cdd:pfam10174  330 KESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEekstLAGEIRDLKDMldvkERKINV-LQKKIENLQE 408

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798245  692 QQKHGNGQPVNLPEY------------NAPALME-LVREKEERILALEADMTKWEQKYLEES 740
Cdd:pfam10174  409 QLRDKDKQLAGLKERvkslqtdssntdTALTTLEeALSEKERIIERLKEQREREDRERLEEL 470
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 593-739 2.54e-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: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  593 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekrg 672
Cdd:COG1579     17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN----- 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958798245  673 qmeRRLRTwLERELDALRTQQKHGngqpvnlpEYNAPALMELVREKEERILALEADMTKWEQKYLEE 739
Cdd:COG1579     89 ---KEYEA-LQKEIESLKRRISDL--------EDEILELMERIEELEEELAELEAELAELEAELEEK 143
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 511-694 2.89e-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: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  511 ADKLHKFEKELQSISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 578
Cdd:COG4942     19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  579 YEGHEDKAAE---SHHMSQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 649
Cdd:COG4942     99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1958798245  650 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 694
Cdd:COG4942    179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 490-674 3.22e-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: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  490 VEILTEENRVLHQELQGCYDNADKLHKFEKEL---------------QSISEAYESLVKSTTKResldkamRNKLEgEIR 554
Cdd:cd00176     35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  555 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAAEshHMSQNKEFLKEKEKLEMELAAVRTASEDhrrhieiLDQALS 631
Cdd:cd00176    107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESVEE--LLKKHKELEEELEAHEPRLKSLNELAEE-------LLEEGH 177

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958798245  632 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKRGQM 674
Cdd:cd00176    178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 488-735 3.62e-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: 3.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  488 QMVEILTEENrvlhqelQGCYDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKAMRNK-------------LEGEI 553
Cdd:TIGR00606  667 QFITQLTDEN-------QSCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  554 RRLHDFNRDLRDRLETANRQLSSR----------------EYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAvRTASE 617
Cdd:TIGR00606  740 DLKEKEIPELRNKLQKVNRDIQRLkndieeqetllgtimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAA-KLQGS 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  618 DHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAL-----------TQLQSACEKRGQMERRLRTwLEREL 686
Cdd:TIGR00606  819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLksktnelksekLQIGTNLQRRQQFEEQLVE-LSTEV 897

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1958798245  687 DALRTQQKHGNGQpvNLPEynAPALMELVREKEERILALEADMTKWEQK 735
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 ...
 499-739 6.67e-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: 43.56  E-value: 6.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  499 VLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLEtanrqlssrE 578
Cdd:pfam05483  364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAE---------E 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  579 YEGHEDkaaESHHMSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 653
Cdd:pfam05483  434 LKGKEQ---ELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  654 VEKLQQALTQLQSACEKRGQMERRLR---------TWLERELDALRTQQKHGNGQ---PVNLPEYNAPALMELVREKEER 721
Cdd:pfam05483  509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQ 588

                          250       260
                   ....*....|....*....|....
gi 1958798245  722 ILALEADMTKWEQ------KYLEE 739
Cdd:pfam05483  589 MKILENKCNNLKKqienknKNIEE 612
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 483-670 7.74e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 7.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  483 VERAQQMVEILTEENRVLHQELQGCYDNADKLhkfEKELQSISEAYESLvksTTKRESLDKAMRNkLEGEIRRLHDFNRD 562
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEEL---ESELEALLNERASL---EEALALLRSELEE-LSEELRELESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  563 LRDRLETANRQLSS--REYEGHEDKAAeshhmsQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIKL 640
Cdd:TIGR02168  913 LRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKRL 977

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958798245  641 E-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 670
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 ...
 502-671 1.20e-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: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  502 QELQGCYDN--------ADKLHKFEKELQSISEAYESLVKSTTK---------------RESLDKAMRNKLE--GEIRRL 556
Cdd:pfam01576  415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  557 HDFNRDLRDRLETanrqlssreyEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 636
Cdd:pfam01576  495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958798245  637 VIKLEEELREKQAYVEKVEK----LQQALT----------QLQSACEKR 671
Cdd:pfam01576  554 LEALTQQLEEKAAAYDKLEKtknrLQQELDdllvdldhqrQLVSNLEKK 602
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
508-717 1.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  508 YDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNR--DLRDRLETANRQLSSREYEGHEDK 585
Cdd:COG4717    343 LDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELL 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  586 AAEshhmsqNKEFLKEK-EKLEMELAAvrtasedhrrhieiLDQALSNAQARVIKLEEELREkqayVEKVEKLQQALTQL 664
Cdd:COG4717    423 EAL------DEEELEEElEELEEELEE--------------LEEELEELREELAELEAELEQ----LEEDGELAELLQEL 478

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958798245  665 QSACEKRGQMERR------LRTWLERELDALRtqqkhgngqpvnlpEYNAPALMELVRE 717
Cdd:COG4717    479 EELKAELRELAEEwaalklALELLEEAREEYR--------------EERLPPVLERASE 523
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 538-827 2.38e-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: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  538 RESLDKAMRNklEGEIRRLHDFNRDLRDRL----ETANR----QLSSREYEGhedkaaeshhmsqnKEFLKEKEKLEMEL 609
Cdd:TIGR02169  176 LEELEEVEEN--IERLDLIIDEKRQQLERLrrerEKAERyqalLKEKREYEG--------------YELLKEKEALERQK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  610 AAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSACEK-RGQMERrlrtwLERELDA 688
Cdd:TIGR02169  240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL--RVKEKIGElEAEIAS-----LERSIAE 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  689 LRTQQKHGNGQPVNL-PEYNapALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHS-- 765
Cdd:TIGR02169  313 KERELEDAEERLAKLeAEID--KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdy 390

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798245  766 --RNGSYGE--SSLEAHIWPEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGK 827
Cdd:TIGR02169  391 reKLEKLKReiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
PRK10361 PRK10361
DNA recombination protein RmuC; Provisional
 586-696 2.90e-03

DNA recombination protein RmuC; Provisional


Pssm-ID: 182409 [Multi-domain]  Cd Length: 475  Bit Score: 41.51  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  586 AAESHHMSQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 657
Cdd:PRK10361    22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1958798245  658 QQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHG 696
Cdd:PRK10361   102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS 140
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
484-693 3.50e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  484 ERAQQMVEILTEENRVLHQELQGCY----DNADKLHKFEKELQSISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDF 559
Cdd:PRK02224   247 EERREELETLEAEIEDLRETIAETErereELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  560 NRDLRDRLETANRQLS--SREYEGHEDKAAEshHMSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL------- 630
Cdd:PRK02224   323 DEELRDRLEECRVAAQahNEEAESLREDADD--LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerf 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  631 ---------------------SNAQARVIKLEEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKRGQMERr 677
Cdd:PRK02224   401 gdapvdlgnaedfleelreerDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE- 479

                          250
                   ....*....|....*.
gi 1958798245  678 lrtwLERELDALRTQQ 693
Cdd:PRK02224   480 ----LEAELEDLEEEV 491
Val_tRNA-synt_C pfam10458
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ...
 600-665 4.82e-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: 4.82e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958798245  600 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 665
Cdd:pfam10458    4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
612-740 4.85e-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: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  612 VRTASEDHRRHIEILDQALSNAQARVIKLEEEL---REKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDA 688
Cdd:COG3206    166 LELRREEARKALEFLEEQLPELRKELEEAEAALeefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE-AEARLAA 244

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958798245  689 LRTQQKHGNGQPVNLPeyNAPALMELvrekEERILALEADMTKWEQKYLEES 740
Cdd:COG3206    245 LRAQLGSGPDALPELL--QSPVIQQL----RAQLAELEAELAELSARYTPNH 290
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
518-759 6.23e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 6.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  518 EKELQSISEAYESLVKSTTKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAESHHMSQNKE 597
Cdd:COG4372     34 RKALFELDKLQEELEQLREELEQAREEL-EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  598 FLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQlQSACEKRGQMERR 677
Cdd:COG4372    113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE-AEAEQALDELLKE 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  678 LRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAER 757
Cdd:COG4372    192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271


                   ..
gi 1958798245  758 DT 759
Cdd:COG4372    272 DT 273
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 593-837 7.17e-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: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  593 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACEKRG 672
Cdd:COG4942     27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  673 QMERRLrtwlereldaLRTQQKHGNGQPVNL---PEYNAPALM------ELVREKEERILALEADMTKWEQKYLEESTIR 743
Cdd:COG4942    104 EELAEL----------LRALYRLGRQPPLALllsPEDFLDAVRrlqylkYLAPARREQAEELRADLAELAALRAELEAER 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  744 HFAMSAAAAATAERDttisnhsrngsygesSLEAHIWPEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRK 823
Cdd:COG4942    174 AELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238

                          250
                   ....*....|....
gi 1958798245  824 DAGKTDSSSLRPAR 837
Cdd:COG4942    239 AAERTPAAGFAALK 252
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 496-834 7.17e-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: 40.11  E-value: 7.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  496 ENRVLHQEL-----QGCYDNADKLHKFEK-ELQSISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLET 569
Cdd:pfam17380  267 ENEFLNQLLhivqhQKAVSERQQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMER 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  570 aNRQLssrEYEGHEDKAAESHHMSQNK-----EFLKEKEKLEMELaavRTASEDHRRHIEildqalsnaQARVIKLEEEL 644
Cdd:pfam17380  347 -EREL---ERIRQEERKRELERIRQEEiameiSRMRELERLQMER---QQKNERVRQELE---------AARKVKILEEE 410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  645 REKQAYVEKVEKLQQALTQLqsacEKRGQMERRLRTWLERELDALRTQQKHGNGQPVNLPEYNAP---ALMELVREKEER 721
Cdd:pfam17380  411 RQRKIQQQKVEMEQIRAEQE----EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEErkrKKLELEKEKRDR 486

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  722 ILA-------LEADMTKWEQKYLEESTIRHFamsaAAAATAERDTTISnhsrngsygessleahiwpEEEEvvqaNRRCQ 794
Cdd:pfam17380  487 KRAeeqrrkiLEKELEERKQAMIEEERKRKL----LEKEMEERQKAIY-------------------EEER----RREAE 539

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1958798245  795 DMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGKTDSSSLR 834
Cdd:pfam17380  540 EERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMR 579
PTZ00121 PTZ00121
MAEBL; Provisional
 495-739 8.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 8.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  495 EENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESldKAMRNKLEgEIRRLHDFNRDLRDRLETANRQL 574
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAE-EAKKAEEAKKKAEEAKKADEAKK 1477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  575 SSREYEGHEDKAAESHHMSQNKEFLKEKEKLEMELAAVRTASEdhRRHIEILDQALSNAQARVIKLEEELReKQAYVEKV 654
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKK-KADELKKA 1554

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958798245  655 EKLQQAlTQLQSACEKRGQMERRlRTWLERELDALRTQQKHGNGQPVNLPEYNAPALMELVREKEERILALEADMTKWEQ 734
Cdd:PTZ00121  1555 EELKKA-EEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632


                   ....*
gi 1958798245  735 KYLEE 739
Cdd:PTZ00121  1633 KKVEQ 1637
PRK11020 PRK11020
YibL family ribosome-associated protein;
549-614 8.93e-03

YibL family ribosome-associated protein;


Pssm-ID: 182904 [Multi-domain]  Cd Length: 118  Bit Score: 37.31  E-value: 8.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958798245  549 LEGEIRRLHDfnrdlrdRLETANRQLSSREYEGHEDKAAEshhmsqnkeFLKEKEKLEMELAAVRT 614
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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