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Conserved domains on  [gi|2462625347|ref|XP_054219249|]
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CDK5 regulatory subunit-associated protein 2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 61-129 5.94e-20

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


:

Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 85.27  E-value: 5.94e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625347   61 KDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASK 129
Cdd:pfam07989    1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-458 4.15e-14

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: 78.05  E-value: 4.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  146 KEDARKK---VQQ----VEDL---LTKRILLLEKDvtAAQAELEKAFAgtetEKALRLRLESKLSEMKKMHEGDLAMALV 215
Cdd:COG1196    174 KEEAERKleaTEEnlerLEDIlgeLERQLEPLERQ--AEKAERYRELK----EELKELEAELLLLKLRELEAELEELEAE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdENVSSGELRglcaapreEKERETEAAQMEHQKERNSFQERIQAL 295
Cdd:COG1196    248 LEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQ--------AEEYELLAELARLEQDIARLEERRREL 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  296 EEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALsg 375
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-- 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  376 KEALSAALRSQNLTKSTENHRLRRSikKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 455
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470


                   ...
gi 2462625347  456 AME 458
Cdd:COG1196    471 EAA 473
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
327-599 2.33e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  327 LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRSIKKITQ 406
Cdd:COG4372     47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQEELEELQK 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  407 ELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQ--EQVIKHLTE 484
Cdd:COG4372    123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEEL 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  485 STNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIY 564
Cdd:COG4372    203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462625347  565 THLVKSLQESDSINNLQAELNKIFALRKQLEQDVL 599
Cdd:COG4372    283 LELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1324-1560 2.57e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1324 EMNTQNELMERIEEDNLTYQHLLPEspepsashaLSDYETSEKSffsrDQKQDNETEKTSVMVNSFSQDLLMEHIQ-EIR 1402
Cdd:TIGR02169  195 EKRQQLERLRREREKAERYQALLKE---------KREYEGYELL----KEKEALERQKEAIERQLASLEEELEKLTeEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1403 TLRKRLEESIKTNEKLRKQLERQGS-EFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAMLIKG--SRDKQK-ENDK 1478
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEI-ASLERSIAEKERELEDAEERLAKLeaEIDKLLaEIEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1479 LRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRV 1558
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420


                   ..
gi 2462625347 1559 EL 1560
Cdd:TIGR02169  421 EL 422
 
Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 61-129 5.94e-20

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 85.27  E-value: 5.94e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625347   61 KDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASK 129
Cdd:pfam07989    1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-458 4.15e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 4.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  146 KEDARKK---VQQ----VEDL---LTKRILLLEKDvtAAQAELEKAFAgtetEKALRLRLESKLSEMKKMHEGDLAMALV 215
Cdd:COG1196    174 KEEAERKleaTEEnlerLEDIlgeLERQLEPLERQ--AEKAERYRELK----EELKELEAELLLLKLRELEAELEELEAE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdENVSSGELRglcaapreEKERETEAAQMEHQKERNSFQERIQAL 295
Cdd:COG1196    248 LEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQ--------AEEYELLAELARLEQDIARLEERRREL 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  296 EEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALsg 375
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-- 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  376 KEALSAALRSQNLTKSTENHRLRRSikKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 455
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470


                   ...
gi 2462625347  456 AME 458
Cdd:COG1196    471 EAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-452 1.03e-13

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: 77.02  E-value: 1.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  104 IELKVEVESLKRELQEREQLLIKASKAVESLAEaggsEIQRVKEDARKKVQQVEDLltkrilllEKDVTAAQAELEKAFA 183
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRK----ELEELEEELEQLRKELEEL--------SRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  184 GTETEKALRLRLESKLSEMKKMHEGDLAMalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrglc 263
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQLKEELKAL---------------- 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  264 aaprEEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEK 343
Cdd:TIGR02168  802 ----REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  344 LSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNltksTENHRLRRSIKKITQELSDLQQE-RERLEKDL 422
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQERlSEEYSLTL 953

                          330       340       350
                   ....*....|....*....|....*....|
gi 2462625347  423 EEAHREKSKGDCTIRDLRNEVEKLRNEVNE 452
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENKIKE 983
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 64-503 3.11e-13

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 75.54  E-value: 3.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   64 ENQITELKKENFN-LKLRIYFLEERMQQ-------EFHGPTEHIYKTNIE---LKVEVESLKRELQEREQLLIKASKAVE 132
Cdd:pfam15921  244 EDQLEALKSESQNkIELLLQQHQDRIEQlisehevEITGLTEKASSARSQansIQSQLEIIQEQARNQNSMYMRQLSDLE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  133 SLAEAGGSEIQRVKEDARKKVQQVEdlltKRILLLEKDVTAAQAE--------------LEKAFAGT-ETEKALRLRLES 197
Cdd:pfam15921  324 STVSQLRSELREAKRMYEDKIEELE----KQLVLANSELTEARTErdqfsqesgnlddqLQKLLADLhKREKELSLEKEQ 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  198 KlsemKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEE-KSQMacpdenvssgelrglcaapreekERETEA 276
Cdd:pfam15921  400 N----KRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQM-----------------------ERQMAA 452

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  277 AQMEHQ--KERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLsaafaKAREA 354
Cdd:pfam15921  453 IQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL-----RSRVD 527

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  355 LQKAQTQEFQGSEDYetaLSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSD-------LQQERERLEKDLEEAHR 427
Cdd:pfam15921  528 LKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRL 604

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  428 E-------KSKGDCTIRDLRNEVE-------KLRNEVNEREKAMenryKSLLSESNKKLHNQEQVIKHLTESTNQKDVLL 493
Cdd:pfam15921  605 ElqefkilKDKKDAKIRELEARVSdlelekvKLVNAGSERLRAV----KDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680

                          490
                   ....*....|
gi 2462625347  494 QKFNEKDLEV 503
Cdd:pfam15921  681 RNFRNKSEEM 690
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-622 1.33e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   59 NMKDFENQITELKKENFNLKLRIYFLEERMQQefhgpTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEag 138
Cdd:PRK03918   156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKR-----TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-- 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  139 gsEIQRVKEDARKKVQqvedlLTKRILLLEKDVTAaqaelekafagtetekalrlrLESKLSEMKKMHEGDLAMALVLDE 218
Cdd:PRK03918   229 --EVKELEELKEEIEE-----LEKELESLEGSKRK---------------------LEEKIRELEERIEELKKEIEELEE 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  219 KDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVS--SGELRGLCA--APREEKERETEaaqmEHQKERNSFQERIQA 294
Cdd:PRK03918   281 KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSrlEEEINGIEEriKELEEKEERLE----ELKKKLKELEKRLEE 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  295 LEEDLREKEReiATEKKNSLKRDKA------IQGLTMALKSKEKKVEELNSEIEKLSAAFA--KAREALQKAQTQEFQGS 366
Cdd:PRK03918   357 LEERHELYEE--AKAKKEELERLKKrltgltPEKLEKELEELEKAKEEIEEEISKITARIGelKKEIKELKKAIEELKKA 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  367 EDyETALSGKEaLSAALRSQNLTKST-ENHRLRRSIKKITQELSDLQQERERLEKDLEEAHR---EKSKGDcTIRDLRNE 442
Cdd:PRK03918   435 KG-KCPVCGRE-LTEEHRKELLEEYTaELKRIEKELKEIEEKERKLRKELRELEKVLKKESElikLKELAE-QLKELEEK 511

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  443 VEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLmaaEDLELRSEG 522
Cdd:PRK03918   512 LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVE 588

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  523 LITEKCSSQQPPGSKtiFSKEKKQSSDYEELIQVLKKEQDiythlvkslQESDSINNLQAELNKIFALRKQLEQ-----D 597
Cdd:PRK03918   589 ELEERLKELEPFYNE--YLELKDAEKELEREEKELKKLEE---------ELDKAFEELAETEKRLEELRKELEElekkyS 657

                          570       580
                   ....*....|....*....|....*
gi 2462625347  598 VLSYQNLRKTLEEQISEIRRREESF 622
Cdd:PRK03918   658 EEEYEELREEYLELSRELAGLRAEL 682
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
327-599 2.33e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  327 LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRSIKKITQ 406
Cdd:COG4372     47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQEELEELQK 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  407 ELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQ--EQVIKHLTE 484
Cdd:COG4372    123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEEL 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  485 STNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIY 564
Cdd:COG4372    203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462625347  565 THLVKSLQESDSINNLQAELNKIFALRKQLEQDVL 599
Cdd:COG4372    283 LELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1324-1560 2.57e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1324 EMNTQNELMERIEEDNLTYQHLLPEspepsashaLSDYETSEKSffsrDQKQDNETEKTSVMVNSFSQDLLMEHIQ-EIR 1402
Cdd:TIGR02169  195 EKRQQLERLRREREKAERYQALLKE---------KREYEGYELL----KEKEALERQKEAIERQLASLEEELEKLTeEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1403 TLRKRLEESIKTNEKLRKQLERQGS-EFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAMLIKG--SRDKQK-ENDK 1478
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEI-ASLERSIAEKERELEDAEERLAKLeaEIDKLLaEIEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1479 LRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRV 1558
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420


                   ..
gi 2462625347 1559 EL 1560
Cdd:TIGR02169  421 EL 422
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1391-1575 5.72e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 5.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1391 QDLLMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIfasgselhSSLTSEIHFLRKQNQALNAMLIKGSR 1470
Cdd:COG1196    252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------ARLEQDIARLEERRRELEERLEELEE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1471 DKQ---KENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRcsgQELSRVQEELKLRQQLLS 1547
Cdd:COG1196    324 ELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAA 400

                          170       180
                   ....*....|....*....|....*...
gi 2462625347 1548 QNDKLLQSLRVELKAYEKLDEEHRRLRD 1575
Cdd:COG1196    401 QLEELEEAEEALLERLERLEEELEELEE 428
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1358-1572 1.61e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1358 LSDYETSEKSFfsRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLRKRLEESIKT-NEKLRKQLERQGSEfVQGSTSI 1436
Cdd:pfam15921  383 LADLHKREKEL--SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAA-IQGKNES 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1437 FASGSELHSSLTSEIHFLRKQNQALNAmlikgsrdKQKENDKLRESLSRKTVSLEHLQReyaSVKEENERLQKEGSEKER 1516
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTA--------KKMTLESSERTVSDLTASLQEKER---AIEATNAEITKLRSRVDL 528

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625347 1517 HNQQLiQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRVELKAYEKLDEEHRR 1572
Cdd:pfam15921  529 KLQEL-QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 412-677 2.33e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  412 QQERERLEKDLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSL---LSESNKKLHNQEQVIKHLTESTNQ 488
Cdd:pfam02463  169 RKKKEALKKLIEETENLAEL----IIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLKLNEERIDLLQE 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  489 KDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEglitEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLV 568
Cdd:pfam02463  245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE----EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  569 KSLQesdsinNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREESFSLySDQTSYLSICLEEN------NRF 642
Cdd:pfam02463  321 KEKK------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ-LEEELLAKKKLESErlssaaKLK 393

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462625347  643 QVEHFSQEELKKKVSDLIQLVKELYTDNQHLKKTI 677
Cdd:pfam02463  394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 289-497 2.89e-03

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 41.94  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  289 QERIQALEEDLREKEREIatekknslKRDKAIQGLTMA-LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSE 367
Cdd:cd08915     90 EELLQECEELLEEEAAED--------DQLRAKFGTLRWrRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESIDP 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  368 DYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEeahrEKSKGDCTIRDLRNEVEKLR 447
Cdd:cd08915    162 NLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELE----IKSRNNDILPKLITEYKKNG 237

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462625347  448 NEVNER--EKAMENrYKSLLSESNKKLHNQEQVIKHLTEStNQKDVLLQKFN 497
Cdd:cd08915    238 TTEFEDlfEEHLKK-FDKDLTYVEKTKKKQIELIKEIDAA-NQEFSQVKNSN 287
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 273-364 4.43e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.49  E-value: 4.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   273 ETEAAQMEHQKERNSFQERIQALEEDLREKEREiatekknsLKRDKAiqglTMALKSKEKKVEELNSEIEKLSAAFAKAR 352
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAELEKLEKELQKLKEK--------LQKDAA----TLSEAAREKKEKELQKKVQEFQRKQQKLQ 82

                            90
                    ....*....|..
gi 2462625347   353 EALQKAQTQEFQ 364
Cdd:smart00935   83 QDLQKRQQEELQ 94
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1395-1569 9.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1395 MEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVqgstsiFASGSELHSSLTSEIHFLRKQNQALNAMliKGSRDKQK 1474
Cdd:PRK03918   548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELG------FESVEELEERLKELEPFYNEYLELKDAE--KELEREEK 619

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1475 ENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNqqLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQ 1554
Cdd:PRK03918   620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLE 697

                          170
                   ....*....|....*
gi 2462625347 1555 SLRVELKAYEKLDEE 1569
Cdd:PRK03918   698 KLKEELEEREKAKKE 712
 
Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 61-129 5.94e-20

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 85.27  E-value: 5.94e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625347   61 KDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASK 129
Cdd:pfam07989    1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAEK 69
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 146-458 4.15e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.05  E-value: 4.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  146 KEDARKK---VQQ----VEDL---LTKRILLLEKDvtAAQAELEKAFAgtetEKALRLRLESKLSEMKKMHEGDLAMALV 215
Cdd:COG1196    174 KEEAERKleaTEEnlerLEDIlgeLERQLEPLERQ--AEKAERYRELK----EELKELEAELLLLKLRELEAELEELEAE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdENVSSGELRglcaapreEKERETEAAQMEHQKERNSFQERIQAL 295
Cdd:COG1196    248 LEELEAELEELEAELAELEAELEELRLELEE-----LELELEEAQ--------AEEYELLAELARLEQDIARLEERRREL 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  296 EEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALsg 375
Cdd:COG1196    315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-- 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  376 KEALSAALRSQNLTKSTENHRLRRSikKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 455
Cdd:COG1196    393 RAAAELAAQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470


                   ...
gi 2462625347  456 AME 458
Cdd:COG1196    471 EAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-452 1.03e-13

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: 77.02  E-value: 1.03e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  104 IELKVEVESLKRELQEREQLLIKASKAVESLAEaggsEIQRVKEDARKKVQQVEDLltkrilllEKDVTAAQAELEKAFA 183
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRK----ELEELEEELEQLRKELEEL--------SRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  184 GTETEKALRLRLESKLSEMKKMHEGDLAMalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrglc 263
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQLKEELKAL---------------- 801

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  264 aaprEEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEK 343
Cdd:TIGR02168  802 ----REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  344 LSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNltksTENHRLRRSIKKITQELSDLQQE-RERLEKDL 422
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQERlSEEYSLTL 953

                          330       340       350
                   ....*....|....*....|....*....|
gi 2462625347  423 EEAHREKSKGDCTIRDLRNEVEKLRNEVNE 452
Cdd:TIGR02168  954 EEAEALENKIEDDEEEARRRLKRLENKIKE 983
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 64-503 3.11e-13

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 75.54  E-value: 3.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   64 ENQITELKKENFN-LKLRIYFLEERMQQ-------EFHGPTEHIYKTNIE---LKVEVESLKRELQEREQLLIKASKAVE 132
Cdd:pfam15921  244 EDQLEALKSESQNkIELLLQQHQDRIEQlisehevEITGLTEKASSARSQansIQSQLEIIQEQARNQNSMYMRQLSDLE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  133 SLAEAGGSEIQRVKEDARKKVQQVEdlltKRILLLEKDVTAAQAE--------------LEKAFAGT-ETEKALRLRLES 197
Cdd:pfam15921  324 STVSQLRSELREAKRMYEDKIEELE----KQLVLANSELTEARTErdqfsqesgnlddqLQKLLADLhKREKELSLEKEQ 399

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  198 KlsemKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEE-KSQMacpdenvssgelrglcaapreekERETEA 276
Cdd:pfam15921  400 N----KRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQM-----------------------ERQMAA 452

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  277 AQMEHQ--KERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLsaafaKAREA 354
Cdd:pfam15921  453 IQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL-----RSRVD 527

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  355 LQKAQTQEFQGSEDYetaLSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSD-------LQQERERLEKDLEEAHR 427
Cdd:pfam15921  528 LKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRL 604

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  428 E-------KSKGDCTIRDLRNEVE-------KLRNEVNEREKAMenryKSLLSESNKKLHNQEQVIKHLTESTNQKDVLL 493
Cdd:pfam15921  605 ElqefkilKDKKDAKIRELEARVSdlelekvKLVNAGSERLRAV----KDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680

                          490
                   ....*....|
gi 2462625347  494 QKFNEKDLEV 503
Cdd:pfam15921  681 RNFRNKSEEM 690
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 147-500 1.91e-12

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: 72.78  E-value: 1.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  147 EDARKKVQQVEDLLTKrillLEKDVTAAQAELEKAfagtetEKALRLRLESKlsemkkmhegDLAMALVLDEKDRLIEEL 226
Cdd:TIGR02168  182 ERTRENLDRLEDILNE----LERQLKSLERQAEKA------ERYKELKAELR----------ELELALLVLRLEELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  227 KLSLKSKEALIQCLKEEKSQMACPDENVSSGELRglcaapREEKERETEAAQ------------MEHQKERnsFQERIQA 294
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLE------VSELEEEIEELQkelyalaneisrLEQQKQI--LRERLAN 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  295 LEEDLREKEREIATEKKnslKRDKAIQgltmALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEfqgsEDYETALS 374
Cdd:TIGR02168  314 LERQLEELEAQLEELES---KLDELAE----ELAELEEKLEELKEELESLEAELEELEAELEELESRL----EELEEQLE 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  375 GKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCtirdlrNEVEKLRNEVNERE 454
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL------EELEEELEELQEEL 456

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2462625347  455 KAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKD 500
Cdd:TIGR02168  457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-623 8.87e-12

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: 70.47  E-value: 8.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   62 DFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNI------ELKVEVESLKRELQEREQLLIKASKAVESLA 135
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEleekleELKEELESLEAELEELEAELEELESRLEELE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  136 EaggsEIQRVKEDARKKVQQVEdLLTKRILLLEKDVTAAQAELEKAFAgtETEKALRLRLESKLSEMKKMHEGDLAMALV 215
Cdd:TIGR02168  379 E----QLETLRSKVAQLELQIA-SLNNEIERLEARLERLEDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEE 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  216 LDEK-DRLIEELKLSLKSKEALIQCLKEEKSQmacpdENVSSGELRGLCAAPRE-EKERETEAAQMEHQKERNSFQERI- 292
Cdd:TIGR02168  452 LQEElERLEEALEELREELEEAEQALDAAERE-----LAQLQARLDSLERLQENlEGFSEGVKALLKNQSGLSGILGVLs 526

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  293 ----------QALEEDLREK------------EREIATEKKNSLKR----------DKAIQGLTMALKSKEKKVEELNSE 340
Cdd:TIGR02168  527 elisvdegyeAAIEAALGGRlqavvvenlnaaKKAIAFLKQNELGRvtflpldsikGTEIQGNDREILKNIEGFLGVAKD 606

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  341 IEKLSAAFAKAREALqkaqtqeFQGS---EDYETALsgkeALSAALRSQNLTKSTENHRLRR-------------SIKKI 404
Cdd:TIGR02168  607 LVKFDPKLRKALSYL-------LGGVlvvDDLDNAL----ELAKKLRPGYRIVTLDGDLVRPggvitggsaktnsSILER 675

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  405 TQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK---AMENRYKSLLSESNKKLHNQEQVIKH 481
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisALRKDLARLEAEVEQLEERIAQLSKE 755

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  482 LTESTNQKDVLLQKFNEKDLEVIQQncyLMAAEDLELRSEGLITEKCSSQQppgSKTIFSKEK--------KQSSDYEEL 553
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQIEQLKEELKALRE---ALDELRAELtllneeaaNLRERLESL 829

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462625347  554 IQVLKKEQDIYTHLVKSL-QESDSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREESFS 623
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIeELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 105-425 2.53e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 2.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  105 ELKVEVESLKRELQEREQLLIKASKAVEsLAEAGGSEIQRVKEDARKKV---QQVEDLLTKRILLLEKDVTAAQAELEKA 181
Cdd:COG1196    236 ELEAELEELEAELEELEAELEELEAELA-ELEAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEERRREL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  182 fagTETEKALRLRLESKLSEMKKMHEgdlAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrg 261
Cdd:COG1196    315 ---EERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-------------- 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  262 lcaAPREEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEI 341
Cdd:COG1196    375 ---AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  342 EKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQN--------LTKSTENHRLRRSIKKITQELSDLQQ 413
Cdd:COG1196    452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeaeadyegFLEGVKAALLLAGLRGLAGAVAVLIG 531

                          330
                   ....*....|..
gi 2462625347  414 ERERLEKDLEEA 425
Cdd:COG1196    532 VEAAYEAALEAA 543
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 106-477 3.31e-11

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 68.61  E-value: 3.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  106 LKVEVESLKRELQ-EREQLLIKASKAVESLAEAGG--SEIQRVKEDARKKVQQvedlLTKRILLLEK------DVTAAQA 176
Cdd:pfam15921  431 LEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSltAQLESTKEMLRKVVEE----LTAKKMTLESsertvsDLTASLQ 506

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  177 ELEKAFAGTETE-KALRLRLESKLSEMKKM-HEGDL---------AMALVLDEKDRLIEELKLSLKSKEALIQ------- 238
Cdd:pfam15921  507 EKERAIEATNAEiTKLRSRVDLKLQELQHLkNEGDHlrnvqteceALKLQMAEKDKVIEILRQQIENMTQLVGqhgrtag 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  239 CLKEEKSQMA--CPDENVSSGELRGLcAAPREEKERETEAA----QMEHQKERNSFQERIQALEeDLREKEREIATEKKN 312
Cdd:pfam15921  587 AMQVEKAQLEkeINDRRLELQEFKIL-KDKKDAKIRELEARvsdlELEKVKLVNAGSERLRAVK-DIKQERDQLLNEVKT 664

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  313 SLKRDKAIQGLTMALKSK-EKKVEELNSEIEKLSAAFAKAREALQKAQT--QEFQGSEDYETALS-GKEALSAALRSQNL 388
Cdd:pfam15921  665 SRNELNSLSEDYEVLKRNfRNKSEEMETTTNKLKMQLKSAQSELEQTRNtlKSMEGSDGHAMKVAmGMQKQITAKRGQID 744

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  389 TKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMEnRYKSLLSES 468
Cdd:pfam15921  745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALD-KASLQFAEC 823


                   ....*....
gi 2462625347  469 NKKLHNQEQ 477
Cdd:pfam15921  824 QDIIQRQEQ 832
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 137-455 3.84e-11

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: 68.56  E-value: 3.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  137 AGGSEIQRVKEDARKKVQQVEDLLtKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLES-----KLSEMKKMHEGDLA 211
Cdd:TIGR02169  163 AGVAEFDRKKEKALEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyeLLKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  212 MALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGL-------------CAAPREEKERETEAAQ 278
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleaeiasLERSIAEKERELEDAE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  279 MEHQKernsFQERIQALEEDLREKEREIATEKKnslKRDKaiqgLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKA 358
Cdd:TIGR02169  322 ERLAK----LEAEIDKLLAEIEELEREIEEERK---RRDK----LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  359 QTQ-EFQGSEDYE--TALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCT 435
Cdd:TIGR02169  391 REKlEKLKREINElkRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470

                          330       340
                   ....*....|....*....|
gi 2462625347  436 IRDLRNEVEKLRNEVNEREK 455
Cdd:TIGR02169  471 LYDLKEEYDRVEKELSKLQR 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 216-618 5.27e-11

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: 68.16  E-value: 5.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQMAcpdenvssGELRGLCAAPrEEKERETEAAQMEHQKERNsfqeRIQAL 295
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELE--------EELEQLRKEL-EELSRQISALRKDLARLEA----EVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  296 EEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSG 375
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  376 KEALSAALRS-----QNLTKSTEnhRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEV 450
Cdd:TIGR02168  826 LESLERRIAAterrlEDLEEQIE--ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  451 NE-REKAMENRYKslLSESNKKLHnqeQVIKHLTESTNQKDVLLQKFNEKdleviqqncYLMAAEDLELRSEGLitekcs 529
Cdd:TIGR02168  904 RElESKRSELRRE--LEELREKLA---QLELRLEGLEVRIDNLQERLSEE---------YSLTLEEAEALENKI------ 963

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  530 sqqppgsktifskEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKifalrkQLEqDVLSyqnLRKTLE 609
Cdd:TIGR02168  964 -------------EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTA------QKE-DLTE---AKETLE 1020


                   ....*....
gi 2462625347  610 EQISEIRRR 618
Cdd:TIGR02168 1021 EAIEEIDRE 1029
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 264-470 9.89e-11

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: 65.56  E-value: 9.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  264 AAPREEKERETEAAQ---MEHQKERNSFQERIQALEEDLREKEREIAtekknslKRDKAIQGLTMALKSKEKKVEELNSE 340
Cdd:COG4942     19 ADAAAEAEAELEQLQqeiAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAELAELEKE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  341 IEKLSAAFAKAREALQK-AQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHR------LRRSIKKITQELSDLQQ 413
Cdd:COG4942     92 IAELRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARreqaeeLRADLAELAALRAELEA 171

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462625347  414 ERERLEKDLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNK 470
Cdd:COG4942    172 ERAELEALLAELEEERAA----LEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 290-601 2.61e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 2.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  290 ERIQALEEDLREKEREIATEKKNSLKRDKA-----IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ 364
Cdd:COG1196    213 ERYRELKEELKELEAELLLLKLRELEAELEeleaeLEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  365 GSEDYETALSGKEAL---SAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREkskgdctIRDLRN 441
Cdd:COG1196    293 LLAELARLEQDIARLeerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-------LAEAEE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  442 EVEKLRNEVNEREKAMENRYKSLLSESNKKLhNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQncylmAAEDLELRSE 521
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEA-----LAELEEEEEE 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  522 GLITEKcssqqppgsktifSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFALRKQLEQDVLSY 601
Cdd:COG1196    440 EEEALE-------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-616 9.16e-10

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: 63.92  E-value: 9.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   59 NMKDFENQITELKKENFNLKLRIYFLEERMQQ---EFHGPTEHIYKTNIE---LKVEVESLKREL----QEREQLLIKAS 128
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEierLEARLERLEDRRerlqQEIEELLKKLE 431

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  129 KAVESLAEAGGSEIQRVKEDARKK---VQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESK----LSE 201
Cdd:TIGR02168  432 EAELKELQAELEELEEELEELQEElerLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvKAL 511

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  202 MKKMHEGDLAMALVL-----DEKDRLIEELKL----------SLKSKEALIQCLKEEKSQMA--CPDENVSSGELRGLCA 264
Cdd:TIGR02168  512 LKNQSGLSGILGVLSelisvDEGYEAAIEAALggrlqavvveNLNAAKKAIAFLKQNELGRVtfLPLDSIKGTEIQGNDR 591

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  265 APREEKERETEAAqMEHQKERNSFQ-------------ERIQALEEDLREKERE--IATEKKNSLKRDKAIQG----LTM 325
Cdd:TIGR02168  592 EILKNIEGFLGVA-KDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGyrIVTLDGDLVRPGGVITGgsakTNS 670

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  326 ALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKStenhRLRRSIKKIT 405
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA----RLEAEVEQLE 746

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  406 QELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMEN---RYKSL---LSESNKKLHNQEQVI 479
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELraeLTLLNEEAANLRERL 826

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  480 KHLTESTNQKdvllqkfnEKDLEVIQQNcylmaAEDLELRSEGLITEKCSSQQPPgsKTIFSKEKKQSSDYEELIQVLKK 559
Cdd:TIGR02168  827 ESLERRIAAT--------ERRLEDLEEQ-----IEELSEDIESLAAEIEELEELI--EELESELEALLNERASLEEALAL 891

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462625347  560 EQDIYTHLVKSLQESDsiNNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIR 616
Cdd:TIGR02168  892 LRSELEELSEELRELE--SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-622 1.33e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 63.16  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   59 NMKDFENQITELKKENFNLKLRIYFLEERMQQefhgpTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEag 138
Cdd:PRK03918   156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKR-----TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-- 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  139 gsEIQRVKEDARKKVQqvedlLTKRILLLEKDVTAaqaelekafagtetekalrlrLESKLSEMKKMHEGDLAMALVLDE 218
Cdd:PRK03918   229 --EVKELEELKEEIEE-----LEKELESLEGSKRK---------------------LEEKIRELEERIEELKKEIEELEE 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  219 KDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVS--SGELRGLCA--APREEKERETEaaqmEHQKERNSFQERIQA 294
Cdd:PRK03918   281 KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSrlEEEINGIEEriKELEEKEERLE----ELKKKLKELEKRLEE 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  295 LEEDLREKEReiATEKKNSLKRDKA------IQGLTMALKSKEKKVEELNSEIEKLSAAFA--KAREALQKAQTQEFQGS 366
Cdd:PRK03918   357 LEERHELYEE--AKAKKEELERLKKrltgltPEKLEKELEELEKAKEEIEEEISKITARIGelKKEIKELKKAIEELKKA 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  367 EDyETALSGKEaLSAALRSQNLTKST-ENHRLRRSIKKITQELSDLQQERERLEKDLEEAHR---EKSKGDcTIRDLRNE 442
Cdd:PRK03918   435 KG-KCPVCGRE-LTEEHRKELLEEYTaELKRIEKELKEIEEKERKLRKELRELEKVLKKESElikLKELAE-QLKELEEK 511

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  443 VEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLmaaEDLELRSEG 522
Cdd:PRK03918   512 LKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVE 588

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  523 LITEKCSSQQPPGSKtiFSKEKKQSSDYEELIQVLKKEQDiythlvkslQESDSINNLQAELNKIFALRKQLEQ-----D 597
Cdd:PRK03918   589 ELEERLKELEPFYNE--YLELKDAEKELEREEKELKKLEE---------ELDKAFEELAETEKRLEELRKELEElekkyS 657

                          570       580
                   ....*....|....*....|....*
gi 2462625347  598 VLSYQNLRKTLEEQISEIRRREESF 622
Cdd:PRK03918   658 EEEYEELREEYLELSRELAGLRAEL 682
PTZ00121 PTZ00121
MAEBL; Provisional
 85-675 2.06e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 2.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   85 EERMQQEFHGPTEHIYKtnIELKVEVESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKRI 164
Cdd:PTZ00121  1113 EARKAEEAKKKAEDARK--AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKA 1190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  165 LLLEKDVTAAQAE-LEKAFAGTETEKALRLRLESKLSEMKKMHEGDL-AMALVLDEKDRLIEELKLSLKSKEALIQ---- 238
Cdd:PTZ00121  1191 EELRKAEDARKAEaARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKdAEEAKKAEEERNNEEIRKFEEARMAHFArrqa 1270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  239 CLKEEKSQMAcpDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFQERIQALE-----EDLREKEREiaTEKKNS 313
Cdd:PTZ00121  1271 AIKAEEARKA--DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakkkaDAAKKKAEE--AKKAAE 1346

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  314 LKRDKAIQGLTMALKSKEKK--VEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKS 391
Cdd:PTZ00121  1347 AAKAEAEAAADEAEAAEEKAeaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  392 TENHRLRRSIKKITQEL---------SDLQQERERLEKDLEEAHR---------EKSKGDctirDLRNEVEKLRNEVNER 453
Cdd:PTZ00121  1427 AEEKKKADEAKKKAEEAkkadeakkkAEEAKKAEEAKKKAEEAKKadeakkkaeEAKKAD----EAKKKAEEAKKKADEA 1502

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  454 EKAMENRYKSLLSESNKKLHNQEQVIKhlTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQP 533
Cdd:PTZ00121  1503 KKAAEAKKKADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  534 PGSKTIFSKEKKQssdYEELIQVLKKEQDIYTHLVKSLQE----SDSINNLQAELNKIFALRKQLEQDVLSYQNLRKtlE 609
Cdd:PTZ00121  1581 RKAEEAKKAEEAR---IEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK--A 1655

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462625347  610 EQISEIRRREESFSLYSDQTSYLSICLEENNRFQVEH--FSQEELKKKVSDLIQLVKELYTDNQHLKK 675
Cdd:PTZ00121  1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEalKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
147-666 2.98e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.00  E-value: 2.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  147 EDARKKVQQVEDLLTKRILLLEKDVtAAQAELEKAFAGTETEKALRLR----LESKLSEMKKMHEGDLAMALVLDEKDRL 222
Cdd:PRK03918   161 ENAYKNLGEVIKEIKRRIERLEKFI-KRTENIEELIKEKEKELEEVLReineISSELPELREELEKLEKEVKELEELKEE 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  223 IEELKLSLKSKEALIQCLKEEKSQMAcpdenvssgelRGLCAAPREEKERETEAAQMEHQKERNSFQERIQALEEDLREK 302
Cdd:PRK03918   240 IEELEKELESLEGSKRKLEEKIRELE-----------ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  303 EREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLS---AAFAKAREALQKAQTQEFQgSEDYETALSGKEAL 379
Cdd:PRK03918   309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEE-LERLKKRLTGLTPE 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  380 SAALRSQNLTKSTEnhRLRRSIKKITQELSDLQQERERLEKDLEEAhrEKSKGDCTI--RDLRNE-----VEKLRNEVNE 452
Cdd:PRK03918   388 KLEKELEELEKAKE--EIEEEISKITARIGELKKEIKELKKAIEEL--KKAKGKCPVcgRELTEEhrkelLEEYTAELKR 463

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  453 REKAMEnRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVL---------LQKFNEKDLEVIQQNCYLMAAEDLELRSEGL 523
Cdd:PRK03918   464 IEKELK-EIEEKERKLRKELRELEKVLKKESELIKLKELAeqlkeleekLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  524 ITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQEsdSINNLQAELNKIFALrKQLEQDVLSYQN 603
Cdd:PRK03918   543 SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE--RLKELEPFYNEYLEL-KDAEKELEREEK 619

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462625347  604 LRKTLEEQISEIRrreESFSLYSDQTSYLSICLEENNRfqveHFSQEELKKKVSDLIQLVKEL 666
Cdd:PRK03918   620 ELKKLEEELDKAF---EELAETEKRLEELRKELEELEK----KYSEEEYEELREEYLELSREL 675
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 116-679 5.06e-09

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: 61.60  E-value: 5.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  116 ELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLL---------TKRILLLEKDVTAAQAELEKA--FAG 184
Cdd:TIGR00606  416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIkelqqlegsSDRILELDQELRKAERELSKAekNSL 495

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  185 TETEKALRLRLES-KLSEMKKMHEGDLAMALVLDEKDRLIEELKLSlKSKEALIQCLKEEKSQmacpdenvSSGELRGLC 263
Cdd:TIGR00606  496 TETLKKEVKSLQNeKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT-KDKMDKDEQIRKIKSR--------HSDELTSLL 566

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  264 AAPREEKEREteaaqmehqKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEiEK 343
Cdd:TIGR00606  567 GYFPNKKQLE---------DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QD 636

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  344 LSAAFAKAREALQKAQTQefqgsedyETALSGKEALSAALRSQNLTKSTE----NHRLRRSIKKITQELSDLQQERERLE 419
Cdd:TIGR00606  637 EESDLERLKEEIEKSSKQ--------RAMLAGATAVYSQFITQLTDENQSccpvCQRVFQTEAELQEFISDLQSKLRLAP 708

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  420 KDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAmenrykslLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEK 499
Cdd:TIGR00606  709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE--------IPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  500 ---------DLEVIQQncYLMAAEDLELRSEGLITEkcsSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDiythLVKS 570
Cdd:TIGR00606  781 eesakvcltDVTIMER--FQMELKDVERKIAQQAAK---LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL----NRKL 851

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  571 LQE-SDSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREESFSLYSDQTSYLSICLEENNRFQVEHFS- 648
Cdd:TIGR00606  852 IQDqQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISs 931

                          570       580       590
                   ....*....|....*....|....*....|.
gi 2462625347  649 QEELKKKVSDLIQLVKELYTDNQHLKKTIFD 679
Cdd:TIGR00606  932 KETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-484 8.10e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 8.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   59 NMKDFENQITELKKENFNLKLRIYFLEERMQQ-EFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEA 137
Cdd:PRK03918   253 SKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  138 GGSEIQRVKEDARKKVQQVEDL--LTKRILLLEkDVTAAQAELE---KAFAGTETEKalrlrLESKLSEMKKMHEgdlAM 212
Cdd:PRK03918   333 LEEKEERLEELKKKLKELEKRLeeLEERHELYE-EAKAKKEELErlkKRLTGLTPEK-----LEKELEELEKAKE---EI 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  213 ALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQmaCPdenvssgelrgLCAAPREEKERETEAAqmEHQKERNSFQERI 292
Cdd:PRK03918   404 EEEISKITARIGELKKEIKELKKAIEELKKAKGK--CP-----------VCGRELTEEHRKELLE--EYTAELKRIEKEL 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  293 QALEEDLREKEREIATEKKNSLKRDKAIQGLTMA--LKSKEKKVEELNSE-IEKLSAAFAKAREALQKAQTQ------EF 363
Cdd:PRK03918   469 KEIEEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEikslkkEL 548

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  364 QGSEDYEtalSGKEALSAALRSQNLTKSTENHRLRR------------------------SIKKITQELSDLQQERERLE 419
Cdd:PRK03918   549 EKLEELK---KKLAELEKKLDELEEELAELLKELEElgfesveeleerlkelepfyneylELKDAEKELEREEKELKKLE 625

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625347  420 KDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNERE-KAMENRYKSLLSESNKKLHNQEQVIKHLTE 484
Cdd:PRK03918   626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREE 691
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 218-562 1.03e-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: 60.47  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  218 EKDRLiEELKLSLKSKEALIQCLKEEKSQMacpdENVSSGELRGLCAAPREEKERETEAAQMEhqKERNSFQERIQALEE 297
Cdd:TIGR02169  672 EPAEL-QRLRERLEGLKRELSSLQSELRRI----ENRLDELSQELSDASRKIGEIEKEIEQLE--QEEEKLKERLEELEE 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  298 DLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEEL-----NSEIEKLSAAFAKAREALQKAQTQefqgSEDYETA 372
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEAR----LREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  373 LSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREkskgdctIRDLRNEVEKLRNEVNE 452
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-------LRDLESRLGDLKKERDE 893

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  453 REK---AMENRYKSLLSESNKKLHNQEQvikhLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGlITEKCS 529
Cdd:TIGR02169  894 LEAqlrELERKIEELEAQIEKKRKRLSE----LKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR-VEEEIR 968

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 2462625347  530 SQQPPGSKTI--FSKEKKQSSDYEELIQVLKKEQD 562
Cdd:TIGR02169  969 ALEPVNMLAIqeYEEVLKRLDELKEKRAKLEEERK 1003
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 268-523 1.32e-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: 60.07  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  268 EEKERETEAAQMEHQKERNSFQERIQALEEDL-------REKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSE 340
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  341 IEKLSAAF---------AKAREALQKAQTQEFQGS-EDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSD 410
Cdd:TIGR02168  318 LEELEAQLeeleskldeLAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  411 LQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRyksllsESNKKLHNQEQVIKHLTESTNQKD 490
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE------ELEELQEELERLEEALEELREELE 471

                          250       260       270
                   ....*....|....*....|....*....|...
gi 2462625347  491 VLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGL 523
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQENLEGF 504
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 141-429 3.05e-08

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: 58.60  E-value: 3.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  141 EIQRVKEDARKKVQQVEdlltkRILLLEKDVTAAQAELEKAFA--------GTETEKAL-RLRLESKLSEMKKMHEGDLA 211
Cdd:pfam17380  297 EQERLRQEKEEKAREVE-----RRRKLEEAEKARQAEMDRQAAiyaeqermAMERERELeRIRQEERKRELERIRQEEIA 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  212 MALV-LDEKDRLIEE-----------------LKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLcaapREEKERE 273
Cdd:pfam17380  372 MEISrMRELERLQMErqqknervrqeleaarkVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL----EEERARE 447

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  274 TEAAQMEHQkERNSFQERIQALEEDLREKEREIATEKKnslKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKARE 353
Cdd:pfam17380  448 MERVRLEEQ-ERQQQVERLRQQEEERKRKKLELEKEKR---DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEME 523

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625347  354 ALQKAQTQEFQGSEDYETALSGKEAlsaalrsqnltksTENHRLRRSIKKITQELSDL---QQERERLEKDLEEAHREK 429
Cdd:pfam17380  524 ERQKAIYEEERRREAEEERRKQQEM-------------EERRRIQEQMRKATEERSRLeamEREREMMRQIVESEKARA 589
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 61-506 5.61e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 57.72  E-value: 5.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   61 KDFENQITELKKENFNLKLRIyfleERMQQEFHGPTEHIYKTN---IELKVEVESLKRELQEREQLLIKASKAVESLaEA 137
Cdd:TIGR04523  214 KSLESQISELKKQNNQLKDNI----EKKQQEINEKTTEISNTQtqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL-EK 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  138 GGSEIQRVKEDARK-KVQQVEDLLTKRILLLEKDVTAAQAELekafagTETEKALRlRLESKLSEMKKMhegdlamalvL 216
Cdd:TIGR04523  289 QLNQLKSEISDLNNqKEQDWNKELKSELKNQEKKLEEIQNQI------SQNNKIIS-QLNEQISQLKKE----------L 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  217 DEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVssgelrglcaaprEEKERETEAAQMEHQKERNSFQERIQALE 296
Cdd:TIGR04523  352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL-------------ESQINDLESKIQNQEKLNQQKDEQIKKLQ 418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  297 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKlsaafakarealQKAQTQEFQGSedYETALSGK 376
Cdd:TIGR04523  419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES------------LETQLKVLSRS--INKIKQNL 484

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  377 EALSAALRSqnltKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNereka 456
Cdd:TIGR04523  485 EQKQKELKS----KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK----- 555

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 2462625347  457 mENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQ 506
Cdd:TIGR04523  556 -KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 105-618 1.04e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  105 ELKVEVESLKRELQEREQLLIKASKAVESLAEaggsEIQRVKEDARKKVQQVEDLLTKRILLLE--KDVTAAQAELEKAF 182
Cdd:COG1196    250 ELEAELEELEAELAELEAELEELRLELEELEL----ELEEAQAEEYELLAELARLEQDIARLEErrRELEERLEELEEEL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  183 AGTETEKALRLRLESKLSEMKKMHEGDLAMAlvldeKDRLIEELKLSLKSKEALIQCLKEEKSqmacpdenvssgelrgl 262
Cdd:COG1196    326 AELEEELEELEEELEELEEELEEAEEELEEA-----EAELAEAEEALLEAEAELAEAEEELEE----------------- 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  263 caapREEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIE 342
Cdd:COG1196    384 ----LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  343 KLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQN-LTKSTENHRLRRSIKKITQELSDLQQERERLEKD 421
Cdd:COG1196    460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  422 LEEA---------HREKSKGDCTIRDLRNE----VEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQ 488
Cdd:COG1196    540 LEAAlaaalqnivVEDDEVAAAAIEYLKAAkagrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLG 619

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  489 KDVLLQKFNEKDLEVIQqncYLMAAEDLELRSEGLITEkcsSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLV 568
Cdd:COG1196    620 DTLLGRTLVAARLEAAL---RRAVTLAGRLREVTLEGE---GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  569 KSLQESDSINNLQAELNKIFALRKQLEQDVLSYQNL--------------------------------RKTLEEQISEIR 616
Cdd:COG1196    694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQleaereelleelleeeelleeealeelpeppdLEELERELERLE 773


                   ..
gi 2462625347  617 RR 618
Cdd:COG1196    774 RE 775
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 268-458 2.19e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.22  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  268 EEKERETEAAQMEHQKERNSFQERIQALEEDLrekerEIATEKKNSLKrdKAIQGLTMALKSKEKKVEELNSEIEKLSAA 347
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDALQAEL-----EELNEEYNELQ--AELEALQAEIDKLQAEIAEAEAEIEERREE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  348 FAKAREALQKAQTQ-----EFQGSEDYETALSGKEALSAALRSQNltksTENHRLRRSIKKITQELSDLQQERERLEKDL 422
Cdd:COG3883     88 LGERARALYRSGGSvsyldVLLGSESFSDFLDRLSALSKIADADA----DLLEELKADKAELEAKKAELEAKLAELEALK 163

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462625347  423 EEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAME 458
Cdd:COG3883    164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 56-474 2.37e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   56 RARNMKDFENQITELKKENFNLKLRIYFLE---ERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLL-------- 124
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriaqlsk 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  125 -IKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTK---RILLLEKDVTAAQAELekafagtETEKALRLRLESKLS 200
Cdd:TIGR02168  755 eLTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAEL-------TLLNEEAANLRERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  201 EMKKMHEgdlamalvldEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdenvssgelrglCAAPREEKERETEaaqmE 280
Cdd:TIGR02168  828 SLERRIA----------ATERRLEDLEEQIEELSEDIESLAAEIEE----------------LEELIEELESELE----A 877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  281 HQKERNSFQERIQALEEDLREKEREIatekknslkrdkaiqgltmalKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT 360
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEEL---------------------RELESKRSELRRELEELREKLAQLELRLEGLEV 936

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  361 --QEFQG--SEDYETALSGKEALSAALrsqnltkSTENHRLRRSIKKITQELSDL-----------QQERERLEKDLEEa 425
Cdd:TIGR02168  937 riDNLQErlSEEYSLTLEEAEALENKI-------EDDEEEARRRLKRLENKIKELgpvnlaaieeyEELKERYDFLTAQ- 1008

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2462625347  426 hrekskgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHN 474
Cdd:TIGR02168 1009 ----------KEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQR 1047
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
166-618 2.76e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.54  E-value: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  166 LLEKDVTAAQAELEKAFAGTETEKALRLR-LESKLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEK 244
Cdd:COG4717     46 MLLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  245 SQMACPDENVS-SGELRGLCAAPREEKERETEAAQMEHQKERNsfQERIQALEEDLREKEREIATEKKNSLKR------- 316
Cdd:COG4717    126 QLLPLYQELEAlEAELAELPERLEELEERLEELRELEEELEEL--EAELAELQEELEELLEQLSLATEEELQDlaeelee 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  317 -DKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEF------------QGSEDYETALSGKEALSA-- 381
Cdd:COG4717    204 lQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLvl 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  382 ---ALRSQNLTKSTENHRLRRSIKKITQELSDLQQerERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAME 458
Cdd:COG4717    284 gllALLFLLLAREKASLGKEAEELQALPALEELEE--EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  459 NRyksllsesnkKLHNQEQVIKHLTESTNQKDV--LLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGS 536
Cdd:COG4717    362 EL----------QLEELEQEIAALLAEAGVEDEeeLRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  537 KTIFSKEKKQSSDYEELIQVLKKEQDIyTHLVKSLQESDSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIR 616
Cdd:COG4717    432 EELEELEEELEELEEELEELREELAEL-EAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510


                   ..
gi 2462625347  617 RR 618
Cdd:COG4717    511 EE 512
PTZ00121 PTZ00121
MAEBL; Provisional
 85-612 2.81e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 2.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   85 EERMQQEFHGPTEHIYKTNiELKVEVESLKRELQEreqlLIKASKAVESLAEAGGSEIQRVKEDARKKVQQvedlltkri 164
Cdd:PTZ00121  1468 EAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADE----AKKAAEAKKKADEAKKAEEAKKADEAKKAEEA--------- 1533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  165 lllEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHEGDLAMALvldekdRLIEELKLSLKSKEALIQCLKEEK 244
Cdd:PTZ00121  1534 ---KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL------RKAEEAKKAEEARIEEVMKLYEEE 1604

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  245 SQMACPDenvssgelrglcaAPREEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKaiqgLT 324
Cdd:PTZ00121  1605 KKMKAEE-------------AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE----EA 1667

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  325 MALKSKEKKVEEL-NSEIEKLSAAFAKAREALQKAQTQEFQGSEDYET----ALSGKEALSAALRSQNLTKSTENHRLRR 399
Cdd:PTZ00121  1668 KKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkkaeELKKAEEENKIKAEEAKKEAEEDKKKAE 1747

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  400 SIKKITQELSDLQQERERLEKDLEEAHREKSKgdCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLsESNKKLHNQEQVI 479
Cdd:PTZ00121  1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA--VIEEELDEEDEKRRMEVDKKIKDIFDNFANII-EGGKEGNLVINDS 1824

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  480 KHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEdlelrseglitekcsSQQPPGSKTIFSKEKKQSSDYEELIQvlkk 559
Cdd:PTZ00121  1825 KEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNE---------------NGEDGNKEADFNKEKDLKEDDEEEIE---- 1885

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462625347  560 EQDIYTHLVKSLQESDSINNLQAELNKIFALRKqLEQDVLSYQNLRKTLEEQI 612
Cdd:PTZ00121  1886 EADEIEKIDKDDIEREIPNNNMAGKNNDIIDDK-LDKDEYIKRDAEETREEII 1937
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 267-471 4.96e-07

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: 54.74  E-value: 4.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  267 REEKERETE------------AAQMEHQKERNSFQERIqALEEDlREKEREIATEKKNSLKRDKAiQGLTMALkSKEKKV 334
Cdd:pfam17380  305 KEEKAREVErrrkleeaekarQAEMDRQAAIYAEQERM-AMERE-RELERIRQEERKRELERIRQ-EEIAMEI-SRMREL 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  335 EELNSEIEKLSAafaKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLR----RSIKKITQELSD 410
Cdd:pfam17380  381 ERLQMERQQKNE---RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEeeraREMERVRLEEQE 457

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462625347  411 LQQERERLEKDLEEAHREKSKGDCTIRDlRNEVEKLRNEVNEREkaMENRYKSLLSESNKK 471
Cdd:pfam17380  458 RQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKE--LEERKQAMIEEERKR 515
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
119-403 8.59e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 8.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  119 EREQLLIKASKAVESLAEAggSEIQRVKEDARKKVQQVEDLLtkrilllekdvtAAQAELEKAFAGTETEKALRLRLESK 198
Cdd:COG4913    219 EEPDTFEAADALVEHFDDL--ERAHEALEDAREQIELLEPIR------------ELAERYAAARERLAELEYLRAALRLW 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  199 LSEMKkmhegdlamalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrglcaaprEEKERETEAAQ 278
Cdd:COG4913    285 FAQRR------------LELLEAELEELRAELARLEAELERLEARLDAL--------------------REELDELEAQI 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  279 MEHQkernsfQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKA 358
Cdd:COG4913    333 RGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2462625347  359 QTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKK 403
Cdd:COG4913    407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 210-431 1.06e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  210 LAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMAcpdenvssGELRGLcaaprEEKERETEAAQMEHQKERNSFQ 289
Cdd:COG4942     16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL--------KQLAAL-----ERRIAALARRIRALEQELAALE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  290 ERIQALEEDLREKEREIATEKKNSLKRDKAIQ------GLTMALKSKE--------KKVEELNSEIEKLSAAFAKAREAL 355
Cdd:COG4942     83 AELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAEL 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625347  356 QKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSK 431
Cdd:COG4942    163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
142-458 2.21e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.73  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  142 IQRVKEDARKKVQQVEDL--------LTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHE------ 207
Cdd:PRK02224   178 VERVLSDQRGSLDQLKAQieekeekdLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREeletle 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  208 ---GDLAMALVLDEKDRliEELKLSLKSKEALIQCLKEEKSQMAcPDENVSSGELRGLCAAPREEKERETE--------- 275
Cdd:PRK02224   258 aeiEDLRETIAETERER--EELAEEVRDLRERLEELEEERDDLL-AEAGLDDADAEAVEARREELEDRDEElrdrleecr 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  276 AAQMEHQKERNSFQERIQALEE---DLREKEREIATEkknslkrdkaIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAR 352
Cdd:PRK02224   335 VAAQAHNEEAESLREDADDLEEraeELREEAAELESE----------LEEAREAVEDRREEIEELEEEIEELRERFGDAP 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  353 EALQKAQTQEFQGSEDYEtALSGKEA-LSAALRS---------------------QNLTKSTENHRL---RRSIKKITQE 407
Cdd:PRK02224   405 VDLGNAEDFLEELREERD-ELREREAeLEATLRTarerveeaealleagkcpecgQPVEGSPHVETIeedRERVEELEAE 483

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462625347  408 LSDLQQERERLEKDLEEAH--REKSKGDCTIRDLRNEVEKL----RNEVNEREKAME 458
Cdd:PRK02224   484 LEDLEEEVEEVEERLERAEdlVEAEDRIERLEERREDLEELiaerRETIEEKRERAE 540
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 290-623 2.57e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  290 ERIQALEEDLREKEREIatekknslkrdkaiqgLTMALKSKEKKVEELNSEIEKlsaafakarealqkAQTQEfqgsEDY 369
Cdd:TIGR02168  213 ERYKELKAELRELELAL----------------LVLRLEELREELEELQEELKE--------------AEEEL----EEL 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  370 ETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNE 449
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  450 VNEREKAME------NRYKSLLSESNKKLHNQEQVIKHL-TESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEG 522
Cdd:TIGR02168  339 LAELEEKLEelkeelESLEAELEELEAELEELESRLEELeEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  523 LITEKCSSQQPPGSKtifsKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQEsdsinnLQAELNKIFALRKQLEQDVLSYQ 602
Cdd:TIGR02168  419 LQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEELERLEEALEE------LREELEEAEQALDAAERELAQLQ 488

                          330       340
                   ....*....|....*....|.
gi 2462625347  603 NLRKTLEeqisEIRRREESFS 623
Cdd:TIGR02168  489 ARLDSLE----RLQENLEGFS 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 84-423 2.60e-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: 52.76  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   84 LEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAE--AGGSEIQRVKEDARKKVQQVEdllt 161
Cdd:TIGR02169  689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleEDLSSLEQEIENVKSELKELE---- 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  162 KRILLLEKDVTAAQAELEKafagtetekalrlrLESKLSEMKkmhegdlamalvLDEKDRLIEELKLSLKSKEALIQCLK 241
Cdd:TIGR02169  765 ARIEELEEDLHKLEEALND--------------LEARLSHSR------------IPEIQAELSKLEEEVSRIEARLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  242 EEksqmacpdENVSSGELRGLcaapreEKERETEAAQMEHQKER-NSFQERIQALEEDLREKEREiatekknslkrdkai 320
Cdd:TIGR02169  819 QK--------LNRLTLEKEYL------EKEIQELQEQRIDLKEQiKSIEKEIENLNGKKEELEEE--------------- 869

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  321 qgltmaLKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALR--SQNLTKSTENHRLR 398
Cdd:TIGR02169  870 ------LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELSEIEDPKGED 943

                          330       340
                   ....*....|....*....|....*
gi 2462625347  399 RSIKKITQELSDLQQERERLEKDLE 423
Cdd:TIGR02169  944 EEIPEEELSLEDVQAELQRVEEEIR 968
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
105-452 5.23e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.58  E-value: 5.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  105 ELKVEVESLKRELQEREQLLiKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKrillLEKDVTAAQAELEKAFAG 184
Cdd:PRK02224   430 ELEATLRTARERVEEAEALL-EAGKCPECGQPVEGSPHVETIEEDRERVEELEAELED----LEEEVEEVEERLERAEDL 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  185 TETEKalrlRLESKLSEMKKMHEgdlamalvldekdrLIEELKLSLKSKEALIQCLKEEKSQMACPDEnvssgELRGLCA 264
Cdd:PRK02224   505 VEAED----RIERLEERREDLEE--------------LIAERRETIEEKRERAEELRERAAELEAEAE-----EKREAAA 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  265 APREEKERETEAAQmEHQKERNSFQERIQALE----------------EDLREKEREIATekKNSLKRDKaiqgltmaLK 328
Cdd:PRK02224   562 EAEEEAEEAREEVA-ELNSKLAELKERIESLErirtllaaiadaedeiERLREKREALAE--LNDERRER--------LA 630

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  329 SKEKKVEELNSEIEklSAAFAKAREalQKAQTQEFQgsEDYETALSGKEALSAALrsQNLTKSTENhrlrrSIKkitqEL 408
Cdd:PRK02224   631 EKRERKRELEAEFD--EARIEEARE--DKERAEEYL--EQVEEKLDELREERDDL--QAEIGAVEN-----ELE----EL 693

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462625347  409 SDLQQERERLE---KDLEEAHREKSKGDCTIRDLRNE-----VEKLRNEVNE 452
Cdd:PRK02224   694 EELRERREALEnrvEALEALYDEAEELESMYGDLRAElrqrnVETLERMLNE 745
PRK01156 PRK01156
chromosome segregation protein; Provisional
 129-666 5.30e-06

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 51.44  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  129 KAVESLAEAGGSEIQRVKEDARKKVQQVEDL------LTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEM 202
Cdd:PRK01156   172 KDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqiadDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  203 KKMH------EGDLAMALVLDEKDRLIEELKLSL------KSKEALIQCLK-----EEKSQMAcpdENVSsGELRGLCAA 265
Cdd:PRK01156   252 NRYEseiktaESDLSMELEKNNYYKELEERHMKIindpvyKNRNYINDYFKykndiENKKQIL---SNID-AEINKYHAI 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  266 PREEKERETEAAQMEHQKERnsfQERIQALEEDLREKEreiatEKKNSLKRDkaIQGLTMALKSKEKKVEELNSEI-EKL 344
Cdd:PRK01156   328 IKKLSVLQKDYNDYIKKKSR---YDDLNNQILELEGYE-----MDYNSYLKS--IESLKKKIEEYSKNIERMSAFIsEIL 397

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  345 SAAFAKArEALQKAQTQEFQGSEDYETALSGKEALSAALRsQNLTKSTENHRLR--RSI----------KKITQELSDLQ 412
Cdd:PRK01156   398 KIQEIDP-DAIKKELNEINVKLQDISSKVSSLNQRIRALR-ENLDELSRNMEMLngQSVcpvcgttlgeEKSNHIINHYN 475

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  413 QERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSEsnkkLHNQEQVIKHLTESTNQKDVL 492
Cdd:PRK01156   476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD----LEDIKIKINELKDKHDKYEEI 551

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  493 LQKFNEKDLeviqqncylmaaEDLELRSEGLIT--EKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKE-QDIYTHLVK 569
Cdd:PRK01156   552 KNRYKSLKL------------EDLDSKRTSWLNalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfPDDKSYIDK 619

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  570 SLQE-SDSINNLQAELNKIFALRKQLEQdvlsyqnLRKTLE---EQISEIRRREESFSLYSDQTSYLSICLEE-NNRFQV 644
Cdd:PRK01156   620 SIREiENEANNLNNKYNEIQENKILIEK-------LRGKIDnykKQIAEIDSIIPDLKEITSRINDIEDNLKKsRKALDD 692

                          570       580
                   ....*....|....*....|..
gi 2462625347  645 EHFSQEELKKKVSDLIQLVKEL 666
Cdd:PRK01156   693 AKANRARLESTIEILRTRINEL 714
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 105-366 1.13e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.76  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  105 ELKVEVESLKRELQEREQLLIKASKAVESLAEaggsEIQRVkEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAfag 184
Cdd:COG4942     24 EAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAEL--- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  185 TETEKALRLRLESKLSEMKKMHEGDLAMALV----LDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelr 260
Cdd:COG4942     96 RAELEAQKEELAELLRALYRLGRQPPLALLLspedFLDAVRRLQYLKYLAPARREQAEELRADLAEL------------- 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  261 glcaaprEEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLtmalkskEKKVEELNSE 340
Cdd:COG4942    163 -------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-------QQEAEELEAL 228

                          250       260
                   ....*....|....*....|....*.
gi 2462625347  341 IEKLSAAFAKAREALQKAQTQEFQGS 366
Cdd:COG4942    229 IARLEAEAAAAAERTPAAGFAALKGK 254
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 78-623 1.30e-05

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: 50.43  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   78 KLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVkEDARKKVQQVE 157
Cdd:TIGR00606  190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEI-EHNLSKIMKLD 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  158 DLLT---KRILLLEKDVTAAQAELEKAFAGTETE---------KALRLRLESKLSEMKKMHEGDLAMALVLDEKDRLIEE 225
Cdd:TIGR00606  269 NEIKalkSRKKQMEKDNSELELKMEKVFQGTDEQlndlyhnhqRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  226 L-KLSLKSKEALIQCLKEEKSQMacpdENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSfqERIQALEEDLREKER 304
Cdd:TIGR00606  349 QgRLQLQADRHQEHIRARDSLIQ----SLATRLELDGFERGPFSERQIKNFHTLVIERQEDEA--KTAAQLCADLQSKER 422

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  305 eIATEKKNSLKRDKAIQGLTMALKSK--EKKVEELNSEIEKLSAAFAKAREALQKaqTQEFQGSEDyETALSGKEALSAA 382
Cdd:TIGR00606  423 -LKQEQADEIRDEKKGLGRTIELKKEilEKKQEELKFVIKELQQLEGSSDRILEL--DQELRKAER-ELSKAEKNSLTET 498

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  383 LRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLeKDLEEAHREKSKGDCTIRD---------------------LRN 441
Cdd:TIGR00606  499 LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTR-TQMEMLTKDKMDKDEQIRKiksrhsdeltsllgyfpnkkqLED 577

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  442 EVEKLRNEVNErekaMENRykslLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIqqncylmAAEDLELRSE 521
Cdd:TIGR00606  578 WLHSKSKEINQ----TRDR----LAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC-------GSQDEESDLE 642

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  522 GLIT--EKCSSQQPP--GSKTIFSKEKKQSSDY--------EELIQVLKKEQDIYTHL-VKSLQESDSINNLQAELNKIF 588
Cdd:TIGR00606  643 RLKEeiEKSSKQRAMlaGATAVYSQFITQLTDEnqsccpvcQRVFQTEAELQEFISDLqSKLRLAPDKLKSTESELKKKE 722

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 2462625347  589 ALRKQLEQDVLSYQNLRKTLEEQISEIRRREESFS 623
Cdd:TIGR00606  723 KRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN 757
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 299-494 1.71e-05

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 48.99  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  299 LREKEREIATEKKNSLKRD-KAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYEtalsgke 377
Cdd:pfam09787   20 LQSKEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSR------- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  378 alsaalrsQNLTKSTENHRLRRSIKKITQ-ELSDLQQERERLEkdlEEAHREKSKGDCTIRDLRNEVEKLRNEVNEreka 456
Cdd:pfam09787   93 --------EQLQELEEQLATERSARREAEaELERLQEELRYLE---EELRRSKATLQSRIKDREAEIEKLRNQLTS---- 157

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462625347  457 menryKSLLSESNKKLhnqEQVIKHLTESTNQKDVLLQ 494
Cdd:pfam09787  158 -----KSQSSSSQSEL---ENRLHQLTETLIQKQTMLE 187
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 87-675 2.15e-05

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: 49.33  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   87 RMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAeaggSEIQRVKEDARKKVQQVEDLL-----T 161
Cdd:pfam05483   78 RLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQ----FENEKVSLKLEEEIQENKDLIkennaT 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  162 KRILLLEKDVTAAQAELEKAFAGTETE-KALRLRLESKLSEMKKMHEGDLAMAlvldEKDRLieELKLSLKSKEALIQCL 240
Cdd:pfam05483  154 RHLCNLLKETCARSAEKTKKYEYEREEtRQVYMDLNNNIEKMILAFEELRVQA----ENARL--EMHFKLKEDHEKIQHL 227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  241 KEEKSQMACPDENVSSgeLRGLCAAPREEKERETEAAQMEHQKERNSFQERIQALEEDLREkereiATEKKNSLKrdkai 320
Cdd:pfam05483  228 EEEYKKEINDKEKQVS--LLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE-----LIEKKDHLT----- 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  321 qgltmalkskeKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALsgkEALSAALRSQNLTKStenhRLRRS 400
Cdd:pfam05483  296 -----------KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQM---EELNKAKAAHSFVVT----EFEAT 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  401 IKKITQELSDLQQERERLEKDLEEAHREKSKGDctirdlrNEVEKLRNEVNEREKAMEnRYKSLLSESNKKLHNQEQVIK 480
Cdd:pfam05483  358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKS-------SELEEMTKFKNNKEVELE-ELKKILAEDEKLLDEKKQFEK 429

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  481 HLTE--STNQKDVLLQKFNEK---DLEV------IQQNCYLMAAEDL--ELRSEGLITEKCSSQqppgSKTIFSKEKKQS 547
Cdd:pfam05483  430 IAEElkGKEQELIFLLQAREKeihDLEIqltaikTSEEHYLKEVEDLktELEKEKLKNIELTAH----CDKLLLENKELT 505

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  548 SDYEELIQVLKKEQDiythlvkslqesDSINNLQAELNKIfalrKQLEQDVLSYQNLRKTLEEQISEIRRREESFSLYSD 627
Cdd:pfam05483  506 QEASDMTLELKKHQE------------DIINCKKQEERML----KQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD 569

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2462625347  628 QT-----SYLSICLEENNRFQVEHFSQEELKKKVSDLIQLVKELYTDNQHLKK 675
Cdd:pfam05483  570 KSeenarSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 216-619 2.16e-05

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: 49.66  E-value: 2.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  216 LDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAQMEHQKERNSFQERIQAL 295
Cdd:TIGR00606  718 LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERF 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  296 EEDLREKEREIATE--KKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ-GSEdyETA 372
Cdd:TIGR00606  798 QMELKDVERKIAQQaaKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElKSE--KLQ 875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  373 LSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQErerLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNE 452
Cdd:TIGR00606  876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF---LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  453 REKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNekdleviqqncylmaaEDLELRSEGLITEKCSSQQ 532
Cdd:TIGR00606  953 IHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN----------------EDMRLMRQDIDTQKIQERW 1016

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  533 PPGSKTIFSKEKKQSSDYEELIQVLKK-EQDIYTHLVKSLQE-SDSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEE 610
Cdd:TIGR00606 1017 LQDNLTLRKRENELKEVEEELKQHLKEmGQMQVLQMKQEHQKlEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQF 1096


                   ....*....
gi 2462625347  611 QISEIRRRE 619
Cdd:TIGR00606 1097 RDAEEKYRE 1105
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
64-456 2.91e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 2.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   64 ENQITELKKENFNLKLRIYFLEERMQQEfhgpteHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEAGgSEIQ 143
Cdd:COG4717     94 QEELEELEEELEELEAELEELREELEKL------EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELE-EELE 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  144 RVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHEgDLAMALVLDEKDRLI 223
Cdd:COG4717    167 ELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-QLENELEAAALEERL 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  224 EELKLSLKSKEALIQCLKEEKSQMACPDEN------VSSGELRGLCAAPREEKERETEAAQMEHQKERNSF-QERIQALE 296
Cdd:COG4717    246 KEARLLLLIAAALLALLGLGGSLLSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELeEEELEELL 325

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  297 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEK---LSAAFAKAREALQKAQTQefqgSEDYETAL 373
Cdd:COG4717    326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAALEQ----AEEYQELK 401

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  374 SGKEALSAALRsqNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSK---------GDCTIRDLRNEVE 444
Cdd:COG4717    402 EELEELEEQLE--ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEleaeleqleEDGELAELLQELE 479

                          410
                   ....*....|..
gi 2462625347  445 KLRNEVNEREKA 456
Cdd:COG4717    480 ELKAELRELAEE 491
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 105-346 3.28e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 3.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  105 ELKVEVESLKRELQEREQLLIKASKAVESLaeaGGSEIQRVKEDARKkvqqvedlLTKRILLLEKDVTAAQAELEKAfag 184
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKIKDL---GEEEQLRVKEKIGE--------LEAEIASLERSIAEKERELEDA--- 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  185 TETEKALRLRLESKLSEMKKMhEGDLAMALVldEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSS-------- 256
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEEL-EREIEEERK--RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDyreklekl 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  257 ----GELRGLCAAPREEKERETEA-AQMEHQKER-----NSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMA 326
Cdd:TIGR02169  398 kreiNELKRELDRLQEELQRLSEElADLNAAIAGieakiNELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477

                          250       260
                   ....*....|....*....|
gi 2462625347  327 LKSKEKKVEELNSEIEKLSA 346
Cdd:TIGR02169  478 YDRVEKELSKLQRELAEAEA 497
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 271-464 3.84e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 47.23  E-value: 3.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  271 ERETEAAQMEHQkeRNSFQERIQALEEDLREKEREIATEKKnslkrdkaiqgltmALKSKEKKVEELNSEIEKLSAAFAK 350
Cdd:COG1579     14 ELDSELDRLEHR--LKELPAELAELEDELAALEARLEAAKT--------------ELEDLEKEIKRLELEIEEVEARIKK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  351 AREALQKAQTQefqgsEDYetalsgkEALSAALRSQNLTKSTENHRLRR---SIKKITQELSDLQQERERLEKDLEEAHR 427
Cdd:COG1579     78 YEEQLGNVRNN-----KEY-------EALQKEIESLKRRISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKA 145

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462625347  428 EKskgDCTIRDLRNEVEKLRNEVNEREKAMENRYKSL 464
Cdd:COG1579    146 EL---DEELAELEAELEELEAEREELAAKIPPELLAL 179
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-364 4.12e-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: 48.90  E-value: 4.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   69 ELKKENFNLKLRIYFLE---------------ERMQQEFHGPTEHIYKTNIEL------KVEVESLKRELQEREQLLika 127
Cdd:TIGR02168  217 ELKAELRELELALLVLRleelreeleelqeelKEAEEELEELTAELQELEEKLeelrleVSELEEEIEELQKELYAL--- 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  128 skaveslaeagGSEIQRVKEDARKKVQQVEDlltkrillLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHE 207
Cdd:TIGR02168  294 -----------ANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  208 GDLAMalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpdenvssgelrglcaapreEKERETEAAQMEHQKER-N 286
Cdd:TIGR02168  355 SLEAE---LEELEAELEELESRLEELEEQLETLRSKVAQL---------------------ELQIASLNNEIERLEARlE 410

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462625347  287 SFQERIQALEEDLREKEREIATEKKNSLKRDkaIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ 364
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 106-484 4.34e-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: 48.63  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  106 LKVEVESLKRELQEREQLLIKASKAVESLaeagGSEIQRVKEDARKKVQQVEDLLTkRILLLEKDVTAAQAELEKAFAGT 185
Cdd:pfam01576  438 LQSELESVSSLLNEAEGKNIKLSKDVSSL----ESQLQDTQELLQEETRQKLNLST-RLRQLEDERNSLQEQLEEEEEAK 512

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  186 ETEKALRLRLESKLSEMKKMHEGDLAMALVLDE-KDRL---IEELKLSLKSKEALIQCLKEEKS--QMACPDENVSSGEL 259
Cdd:pfam01576  513 RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEgKKRLqreLEALTQQLEEKAAAYDKLEKTKNrlQQELDDLLVDLDHQ 592

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  260 RGLCAApREEKERETEAAQMEHQKERNSFQERIQALEEDLREKER---------EIATEKKNSLKRDKAIQGLTMA--LK 328
Cdd:pfam01576  593 RQLVSN-LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETralslaralEEALEAKEELERTNKQLRAEMEdlVS 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  329 SKE---KKVEELNSEIEKLSAAFAKAREALQKAQtQEFQGSED---------------YETALSGKEALSAALRSQ---- 386
Cdd:pfam01576  672 SKDdvgKNVHELERSKRALEQQVEEMKTQLEELE-DELQATEDaklrlevnmqalkaqFERDLQARDEQGEEKRRQlvkq 750

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  387 --NLTKSTENHRLRRSI-----KKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRnevNEREKAMen 459
Cdd:pfam01576  751 vrELEAELEDERKQRAQavaakKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEAR---ASRDEIL-- 825

                          410       420
                   ....*....|....*....|....*
gi 2462625347  460 rykSLLSESNKKLHNQEQVIKHLTE 484
Cdd:pfam01576  826 ---AQSKESEKKLKNLEAELLQLQE 847
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 64-495 4.86e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 48.43  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   64 ENQITELKKENFNLKLRIYFLEERMQQEfhGPTEHIYKTNIELKVEVESLKRELQEREQLLIK-----ASKAVESLAEAG 138
Cdd:TIGR00618  448 TCTAQCEKLEKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGscihpNPARQDIDNPGP 525

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  139 GSEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMHEgdlamaLVLDE 218
Cdd:TIGR00618  526 LTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV------RLQDL 599

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  219 KDRLIEELKLSLKSKEALIQCLKEE--KSQMACPDENVSSGELRGLCAAPREE----KERETEAAQMEHQKERNSFQERi 292
Cdd:TIGR00618  600 TEKLSEAEDMLACEQHALLRKLQPEqdLQDVRLHLQQCSQELALKLTALHALQltltQERVREHALSIRVLPKELLASR- 678

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  293 QALEEDLREKEREIATEKKnslkrdkAIQGLTMALKSKEKKVEELNSEIEKLSAAfakarealQKAQTQEFQGSEDYETA 372
Cdd:TIGR00618  679 QLALQKMQSEKEQLTYWKE-------MLAQCQTLLRELETHIEEYDREFNEIENA--------SSSLGSDLAAREDALNQ 743

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  373 LSGKEALSAALRSQNLTKSTENHRLRRSIKKIT-QELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVN 451
Cdd:TIGR00618  744 SLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 2462625347  452 EREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQK 495
Cdd:TIGR00618  824 ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE 867
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 263-454 5.21e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.97  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  263 CAAPREEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIAtEKKNSLKRdkaiqgltmaLKSKEKKVEELNSEIE 342
Cdd:pfam07888   39 CLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQ----------SREKHEELEEKYKELS 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  343 KLSAAFAKAREALQKAQtqefqgsEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDL 422
Cdd:pfam07888  108 ASSEELSEEKDALLAQR-------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462625347  423 EEAHREkskgdctIRDLRNEVEKLRNEVNERE 454
Cdd:pfam07888  181 QQTEEE-------LRSLSKEFQELRNSLAQRD 205
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 221-573 5.40e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.43  E-value: 5.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  221 RLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELrglcAAPREEKERETEAAQMEHQKERNSFQ-------ERIQ 293
Cdd:pfam02463  123 ELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEE----AAGSRLKRKKKEALKKLIEETENLAEliidleeLKLQ 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  294 ALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETA- 372
Cdd:pfam02463  199 ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEe 278

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  373 ---------LSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEV 443
Cdd:pfam02463  279 kekklqeeeLKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE 358

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  444 EKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTE-STNQKDVLLQKFNEKDLEVIQQNcyLMAAEDLELRSEG 522
Cdd:pfam02463  359 EELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkSEEEKEAQLLLELARQLEDLLKE--EKKEELEILEEEE 436

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462625347  523 LITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQE 573
Cdd:pfam02463  437 ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
326-502 6.43e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 6.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  326 ALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ--EFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRS--- 400
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERreALQRLAEYSWDEIDVASAEREIAE----LEAELERLDASsdd 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  401 IKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIK 480
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766

                          170       180
                   ....*....|....*....|....
gi 2462625347  481 HLTESTNQKDVLLQKFN--EKDLE 502
Cdd:COG4913    767 LRENLEERIDALRARLNraEEELE 790
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
126-386 7.05e-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: 7.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  126 KASKAVESLAEAggsEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEkafagtetekalRLRLESKLSEMKKm 205
Cdd:COG3206    149 LAAAVANALAEA---YLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALE------------EFRQKNGLVDLSE- 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  206 hEGDLAMALvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQmacpdenvSSGELRGLCAAPREEKERETEA-AQMEHQKE 284
Cdd:COG3206    213 -EAKLLLQQ-LSELESQLAEARAELAEAEARLAALRAQLGS--------GPDALPELLQSPVIQQLRAQLAeLEAELAEL 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  285 RNSFQE---RIQALEEDLREKEREIATEKKNSL-KRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT 360
Cdd:COG3206    283 SARYTPnhpDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362

                          250       260
                   ....*....|....*....|....*.
gi 2462625347  361 QEfqgsEDYETALSGKEALSAALRSQ 386
Cdd:COG3206    363 AR----ELYESLLQRLEEARLAEALT 384
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 56-665 7.71e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 7.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   56 RARNMKDFENQITELKKENFNLKLRIYFLEERMQQEfhgpTEHIYKTNIELK----------VEVESLKRELQEREQLLI 125
Cdd:TIGR04523   66 DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKL----NSDLSKINSEIKndkeqknkleVELNKLEKQKKENKKNID 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  126 KASKAVESLaEAGGSEIQRVKEDARKKVQQVEDLLTKrillLEKDVTAAQAELEKAfagteteKALRLRLESKLSEMKKm 205
Cdd:TIGR04523  142 KFLTEIKKK-EKELEKLNNKYNDLKKQKEELENELNL----LEKEKLNIQKNIDKI-------KNKLLKLELLLSNLKK- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  206 hegdlamalvLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELRGLCAAPREEKERETEAAqmEHQKER 285
Cdd:TIGR04523  209 ----------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS--EKQKEL 276

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  286 NSFQERIQALEEDLREKEREIatEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQtQEFQG 365
Cdd:TIGR04523  277 EQNNKKIKELEKQLNQLKSEI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK-KELTN 353

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  366 SE----DYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSD--------------LQQERERLEKDLEEAHR 427
Cdd:TIGR04523  354 SEsensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNqeklnqqkdeqikkLQQEKELLEKEIERLKE 433

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  428 EKSKGDCTIRDLRNEV---EKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQkdvlLQKFNEKDLEVI 504
Cdd:TIGR04523  434 TIIKNNSEIKDLTNQDsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE----LKKLNEEKKELE 509

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  505 QQNCYLMAAED-LELRSEGLITEKcssqqppgsKTIFSKEKKQSSDYEELIQVLKKEQdiythLVKSLQESD-SINNLQA 582
Cdd:TIGR04523  510 EKVKDLTKKISsLKEKIEKLESEK---------KEKESKISDLEDELNKDDFELKKEN-----LEKEIDEKNkEIEELKQ 575

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  583 ELNKIFALRKQLEQDVLSYQNLRKTLEEQIseirrrEESFSLYSDQTSYLSICLEENNRFQVEHFSQEELKKKVSDLIQL 662
Cdd:TIGR04523  576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEI------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649


                   ...
gi 2462625347  663 VKE 665
Cdd:TIGR04523  650 IKE 652
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 282-618 9.28e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 47.16  E-value: 9.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  282 QKERNSFQERIQALEEDLREKEREIA----TEKKNSlkrdKAIQGLtmalkskEKKVEELNSEIEKLSAAFAKAREALQK 357
Cdd:pfam06160   85 KKALDEIEELLDDIEEDIKQILEELDelleSEEKNR----EEVEEL-------KDKYRELRKTLLANRFSYGPAIDELEK 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  358 AQTQEFQGSEDYETALSGKEALSAalRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHRE-KSKG---- 432
Cdd:pfam06160  154 QLAEIEEEFSQFEELTESGDYLEA--REVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREmEEEGyale 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  433 ----DCTIRDLRNEVEKLRN--------EVNEREKAMENR----YKSLLSESNKK---LHNQEQVIKHLTESTNQKDVLL 493
Cdd:pfam06160  232 hlnvDKEIQQLEEQLEENLAllenleldEAEEALEEIEERidqlYDLLEKEVDAKkyvEKNLPEIEDYLEHAEEQNKELK 311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  494 qkfneKDLEVIQQNcYLMAAEDLElRSEGLITEKcssqqppgsktifskeKKQSSDYEELIQVLKKEQDIYTHLVKSLQE 573
Cdd:pfam06160  312 -----EELERVQQS-YTLNENELE-RVRGLEKQL----------------EELEKRYDEIVERLEEKEVAYSELQEELEE 368

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 2462625347  574 S-DSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRR 618
Cdd:pfam06160  369 IlEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRL 414
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 40-596 9.68e-05

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: 47.51  E-value: 9.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   40 GNGLLPNVSEETVSptRARNMKDFENQITEL-----KKENFNLKLRIYfLEERMQQEFHGPTEHIYKTNIELK-VEVESL 113
Cdd:pfam10174  169 SKGLPKKSGEEDWE--RTRRIAEAEMQLGHLevlldQKEKENIHLREE-LHRRNQLQPDPAKTKALQTVIEMKdTKISSL 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  114 KRELQEREQLL-----------------IKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTK-------------R 163
Cdd:pfam10174  246 ERNIRDLEDEVqmlktngllhtedreeeIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKletltnqnsdckqH 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  164 ILLLEKDVTAAqaELEKAFAGTETEkALRLRLESKLSemkkmhegdlamalVLDEKDRLIEELKlslkskealiqclkEE 243
Cdd:pfam10174  326 IEVLKESLTAK--EQRAAILQTEVD-ALRLRLEEKES--------------FLNKKTKQLQDLT--------------EE 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  244 KSQMAcpdenvssGELRGLcaapreekereteaAQMEHQKER--NSFQERIQALEEDLREKEREIATEKK-------NSL 314
Cdd:pfam10174  375 KSTLA--------GEIRDL--------------KDMLDVKERkiNVLQKKIENLQEQLRDKDKQLAGLKErvkslqtDSS 432

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  315 KRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREAL--------QKAQTQEFQGSEDYETALSGKEALSaALRSQ 386
Cdd:pfam10174  433 NTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLkkenkdlkEKVSALQPELTEKESSLIDLKEHAS-SLASS 511

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  387 NLTKSTENHRLRRSIKKITQELSDLQQERERLEkDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMEnRYKSLLS 466
Cdd:pfam10174  512 GLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH-NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVE-RLLGILR 589

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  467 ESNKKLHNQEQVIKHLtESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQ 546
Cdd:pfam10174  590 EVENEKNDKDKKIAEL-ESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTR 668

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462625347  547 ssdyeeliQVLKKEQDIYTHLVKSLQESDSI-NNLQAElnkifaLRKQLEQ 596
Cdd:pfam10174  669 --------QELDATKARLSSTQQSLAEKDGHlTNLRAE------RRKQLEE 705
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
110-464 1.16e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  110 VESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKRILLlEKDVTAAQAELEKAFAGTETek 189
Cdd:PRK02224   312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL-ESELEEAREAVEDRREEIEE-- 388

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  190 alrlrLESKLSEMKKMHE------GDLA--MALVLDEKDRLIE---ELKLSLKSKEALIQCLKEEKSQMACPDENVSSGE 258
Cdd:PRK02224   389 -----LEEEIEELRERFGdapvdlGNAEdfLEELREERDELREreaELEATLRTARERVEEAEALLEAGKCPECGQPVEG 463

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  259 LRGLCAAPREEKERETEAAQMEHQK-ERNSFQERIQALEeDLREKEREIAT--EKKNSLKRDKAIQGLTM-----ALKSK 330
Cdd:PRK02224   464 SPHVETIEEDRERVEELEAELEDLEeEVEEVEERLERAE-DLVEAEDRIERleERREDLEELIAERRETIeekreRAEEL 542

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  331 EKKVEELNSEIEKLSAAFAKAREALQKAQ-------------TQEFQGSEDYETALSGKEALSAAL-----RSQNLTKST 392
Cdd:PRK02224   543 RERAAELEAEAEEKREAAAEAEEEAEEAReevaelnsklaelKERIESLERIRTLLAAIADAEDEIerlreKREALAELN 622

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  393 ENHR-----LRRSIKKITQE-----LSDLQQERERLEK-------DLEEAHREKSKGDCTIRDLRNEVEKLrNEVNEREK 455
Cdd:PRK02224   623 DERRerlaeKRERKRELEAEfdearIEEAREDKERAEEyleqveeKLDELREERDDLQAEIGAVENELEEL-EELRERRE 701


                   ....*....
gi 2462625347  456 AMENRYKSL 464
Cdd:PRK02224   702 ALENRVEAL 710
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 332-472 1.75e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 44.15  E-value: 1.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  332 KKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGK-----EALSAALRSQN------LTKSTENHRLRRS 400
Cdd:pfam08614   14 DRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLlaqlrEELAELYRSRGelaqrlVDLNEELQELEKK 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462625347  401 IKKITQELSDLQQERERLE---KDLEEAHREKSKGdctIRDLRNEVEKLRNEVNEREKAMENrykslLSESNKKL 472
Cdd:pfam08614   94 LREDERRLAALEAERAQLEeklKDREEELREKRKL---NQDLQDELVALQLQLNMAEEKLRK-----LEKENREL 160
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 86-337 2.04e-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: 46.35  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   86 ERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQLLIKASKAVESLAEAGGS----------EIQRVKEDARK---- 151
Cdd:pfam10174  460 EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKkdsklksleiAVEQKKEECSKlenq 539

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  152 --KVQQVEDL------LTKRILLLEKDV-------TAAQAELEK---AFAGTETEKALRlrlESKLSEMKKMHEGDLAMA 213
Cdd:pfam10174  540 lkKAHNAEEAvrtnpeINDRIRLLEQEVarykeesGKAQAEVERllgILREVENEKNDK---DKKIAELESLTLRQMKEQ 616

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  214 LVLDEKDRLIEELKLSlKSKEALIQCLKEEKSQMACPDENVSSgELRGLCAAPREE----KERETEAAQMEHQKER---N 286
Cdd:pfam10174  617 NKKVANIKHGQQEMKK-KGAQLLEEARRREDNLADNSQQLQLE-ELMGALEKTRQEldatKARLSSTQQSLAEKDGhltN 694

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462625347  287 SFQERIQALEEDLR-----------EKEREIATEKKNSLKRDKAiQGLTMALK-SKEKKVEEL 337
Cdd:pfam10174  695 LRAERRKQLEEILEmkqeallaaisEKDANIALLELSSSKKKKT-QEEVMALKrEKDRLVHQL 756
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
327-599 2.33e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  327 LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRSIKKITQ 406
Cdd:COG4372     47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQEELEELQK 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  407 ELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQ--EQVIKHLTE 484
Cdd:COG4372    123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEEL 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  485 STNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIY 564
Cdd:COG4372    203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462625347  565 THLVKSLQESDSINNLQAELNKIFALRKQLEQDVL 599
Cdd:COG4372    283 LELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1324-1560 2.57e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1324 EMNTQNELMERIEEDNLTYQHLLPEspepsashaLSDYETSEKSffsrDQKQDNETEKTSVMVNSFSQDLLMEHIQ-EIR 1402
Cdd:TIGR02169  195 EKRQQLERLRREREKAERYQALLKE---------KREYEGYELL----KEKEALERQKEAIERQLASLEEELEKLTeEIS 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1403 TLRKRLEESIKTNEKLRKQLERQGS-EFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAMLIKG--SRDKQK-ENDK 1478
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEI-ASLERSIAEKERELEDAEERLAKLeaEIDKLLaEIEE 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1479 LRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRV 1558
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420


                   ..
gi 2462625347 1559 EL 1560
Cdd:TIGR02169  421 EL 422
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
257-452 2.64e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  257 GELRGLCAAPREEKERETEAAQMEH-------QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKS 329
Cdd:COG4913    255 EPIRELAERYAAARERLAELEYLRAalrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  330 KE-KKVEELNSEIEKLSAAFAKAREALQKaqtqefqgsedyetalsgkeaLSAALRSQNLTKSTENHRLRRSIKKITQEL 408
Cdd:COG4913    335 NGgDRLEQLEREIERLERELEERERRRAR---------------------LEALLAALGLPLPASAEEFAALRAEAAALL 393

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2462625347  409 SDLQQERERLEKDLEEAHREKskgdctiRDLRNEVEKLRNEVNE 452
Cdd:COG4913    394 EALEEELEALEEALAEAEAAL-------RDLRRELRELEAEIAS 430
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
268-430 2.84e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 2.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  268 EEKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIA---TEKKNSLKRDkaIQGLTMALKSKEKKVEELNSEIEKL 344
Cdd:COG4913    294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgngGDRLEQLERE--IERLERELEERERRRARLEALLAAL 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  345 SAAFAKAREALQKAQTQefqgsedyetALSGKEALSAALrsqnltkstenHRLRRSIKKITQELSDLQQERERLEKDLEE 424
Cdd:COG4913    372 GLPLPASAEEFAALRAE----------AAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIAS 430


                   ....*.
gi 2462625347  425 AHREKS 430
Cdd:COG4913    431 LERRKS 436
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 141-449 3.00e-04

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: 45.94  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  141 EIQRVKEDARKKVQQVEDLLTKRILLL-EKDVTAAQAELEKAFAGTETEKALRL-----RLESKLSEMK-KMHEGDLAMA 213
Cdd:pfam01576   13 ELQKVKERQQKAESELKELEKKHQQLCeEKNALQEQLQAETELCAEAEEMRARLaarkqELEEILHELEsRLEEEEERSQ 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  214 LVLDEKDRL---IEELKLSLKSKEALIQCLKEEKSqmacpdenVSSGELRGLcaaprEEKERETEAAQMEHQKERNSFQE 290
Cdd:pfam01576   93 QLQNEKKKMqqhIQDLEEQLDEEEAARQKLQLEKV--------TTEAKIKKL-----EEDILLLEDQNSKLSKERKLLEE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  291 RIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgSEDYE 370
Cdd:pfam01576  160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ----IAELR 235

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625347  371 TALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERlekdlEEAHREKSKGDCtiRDLRNEVEKLRNE 449
Cdd:pfam01576  236 AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES-----ERAARNKAEKQR--RDLGEELEALKTE 307
PRK12704 PRK12704
phosphodiesterase; Provisional
 265-357 3.48e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.15  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  265 APREEKERETEA------AQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELN 338
Cdd:PRK12704    51 AEAIKKEALLEAkeeihkLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKE 130

                           90
                   ....*....|....*....
gi 2462625347  339 SEIEKLSaafAKAREALQK 357
Cdd:PRK12704   131 EELEELI---EEQLQELER 146
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 320-482 3.63e-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: 44.15  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  320 IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgSEDYETALSGKEALSAALRsQNLTKSTE---NHR 396
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVE-ARIKKYEEqlgNVR 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  397 LRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQE 476
Cdd:COG1579     87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166


                   ....*.
gi 2462625347  477 QVIKHL 482
Cdd:COG1579    167 ELAAKI 172
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 268-507 4.20e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 45.43  E-value: 4.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  268 EEKERETEAAQMEHQKERNSFQERIQALEEDLREKERE---IATEKKNSLKRDKAIQGLTMAlkskekkVEELNSEIEKL 344
Cdd:TIGR01612 1540 AKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEkfrIEDDAAKNDKSNKAAIDIQLS-------LENFENKFLKI 1612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  345 SAAFAKAREALQKAQTQEfqgsedyetalsgKEALSAALRSQNlTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEE 424
Cdd:TIGR01612 1613 SDIKKKINDCLKETESIE-------------KKISSFSIDSQD-TELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE 1678

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  425 ahrekskgdctirdLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKdvLLQKFNEKDLEVI 504
Cdd:TIGR01612 1679 --------------LDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIEN--LISSFNTNDLEGI 1742


                   ...
gi 2462625347  505 QQN 507
Cdd:TIGR01612 1743 DPN 1745
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 78-665 5.13e-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: 45.10  E-value: 5.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   78 KLRIYFLEERMQQEFHGPTEHIYKTNIElkvevESLKRELQEREQ----LLIKASKAveslaEAGGSEIQRVKEDARKKV 153
Cdd:pfam05483  201 ELRVQAENARLEMHFKLKEDHEKIQHLE-----EEYKKEINDKEKqvslLLIQITEK-----ENKMKDLTFLLEESRDKA 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  154 QQVEDlltkRILLLEKDVtaaQAELEKAFAGTETEKALRLRLESKLSEMKKMHEgDLAMAL-----VLDEKDRLIEELKl 228
Cdd:pfam05483  271 NQLEE----KTKLQDENL---KELIEKKDHLTKELEDIKMSLQRSMSTQKALEE-DLQIATkticqLTEEKEAQMEELN- 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  229 slKSKEALIQCLKEEKSQMACPDENVSSGELRglcaapREEKERETEAAQMEHQKERNSFQE--RIQALEEDLREKEREI 306
Cdd:pfam05483  342 --KAKAAHSFVVTEFEATTCSLEELLRTEQQR------LEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVELEELKKI 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  307 ATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQ 386
Cdd:pfam05483  414 LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH 493

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  387 NLTKSTENhrlrrsiKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLS 466
Cdd:pfam05483  494 CDKLLLEN-------KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC 566

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  467 ESNKKLHNQEQVIKHLTESTNQKDVLLQKFN--EKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEK 544
Cdd:pfam05483  567 KLDKSEENARSIEYEVLKKEKQMKILENKCNnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELA 646

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  545 KQSSDYEELIQVLKK--------EQDIYTHLVKSLQESDSINNLQAELN-----KIFALRKQLEQDVLSYQnlrKTLEEQ 611
Cdd:pfam05483  647 SAKQKFEEIIDNYQKeiedkkisEEKLLEEVEKAKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQYD---KIIEER 723

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462625347  612 ISEI-----RRREES---FSLYSDQTSYLSICLEENNRFQVEHFSQEELKKKVSDLIQLVKE 665
Cdd:pfam05483  724 DSELglyknKEQEQSsakAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 105-420 5.26e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 5.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  105 ELKVEVESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAG 184
Cdd:COG1196    467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  185 ------TETEKALRLRLESkLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGE 258
Cdd:COG1196    547 alqnivVEDDEVAAAAIEY-LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  259 -------LRGLCAAPREEKERETEAAQMEHQKERNS---FQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALK 328
Cdd:COG1196    626 tlvaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSltgGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  329 SKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTEnhRLRRSIKKI---- 404
Cdd:COG1196    706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE--RLEREIEALgpvn 783

                          330       340       350
                   ....*....|....*....|....*....|...
gi 2462625347  405 -----------------TQELSDLQQERERLEK 420
Cdd:COG1196    784 llaieeyeeleerydflSEQREDLEEARETLEE 816
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1391-1575 5.72e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 5.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1391 QDLLMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIfasgselhSSLTSEIHFLRKQNQALNAMLIKGSR 1470
Cdd:COG1196    252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------ARLEQDIARLEERRRELEERLEELEE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1471 DKQ---KENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRcsgQELSRVQEELKLRQQLLS 1547
Cdd:COG1196    324 ELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAA 400

                          170       180
                   ....*....|....*....|....*...
gi 2462625347 1548 QNDKLLQSLRVELKAYEKLDEEHRRLRD 1575
Cdd:COG1196    401 QLEELEEAEEALLERLERLEEELEELEE 428
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
331-618 7.02e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 7.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  331 EKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgsedyetalsgKEALSAalRSQNLTKSTENHRLRRSIKKITQELSD 410
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAE--------------LDALQE--RREALQRLAEYSWDEIDVASAEREIAE 672

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  411 LQQERERLEK---DLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKhltestN 487
Cdd:COG4913    673 LEAELERLDAssdDLAALEEQLEE----LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED------L 742

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  488 QKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLitekcssqqppgsktifskEKKQSSDYEELIQVLKKEQDIYTHL 567
Cdd:COG4913    743 ARLELRALLEERFAAALGDAVERELRENLEERIDAL-------------------RARLNRAEEELERAMRAFNREWPAE 803

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462625347  568 VKSLQES-DSINNLQAELNKI-----------F--ALRKQLEQDVLsyqNLRKTLEEQISEIRRR 618
Cdd:COG4913    804 TADLDADlESLPEYLALLDRLeedglpeyeerFkeLLNENSIEFVA---DLLSKLRRAIREIKER 865
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1394-1575 8.53e-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: 44.28  E-value: 8.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1394 LMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAMLikgsRDKQ 1473
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREAL----DELR 809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1474 KENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLL 1553
Cdd:TIGR02168  810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889

                          170       180
                   ....*....|....*....|..
gi 2462625347 1554 QSLRvelKAYEKLDEEHRRLRD 1575
Cdd:TIGR02168  890 ALLR---SELEELSEELRELES 908
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1398-1575 1.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1398 IQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELHSSLTSEIHFLRKQNQALNAM---LIKGSRDKQK 1474
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaeLAEAEEELEE 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1475 ENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQ 1554
Cdd:COG1196    384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                          170       180
                   ....*....|....*....|.
gi 2462625347 1555 SLRVELKAYEKLDEEHRRLRD 1575
Cdd:COG1196    464 LLAELLEEAALLEAALAELLE 484
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 105-431 1.23e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 43.35  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  105 ELKVEVESLKRELQEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVEDLLTKrilllEKDVTAAQAELekafag 184
Cdd:pfam07888   45 ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK-----YKELSASSEEL------ 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  185 TETEKALRLRLESKLSEMKKMHEGDLAMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDEnVSSGELRGLCA 264
Cdd:pfam07888  114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ-QTEEELRSLSK 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  265 APREEK----ERETEAAQMehqkernsfQERIQALEEDLREKEREIAtEKKNSLKRDKAIQGLtmaLKSKEKKVEELNSE 340
Cdd:pfam07888  193 EFQELRnslaQRDTQVLQL---------QDTITTLTQKLTTAHRKEA-ENEALLEELRSLQER---LNASERKVEGLGEE 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  341 IEKLSAAFAKAREALQKAQTQEFQgsedyetaLSGKEA-LSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLE 419
Cdd:pfam07888  260 LSSMAAQRDRTQAELHQARLQAAQ--------LTLQLAdASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLE 331

                          330
                   ....*....|..
gi 2462625347  420 KDLEEAHREKSK 431
Cdd:pfam07888  332 ERLQEERMEREK 343
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
287-448 1.47e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  287 SFQERIQALEEDLREKEREiaTEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALqkaqtqefqgs 366
Cdd:COG2433    377 SIEEALEELIEKELPEEEP--EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI----------- 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  367 EDYETALSgkealsaalrsqnLTKSTENHRLRRSikkitQELSDLQQERERLEKDLEEAHREkskgdctIRDLRNEVEKL 446
Cdd:COG2433    444 ERLERELS-------------EARSEERREIRKD-----REISRLDREIERLERELEEERER-------IEELKRKLERL 498


                   ..
gi 2462625347  447 RN 448
Cdd:COG2433    499 KE 500
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 1358-1572 1.61e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 43.57  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1358 LSDYETSEKSFfsRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLRKRLEESIKT-NEKLRKQLERQGSEfVQGSTSI 1436
Cdd:pfam15921  383 LADLHKREKEL--SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAA-IQGKNES 459

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1437 FASGSELHSSLTSEIHFLRKQNQALNAmlikgsrdKQKENDKLRESLSRKTVSLEHLQReyaSVKEENERLQKEGSEKER 1516
Cdd:pfam15921  460 LEKVSSLTAQLESTKEMLRKVVEELTA--------KKMTLESSERTVSDLTASLQEKER---AIEATNAEITKLRSRVDL 528

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625347 1517 HNQQLiQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRVELKAYEKLDEEHRR 1572
Cdd:pfam15921  529 KLQEL-QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 335-488 1.62e-03

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 42.61  E-value: 1.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  335 EELNSEIEKLSAAFAKAREALQKAQtQEFQGSEDYETALSG-KEALSAALRSQNLTKSTEN-HRLRRSIKKITQELSDLQ 412
Cdd:pfam13949   75 ATLRAEIRKYREILEQASESDSQVR-SKFREHEEDLELLSGpDEDLEAFLPSSRRAKNSPSvEEQVAKLRELLNKLNELK 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  413 QERERLEKDLeeahREKSKGDctirDLRNEV--EKLRNEVNEREKAMENR----YKSLLSESNKKLHNQEQVIKHLTEST 486
Cdd:pfam13949  154 REREQLLKDL----KEKARND----DISPKLllEKARLIAPNQEEQLFEEelekYDPLQNRLEQNLHKQEELLKEITEAN 225


                   ..
gi 2462625347  487 NQ 488
Cdd:pfam13949  226 NE 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
110-419 2.05e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  110 VESLKRELQEREQLLIKASKAVESLAEAGgSEIQRVKEDARKKVQQVEDLLtkRILLLEKDVTAAQAELEKAFAGTETEK 189
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDEI--DVASAEREIAELEAELERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  190 ALRLRLESKLSEMKKMHEgdlamalVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPDENVSSGELrglcaapreE 269
Cdd:COG4913    689 ALEEQLEELEAELEELEE-------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---------E 752

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  270 KERETEAAQMEHQKERNSFQERIQALEEDLREKEREIaTEKKNSLKRD--KAIQGLTMALKSKEKKVEELNS-EIEKLSA 346
Cdd:COG4913    753 ERFAAALGDAVERELRENLEERIDALRARLNRAEEEL-ERAMRAFNREwpAETADLDADLESLPEYLALLDRlEEDGLPE 831

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462625347  347 AFAKAREALQKAQTQEFqgsedyeTALsgkealsaalrsqnltksteNHRLRRSIKKITQELSDLQQERERLE 419
Cdd:COG4913    832 YEERFKELLNENSIEFV-------ADL--------------------LSKLRRAIREIKERIDPLNDSLKRIP 877
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1399-1565 2.13e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1399 QEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSE------LHSS----LTSEIHFLRKQNQALNAmLIKG 1468
Cdd:COG4942     76 QELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplallLSPEdfldAVRRLQYLKYLAPARRE-QAEE 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1469 SRDKQKENDKLRESLSRKTVSLEHLQREyasVKEENERLQKEGSEKerhnQQLIQEVRcsgQELSRVQEELKLRQQLLSQ 1548
Cdd:COG4942    155 LRADLAELAALRAELEAERAELEALLAE---LEEERAALEALKAER----QKLLARLE---KELAELAAELAELQQEAEE 224

                          170
                   ....*....|....*..
gi 2462625347 1549 NDKLLQSLRVELKAYEK 1565
Cdd:COG4942    225 LEALIARLEAEAAAAAE 241
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 412-677 2.33e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  412 QQERERLEKDLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSL---LSESNKKLHNQEQVIKHLTESTNQ 488
Cdd:pfam02463  169 RKKKEALKKLIEETENLAEL----IIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLKLNEERIDLLQE 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  489 KDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEglitEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLV 568
Cdd:pfam02463  245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE----EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  569 KSLQesdsinNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREESFSLySDQTSYLSICLEEN------NRF 642
Cdd:pfam02463  321 KEKK------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ-LEEELLAKKKLESErlssaaKLK 393

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2462625347  643 QVEHFSQEELKKKVSDLIQLVKELYTDNQHLKKTI 677
Cdd:pfam02463  394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 232-458 2.37e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.81  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  232 SKEALIQcLKEEKSQMacpdenvssgELRGLCAAPREEKERETEAAQMEHQKERN-SFQERIQALEEDLREKEREIATEK 310
Cdd:pfam05557    7 SKARLSQ-LQNEKKQM----------ELEHKRARIELEKKASALKRQLDRESDRNqELQKRIRLLEKREAEAEEALREQA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  311 KNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT---------QEFQGSED-YETALSGKEALS 380
Cdd:pfam05557   76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELelqstnselEELQERLDlLKAKASEAEQLR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  381 AALRSQNLTKSTENHRLRRSIKKITQ------ELSDLQQERER---LEKDLEEAHREKSKGDCTIRD---LRNEVEKLRN 448
Cdd:pfam05557  156 QNLEKQQSSLAEAEQRIKELEFEIQSqeqdseIVKNSKSELARipeLEKELERLREHNKHLNENIENkllLKEEVEDLKR 235

                          250
                   ....*....|
gi 2462625347  449 EVNEREKAME 458
Cdd:pfam05557  236 KLEREEKYRE 245
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
54-453 2.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   54 PTRARNMKDFENQITELKKENFNLKLRIYFLEERMQQEFHGPTEHIYKTNIELKVEVESLKRELQEREQllikaskaves 133
Cdd:COG4717    145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEE----------- 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  134 laeaggsEIQRVKEDARKKVQQVEDLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLESKLSEMKKMH---EGDL 210
Cdd:COG4717    214 -------ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvLGLL 286

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  211 AMALVLDEKDRLIEELKLSLKSKEALIQCLKEEKSQMACPD----ENVSSGELRGLCAAPREEKERETEAAQMEHQKERN 286
Cdd:COG4717    287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglpPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  287 SFQERIQALEEDLREKEREIATEKknsLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKA--REALQKAQTQEFQ 364
Cdd:COG4717    367 ELEQEIAALLAEAGVEDEEELRAA---LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEE 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  365 GSEDYETALSGKEALSAALRsqnltkstenhRLRRSikkitQELSDLQQERERLEKDLEEAHREKSK---GDCTIRDLRN 441
Cdd:COG4717    444 LEEELEELREELAELEAELE-----------QLEED-----GELAELLQELEELKAELRELAEEWAAlklALELLEEARE 507

                          410
                   ....*....|...
gi 2462625347  442 EVEKLR-NEVNER 453
Cdd:COG4717    508 EYREERlPPVLER 520
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 289-497 2.89e-03

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 41.94  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  289 QERIQALEEDLREKEREIatekknslKRDKAIQGLTMA-LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSE 367
Cdd:cd08915     90 EELLQECEELLEEEAAED--------DQLRAKFGTLRWrRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESIDP 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  368 DYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEeahrEKSKGDCTIRDLRNEVEKLR 447
Cdd:cd08915    162 NLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELE----IKSRNNDILPKLITEYKKNG 237

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462625347  448 NEVNER--EKAMENrYKSLLSESNKKLHNQEQVIKHLTEStNQKDVLLQKFN 497
Cdd:cd08915    238 TTEFEDlfEEHLKK-FDKDLTYVEKTKKKQIELIKEIDAA-NQEFSQVKNSN 287
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 279-499 3.33e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  279 MEHQKERNSFQERIQALEEDLREKEREIATEKKnslkrdkaiqgltmalkskeKKVEELNSEIEKLSAAFAKAREALQKA 358
Cdd:pfam12128  268 KSDETLIASRQEERQETSAELNQLLRTLDDQWK--------------------EKRDELNGELSAADAAVAKDRSELEAL 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  359 QTQEFQ-GSEDYETALSGKEALSaALRSQNLTKSTENHRLRRSIKKITQELSDLQQER--------ERLEKDLEEAHREK 429
Cdd:pfam12128  328 EDQHGAfLDADIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkeqnnrdiAGIKDKLAKIREAR 406

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462625347  430 SKGDCTIRD--------LRNEVEKLRNEVNEREKamenRYKSLLSESNKKLhNQEQVIKHLTESTNQKDVLLQKFNEK 499
Cdd:pfam12128  407 DRQLAVAEDdlqaleseLREQLEAGKLEFNEEEY----RLKSRLGELKLRL-NQATATPELLLQLENFDERIERAREE 479
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 270-383 3.90e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 42.24  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  270 KERETEAAQMEHQKERnsFQERIQALEedlREK-EREIATEKKNSLKRDKAIQGLTMAL-KSKEKKVEELNSEIEKLSA- 346
Cdd:PRK05035   439 RAIEQEKKKAEEAKAR--FEARQARLE---REKaAREARHKKAAEARAAKDKDAVAAALaRVKAKKAAATQPIVIKAGAr 513

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462625347  347 ----AFAKAREALQKAQTQEFQGSEDYETALSGKEALSAAL 383
Cdd:PRK05035   514 pdnsAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAI 554
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 118-506 4.02e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.87  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  118 QEREQLLIKASKAVESLAEAGGSEIQRVKEDARKKVQQVE----DLLTKRILLLEKDVTAAQAELEKAFAGTETEKALRL 193
Cdd:COG5185    170 QELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKEsetgNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLA 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  194 RLESKLSEMKKMHEgDLAMAlVLDEKDRLIEELKLSLKSKEALIQCLKE-----EKSQMACPDENVSSGELRGLCA-APR 267
Cdd:COG5185    250 QTSDKLEKLVEQNT-DLRLE-KLGENAESSKRLNENANNLIKQFENTKEkiaeyTKSIDIKKATESLEEQLAAAEAeQEL 327

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  268 EEKERETEAA----QMEHQKERNSFQERIQALEEDLREKEREIATEKknslkrdkaiqgltmalksKEKKVEELNSEIEK 343
Cdd:COG5185    328 EESKRETETGiqnlTAEIEQGQESLTENLEAIKEEIENIVGEVELSK-------------------SSEELDSFKDTIES 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  344 LSaafakaREALQKAQTQEFQGSEdyetalsGKEALSAALRSQnltkSTENHRLRRSIKKITQELSDLQQERERLEKDLE 423
Cdd:COG5185    389 TK------ESLDEIPQNQRGYAQE-------ILATLEDTLKAA----DRQIEELQRQIEQATSSNEEVSKLLNELISELN 451

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  424 EAHRE-----KSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSE-------SNKKLHNQEQVIKHLTESTNQKDV 491
Cdd:COG5185    452 KVMREadeesQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATleklrakLERQLEGVRSKLDQVAESLKDFMR 531

                          410
                   ....*....|....*
gi 2462625347  492 LLQKFNEKDLEVIQQ 506
Cdd:COG5185    532 ARGYAHILALENLIP 546
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 378-621 4.08e-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: 41.67  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  378 ALSAALRSQNLTKSTEN--HRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 455
Cdd:COG4942     11 LALAAAAQADAAAEAEAelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  456 AMEnryksllsESNKKLHNQEQVIKHLTES---TNQKDVLLQKFNEKDLEVIQQNCYLMA--AEDLELRSEGLITEKcss 530
Cdd:COG4942     91 EIA--------ELRAELEAQKEELAELLRAlyrLGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREQAEELRADL--- 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  531 qqppgsKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDS-INNLQAELNKIFALRKQLEQDVLSYQNLRKTLE 609
Cdd:COG4942    160 ------AELAALRAELEAERAELEALLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLE 233

                          250
                   ....*....|..
gi 2462625347  610 EQISEIRRREES 621
Cdd:COG4942    234 AEAAAAAERTPA 245
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 273-364 4.43e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 39.49  E-value: 4.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   273 ETEAAQMEHQKERNSFQERIQALEEDLREKEREiatekknsLKRDKAiqglTMALKSKEKKVEELNSEIEKLSAAFAKAR 352
Cdd:smart00935   15 AGKAAQKQLEKEFKKRQAELEKLEKELQKLKEK--------LQKDAA----TLSEAAREKKEKELQKKVQEFQRKQQKLQ 82

                            90
                    ....*....|..
gi 2462625347   353 EALQKAQTQEFQ 364
Cdd:smart00935   83 QDLQKRQQEELQ 94
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 273-364 5.25e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 39.82  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  273 ETEAAQMEHQKERNSFQERIQALEEDLREKEREiatekknsLKRDKAiqglTMALKSKEKKVEELNSEIEKLSAAFAKAR 352
Cdd:COG2825     40 EGKAAQKKLEKEFKKRQAELQKLEKELQALQEK--------LQKEAA----TLSEEERQKKERELQKKQQELQRKQQEAQ 107

                           90
                   ....*....|..
gi 2462625347  353 EALQKAQTQEFQ 364
Cdd:COG2825    108 QDLQKRQQELLQ 119
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 377-494 5.49e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  377 EAlSAALRSQNLTKSTEnhrlrrsIKKITQELSDLQQERERLEKDLEEAHREKskgdctIRDLRNEVEKLRNEVN----- 451
Cdd:COG0542    397 EA-AARVRMEIDSKPEE-------LDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEalkar 462

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462625347  452 -EREKAMENRYKSL---LSESNKKLHNQEQVIKHLTESTNQKDVLLQ 494
Cdd:COG0542    463 wEAEKELIEEIQELkeeLEQRYGKIPELEKELAELEEELAELAPLLR 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1399-1575 5.51e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1399 QEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELHSSLTSEIHFLRKQNQalnamLIKGSRDKQKENDK 1478
Cdd:COG1196    239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-----LEQDIARLEERRRE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1479 LRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEL-KLRQQLLSQNDKLLQSLR 1557
Cdd:COG1196    314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELaEAEEELEELAEELLEALR 393

                          170
                   ....*....|....*...
gi 2462625347 1558 VELKAYEKLDEEHRRLRD 1575
Cdd:COG1196    394 AAAELAAQLEELEEAEEA 411
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
189-347 6.86e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  189 KALRlRLESKLSE-MKKMHEG---DLAMALVLDEK--DRLIEELKLSLKSKEaliqclkEEKSQMACPDENVSSGELRGL 262
Cdd:COG2433    343 KAYD-AYKNKFERvEKKVPPDvdrDEVKARVIRGLsiEEALEELIEKELPEE-------EPEAEREKEHEERELTEEEEE 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  263 CAAPREEKER-ETEAAQMEHQKERNsfQERIQALEEDL----REKEREIATEKKNSlKRDKAIQGLTMALKSKEKKVEEL 337
Cdd:COG2433    415 IRRLEEQVERlEAEVEELEAELEEK--DERIERLERELsearSEERREIRKDREIS-RLDREIERLERELEEERERIEEL 491

                          170
                   ....*....|
gi 2462625347  338 NSEIEKLSAA 347
Cdd:COG2433    492 KRKLERLKEL 501
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 65-521 7.69e-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: 41.31  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   65 NQITELKKENFNLKLRIYFLEERMQQEfHGPTEHIYKTNIELKVEVESLKRELQE--------------REQLLIKASKA 130
Cdd:pfam01576  257 AQKNNALKKIRELEAQISELQEDLESE-RAARNKAEKQRRDLGEELEALKTELEDtldttaaqqelrskREQEVTELKKA 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  131 VEslaEAGGSEIQRVKEDARKKVQQVEDL-------------LTKRILLLEKDVTAAQAELEKAFAGTETEKALRLRLES 197
Cdd:pfam01576  336 LE---EETRSHEAQLQEMRQKHTQALEELteqleqakrnkanLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG 412

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  198 KLSEMK-KMHEGDLAMALVLDEKDRLIEELK-LSLKSKEALIQCLKEEKSQMACPDENVSSGELrgLCAAPREEKERETE 275
Cdd:pfam01576  413 QLQELQaRLSESERQRAELAEKLSKLQSELEsVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEL--LQEETRQKLNLSTR 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  276 AAQMEhqKERNSFQERIQALEEDLREKEREIATekknslkrdkaiqgLTMALKSKEKKVEELNSEIEKLSAAFAKAREAL 355
Cdd:pfam01576  491 LRQLE--DERNSLQEQLEEEEEAKRNVERQLST--------------LQAQLSDMKKKLEEDAGTLEALEEGKKRLQREL 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  356 QKAQTQEFQGSEDYETALSGKEALSAALrsQNLTKSTENHR-----LRRSIKKITQELSDLQQERERLEKDLEEAHREKS 430
Cdd:pfam01576  555 EALTQQLEEKAAAYDKLEKTKNRLQQEL--DDLLVDLDHQRqlvsnLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAR 632

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  431 KGDCTIRDLRNEVEKLRNEVNEREKAMenryKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYL 510
Cdd:pfam01576  633 EKETRALSLARALEEALEAKEELERTN----KQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL 708

                          490
                   ....*....|.
gi 2462625347  511 MAAEDLELRSE 521
Cdd:pfam01576  709 QATEDAKLRLE 719
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1397-1572 8.41e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 8.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1397 HIQEIRTLRKRLEESIKTNEKLRKQLERQGSEfvqgstsifasgselhssLTSEIHFLRKQNQALNAMLikgsRDKQKEN 1476
Cdd:COG1196    233 KLRELEAELEELEAELEELEAELEELEAELAE------------------LEAELEELRLELEELELEL----EEAQAEE 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1477 DKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSL 1556
Cdd:COG1196    291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                          170
                   ....*....|....*.
gi 2462625347 1557 RVELKAYEKLDEEHRR 1572
Cdd:COG1196    371 EAELAEAEEELEELAE 386
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1399-1575 8.42e-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: 40.52  E-value: 8.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1399 QEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELH------SSLTSEIHFLRKQNQALNAMLIK--GSR 1470
Cdd:COG4942     34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleaelAELEKEIAELRAELEAQKEELAEllRAL 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1471 DKQKENDKLR-----ESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQL 1545
Cdd:COG4942    114 YRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2462625347 1546 LSQNDKLLQSLRVELKAYEK----LDEEHRRLRD 1575
Cdd:COG4942    194 KAERQKLLARLEKELAELAAelaeLQQEAEELEA 227
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1328-1573 8.60e-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: 41.21  E-value: 8.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1328 QNELmERIEEDNLTYQHLLPESPE--PSASHALSDYETSEKSFFSRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLR 1405
Cdd:TIGR02169  722 EKEI-EQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1406 KRLEESIKTNEKLRKQLERQgsefvqgstsifasgselHSSLTSEIHFLRKQNQALNAMLI-----KGSRDKQKENDKLR 1480
Cdd:TIGR02169  801 SKLEEEVSRIEARLREIEQK------------------LNRLTLEKEYLEKEIQELQEQRIdlkeqIKSIEKEIENLNGK 862

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1481 -----ESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLL-- 1553
Cdd:TIGR02169  863 keeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKge 942

                          250       260
                   ....*....|....*....|.
gi 2462625347 1554 -QSLRVELKAYEKLDEEHRRL 1573
Cdd:TIGR02169  943 dEEIPEEELSLEDVQAELQRV 963
46 PHA02562
endonuclease subunit; Provisional
 284-459 8.83e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 8.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  284 ERNSFQERI---QALEEDLREKEREIATEKKNslKRDKA---IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQK 357
Cdd:PHA02562   189 KIDHIQQQIktyNKNIEEQRKKNGENIARKQN--KYDELveeAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAK 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  358 AQTQEFQGSEDYETALSGKEALSAalrSQNLtkSTENHRL---RRSIKKITQELSDLQQERERLEKDLEEAhREKSKgdc 434
Cdd:PHA02562   267 IKSKIEQFQKVIKMYEKGGVCPTC---TQQI--SEGPDRItkiKDKLKELQHSLEKLDTAIDELEEIMDEF-NEQSK--- 337

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462625347  435 TIRDLRNEVEK-------LRNEVNEREKAMEN 459
Cdd:PHA02562   338 KLLELKNKISTnkqslitLVDKAKKVKAAIEE 369
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 55-499 9.22e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 9.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347   55 TRARNMKDFENQITELKKENFNLKLRIYfleermqqefhgptehiyktniELKVEVESLKRELQEREQllikaskavesL 134
Cdd:TIGR04523  360 EKQRELEEKQNEIEKLKKENQSYKQEIK----------------------NLESQINDLESKIQNQEK-----------L 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  135 AEAGGSEIQRVKEDARKKVQQVEDLLTKRILLLE--KDVTAAQAELEKAFagtETEKALRLRLESKLSEMKKMHEgdlam 212
Cdd:TIGR04523  407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeiKDLTNQDSVKELII---KNLDNTRESLETQLKVLSRSIN----- 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  213 alvldEKDRLIEELKLSLKSKEALIQCLKEEKSQMacpDENVSsgelrglcaapreekereteaaqmEHQKERNSFQERI 292
Cdd:TIGR04523  479 -----KIKQNLEQKQKELKSKEKELKKLNEEKKEL---EEKVK------------------------DLTKKISSLKEKI 526

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  293 QALEEDLREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFqgseDYE 370
Cdd:TIGR04523  527 EKLESEKKEKESKISDleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK----DLI 602

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  371 TALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEV 450
Cdd:TIGR04523  603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELM 682

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462625347  451 NEREKAMENRYK---------SLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEK 499
Cdd:TIGR04523  683 KDWLKELSLHYKkyitrmiriKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKK 740
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
115-358 9.95e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  115 RELQEREQLLIKASKAVESLA--EAGGSEIQRVKEDARKKVQQVEDL----LTKRILLLEKDVTAAQAELEKAfagtete 188
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELRAELARL------- 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  189 KALRLRLESKLSEMKKMHEGdlAMALVLDEKDRLIEELKLSLKSKEALiqclKEEKSQmacpdenvSSGELRGLCAApRE 268
Cdd:COG4913    308 EAELERLEARLDALREELDE--LEAQIRGNGGDRLEQLEREIERLERE----LEERER--------RRARLEALLAA-LG 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347  269 EKERETEAAQMEHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRdkaiqgltmaLKSKEKKVEELNSEIEKLSAAF 348
Cdd:COG4913    373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE----------LRELEAEIASLERRKSNIPARL 442

                          250
                   ....*....|
gi 2462625347  349 AKAREALQKA 358
Cdd:COG4913    443 LALRDALAEA 452
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1395-1569 9.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1395 MEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVqgstsiFASGSELHSSLTSEIHFLRKQNQALNAMliKGSRDKQK 1474
Cdd:PRK03918   548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELG------FESVEELEERLKELEPFYNEYLELKDAE--KELEREEK 619

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625347 1475 ENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNqqLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQ 1554
Cdd:PRK03918   620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLE 697

                          170
                   ....*....|....*
gi 2462625347 1555 SLRVELKAYEKLDEE 1569
Cdd:PRK03918   698 KLKEELEEREKAKKE 712
 
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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