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Conserved domains on  [gi|1622828953|ref|XP_028709307|]
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transport and Golgi organization protein 1 homolog isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 98-404 9.34e-16

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: 82.04  E-value: 9.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   98 LKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLE------SE 171
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleariEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  172 REQNVKN-------------QDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:TIGR02169  770 LEEDLHKleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVG 318
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  319 GDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKV 398
Cdd:TIGR02169  930 EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009


                   ....*.
gi 1622828953  399 EILNEL 404
Cdd:TIGR02169 1010 EEYEKK 1015
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 525-795 6.17e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 6.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  525 PGRPNTQNPPRRGPL--SQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPRWSAEASGKP 602
Cdd:PHA03247  2670 LGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  603 SPSDPGSGTAAMMNSSSRGSSPNRVIDEGKQTVLQEPEV-------PSVPSITSLAEHPVAVNM-----------APKGP 664
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaslsesrESLPSPWDPADPPAAVLApaaalppaaspAGPLP 2829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  665 PPFSGVPLMSTPMGGPIPPPIRYGPPP----QLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGKRDLPLHPREFLPG 740
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVapggDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERP 2908

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953  741 HTPFRPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQ 795
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 348-517 4.48e-05

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: 47.24  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 348 DLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILN---ELYQQKEMALQKKLSQEEYERQ 424
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELElelEEAQAEEYELLAELARLEQDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 425 EREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL---QKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLR 501
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170
                  ....*....|....*.
gi 1622828953 502 HKLLELTQKMAMLQEE 517
Cdd:COG1196   386 EELLEALRAAAELAAQ 401
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-404 9.34e-16

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: 82.04  E-value: 9.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   98 LKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLE------SE 171
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleariEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  172 REQNVKN-------------QDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:TIGR02169  770 LEEDLHKleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVG 318
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  319 GDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKV 398
Cdd:TIGR02169  930 EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009


                   ....*.
gi 1622828953  399 EILNEL 404
Cdd:TIGR02169 1010 EEYEKK 1015
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 96-414 2.10e-11

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: 67.69  E-value: 2.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   96 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRK---------------QNMILSDEAIKFKDKIKTLEKNNEILGDA 160
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeEYLLYLDYLKLNEERIDLLQELLRDEQEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  161 AKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 240
Cdd:pfam02463  253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  241 LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddniNALTNCITQLNRLECESESEGQnKGGNDSDELANGEVGGD 320
Cdd:pfam02463  333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----EQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKEA 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  321 QNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEI 400
Cdd:pfam02463  408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487

                          330
                   ....*....|....
gi 1622828953  401 LNELYQQKEMALQK 414
Cdd:pfam02463  488 LLLSRQKLEERSQK 501
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-517 4.39e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEkLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 170
Cdd:COG4717    77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 171 EREqnvknqdlISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKvksechRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:COG4717   155 LEE--------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------DLAEELEELQQRLAELEEELEEAQE 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 251 LHAELSEQIKSFEKSQKDLE------------------VALTHKDDNINALTNCIT-------QLNRLECESESEGQNKG 305
Cdd:COG4717   221 ELEELEEELEQLENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAgvlflvlGLLALLFLLLAREKASL 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 306 GNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLqAAKA 385
Cdd:COG4717   301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEA 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 386 GLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVsaAEEVKTYKRRIEEMEDE---LQKTE 462
Cdd:COG4717   380 GVEDE-EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREEL 455

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953 463 RSFKNQIATHEKkahenwlkaraaeraiaeeKREAANLRHKLLELTQKMAMLQEE 517
Cdd:COG4717   456 AELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEE 491
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
91-463 6.70e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 62.75  E-value: 6.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEKlkiimkENTELVQKLSNYEQKIKESK---KHVQETRKQ--------NMILS------------DEAI-KFKDK 146
Cdd:PRK02224  193 KAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerreeletlEAEIeDLRET 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 147 IKTLEKNNEILGDAAKNLRVM---LESEREQNVKNQDLISENKKSIEKLKDAISmnaSEFSEVQIALNEAKLSEEKVKSE 223
Cdd:PRK02224  267 IAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEAVEARREELE---DRDEELRDRLEECRVAAQAHNEE 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 224 CHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNRLECESESEGQN 303
Cdd:PRK02224  344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGNAEDFLEELREE 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 304 KGGNDSDElANGEVGGDQNEKMKNQIKQMMDVSRTQTA---------ISVVEEDLKLLQlKLRASVSTkcnLEDQIKKLE 374
Cdd:PRK02224  421 RDELRERE-AELEATLRTARERVEEAEALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELED---LEEEVEEVE 495

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 375 DDRNSLQAAKAgLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEK----------AVSAAEEV 444
Cdd:PRK02224  496 ERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeAEEAREEV 574

                         410
                  ....*....|....*....
gi 1622828953 445 KTYKRRIEEMEDELQKTER 463
Cdd:PRK02224  575 AELNSKLAELKERIESLER 593
PHA03247 PHA03247
large tegument protein UL36; Provisional
 525-795 6.17e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 6.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  525 PGRPNTQNPPRRGPL--SQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPRWSAEASGKP 602
Cdd:PHA03247  2670 LGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  603 SPSDPGSGTAAMMNSSSRGSSPNRVIDEGKQTVLQEPEV-------PSVPSITSLAEHPVAVNM-----------APKGP 664
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaslsesrESLPSPWDPADPPAAVLApaaalppaaspAGPLP 2829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  665 PPFSGVPLMSTPMGGPIPPPIRYGPPP----QLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGKRDLPLHPREFLPG 740
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVapggDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERP 2908

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953  741 HTPFRPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQ 795
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 348-517 4.48e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 348 DLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILN---ELYQQKEMALQKKLSQEEYERQ 424
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELElelEEAQAEEYELLAELARLEQDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 425 EREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL---QKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLR 501
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170
                  ....*....|....*.
gi 1622828953 502 HKLLELTQKMAMLQEE 517
Cdd:COG1196   386 EELLEALRAAAELAAQ 401
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 93-256 9.32e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 45.39  E-value: 9.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   93 QISEKLKIIMKENTELVqklsnyeqkiKESKKHVqetRKQNMILSDEAIKFKDKIKTLEKNneilgdaaknLRVMLESER 172
Cdd:smart00787 140 KLLEGLKEGLDENLEGL----------KEDYKLL---MKELELLNSIKPKLRDRKDALEEE----------LRQLKQLED 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  173 EQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ-EIEDWSKL 251
Cdd:smart00787 197 ELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKL 276


                   ....*
gi 1622828953  252 HAELS 256
Cdd:smart00787 277 KEQLK 281
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 63-202 4.45e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 40.88  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  63 TAFLGIVSFAV-------FFWRTVL-VVKSRvyqvtEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnm 134
Cdd:cd06503     1 TLIWQIINFLIllfilkkFLWKPILkALDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------ 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828953 135 ILsDEAIKFKDKIKtleknNEILGDAAKnlrvmlESEREQNVKNQDLISENKKSIEKLKD---AISMNASE 202
Cdd:cd06503    70 II-EEARKEAEKIK-----EEILAEAKE------EAERILEQAKAEIEQEKEKALAELRKevaDLAVEAAE 128
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 513-809 1.39e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 513 MLQEEPVIVKPMPGRPNTQNPPRRGPlSQNGSFGPSPvsgGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSvdGPLPHP 592
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGT-TQAATAGPTP---SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ--TPTLHP 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 593 RwsaeasGKPSPSDPgsgtaamMNSSSRGSSPNRVIDEGKQTVLQEPEVPSVP----SITSLAEHPVAvnmapkgPPPFS 668
Cdd:pfam03154 240 Q------RLPSPHPP-------LQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPhslqTGPSHMQHPVP-------PQPFP 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 669 GVPLMSTPMGGPIPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLglrefapgvPPGKRDLP-LHPreflPGHTPFRPL 747
Cdd:pfam03154 300 LTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL---------PPAPLSMPhIKP----PPTTPIPQL 366

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953 748 gPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLPPSGSRDDP---PPASQSTSQdcSQALKQSP 809
Cdd:pfam03154 367 -PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPsahPPPLQLMPQ--SQQLPPPP 428
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 98-404 9.34e-16

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: 82.04  E-value: 9.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   98 LKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLE------SE 171
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleariEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  172 REQNVKN-------------QDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:TIGR02169  770 LEEDLHKleealndlearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVG 318
Cdd:TIGR02169  850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  319 GDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKV 398
Cdd:TIGR02169  930 EEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009


                   ....*.
gi 1622828953  399 EILNEL 404
Cdd:TIGR02169 1010 EEYEKK 1015
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 92-469 5.36e-15

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: 79.29  E-value: 5.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  92 QQISEKLKIIMKENTELVQkLSNYEQKIK----ESKKHVQETRKQNMILSDEAIKFKDKIKTLekNNEILGDAAKNLRVM 167
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQ-LKDEQNKIKkqlsEKQKELEQNNKKIKELEKQLNQLKSEISDL--NNQKEQDWNKELKSE 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 168 LESEREQNVKNQDLISENKKSIEKLKDAIS------MNA-SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 240
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkelTNSeSENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 241 LQQEIEDWSKLHAELSEQIKSF-------EKSQKDLEVALTHKDDNINALTNCITQL----NRLECESESEGQN------ 303
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLqqekellEKEIERLKETIIKNNSEIKDLTNQDSVKeliiKNLDNTRESLETQlkvlsr 475

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 304 KGGNDSDELANGEVGGDQNEKMKNQIKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQA- 382
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNE--EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFe 553

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 383 -AKAGLEDECKTLRQKVEIL---NELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYK---RRIEEME 455
Cdd:TIGR04523 554 lKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKkenEKLSSII 633

                         410
                  ....*....|....
gi 1622828953 456 DELQKTERSFKNQI 469
Cdd:TIGR04523 634 KNIKSKKNKLKQEV 647
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 88-399 2.06e-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: 74.32  E-value: 2.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   88 QVTEQQisEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVM 167
Cdd:TIGR02168  685 KIEELE--EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  168 LESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 247
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  248 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKggndSDELANGEvggDQNEKMKN 327
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL----SEELRELE---SKRSELRR 915

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622828953  328 QIKQMMD-VSRTQTAISVVEEDLKLLQLKLRASVSTkcNLEDQIKKLEDDRNSLQAAkaglEDECKTLRQKVE 399
Cdd:TIGR02168  916 ELEELREkLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEEAEALENKIEDDEEEA----RRRLKRLENKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 110-455 2.78e-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: 70.86  E-value: 2.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  110 QKLSNYEQKIKESKKHVQETRKQnmilsdeaikfkdkIKTLEKNNEILGDAAKNLRVMLESEREQnvknqdlISENKKSI 189
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKA--------------LAELRKELEELEEELEQLRKELEELSRQ-------ISALRKDL 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  190 EKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDL 269
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  270 EVALTHKDDNINALTN----CITQLNRLECESESEgqnkggNDSDELANGEVG--GDQNEKMKNQIKQMMDvsrtqtAIS 343
Cdd:TIGR02168  816 NEEAANLRERLESLERriaaTERRLEDLEEQIEEL------SEDIESLAAEIEelEELIEELESELEALLN------ERA 883

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  344 VVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKV----EILNELYQQKEMALQKKLSQE 419
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTLEEAEALENKI 963

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1622828953  420 EYERQEREHRLSAADEK-----AV--SAAEEVKTYKRRIEEME 455
Cdd:TIGR02168  964 EDDEEEARRRLKRLENKikelgPVnlAAIEEYEELKERYDFLT 1006
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 91-469 2.91e-12

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: 70.43  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEKLKIIMKENTELVQKlsnyEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 170
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 171 EREQNVKNQDL---ISENKKSIEKLKDAISMNASEFSEVQIALNeaklseeKVKSECHRVQEENARLKKKKEQLQQEIE- 246
Cdd:TIGR04523 206 LKKKIQKNKSLesqISELKKQNNQLKDNIEKKQQEINEKTTEIS-------NTQTQLNQLKDEQNKIKKQLSEKQKELEq 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 247 ----------------------------DWSKlhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESE 298
Cdd:TIGR04523 279 nnkkikelekqlnqlkseisdlnnqkeqDWNK---ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 299 SEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQM-MDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDR 377
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLeSQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 378 NSLQAAKAGLEDECKTLRQKVEILNELYQQkemaLQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 457
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRES----LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511

                         410
                  ....*....|....*
gi 1622828953 458 LQKTER---SFKNQI 469
Cdd:TIGR04523 512 VKDLTKkisSLKEKI 526
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 96-414 2.10e-11

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: 67.69  E-value: 2.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   96 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRK---------------QNMILSDEAIKFKDKIKTLEKNNEILGDA 160
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeEYLLYLDYLKLNEERIDLLQELLRDEQEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  161 AKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQ 240
Cdd:pfam02463  253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  241 LQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKddniNALTNCITQLNRLECESESEGQnKGGNDSDELANGEVGGD 320
Cdd:pfam02463  333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----EQLEEELLAKKKLESERLSSAA-KLKEEELELKSEEEKEA 407

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  321 QNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEI 400
Cdd:pfam02463  408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487

                          330
                   ....*....|....
gi 1622828953  401 LNELYQQKEMALQK 414
Cdd:pfam02463  488 LLLSRQKLEERSQK 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-470 6.62e-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: 66.23  E-value: 6.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  159 DAAKNLRVMLESEREQNVKNQDLISEnkkSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEE---KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRlECESESEG----QNKGGNDSDELAN 314
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREAldelRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  315 GEVGGDQNEKMKNQIKQMMDvsRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTL 394
Cdd:TIGR02168  822 LRERLESLERRIAATERRLE--DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  395 RQKVEILN----ELYQQKEmALQKKLSQEEYERQEREHRL----SAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFK 466
Cdd:TIGR02168  900 SEELRELEskrsELRRELE-ELREKLAQLELRLEGLEVRIdnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978


                   ....
gi 1622828953  467 NQIA 470
Cdd:TIGR02168  979 NKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 119-462 3.86e-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: 3.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  119 IKESKKHVQETRKQnmilSDEAIKFKdkiktlEKNNEiLGDAAKNLRVM-LESEREQNVKNQDLISENKKSIEKLKDAIS 197
Cdd:TIGR02168  195 LNELERQLKSLERQ----AEKAERYK------ELKAE-LRELELALLVLrLEELREELEELQEELKEAEEELEELTAELQ 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  198 MNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKD 277
Cdd:TIGR02168  264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  278 DNINALTNCITQLNRLECESESEGQNkggndsdelangevggdQNEKMKNQIKQMMDVSRtqtAISVVEEDLKLLQLKLR 357
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEE-----------------LESRLEELEEQLETLRS---KVAQLELQIASLNNEIE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  358 asvstkcNLEDQIKKLEDDRNSLQAAKAGLEDEcKTLRQKVEILNELYQQKEMA--LQKKLSQEEYERQEREHRLSAADE 435
Cdd:TIGR02168  404 -------RLEARLERLEDRRERLQQEIEELLKK-LEEAELKELQAELEELEEELeeLQEELERLEEALEELREELEEAEQ 475

                          330       340
                   ....*....|....*....|....*..
gi 1622828953  436 KAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQENLE 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
91-517 4.39e-10

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEkLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILsDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 170
Cdd:COG4717    77 EEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAELPERLEELEER 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 171 EREqnvknqdlISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKvksechRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:COG4717   155 LEE--------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ------DLAEELEELQQRLAELEEELEEAQE 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 251 LHAELSEQIKSFEKSQKDLE------------------VALTHKDDNINALTNCIT-------QLNRLECESESEGQNKG 305
Cdd:COG4717   221 ELEELEEELEQLENELEAAAleerlkearlllliaaalLALLGLGGSLLSLILTIAgvlflvlGLLALLFLLLAREKASL 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 306 GNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLqAAKA 385
Cdd:COG4717   301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LAEA 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 386 GLEDEcKTLRQKVEILNElYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVsaAEEVKTYKRRIEEMEDE---LQKTE 462
Cdd:COG4717   380 GVEDE-EELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEEleeLREEL 455

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953 463 RSFKNQIATHEKkahenwlkaraaeraiaeeKREAANLRHKLLELTQKMAMLQEE 517
Cdd:COG4717   456 AELEAELEQLEE-------------------DGELAELLQELEELKAELRELAEE 491
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 91-414 6.03e-10

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: 62.73  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEKLKIIMKE--NTELVQK-----LSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKN 163
Cdd:TIGR04523  35 EKQLEKKLKTIKNElkNKEKELKnldknLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 164 lrvmlesEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ 243
Cdd:TIGR04523 115 -------DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 244 EIED-----------------WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI----TQLNRLEcESESEGQ 302
Cdd:TIGR04523 188 NIDKiknkllklelllsnlkkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEIsntqTQLNQLK-DEQNKIK 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 303 NKGGNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQ----------TAISVVEEDLKLLQLKLRASVSTKCNLEDQIKK 372
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1622828953 373 LEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQK 414
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
91-463 6.70e-10

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 62.75  E-value: 6.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEKlkiimkENTELVQKLSNYEQKIKESK---KHVQETRKQ--------NMILS------------DEAI-KFKDK 146
Cdd:PRK02224  193 KAQIEEK------EEKDLHERLNGLESELAELDeeiERYEEQREQaretrdeaDEVLEeheerreeletlEAEIeDLRET 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 147 IKTLEKNNEILGDAAKNLRVM---LESEREQNVKNQDLISENKKSIEKLKDAISmnaSEFSEVQIALNEAKLSEEKVKSE 223
Cdd:PRK02224  267 IAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEAVEARREELE---DRDEELRDRLEECRVAAQAHNEE 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 224 CHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNRLECESESEGQN 303
Cdd:PRK02224  344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI---EELRERFGDAPVDLGNAEDFLEELREE 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 304 KGGNDSDElANGEVGGDQNEKMKNQIKQMMDVSRTQTA---------ISVVEEDLKLLQlKLRASVSTkcnLEDQIKKLE 374
Cdd:PRK02224  421 RDELRERE-AELEATLRTARERVEEAEALLEAGKCPECgqpvegsphVETIEEDRERVE-ELEAELED---LEEEVEEVE 495

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 375 DDRNSLQAAKAgLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEK----------AVSAAEEV 444
Cdd:PRK02224  496 ERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKreaaaeaeeeAEEAREEV 574

                         410
                  ....*....|....*....
gi 1622828953 445 KTYKRRIEEMEDELQKTER 463
Cdd:PRK02224  575 AELNSKLAELKERIESLER 593
PTZ00121 PTZ00121
MAEBL; Provisional
 103-478 7.00e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 7.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  103 KENTELVQKLSNYEQKIKESKKHVQETRKqnmilSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLI 182
Cdd:PTZ00121  1404 KKKADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  183 SENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEE--NARLKKKKEQLQQEIEDWSKLHAELSEQIK 260
Cdd:PTZ00121  1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  261 SFEKSQKdLEVALTHKDDNINALTNCiTQLNRLEcESESEGQNKGGNDSDELANGEVGGDQNEKMK-NQIKQMMDVSRT- 338
Cdd:PTZ00121  1559 KAEEKKK-AEEAKKAEEDKNMALRKA-EEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKKKv 1635

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  339 -QTAISVVEEDLKLLQLKlRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQkkLS 417
Cdd:PTZ00121  1636 eQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE----KKAAEALKKEAEEAKKAEE--LK 1708

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828953  418 QEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSfKNQIAtHEKKAHE 478
Cdd:PTZ00121  1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKIA-HLKKEEE 1767
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
91-507 9.04e-10

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 62.39  E-value: 9.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEKLKIIMKENtELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 170
Cdd:PRK03918  175 KRRIERLEKFIKRTE-NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 171 ER--EQNVKN-QDLISENKKSIEKLKDaismNASEFSEVQ-IALNEAKLSE--EKVKSECHRVQEENARLKKKKEQLQQE 244
Cdd:PRK03918  254 KRklEEKIRElEERIEELKKEIEELEE----KVKELKELKeKAEEYIKLSEfyEEYLDELREIEKRLSRLEEEINGIEER 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 245 IEDWSKLHAELSEQIKSFEKSQKDLEVaLTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDEL--ANGEVGGDQN 322
Cdd:PRK03918  330 IKELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELekAKEEIEEEIS 408

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 323 E------KMKNQIKQMMD-VSRTQTAISVV--------EEDLKLLQLKLRASVStkcNLEDQIKKLEDDRNSLQAAKAGL 387
Cdd:PRK03918  409 KitarigELKKEIKELKKaIEELKKAKGKCpvcgreltEEHRKELLEEYTAELK---RIEKELKEIEEKERKLRKELREL 485

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 388 EDECKTLRqKVEILNELYQQKEmALQKKLSQEEYErqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTErSFKN 467
Cdd:PRK03918  486 EKVLKKES-ELIKLKELAEQLK-ELEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKK 556

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1622828953 468 QIATHEKKAHEnwlkaraaeraiaeEKREAANLRHKLLEL 507
Cdd:PRK03918  557 KLAELEKKLDE--------------LEEELAELLKELEEL 582
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 155-482 4.56e-09

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: 60.37  E-value: 4.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  155 EILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKV-KSECHRVQEENAR 233
Cdd:pfam02463  169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRD 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  234 LKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEG---QNKGGNDSD 310
Cdd:pfam02463  249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLkesEKEKKKAEK 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  311 ELANgevggdQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcNLEDQIKKLEDDRNSLQAAKAGLEDE 390
Cdd:pfam02463  329 ELKK------EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ------LEEELLAKKKLESERLSSAAKLKEEE 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  391 cKTLR----QKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFK 466
Cdd:pfam02463  397 -LELKseeeKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475

                          330
                   ....*....|....*.
gi 1622828953  467 NQIATHEKKAHENWLK 482
Cdd:pfam02463  476 ETQLVKLQEQLELLLS 491
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 87-373 9.10e-09

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: 58.88  E-value: 9.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  87 YQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRV 166
Cdd:TIGR04523 403 QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQ 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 167 MLE-SEREQNVKNQD---LISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK---KKE 239
Cdd:TIGR04523 483 NLEqKQKELKSKEKElkkLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKE 562

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 240 --QLQQEIEdwsklhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCItqlnrleceseSEGQNKGGNDSDELANGEv 317
Cdd:TIGR04523 563 idEKNKEIE-------ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-----------EEKEKKISSLEKELEKAK- 623

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828953 318 ggDQNEKMKNQIKQMmdvsrtQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKL 373
Cdd:TIGR04523 624 --KENEKLSSIIKNI------KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 90-401 1.25e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 58.93  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   90 TEQQISEKLKIIMK-----ENTELVQKLSNYEQKIKESKKHVQETRKQnmiLSDEAIKFKDKIKTLEKNNEILGDAakNL 164
Cdd:TIGR02169  205 REREKAERYQALLKekreyEGYELLKEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEEL--NK 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  165 RVMLESEREQN-VKNQdlISENKKSIEKLKDAISMNASEfsevqiaLNEAKLSEEKVKSECHRVQEEnarlkkkKEQLQQ 243
Cdd:TIGR02169  280 KIKDLGEEEQLrVKEK--IGELEAEIASLERSIAEKERE-------LEDAEERLAKLEAEIDKLLAE-------IEELER 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  244 EIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALtncitqlnRLECESESEGQNKGGNDSDELaNGEVGGDQNE 323
Cdd:TIGR02169  344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET--------RDELKDYREKLEKLKREINEL-KRELDRLQEE 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  324 KMKNQIKQM---MDVSRTQTAISVVEEDLKLLQLKLRAS----VSTKCNLEDQIKKLEDDRNSLQAakagLEDECKTLRQ 396
Cdd:TIGR02169  415 LQRLSEELAdlnAAIAGIEAKINELEEEKEDKALEIKKQewklEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQR 490


                   ....*
gi 1622828953  397 KVEIL 401
Cdd:TIGR02169  491 ELAEA 495
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
94-478 1.75e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  94 ISEKLKIIMKENTELVQKLSNYEQKIKESKKhVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLEsERE 173
Cdd:PRK03918  257 LEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELE 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 174 QNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEA-KLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLH 252
Cdd:PRK03918  335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 253 AELSEQIKSFEKSQKDLEVA----------LT--HKDDNINALTnciTQLNRLECESE--SEGQNKGGNDSDELANGEVG 318
Cdd:PRK03918  415 GELKKEIKELKKAIEELKKAkgkcpvcgreLTeeHRKELLEEYT---AELKRIEKELKeiEEKERKLRKELRELEKVLKK 491

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 319 GDQNEKMKNQIKQMMDVSRTQTAISVVE--------EDLKLLQLKLRASVStkcNLEDQIKKLEDDRNSLQA---AKAGL 387
Cdd:PRK03918  492 ESELIKLKELAEQLKELEEKLKKYNLEElekkaeeyEKLKEKLIKLKGEIK---SLKKELEKLEELKKKLAElekKLDEL 568

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 388 EDECKTLRQK--------VEILNELYQQKEMALQK--KLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 457
Cdd:PRK03918  569 EEELAELLKEleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648

                         410       420
                  ....*....|....*....|.
gi 1622828953 458 LQKTERSFKNQiaTHEKKAHE 478
Cdd:PRK03918  649 LEELEKKYSEE--EYEELREE 667
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 168-435 2.20e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 168 LESEREQNVKNQDLIsenKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 247
Cdd:COG1196   251 LEAELEELEAELAEL---EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 248 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTnciTQLNRLECESESEGQNKggnDSDELANGEVGGDQNEKMKN 327
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAEEEL---EELAEELLEALRAAAELAAQ 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 328 QIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQ 407
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAE-------LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                         250       260
                  ....*....|....*....|....*...
gi 1622828953 408 KEMALQKKLSQEEYERQEREHRLSAADE 435
Cdd:COG1196   475 LEAALAELLEELAEAAARLLLLLEAEAD 502
PTZ00121 PTZ00121
MAEBL; Provisional
 83-517 2.44e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 2.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   83 KSRVYQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKqnmilSDEAIKFKDKIKtlEKNNEILGDAAK 162
Cdd:PTZ00121  1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDK--KKADELKKAAAA 1416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  163 NLRVMLESEREQNVKNQDlisENKKSIEKLKDAISMNaSEFSEVQIALNEAKLSEEKVKSECHRVQEENAR----LKKKK 238
Cdd:PTZ00121  1417 KKKADEAKKKAEEKKKAD---EAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadeAKKKA 1492

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  239 EQLQQEIEDWSKLHAEL--SEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGE 316
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKkkADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  317 VGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEdQIKKLEDDRNSLQAAKAGLEDECKTLRQ 396
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  397 kVEILNELYQQKEMALQKKlsqeEYERQEREHRLSAADEKAVSAAEEVKtykRRIEEME--DELQKTERSFKNQIATHEK 474
Cdd:PTZ00121  1652 -LKKAEEENKIKAAEEAKK----AEEDKKKAEEAKKAEEDEKKAAEALK---KEAEEAKkaEELKKKEAEEKKKAEELKK 1723

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1622828953  475 KAHENWLKARAAERAIAEEKREAANLRhKLLELTQKMAMLQEE 517
Cdd:PTZ00121  1724 AEEENKIKAEEAKKEAEEDKKKAEEAK-KDEEEKKKIAHLKKE 1765
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
93-463 4.79e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  93 QISEKLKIIMKENTELVQKLSNYEqKIKESKKHVQETRKQNMILSDEaiKFKDKIKTLEKNNEILGDAAKNLRvmlesER 172
Cdd:PRK03918  342 ELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKIT-----AR 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 173 EQNVKNQdlISENKKSIEKLKDA------ISMNASEFSEVQIaLNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIE 246
Cdd:PRK03918  414 IGELKKE--IKELKKAIEELKKAkgkcpvCGRELTEEHRKEL-LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 247 DWSKLHA--ELSEQIKSFEKSQKDLEVALTHKD--------DNINALTNCITQLNRlECESESEGQNKGGNDSDELANGE 316
Cdd:PRK03918  491 KESELIKlkELAEQLKELEEKLKKYNLEELEKKaeeyeklkEKLIKLKGEIKSLKK-ELEKLEELKKKLAELEKKLDELE 569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 317 vggdqnEKMKNQIKQMMdvSRTQTAISVVEEDLKLLQ------LKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDE 390
Cdd:PRK03918  570 ------EELAELLKELE--ELGFESVEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828953 391 CKTLRQKVEILNELYQQKEMA----LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:PRK03918  642 LEELRKELEELEKKYSEEEYEelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
PHA03247 PHA03247
large tegument protein UL36; Provisional
 525-795 6.17e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 6.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  525 PGRPNTQNPPRRGPL--SQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPRWSAEASGKP 602
Cdd:PHA03247  2670 LGRAAQASSPPQRPRrrAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPA 2749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  603 SPSDPGSGTAAMMNSSSRGSSPNRVIDEGKQTVLQEPEV-------PSVPSITSLAEHPVAVNM-----------APKGP 664
Cdd:PHA03247  2750 TPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVaslsesrESLPSPWDPADPPAAVLApaaalppaaspAGPLP 2829

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  665 PPFSGVPLMSTPMGGPIPPPIRYGPPP----QLCGPFGPRPLPPPFGPGMRPPLGlREFAPGVPPGKRDLPLHPREFLPG 740
Cdd:PHA03247  2830 PPTSAQPTAPPPPPGPPPPSLPLGGSVapggDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRSTESFALPPDQPERP 2908

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953  741 HTPFRPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQ 795
Cdd:PHA03247  2909 PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 90-463 7.52e-08

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: 55.90  E-value: 7.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  90 TEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILgdAAKNLRVMlE 169
Cdd:pfam05557  98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL--AEAEQRIK-E 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 170 SEREQNVKNQD-LISENKKS-------IEKLKDAI-SMNA--SEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:pfam05557 175 LEFEIQSQEQDsEIVKNSKSelaripeLEKELERLrEHNKhlNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEK 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 239 EQLQQEIEDWSKLHAE----------LSEQIKSFEKSQkdlevaLTHKDDNiNALTNCITQLNRLECESESEGQNKGGND 308
Cdd:pfam05557 255 EKLEQELQSWVKLAQDtglnlrspedLSRRIEQLQQRE------IVLKEEN-SSLTSSARQLEKARRELEQELAQYLKKI 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 309 SDElangevggdqNEKMKNQIKQmmdVSRTQTAISVVEEDLKLLQLKLR------ASVSTKCNLEDQIKKLEDDRNSLQA 382
Cdd:pfam05557 328 EDL----------NKKLKRHKAL---VRRLQRRVLLLTKERDGYRAILEsydkelTMSNYSPQLLERIEEAEDMTQKMQA 394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 383 AKAGLEDECKTLRQKVEILNELYQQKEMALQKKlsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:pfam05557 395 HNEEMEAQLSVAEEELGGYKQQAQTLERELQAL-------------RQQESLADPSYSKEEVDSLRRKLETLELERQRLR 461


                  .
gi 1622828953 463 R 463
Cdd:pfam05557 462 E 462
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 92-482 1.09e-07

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: 55.89  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   92 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHV-------QETRKQNMILSDEAIKFKDKIKTLeknneiLGDAAKNL 164
Cdd:pfam15921  317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKL------LADLHKRE 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  165 RvMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALneaklseEKVKSECH-RVQEENARLKKKKE---- 239
Cdd:pfam15921  391 K-ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-------KAMKSECQgQMERQMAAIQGKNEslek 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  240 ------QLQQEIEDWSKLHAELSEQIKSFEKSQK---DLEVALTHKDDNINALTNCITQL-NRLECESESEGQNKggNDS 309
Cdd:pfam15921  463 vssltaQLESTKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEITKLrSRVDLKLQELQHLK--NEG 540

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  310 DELANGEV----------GGDQN-EKMKNQIKQMMDV----SRTQTAISV----VEEDLKLLQLKLRASVSTKCNLEDQI 370
Cdd:pfam15921  541 DHLRNVQTecealklqmaEKDKViEILRQQIENMTQLvgqhGRTAGAMQVekaqLEKEINDRRLELQEFKILKDKKDAKI 620

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  371 KKLEDDRNSLQAAKAGLEDECKtlrQKVEILNELYQQKEMALQkklsqeeyerqerehrlsaadekavsaaeEVKTYKRR 450
Cdd:pfam15921  621 RELEARVSDLELEKVKLVNAGS---ERLRAVKDIKQERDQLLN-----------------------------EVKTSRNE 668

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1622828953  451 IEEMEDELQKTERSFKNQiaTHEKKAHENWLK 482
Cdd:pfam15921  669 LNSLSEDYEVLKRNFRNK--SEEMETTTNKLK 698
46 PHA02562
endonuclease subunit; Provisional
 173-410 1.23e-07

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 55.02  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 173 EQNVKNQDLISENK---KSIEKLKDAIsmnasefsEVQIALNEAKLSEEKVKSEchrvqEENARLKKKKEQLQQEIEDWS 249
Cdd:PHA02562  167 EMDKLNKDKIRELNqqiQTLDMKIDHI--------QQQIKTYNKNIEEQRKKNG-----ENIARKQNKYDELVEEAKTIK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 250 KLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLE-----------CESE-SEGQNKGGNDSDELANGEV 317
Cdd:PHA02562  234 AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQiSEGPDRITKIKDKLKELQH 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 318 GGDQNEKMKNQIKQMMDVSRTQTaisvveEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQK 397
Cdd:PHA02562  314 SLEKLDTAIDELEEIMDEFNEQS------KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387

                         250
                  ....*....|...
gi 1622828953 398 VEILNELYQQKEM 410
Cdd:PHA02562  388 LDKIVKTKSELVK 400
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 81-416 1.43e-07

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: 54.96  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  81 VVKSRVYQVTEQQISEKLKIIMKENTELVQKLS-NYEQKIKESKKHVQETRKQNMILSDEAIKFKdkiKTLEKNNEILGD 159
Cdd:COG5185   192 ISELKKAEPSGTVNSIKESETGNLGSESTLLEKaKEIINIEEALKGFQDPESELEDLAQTSDKLE---KLVEQNTDLRLE 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 160 AAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNAS-EFSEVQIALNEAKLSEEKVKSEchrVQEENARLKKKK 238
Cdd:COG5185   269 KLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKAtESLEEQLAAAEAEQELEESKRE---TETGIQNLTAEI 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 239 EQLQQEI-EDWSKLHAELSE--QIKSFEKSQKDLEVALTH----KDDNINALTNCITQLNRLEcesESEGQNKGGNDSD- 310
Cdd:COG5185   346 EQGQESLtENLEAIKEEIENivGEVELSKSSEELDSFKDTiestKESLDEIPQNQRGYAQEIL---ATLEDTLKAADRQi 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 311 ELANGEVGGD--QNEKMKNQIKQMMDvSRTQTAISVVEEDLKLLQLKLRASVSTkcnLEDQIKKLEDDRNSLQAAKAGLE 388
Cdd:COG5185   423 EELQRQIEQAtsSNEEVSKLLNELIS-ELNKVMREADEESQSRLEEAYDEINRS---VRSKKEDLNEELTQIESRVSTLK 498

                         330       340
                  ....*....|....*....|....*...
gi 1622828953 389 DECKTLRQKVEILNELYQQKEMALQKKL 416
Cdd:COG5185   499 ATLEKLRAKLERQLEGVRSKLDQVAESL 526
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 92-283 1.58e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.38  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  92 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKN-NEILGDAAKNLRVMLES 170
Cdd:COG4942    37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAElEAQKEELAELLRALYRL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 171 EREQNVK---NQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 247
Cdd:COG4942   117 GRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622828953 248 WSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINAL 283
Cdd:COG4942   197 RQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 92-461 4.14e-07

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: 53.82  E-value: 4.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   92 QQISEKLKIIMKENTELVQKLSNYEQKIKESKkhvqetRKQNMILSDEAIKFKDKIKTLEKNNeilGDAAKNLRVMLESE 171
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILR------RQLEIKKKEQREKEELKKLKLEAEE---LLADRVQEAQDKIN 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  172 REQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQialNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEdwskl 251
Cdd:pfam02463  736 EELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE----- 807

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  252 hAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKggndsDELANGEVGGDQNEKMKNQIKQ 331
Cdd:pfam02463  808 -EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL-----EEEITKEELLQELLLKEEELEE 881

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  332 MMDVSRTQTAISVVEEDLKLLQLKLRASV-----STKCNLEDQIKKLEDDRNSLQAAK-----AGLEDECKTLRQKVEIL 401
Cdd:pfam02463  882 QKLKDELESKEEKEKEEKKELEEESQKLNlleekENEIEERIKEEAEILLKYEEEPEEllleeADEKEKEENNKEEEEER 961

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828953  402 NELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVK---------TYKRRIEEMEDELQKT 461
Cdd:pfam02463  962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKkliraiieeTCQRLKEFLELFVSIN 1030
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 195-443 4.48e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 195 AISMNASEFSEVQIALNEAKLSEekvksechrVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALT 274
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSE---------LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 275 HKDDNINALTNCITQLNRLEcesesegQNKGGNDS--DELANGEVGGDQNEKMkNQIKQMMDvsRTQTAISVVEEDLKLL 352
Cdd:COG3883    76 EAEAEIEERREELGERARAL-------YRSGGSVSylDVLLGSESFSDFLDRL-SALSKIAD--ADADLLEELKADKAEL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 353 QLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 432
Cdd:COG3883   146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225

                         250
                  ....*....|.
gi 1622828953 433 ADEKAVSAAEE 443
Cdd:COG3883   226 AAAAAAAAAAA 236
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 96-409 4.66e-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: 53.52  E-value: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   96 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLekNNEIlgdAAKNLRVMLESEREQN 175
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL--ANEI---SRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  176 VKNQ-----DLISENKKSIEKLKDAISMNASEFSEVQIALNEAklsEEKVKsECHRVQEEnarLKKKKEQLQQEIEDWSK 250
Cdd:TIGR02168  314 LERQleeleAQLEELESKLDELAEELAELEEKLEELKEELESL---EAELE-ELEAELEE---LESRLEELEEQLETLRS 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  251 LHAELSEQIKSFEKSQKDLEVALTHKDDNinaltncitqLNRLECESESEGQNKGGNDSDELangevggdqnekmknqik 330
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDR----------RERLQQEIEELLKKLEEAELKEL------------------ 438

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828953  331 qmmdvsrtQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSlqaakagLEDECKTLRQKVEILNELYQQKE 409
Cdd:TIGR02168  439 --------QAELEELEEELEELQEELERLEEALEELREELEEAEQALDA-------AERELAQLQARLDSLERLQENLE 502
PTZ00121 PTZ00121
MAEBL; Provisional
 116-501 6.49e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 6.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  116 EQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEK-NNEILGDAAKNLRVMLESEREQNVKnqdliSENKKSIEKLKD 194
Cdd:PTZ00121  1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEeRNNEEIRKFEEARMAHFARRQAAIK-----AEEARKADELKK 1285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  195 AismnasefSEVQIAlNEAKLSEEKVKSECHRVQEENARlkkKKEQLQQEIEDWSKLHAELSeqiKSFEKSQKDLEVAlt 274
Cdd:PTZ00121  1286 A--------EEKKKA-DEAKKAEEKKKADEAKKKAEEAK---KADEAKKKAEEAKKKADAAK---KKAEEAKKAAEAA-- 1348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  275 hkddninaltncitqlnrlecesesegQNKGGNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQTaisvvEEDLKLLQL 354
Cdd:PTZ00121  1349 ---------------------------KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA-----EEKKKADEA 1396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  355 KLRASVSTKcnLEDQIKKLEDDRNSLQAAKAGLEDECKT--LRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSA 432
Cdd:PTZ00121  1397 KKKAEEDKK--KADELKKAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828953  433 ADEKAVSA--AEEVKTYKRRIEEMEDELQKTERSFKNqiATHEKKAHEnwlKARAAERAIAEEKREAANLR 501
Cdd:PTZ00121  1475 AKKKAEEAkkADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKAEE---AKKADEAKKAEEAKKADEAK 1540
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-517 6.94e-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: 53.14  E-value: 6.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   92 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESE 171
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  172 REQNVKNQDLISENKK-----SIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK---EQLQQ 243
Cdd:TIGR02168  420 QQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQE 499

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  244 EIEDWSK--------------LHAELSEQIKSFEKSQKDLEVAL-------THKDDN-----INALT-NCITQLNRLECE 296
Cdd:TIGR02168  500 NLEGFSEgvkallknqsglsgILGVLSELISVDEGYEAAIEAALggrlqavVVENLNaakkaIAFLKqNELGRVTFLPLD 579

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  297 SESEGQNKgGNDSDELAN--GEVG-GDQNEKMKNQIKQMMD--------VSRTQTAIsvveEDLKLLQLKLR-------- 357
Cdd:TIGR02168  580 SIKGTEIQ-GNDREILKNieGFLGvAKDLVKFDPKLRKALSyllggvlvVDDLDNAL----ELAKKLRPGYRivtldgdl 654

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  358 ---------ASVSTKC----------NLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEM---ALQKK 415
Cdd:TIGR02168  655 vrpggvitgGSAKTNSsilerrreieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisALRKD 734

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  416 LSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER---SFKNQIATHEKKAHENWLKARAAERAIAE 492
Cdd:TIGR02168  735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAeieELEAQIEQLKEELKALREALDELRAELTL 814

                          490       500
                   ....*....|....*....|....*
gi 1622828953  493 EKREAANLRHKLLELTQKMAMLQEE 517
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERR 839
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
152-481 8.14e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 8.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 152 KNNEILGDAAKNLRVMLES----EREQNVKNQDLiSENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRV 227
Cdd:COG4372    21 KTGILIAALSEQLRKALFEldklQEELEQLREEL-EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 228 QEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGN 307
Cdd:COG4372   100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 308 DSDE-----LANGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQA 382
Cdd:COG4372   180 EAEQaldelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 383 AKAGLEDECKTLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:COG4372   260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339

                         330
                  ....*....|....*....
gi 1622828953 463 RSFKNQIATHEKKAHENWL 481
Cdd:COG4372   340 ADLLQLLLVGLLDNDVLEL 358
COG5022 COG5022
Myosin heavy chain [General function prediction only];
78-457 8.59e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 52.77  E-value: 8.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   78 TVLVVK-SRVYQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLE-KNNE 155
Cdd:COG5022    845 EVLIQKfGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLiENLE 924

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  156 ILGDAAKNLRVMLES---------EREQNVKNQDLISEN---KKSIEKLKDAISMNASEFSEVQIALNEAKlseeKVKSE 223
Cdd:COG5022    925 FKTELIARLKKLLNNidleegpsiEYVKLPELNKLHEVEsklKETSEEYEDLLKKSTILVREGNKANSELK----NFKKE 1000

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  224 CHRVQEENARLKKKKEQLQQEIEDWSKLHAELS--EQIKSFEKSQKDLevalthkDDNINALTnciTQLNRLECESESEG 301
Cdd:COG5022   1001 LAELSKQYGALQESTKQLKELPVEVAELQSASKiiSSESTELSILKPL-------QKLKGLLL---LENNQLQARYKALK 1070

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  302 QNKGGNDSDELangevggdqnekmknQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVST-------KCNLEDQIKKle 374
Cdd:COG5022   1071 LRRENSLLDDK---------------QLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQfivaqmiKLNLLQEISK-- 1133

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  375 ddrnSLQAAKAGLEDECKTLRQKVEILNELYQQKemALQKKLSQEEYERQEREHRLSAA--DEKAVSAAEEVKTYKRRIE 452
Cdd:COG5022   1134 ----FLSQLVNTLEPVFQKLSVLQLELDGLFWEA--NLEALPSPPPFAALSEKRLYQSAlyDEKSKLSSSEVNDLKNELI 1207


                   ....*
gi 1622828953  453 EMEDE 457
Cdd:COG5022   1208 ALFSK 1212
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
94-478 1.01e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 52.37  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  94 ISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNmilsDEAIKFKDKIKTLEKNNEILG------DAAKNLRVM 167
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEerhelyEEAKAKKEE 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 168 LES--------EREQNVKNQDLISENKKSIE----KLKDAISMNASEFSEVQIALNEAKLSEEKVKSeCHRVQEENARlK 235
Cdd:PRK03918  374 LERlkkrltglTPEKLEKELEELEKAKEEIEeeisKITARIGELKKEIKELKKAIEELKKAKGKCPV-CGRELTEEHR-K 451

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 236 KKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALThKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELAN- 314
Cdd:PRK03918  452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKl 530

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 315 ----GEVGGDQnEKMKNQIKQMMDVSRTQTAISV----VEEDLKLLQLKLRA-SVSTKCNLEDQIKKLE----------D 375
Cdd:PRK03918  531 keklIKLKGEI-KSLKKELEKLEELKKKLAELEKkldeLEEELAELLKELEElGFESVEELEERLKELEpfyneylelkD 609

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 376 DRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMaLQKKLSQEEYERQEREHRlsAADEKAVSAAEEVKTYKRRIEEME 455
Cdd:PRK03918  610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEE-LRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELE 686

                         410       420
                  ....*....|....*....|....*.
gi 1622828953 456 ---DELQKTERSFKNQIATHEKKAHE 478
Cdd:PRK03918  687 krrEEIKKTLEKLKEELEEREKAKKE 712
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 226-517 1.12e-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: 52.37  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  226 RVQEENARLKKKkeqlqQEIEdwsklhaELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESEsegqnkg 305
Cdd:TIGR02168  665 SAKTNSSILERR-----REIE-------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS------- 725

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  306 gndsDELANGEvggdqnekmknqikqmMDVSRTQTAISVVEEDLKLLQLKLRasvstkcNLEDQIKKLEDDRNSLQAAKA 385
Cdd:TIGR02168  726 ----RQISALR----------------KDLARLEAEVEQLEERIAQLSKELT-------ELEAEIEELEERLEEAEEELA 778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  386 GLEDECKTLRQKVE-ILNELYQQKEM--ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02168  779 EAEAEIEELEAQIEqLKEELKALREAldELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953  463 RSFKNQIATHEK--KAHENWLKARAAERAIAEEKREAA--------NLRHKLLELTQKMAMLQEE 517
Cdd:TIGR02168  859 AEIEELEELIEEleSELEALLNERASLEEALALLRSELeelseelrELESKRSELRRELEELREK 923
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 191-457 1.13e-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: 52.38  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  191 KLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLE 270
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  271 VALTHKDDNINALtncITQLNRLEcESESEGQNKGGNDSDELANGEVggDQNEKMKNQIKQmmDVSRTQTAISVVEEDLK 350
Cdd:TIGR02169  751 QEIENVKSELKEL---EARIEELE-EDLHKLEEALNDLEARLSHSRI--PEIQAELSKLEE--EVSRIEARLREIEQKLN 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  351 LLQLKLRASVSTKCNLEDQIKKLEDDRNS-------LQAAKAGLEDECKTLRQKVEILNELYQ---------QKEM-ALQ 413
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELEAALRDLESRLGdlkkerdelEAQLrELE 902

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1622828953  414 KKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDE 457
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
PHA03247 PHA03247
large tegument protein UL36; Provisional
 523-794 1.33e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  523 PMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPrwSAEASGKP 602
Cdd:PHA03247  2769 PAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA--PPPPPGPP 2846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  603 SPSDPGSGTAAMMNSSSRGSSPnrvidegkQTVLQEPEVPSVPSITSLAEHPVAVNMAPKGPPPFSGVPLMSTPMGGPIP 682
Cdd:PHA03247  2847 PPSLPLGGSVAPGGDVRRRPPS--------RSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQ 2918

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  683 PPIRygpppqlcgpfgprplpppfgpgmrPPLGLREFAPGVPPGKRDLPLHPR---EFLPGHTPFRP---LGPLGPREYF 756
Cdd:PHA03247  2919 PQPQ-------------------------PPPPPQPQPPPPPPPRPQPPLAPTtdpAGAGEPSGAVPqpwLGALVPGRVA 2973

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622828953  757 IPGARLPPPTHG-PQDYPPPPAARDLPPSG-----------SRDDPPPAS 794
Cdd:PHA03247  2974 VPRFRVPQPAPSrEAPASSTPPLTGHSLSRvsswasslalhEETDPPPVS 3023
PTZ00121 PTZ00121
MAEBL; Provisional
 96-510 1.42e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   96 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTleknneilgdaAKNLRVMLESEREQN 175
Cdd:PTZ00121  1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKK-----------AEDARKAEEARKAED 1138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  176 VKNqdlISENKKSIEKLKDAISMNASEFSEVQIA--------LNEAKLSEEKVKSECHRVQEENARLKK-KKEQLQQEIE 246
Cdd:PTZ00121  1139 ARK---AEEARKAEDAKRVEIARKAEDARKAEEArkaedakkAEAARKAEEVRKAEELRKAEDARKAEAaRKAEEERKAE 1215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  247 DWSKLH-AELSEQIKSFEKSQKDLEVALTHKDDNINALTNC-----ITQLNRLECESESEGQNKggndSDELANGEvggd 320
Cdd:PTZ00121  1216 EARKAEdAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeearMAHFARRQAAIKAEEARK----ADELKKAE---- 1287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  321 qNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRASVSTKcNLEDQIKKLEDDRNSLQAAKAGLEDECKTL------ 394
Cdd:PTZ00121  1288 -EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAEEAKKAAEAAKAEAEAAADEAeaaeek 1365

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  395 -----------RQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:PTZ00121  1366 aeaaekkkeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1622828953  464 SFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRhKLLELTQK 510
Cdd:PTZ00121  1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK-KADEAKKK 1491
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
108-469 1.51e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.96  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 108 LVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQnvknqdlISENKK 187
Cdd:PRK02224  312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA-------VEDRRE 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 188 SIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLK----------KKKEQLQ---------QEIEDW 248
Cdd:PRK02224  385 EIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlrtarervEEAEALLeagkcpecgQPVEGS 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 249 SKLHA--ELSEQIKSFEKSQKDLEVALTHKDDNINALTNCI---TQLNRLECESESEGQ----NKGGNDSDELA------ 313
Cdd:PRK02224  465 PHVETieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaeDRIERLEERREDLEEliaeRRETIEEKRERaeelre 544

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 314 -NGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKllqlklrasvstkcNLEDQIKKLEDDRNSLqAAKAGLEDECK 392
Cdd:PRK02224  545 rAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA--------------ELKERIESLERIRTLL-AAIADAEDEIE 609

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 393 TLRQKVEILNELY-QQKEMALQKKLSQEEYERQEREHRLSAADEK---AVSAAEEVKTYKRRIEEMEDELQKTERSFKNQ 468
Cdd:PRK02224  610 RLREKREALAELNdERRERLAEKRERKRELEAEFDEARIEEAREDkerAEEYLEQVEEKLDELREERDDLQAEIGAVENE 689


                  .
gi 1622828953 469 I 469
Cdd:PRK02224  690 L 690
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 228-463 1.95e-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: 50.92  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 228 QEENARLKKKKEQLQQEIedwsklhAELSEQIKSFEKSQKDLEVALTHKDDNINALTNcitQLNRLECESESEGQNKGGN 307
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI-------AELEKELAALKKEEKALLKQLAALERRIAALAR---RIRALEQELAALEAELAEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 308 DSDELANGEVGGDQNEKMKNQIKQMMDVSRT--------QTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNS 379
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPA-------RREQAEELRADLAE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 380 LQAAKAGLEDECKTLRQkveILNELYQQKEmALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQ 459
Cdd:COG4942   162 LAALRAELEAERAELEA---LLAELEEERA-ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237


                  ....
gi 1622828953 460 KTER 463
Cdd:COG4942   238 AAAE 241
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 91-282 2.07e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  91 EQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLES 170
Cdd:COG3883    32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 171 EreqNVknQDLISenkkSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:COG3883   112 E---SF--SDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622828953 251 LHAELSEQIKSFEKSQKDLEVALTHKDDNINA 282
Cdd:COG3883   183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 184-517 2.21e-06

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: 51.51  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  184 ENKKSIEKLKDAISMNAS----EFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQI 259
Cdd:pfam02463  174 ALKKLIEETENLAELIIDleelKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  260 KSFEKSQKDLE--VALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQmmdvSR 337
Cdd:pfam02463  254 ESSKQEIEKEEekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE----KE 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  338 TQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKKLS 417
Cdd:pfam02463  330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  418 QEEYERQEREHRLSAADEKA--VSAAEEVKTYKRRIEEMEDELQKTERSfKNQIATHEKKAHENWLKarAAERAIAEEKR 495
Cdd:pfam02463  410 LLELARQLEDLLKEEKKEELeiLEEEEESIELKQGKLTEEKEELEKQEL-KLLKDELELKKSEDLLK--ETQLVKLQEQL 486

                          330       340
                   ....*....|....*....|..
gi 1622828953  496 EAANLRHKLLELTQKMAMLQEE 517
Cdd:pfam02463  487 ELLLSRQKLEERSQKESKARSG 508
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 69-469 3.43e-06

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: 50.73  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  69 VSFAVFFWRTVLVVKSRVYqVTEQQISEKLKIIMKENTELVQKlsnyeQKIKESKKHVQETrkqnmilsdEAIKFKDKIK 148
Cdd:COG5185   148 DIEASYGEVETGIIKDIFG-KLTQELNQNLKKLEIFGLTLGLL-----KGISELKKAEPSG---------TVNSIKESET 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 149 TLEKNNEILGDAAKNLRVMLESEREQNVKNQDLisenkKSIEKLKDAISMNASEFSEvqiaLNEAKLSEEKVKSEchRVQ 228
Cdd:COG5185   213 GNLGSESTLLEKAKEIINIEEALKGFQDPESEL-----EDLAQTSDKLEKLVEQNTD----LRLEKLGENAESSK--RLN 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 229 EENARLKKKKEQLQQEIE------DWSKLHAELSEQIKSFEKSQKdLEVALTHKDDNINALTNCITQLNrlecESESEGQ 302
Cdd:COG5185   282 ENANNLIKQFENTKEKIAeytksiDIKKATESLEEQLAAAEAEQE-LEESKRETETGIQNLTAEIEQGQ----ESLTENL 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 303 NKGGNDSDELAnGEVGGDQNEKMKNQIKQMMDVSRT--------------------QTAISVVEEDLKLLQLKLRASVST 362
Cdd:COG5185   357 EAIKEEIENIV-GEVELSKSSEELDSFKDTIESTKEsldeipqnqrgyaqeilatlEDTLKAADRQIEELQRQIEQATSS 435

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 363 KCNLEDQIKKLED-----DRNSLQAAKAGLEDECK----TLRQKVEILNELYQQKEMALQKKLSQEEYERQEREHRLSAA 433
Cdd:COG5185   436 NEEVSKLLNELISelnkvMREADEESQSRLEEAYDeinrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGV 515

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1622828953 434 DEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQI 469
Cdd:COG5185   516 RSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-294 3.55e-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: 50.83  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   92 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESE 171
Cdd:TIGR02168  277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  172 REQNVKNQDLISENKKSIEKLKDAISMNASEFSEV--QIALNEAKLSEEKVKSEchrvqeenaRLKKKKEQLQQEIEDWS 249
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLelQIASLNNEIERLEARLE---------RLEDRRERLQQEIEELL 427

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622828953  250 K--LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLE 294
Cdd:TIGR02168  428 KklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
PHA03247 PHA03247
large tegument protein UL36; Provisional
 523-799 3.62e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  523 PMPGRPNTQNPPRRGPLSQNGSFGPSPV-SGGECSPPLTVEPPVRPLSATLS----RRDMPRSEFGSV--------DGPL 589
Cdd:PHA03247  2628 PPSPSPAANEPDPHPPPTVPPPERPRDDpAPGRVSRPRRARRLGRAAQASSPpqrpRRRAARPTVGSLtsladpppPPPT 2707

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  590 PHPRWSAEASGKPSPSDPGSGtaammnsssRGSSPNRVIDEGKQTVLQEPEVP------SVPSITSLAEHPVAVNMAPKG 663
Cdd:PHA03247  2708 PEPAPHALVSATPLPPGPAAA---------RQASPALPAAPAPPAVPAGPATPggparpARPPTTAGPPAPAPPAAPAAG 2778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  664 PPPFSGVPLMSTPMGGPIPPPIRYGPPPqlcGPFGPRPLPPPFGPGMRPplglrefAPGVPPGKRDLPLHPReflPGHTP 743
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPAD---PPAAVLAPAAALPPAASP-------AGPLPPPTSAQPTAPP---PPPGP 2845

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828953  744 FRPLGPLGprEYFIPG---ARLPPPthgpQDYPPPPAARDLPPSGSRDDPPPASQSTSQ 799
Cdd:PHA03247  2846 PPPSLPLG--GSVAPGgdvRRRPPS----RSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 103-292 4.14e-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: 49.76  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 103 KENTELVQKLSNYEQKIKESKKHVQETRKQnmilsdeAIKFKDKIKTLEKNneiLGDAAKNLRvmlESEREQNVKNQDL- 181
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERR---IAALARRIR---ALEQELAALEAELa 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 182 -----ISENKKSIEKLKDAIS------------------MNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:COG4942    87 elekeIAELRAELEAQKEELAellralyrlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622828953 239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNR 292
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 80-415 4.52e-06

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: 50.49  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  80 LVVKSRVYQVTEQQISEKLKIIMKE-------NTELVqklSNYEQKIKESKKHVQETRKQNMIL---SDEAIKFKDKIKT 149
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLKEVEDLKTElekeklkNIELT---AHCDKLLLENKELTQEASDMTLELkkhQEDIINCKKQEER 531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 150 LEKNNEILGDAAKNLRVMLESEREQNVKNQDlisENKKSIEKlkdaiSMNASEFSEVQIALNEAKLSEEKVKSECHRVQE 229
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGD---EVKCKLDK-----SEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 230 ENArlKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNciTQLNRLECESESEGQNKGgnds 309
Cdd:pfam05483 604 ENK--NKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIID--NYQKEIEDKKISEEKLLE---- 675

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 310 dELANGEVGGDQNEKMKNQIKQ-----------MMDVSRTQTAISVVEED--LKLLQLKLRASVSTKCNLEDQIKKLedd 376
Cdd:pfam05483 676 -EVEKAKAIADEAVKLQKEIDKrcqhkiaemvaLMEKHKHQYDKIIEERDseLGLYKNKEQEQSSAKAALEIELSNI--- 751

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1622828953 377 RNSLQAAKAGLEDEcktlRQKVEILNELYQQKEMALQKK 415
Cdd:pfam05483 752 KAELLSLKKQLEIE----KEEKEKLKMEAKENTAILKDK 786
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 111-404 5.50e-06

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: 50.44  E-value: 5.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  111 KLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEI---------------LGDAAKNLRV----MLESE 171
Cdd:TIGR01612 1356 KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLeeckskiestlddkdIDECIKKIKElknhILSEE 1435

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  172 REQNV--KNQDlisENKKSIEKLKDAISM--NASEF----------SEVQIALNEakLSEEKVKSE-CHRVQEENAR-LK 235
Cdd:TIGR01612 1436 SNIDTyfKNAD---ENNENVLLLFKNIEMadNKSQHilkikkdnatNDHDFNINE--LKEHIDKSKgCKDEADKNAKaIE 1510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  236 KKKEQLQQEIEDWSKLHAELSE-QIKS-FEKSQKDLEVALthkdDNINALTNCITqlnrLECESESEGQNKGGND----S 309
Cdd:TIGR01612 1511 KNKELFEQYKKDVTELLNKYSAlAIKNkFAKTKKDSEIII----KEIKDAHKKFI----LEAEKSEQKIKEIKKEkfriE 1582

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  310 DELANGEVGG----DQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRA-SVSTKcnlEDQIKKLEDDRNSLQAAK 384
Cdd:TIGR01612 1583 DDAAKNDKSNkaaiDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSfSIDSQ---DTELKENGDNLNSLQEFL 1659

                          330       340
                   ....*....|....*....|
gi 1622828953  385 AGLEDECKTLRQKVEILNEL 404
Cdd:TIGR01612 1660 ESLKDQKKNIEDKKKELDEL 1679
PTZ00121 PTZ00121
MAEBL; Provisional
 88-390 7.33e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 7.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   88 QVTEQQISEKLKIIMKENTELVQKLSNYEQ-KIK-ESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLR 165
Cdd:PTZ00121  1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEaKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  166 VMLESEREQNVKNQDLISENKKSIEKL-------KDAISMNASEFSEVQIAlNEAKLSEEKVKSECHRVQEENARLKKKK 238
Cdd:PTZ00121  1668 KKAEEDKKKAEEAKKAEEDEKKAAEALkkeaeeaKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKA 1746

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  239 EQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHkddninaltncitQLNRLECESESEGQNKGGNDSDELANGEVG 318
Cdd:PTZ00121  1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-------------ELDEEDEKRRMEVDKKIKDIFDNFANIIEG 1813

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  319 GDQNEKMKNQIKQMMDVSRTQTAIS---VVEEDLKLLQLKLRA-------------SVSTKCNLEDQIKKLEDDRNSLQA 382
Cdd:PTZ00121  1814 GKEGNLVINDSKEMEDSAIKEVADSknmQLEEADAFEKHKFNKnnengedgnkeadFNKEKDLKEDDEEEIEEADEIEKI 1893


                   ....*...
gi 1622828953  383 AKAGLEDE 390
Cdd:PTZ00121  1894 DKDDIERE 1901
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 325-478 9.69e-06

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: 47.61  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 325 MKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEL 404
Cdd:COG1579     2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 405 ---YQQ--------KEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 472
Cdd:COG1579    75 ikkYEEqlgnvrnnKEYeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154


                  ....*.
gi 1622828953 473 EKKAHE 478
Cdd:COG1579   155 EAELEE 160
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-413 1.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  92 QQISEKLKIimKENTELVQKLSNYEQKIKESKKHVQETrkqnmilsdeaikfKDKIKTLEKNNEILGDAAKNLRVMLESE 171
Cdd:COG1196   216 RELKEELKE--LEAELLLLKLRELEAELEELEAELEEL--------------EAELEELEAELAELEAELEELRLELEEL 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 172 REQNVKNQDLISENKKSIEKLkdaismnasefsEVQIALNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQEIEDWSKL 251
Cdd:COG1196   280 ELELEEAQAEEYELLAELARL------------EQDIARLEERRRELEERLE--ELEEELAELEEELEELEEELEELEEE 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 252 HAELSEQIKSFEKSQKDLEVALTHKDDNINALtncITQLNRLEcESESEGQNKGGNDSDELANGEvgGDQNEKMKNQIKQ 331
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEA---EEELEELA-EELLEALRAAAELAAQLEELE--EAEEALLERLERL 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 332 MMDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDEcktLRQKVEILNELYQQKEMA 411
Cdd:COG1196   420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA---LAELLEELAEAAARLLLL 496


                  ..
gi 1622828953 412 LQ 413
Cdd:COG1196   497 LE 498
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
179-474 1.35e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 179 QDLISENKKSIEKLKDAISmnASEFSEVQIALNEAKLseEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSE- 257
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIK--RTENIEELIKEKEKEL--EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEl 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 258 --QIKSFEKSQKDLEVALTHKDDNINaltncitqlnrlECESESEGQNKGGNDSDELangEVGGDQNEKMKNQIKQMMDV 335
Cdd:PRK03918  244 ekELESLEGSKRKLEEKIRELEERIE------------ELKKEIEELEEKVKELKEL---KEKAEEYIKLSEFYEEYLDE 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 336 SRTqtaisvVEEDLKLLQLKLRasvstkcNLEDQIKKLEDDRNSLQAakagLEDECKTLRQKVEILNELYQQKEMALQKK 415
Cdd:PRK03918  309 LRE------IEKRLSRLEEEIN-------GIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEAKAKK 371

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622828953 416 LSQEEYERQEREHRLsaadEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQIATHEK 474
Cdd:PRK03918  372 EELERLKKRLTGLTP----EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
198-412 1.60e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 198 MNASEFSEVQIALNEAKLSEEkvksECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQ--KDLEVALTH 275
Cdd:COG4717    68 LNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAE 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 276 KDDNINALTNCITQLNRLEcesesegqnkggndsDELANGEvggDQNEKMKNQIKQMMDVSRTQTaisvvEEDLKLLQLK 355
Cdd:COG4717   144 LPERLEELEERLEELRELE---------------EELEELE---AELAELQEELEELLEQLSLAT-----EEELQDLAEE 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828953 356 LRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMAL 412
Cdd:COG4717   201 LEE-------LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 83-509 1.64e-05

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: 48.89  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   83 KSRVYQVTEQQISEKLKIIMKENTELVQK---------LSNYEQKIKESKKHVQETRK------QN---MILSDEAIKF- 143
Cdd:TIGR01612  847 KVDKFINFENNCKEKIDSEHEQFAELTNKikaeisddkLNDYEKKFNDSKSLINEINKsieeeyQNintLKKVDEYIKIc 926

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  144 ---KDKIKTLEKNNEILGDAA-KNLRVMLESER-EQNVKNQ--DLISENKKSIEKLKDAISMNASEF--SEVQIALNEAK 214
Cdd:TIGR01612  927 entKESIEKFHNKQNILKEILnKNIDTIKESNLiEKSYKDKfdNTLIDKINELDKAFKDASLNDYEAknNELIKYFNDLK 1006

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  215 --LSEEKVKSECHRVQEEnarlKKKKEQLQQEIEDWSK-------------------LHAELSEQIKSFEKS-QKDLEVA 272
Cdd:TIGR01612 1007 anLGKNKENMLYHQFDEK----EKATNDIEQKIEDANKnipnieiaihtsiyniideIEKEIGKNIELLNKEiLEEAEIN 1082

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  273 LTH-----------------KDDNI------NALTNCITQLNRL---ECESESEGQNKGGNDSDElangevggdqnekMK 326
Cdd:TIGR01612 1083 ITNfneikeklkhynfddfgKEENIkyadeiNKIKDDIKNLDQKidhHIKALEEIKKKSENYIDE-------------IK 1149

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  327 NQIKQMMDVsrTQTAISvvEEDLKLLQLKLRASVS---TKCNLEDQIKKLEDDRNSLQAAKAGLEdecktlrqKVEILNE 403
Cdd:TIGR01612 1150 AQINDLEDV--ADKAIS--NDDPEEIEKKIENIVTkidKKKNIYDEIKKLLNEIAEIEKDKTSLE--------EVKGINL 1217

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  404 LYQQKEMALqkklsqeeyerqerehRLSAADEKAVSAAEEVKTYKRRIEEMeDELQKTERSFKNQIATH-EKKAHENWL- 481
Cdd:TIGR01612 1218 SYGKNLGKL----------------FLEKIDEEKKKSEHMIKAMEAYIEDL-DEIKEKSPEIENEMGIEmDIKAEMETFn 1280

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1622828953  482 ----KARAAERAIAEEKREAANLRHKLLELTQ 509
Cdd:TIGR01612 1281 ishdDDKDHHIISKKHDENISDIREKSLKIIE 1312
PHA03247 PHA03247
large tegument protein UL36; Provisional
 523-792 1.74e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  523 PMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSVDGPLPHPRWSAEASGKP 602
Cdd:PHA03247  2554 PLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSP 2633

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  603 SPSDPGSGTAAMMN---------SSSRGSSPNRVIDEGKQTVLQEPEV--------PSVPSITSLAE-HPVAVNMAPKGP 664
Cdd:PHA03247  2634 AANEPDPHPPPTVPpperprddpAPGRVSRPRRARRLGRAAQASSPPQrprrraarPTVGSLTSLADpPPPPPTPEPAPH 2713

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  665 PPFSGVPLmSTPMGGPIPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLGLREFAPGVP--PGKRDLPLHPREFLPGHT 742
Cdd:PHA03247  2714 ALVSATPL-PPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPaaPAAGPPRRLTRPAVASLS 2792

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828953  743 PFRPLGPLGPREYFIPGARLPPPTHGPQDY------PPPPAARDLPPSGSRDDPPP 792
Cdd:PHA03247  2793 ESRESLPSPWDPADPPAAVLAPAAALPPAAspagplPPPTSAQPTAPPPPPGPPPP 2848
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 142-517 2.82e-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: 47.76  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  142 KFKDKIKTLEKN---NEILGDAAKNLRVMLESEREQNVKNQDLISENKKSieklkdaismnasEFSEVQIALNEAKLSEE 218
Cdd:TIGR02169  174 KALEELEEVEENierLDLIIDEKRQQLERLRREREKAERYQALLKEKREY-------------EGYELLKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  219 KVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIKsfeKSQKDLEVALTHKddnINALTNCITQLNRLECESE 298
Cdd:TIGR02169  241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEK---IGELEAEIASLERSIAEKE 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  299 segqnkggndsdelangevggDQNEKMKNQIKQM-MDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDR 377
Cdd:TIGR02169  315 ---------------------RELEDAEERLAKLeAEIDKLLAEIEELEREIEEERKRRDK-------LTEEYAELKEEL 366

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  378 NSLQAAKAGLEDECKTLRQKVEilneLYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKtykrRIEEMEDE 457
Cdd:TIGR02169  367 EDLRAELEEVDKEFAETRDELK----DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA----GIEAKINE 438

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  458 LQKTERSFKNQIATHEKKAHENwlkaraaERAIAEEKREAANLRHKLLELTQKMAMLQEE 517
Cdd:TIGR02169  439 LEEEKEDKALEIKKQEWKLEQL-------AADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 119-409 3.69e-05

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 47.36  E-value: 3.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 119 IKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKD---A 195
Cdd:pfam05911 481 IRCALQDINDSLPEADSCLSSGHPSTDASCDYITCKENSSVVEKEGSVSGDDKSSEETSKQSIQQDLSKAISKIIDfveG 560

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 196 ISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQqEIEDWSKLH-------AELSEQIKSFEKSQKD 268
Cdd:pfam05911 561 LSKEALDDQDTSSDSSELSEVLQQFSATCNDVLSGKADLEDFVLELS-HILDWISNHcfslldvSSMEDEIKKHDCIDKV 639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 269 --LEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAIS--- 343
Cdd:pfam05911 640 tlSENKVAQVDNGCSEIDNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSqlq 719

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828953 344 VVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEIL-NELYQQKE 409
Cdd:pfam05911 720 ESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELNELRQKFEALeVELEEEKN 786
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 189-441 3.97e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 189 IEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEI----EDWSKLHAELSEQIKSFEK 264
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIaeaeAEIEERREELGERARALYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 265 SQKD---LEVALTHKDdninaLTNCITQLNRLECESESegqnkggndsdelangevggdQNEKMKNQIKQMMDVSRTQTA 341
Cdd:COG3883    98 SGGSvsyLDVLLGSES-----FSDFLDRLSALSKIADA---------------------DADLLEELKADKAELEAKKAE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 342 ISVVEEDLKLLQLKlrasvstkcnLEDQIKKLEDDRNSLQAAKAGLE-DECKTLRQKVEILNELYQQKEMALQKKLSQEE 420
Cdd:COG3883   152 LEAKLAELEALKAE----------LEAAKAELEAQQAEQEALLAQLSaEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221

                         250       260
                  ....*....|....*....|.
gi 1622828953 421 YERQEREHRLSAADEKAVSAA 441
Cdd:COG3883   222 AAAAAAAAAAAAAAAAAAAAA 242
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 88-467 4.41e-05

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: 47.35  E-value: 4.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   88 QVTEQQISEKLKIIMKENTELVQK--LSNYEQKIK--ESKKHVQETRKQN----MILSdEAIKFKDKIKTLE-------- 151
Cdd:TIGR01612  443 NIFKDDFDEFNKPIPKSKLKALEKrfFEIFEEEWGsyDIKKDIDENSKQDntvkLILM-RMKDFKDIIDFMElykpdevp 521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  152 KNNEILGDAAKNLRVMLESEREQNVK----------------NQDLISENKKSIeKLKDAISMNASEFSEV---QIALNE 212
Cdd:TIGR01612  522 SKNIIGFDIDQNIKAKLYKEIEAGLKesyelaknwkkliheiKKELEEENEDSI-HLEKEIKDLFDKYLEIddeIIYINK 600

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  213 AKLS-EEKVK--SECHRVQEENARLKKKKEQLQQEIEDWSKLHA-ELSEQIKSFEKSQKDLEVALTH-KDDNINALTNci 287
Cdd:TIGR01612  601 LKLElKEKIKniSDKNEYIKKAIDLKKIIENNNAYIDELAKISPyQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYN-- 678

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  288 tQLNRLECEsesegqnkggNDSDELANGEVGGDQNEKMKNQIK--QMMDVSRTQTAISVVEEDL-KLLQ--LKLRASVST 362
Cdd:TIGR01612  679 -ELSSIVKE----------NAIDNTEDKAKLDDLKSKIDKEYDkiQNMETATVELHLSNIENKKnELLDiiVEIKKHIHG 747

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  363 KCNlEDQIKKLEDDRNSLQAAKAGLEDECKtlrqkveilnelYQQKEMALQKKLSQEEYERQEREHRLSAADEKAVSAAE 442
Cdd:TIGR01612  748 EIN-KDLNKILEDFKNKEKELSNKINDYAK------------EKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYD 814

                          410       420
                   ....*....|....*....|....*
gi 1622828953  443 EVKTYKRRIEEMEDELQKTERSFKN 467
Cdd:TIGR01612  815 KSKEYIKTISIKEDEIFKIINEMKF 839
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 348-517 4.48e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 348 DLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILN---ELYQQKEMALQKKLSQEEYERQ 424
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELElelEEAQAEEYELLAELARLEQDIA 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 425 EREHRLSAADEKAVSAAEEVKTYKRRIEEMEDEL---QKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLR 501
Cdd:COG1196   306 RLEERRRELEERLEELEEELAELEEELEELEEELeelEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

                         170
                  ....*....|....*.
gi 1622828953 502 HKLLELTQKMAMLQEE 517
Cdd:COG1196   386 EELLEALRAAAELAAQ 401
PRK12704 PRK12704
phosphodiesterase; Provisional
 169-284 6.20e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 169 ESEREQNVKNQDLISENKKSIEKLKdaismnaSEF-SEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED 247
Cdd:PRK12704   46 EAKKEAEAIKKEALLEAKEEIHKLR-------NEFeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKE 118

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622828953 248 WSKLHAELSEQIKSFEKSQKDLEVALthkdDNINALT 284
Cdd:PRK12704  119 LEQKQQELEKKEEELEELIEEQLQEL----ERISGLT 151
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
96-273 6.33e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 6.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  96 EKLKIIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnmiLSDEAIK-FKDKIKTLEK-NNEI--LGDAAKNLRVM---L 168
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEEELAELLKELEE-------LGFESVEeLEERLKELEPfYNEYleLKDAEKELEREekeL 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 169 ESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQialnEAKLSEEKVK--SECHRVQEENARLKKKKEQLQQEIE 246
Cdd:PRK03918  622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE----YEELREEYLElsRELAGLRAELEELEKRREEIKKTLE 697

                         170       180
                  ....*....|....*....|....*..
gi 1622828953 247 dwsKLHAELsEQIKSFEKSQKDLEVAL 273
Cdd:PRK03918  698 ---KLKEEL-EEREKAKKELEKLEKAL 720
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 160-434 6.49e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.91  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 160 AAKNLRVMLESEREQNVKNqdlISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKE 239
Cdd:COG4942    17 AQADAAAEAEAELEQLQQE---IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 240 QLQQEIEdwsKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLecesesegqnkggndsdelangevgg 319
Cdd:COG4942    94 ELRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYL-------------------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 320 dqNEKMKNQIKQMMdvsRTQTAISVVEEDLKLLQLKLRASVStkcNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVE 399
Cdd:COG4942   145 --APARREQAEELR---ADLAELAALRAELEAERAELEALLA---ELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622828953 400 ILnelyQQKEMALQKKLSQEEYERQEREHRLSAAD 434
Cdd:COG4942   217 EL----QQEAEELEALIARLEAEAAAAAERTPAAG 247
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 107-264 6.53e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 6.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 107 ELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQ--NVKN----QD 180
Cdd:COG1579    14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNnkeyEA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 181 LISE---NKKSIEKLKDAIS--MNASEFSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEdwsKLHAEL 255
Cdd:COG1579    94 LQKEiesLKRRISDLEDEILelMERIEELEEELAELEAELAELEA-----ELEEKKAELDEELAELEAELE---ELEAER 165


                  ....*....
gi 1622828953 256 SEQIKSFEK 264
Cdd:COG1579   166 EELAAKIPP 174
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 522-798 7.21e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.70  E-value: 7.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  522 KPMPGRPNTQNPPRRGPLSQNGSFGPSPVSGGEcSPPLTVEPPVRPLSATLSRRDMPRSEfGSVDGPLPHPRWSAEASGK 601
Cdd:PHA03307    83 ESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD-PPPPTPPPASPPPSPAPDLSEMLRPV-GSPGPPPAASPPAAGASPA 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  602 PSPSDPGSGTAAMMNSSSrGSSPNRVIDEGKqtvlqEPEVPSVPSI-TSLAEHPVAVNMAPKGPPPfSGVPLMSTPMGGP 680
Cdd:PHA03307   161 AVASDAASSRQAALPLSS-PEETARAPSSPP-----AEPPPSTPPAaASPRPPRRSSPISASASSP-APAPGRSAADDAG 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  681 IPPPIRYGPPPQLCGPfgprplpppfgpgmrpplGLREFAPGVPPGKRDLPLHPREFLPGHTPFRPLGPLGPREYFIPGA 760
Cdd:PHA03307   234 ASSSDSSSSESSGCGW------------------GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERS 295

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1622828953  761 RLPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQSTS 798
Cdd:PHA03307   296 PSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSS 333
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 91-335 7.58e-05

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 46.75  E-value: 7.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   91 EQQISEKLKIIMKENTELVQKLSnyEQKIKESKKHVQETRK--QNMILSDEAIKFKDKIKTLEKN-----NEILGDAAKN 163
Cdd:PTZ00440  1030 DKLIKEKGKEIEEKVDQYISLLE--KMKTKLSSFHFNIDIKkyKNPKIKEEIKLLEEKVEALLKKidenkNKLIEIKNKS 1107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  164 LRVMLESEREQNvKNQDLISENKKSIEKLKDAISMNASEFSEVQiaLNEAKLSE-EKVKSE---------CHRVQEENAR 233
Cdd:PTZ00440  1108 HEHVVNADKEKN-KQTEHYNKKKKSLEKIYKQMEKTLKELENMN--LEDITLNEvNEIEIEyerilidhiVEQINNEAKK 1184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  234 LKKKKEQLQQEIEDWSKLHAELSEQIKS----FEKSQKDLEvaLTHKDDNINALtncITQLNRLECESESEGQNK--GGN 307
Cdd:PTZ00440  1185 SKTIMEEIESYKKDIDQVKKNMSKERNDhlttFEYNAYYDK--ATASYENIEEL---TTEAKGLKGEANRSTNVDelKEI 1259

                          250       260
                   ....*....|....*....|....*...
gi 1622828953  308 DSDELANGEVGGDQNEKMKNQIKQMMDV 335
Cdd:PTZ00440  1260 KLQVFSYLQQVIKENNKMENALHEIKNM 1287
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 115-473 9.13e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 45.84  E-value: 9.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 115 YEQKIKESKKHVQETRKQN---MILSDEAIKFKDKIKTLEKNNeilgDAAKNLRVMLESEREQ-----NVKNQDLISENK 186
Cdd:pfam05622  85 YRIKCEELEKEVLELQHRNeelTSLAEEAQALKDEMDILRESS----DKVKKLEATVETYKKKledlgDLRRQVKLLEER 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 187 KSI---------EKLKDAISMNAS-EFSEVQIALNEAKLSEEKVKSEchRVQEENARLKKKKEQLQQE----IEDWSKLH 252
Cdd:pfam05622 161 NAEymqrtlqleEELKKANALRGQlETYKRQVQELHGKLSEESKKAD--KLEFEYKKLEEKLEALQKEkerlIIERDTLR 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 253 aELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQ---------LNRLECESESEGQNKGGNDSDELANGEVGGDQNE 323
Cdd:pfam05622 239 -ETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEimpaeirekLIRLQHENKMLRLGQEGSYRERLTELQQLLEDAN 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 324 KMKNQIKQMMDVSRTQtaISVVEEDLKLLQLKLRA-------SVSTKCNLEDQIKKLEDDRNSLQAAKAGLED-ECKTLR 395
Cdd:pfam05622 318 RRKNELETQNRLANQR--ILELQQQVEELQKALQEqgskaedSSLLKQKLEEHLEKLHEAQSELQKKKEQIEElEPKQDS 395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 396 QKveilnelyQQKEMALQKKLSQEEYERQEREHRLSAADEKA------------VSAAEEVKTYKRRIEEMEDELQKTER 463
Cdd:pfam05622 396 NL--------AQKIDELQEALRKKDEDMKAMEERYKKYVEKAksviktldpkqnPASPPEIQALKNQLLEKDKKIEHLER 467

                         410
                  ....*....|
gi 1622828953 464 SFKNQIATHE 473
Cdd:pfam05622 468 DFEKSKLQRE 477
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 93-256 9.32e-05

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 45.39  E-value: 9.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   93 QISEKLKIIMKENTELVqklsnyeqkiKESKKHVqetRKQNMILSDEAIKFKDKIKTLEKNneilgdaaknLRVMLESER 172
Cdd:smart00787 140 KLLEGLKEGLDENLEGL----------KEDYKLL---MKELELLNSIKPKLRDRKDALEEE----------LRQLKQLED 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  173 EQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQ-EIEDWSKL 251
Cdd:smart00787 197 ELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGfTFKEIEKL 276


                   ....*
gi 1622828953  252 HAELS 256
Cdd:smart00787 277 KEQLK 281
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 151-464 9.55e-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: 46.32  E-value: 9.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  151 EKNNEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAIsmnasefsEVQIALNEAKLSEEKVK--SECHRVQ 228
Cdd:pfam01576  291 EKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKAL--------EEETRSHEAQLQEMRQKhtQALEELT 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  229 EENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEvaltHKDDNINAltncitQLNRLEC---ESE---SEGQ 302
Cdd:pfam01576  363 EQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSE----HKRKKLEG------QLQELQArlsESErqrAELA 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  303 NKGGNDSDELANgeVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEdlkLLQLKLRAsvstKCNLEDQIKKLEDDRNSLQA 382
Cdd:pfam01576  433 EKLSKLQSELES--VSSLLNEAEGKNIKLSKDVSSLESQLQDTQE---LLQEETRQ----KLNLSTRLRQLEDERNSLQE 503

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  383 AkagLEDECKTlRQKVEILNELYQQKEMALQKKLSQEEYErqerehrLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:pfam01576  504 Q---LEEEEEA-KRNVERQLSTLQAQLSDMKKKLEEDAGT-------LEALEEGKKRLQRELEALTQQLEEKAAAYDKLE 572


                   ..
gi 1622828953  463 RS 464
Cdd:pfam01576  573 KT 574
46 PHA02562
endonuclease subunit; Provisional
 97-268 1.34e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.39  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  97 KLKIIMKENTELVQKLSNYEQKIKESKKHVQE---------TRKQNMI--LSDEAIKFK-------DKIKTLEKNNEILG 158
Cdd:PHA02562  175 KIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEqrkkngeniARKQNKYdeLVEEAKTIKaeieeltDELLNLVMDIEDPS 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 159 DAAKNLR-----------------VM-------------LESEREQNVKNQDLISENKKSIEKLKDAI---SMNASEFSE 205
Cdd:PHA02562  255 AALNKLNtaaakikskieqfqkviKMyekggvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAIdelEEIMDEFNE 334

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828953 206 VQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEI----EDWSKLHAELSEQIKSFEKSQKD 268
Cdd:PHA02562  335 QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnaEELAKLQDELDKIVKTKSELVKE 401
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
103-264 2.11e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.13  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 103 KENtELVQKLSNYEQKIKESKKhvqetrkqnmilsdeAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLI 182
Cdd:COG1340   134 EEK-ELVEKIKELEKELEKAKK---------------ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEM 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 183 SENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIED--WSKLHAELSEQIK 260
Cdd:COG1340   198 IELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLK 277


                  ....
gi 1622828953 261 SFEK 264
Cdd:COG1340   278 KGEK 281
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 98-429 2.85e-04

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 44.65  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   98 LKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQ-----------NMILSDEAI--KFKDKIKTLEKNNEILG---DAA 161
Cdd:TIGR00606  739 IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlgtimpeeesaKVCLTDVTImeRFQMELKDVERKIAQQAaklQGS 818

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  162 KNLRVMLESEREQNVK-------------NQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQ 228
Cdd:TIGR00606  819 DLDRTVQQVNQEKQEKqheldtvvskielNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQ 898

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  229 EENARLKKKKEQLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALthkDDNINALTNCITQLNRLECESESEGQNKGGND 308
Cdd:TIGR00606  899 SLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKV---NDIKEKVKNIHGYMKDIENKIQDGKDDYLKQK 975

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  309 SDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNS--------- 379
Cdd:TIGR00606  976 ETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK-------RENELKEVEEELKQhlkemgqmq 1048

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828953  380 ---LQAAKAGLEDECKTL-RQKVEILNEL--YQQKEMALQKKLSQEEYERQEREHR 429
Cdd:TIGR00606 1049 vlqMKQEHQKLEENIDLIkRNHVLALGRQkgYEKEIKHFKKELREPQFRDAEEKYR 1104
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
92-326 2.87e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  92 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLrvmlese 171
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL------- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 172 REQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSE-EKVKSECHRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828953 251 LHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELANGEVGGDQNEKMK 326
Cdd:COG4372   215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 90-272 3.77e-04

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: 43.96  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  90 TEQQISEKLKIIMKENTELVQKLsnyeqkikesKKHVQETRKQNMILSDEAIKFKDKIKTLE------KNNEILGDAAK- 162
Cdd:pfam05557 370 TMSNYSPQLLERIEEAEDMTQKM----------QAHNEEMEAQLSVAEEELGGYKQQAQTLErelqalRQQESLADPSYs 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 163 -----NLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKK 237
Cdd:pfam05557 440 keevdSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRL 519

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622828953 238 KEQLQQEIEDWSKLHAELSE-QIKSFEKSQKDLEVA 272
Cdd:pfam05557 520 LKKLEDDLEQVLRLPETTSTmNFKEVLDLRKELESA 555
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 92-405 4.37e-04

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: 43.69  E-value: 4.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  92 QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRkqnmilsdeaikfkdkiKTLEKNNEILGDAAKNLRVMLE-- 169
Cdd:pfam06160  96 DDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELR-----------------KTLLANRFSYGPAIDELEKQLAei 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 170 ----SEREQNVKNQDLIsENKKSIEKLK---DAISMNASEF--------SEVQIALNE-----AKLSEEKVKSECHRVQE 229
Cdd:pfam06160 159 eeefSQFEELTESGDYL-EAREVLEKLEeetDALEELMEDIpplyeelkTELPDQLEElkegyREMEEEGYALEHLNVDK 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 230 ENARLKKKKEQL-----QQEIEDWSKLHAELSEQI--------------KSFEKSQKDLEVALTHKDDNINALTNCITQL 290
Cdd:pfam06160 238 EIQQLEEQLEENlalleNLELDEAEEALEEIEERIdqlydllekevdakKYVEKNLPEIEDYLEHAEEQNKELKEELERV 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 291 NrlecesesegQNKGGNDsDELANGEVGGDQNEKMKNQIKQMMDVSRTQTAI-SVVEEDLKllqlklrasvstkcNLEDQ 369
Cdd:pfam06160 318 Q----------QSYTLNE-NELERVRGLEKQLEELEKRYDEIVERLEEKEVAySELQEELE--------------EILEQ 372

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1622828953 370 IKKLEDDRNSLQAAKAGLEDECKTLRQKVE----ILNELY 405
Cdd:pfam06160 373 LEEIEEEQEEFKESLQSLRKDELEAREKLDefklELREIK 412
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 63-202 4.45e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 40.88  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  63 TAFLGIVSFAV-------FFWRTVL-VVKSRvyqvtEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQEtrkqnm 134
Cdd:cd06503     1 TLIWQIINFLIllfilkkFLWKPILkALDER-----EEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQE------ 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828953 135 ILsDEAIKFKDKIKtleknNEILGDAAKnlrvmlESEREQNVKNQDLISENKKSIEKLKD---AISMNASE 202
Cdd:cd06503    70 II-EEARKEAEKIK-----EEILAEAKE------EAERILEQAKAEIEQEKEKALAELRKevaDLAVEAAE 128
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 90-460 4.47e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.80  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   90 TEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNmilsdeaiKFKDKIKTLEKNNEILGDAAKNLRVMLE 169
Cdd:TIGR00618  227 ELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE--------ELRAQEAVLEETQERINRARKAAPLAAH 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  170 SER-EQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDW 248
Cdd:TIGR00618  299 IKAvTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  249 SKLHAElsEQIKSFEKSQKDLEVALTHKDDNINAltnciTQLNRLECESESEGQnkggndsdeLANGEvGGDQNEKMKNQ 328
Cdd:TIGR00618  379 QHIHTL--QQQKTTLTQKLQSLCKELDILQREQA-----TIDTRTSAFRDLQGQ---------LAHAK-KQQELQQRYAE 441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  329 IKQMMDVSRTQTAISVVEEDLKLLQ-----LKLRASVSTKCNLEDQIKKLEDDRNSLQAakaglEDECKTLRQKVEILNE 403
Cdd:TIGR00618  442 LCAAAITCTAQCEKLEKIHLQESAQslkerEQQLQTKEQIHLQETRKKAVVLARLLELQ-----EEPCPLCGSCIHPNPA 516

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828953  404 LYQQKEM-ALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQK 460
Cdd:TIGR00618  517 RQDIDNPgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
PRK01156 PRK01156
chromosome segregation protein; Provisional
 93-516 4.95e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  93 QISEKLKIIMKENTELVQKLSNYEQKikesKKHVQETRKQNMILSDEAIKFKDKIKT--------LEKNNEILGDAAKNL 164
Cdd:PRK01156  208 DDEKSHSITLKEIERLSIEYNNAMDD----YNNLKSALNELSSLEDMKNRYESEIKTaesdlsmeLEKNNYYKELEERHM 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 165 RVmlesEREQNVKNQDLISE---NKKSIEKLKDAISMNASEFSEVQIALNEAKLSE------EKVKSECHRVQEENARLK 235
Cdd:PRK01156  284 KI----INDPVYKNRNYINDyfkYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQkdyndyIKKKSRYDDLNNQILELE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 236 ----------KKKEQLQQEIEDWSK----LHAELSEQIKSFE-------KSQKDLEVALTHKDDNINALTNCITQLNRLE 294
Cdd:PRK01156  360 gyemdynsylKSIESLKKKIEEYSKnierMSAFISEILKIQEidpdaikKELNEINVKLQDISSKVSSLNQRIRALRENL 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 295 CESESEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQmmDVSRTQTAISVVEEDLKLLQLKLRASVSTKCNLE-DQIKKL 373
Cdd:PRK01156  440 DELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE--KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKS 517

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 374 EDDRNSLQAAKAGLED---ECKTLRQKVEILNELYQQ-KEMALQKKLSQEEYERQEREHRLSAADEKAVSAAEEVktyKR 449
Cdd:PRK01156  518 INEYNKIESARADLEDikiKINELKDKHDKYEEIKNRyKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEI---KK 594

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828953 450 RIEEMEDELQKTERSFKNqiathEKKAHENWLKaraaeraiaEEKREAANLRHKLLELTQKMAMLQE 516
Cdd:PRK01156  595 QLNDLESRLQEIEIGFPD-----DKSYIDKSIR---------EIENEANNLNNKYNEIQENKILIEK 647
PRK01156 PRK01156
chromosome segregation protein; Provisional
 89-415 5.03e-04

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 43.74  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  89 VTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAI-KFKDKIKTLEKNNEILGDAAKNLRVM 167
Cdd:PRK01156  402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcPVCGTTLGEEKSNHIINHYNEKKSRL 481

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 168 LESEREQNVKNQDlISENKKSIEKLKDAIS---MNASEFSEVQIALNEAKLSEEKVKSechrvqeenARLKKKKEQLQQE 244
Cdd:PRK01156  482 EEKIREIEIEVKD-IDEKIVDLKKRKEYLEseeINKSINEYNKIESARADLEDIKIKI---------NELKDKHDKYEEI 551

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 245 IEDWSKLHAELSEQIKS------FEKSQKDLEVALTHKDDNINALTNCITQLNRLECE---SESEGQNKGGNDSDELANG 315
Cdd:PRK01156  552 KNRYKSLKLEDLDSKRTswlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGfpdDKSYIDKSIREIENEANNL 631

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 316 EVGGDQNEKMKNQIKQM---MDVSRTQTA-ISVVEEDLKLLQLKLRASvstkcnlEDQIKKLEDDRNSLQAAKAGLEDEC 391
Cdd:PRK01156  632 NNKYNEIQENKILIEKLrgkIDNYKKQIAeIDSIIPDLKEITSRINDI-------EDNLKKSRKALDDAKANRARLESTI 704

                         330       340
                  ....*....|....*....|....
gi 1622828953 392 KTLRQKVEILNELYQQKEMALQKK 415
Cdd:PRK01156  705 EILRTRINELSDRINDINETLESM 728
ClyA-like cd21116
family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including ...
 81-268 5.05e-04

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).


Pssm-ID: 439149 [Multi-domain]  Cd Length: 224  Bit Score: 42.40  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  81 VVKSRVYQVTEQQIseklkiIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIK--------FKDKIKTLEK 152
Cdd:cd21116    10 LVQAYVTAILNQPN------INLIPLDLLPSLNTHQALARAHALEWLNEIKPKLLSLPNDIIgynntfqsYYPDLIELAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 153 N-NEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKSECHRVQEEN 231
Cdd:cd21116    84 NlIKGDQGAKQQLLQGLEALQSQVTKKQTSVTSFINELTTFKNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQI 163

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622828953 232 ARLKKKKEQLQQeieDWSKLHAELSEQIKSFEKSQKD 268
Cdd:cd21116   164 DAAIDALEKLSN---DWQTLDSDIKELITDLEDAESS 197
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 320-518 5.98e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 320 DQNEKMKNQIKQMMD-----VSRTQTAISVVEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTL 394
Cdd:COG4942    23 AEAEAELEQLQQEIAelekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 395 RQKV-EILNELYQQK-----EMALQKKLSQEEYERQEREHRLSAADEKAVSA-----------AEEVKTYKRRIEEMEDE 457
Cdd:COG4942   103 KEELaELLRALYRLGrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElradlaelaalRAELEAERAELEALLAE 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828953 458 LQKTERSFKNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMAMLQEEP 518
Cdd:COG4942   183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 102-531 6.16e-04

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


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.56  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 102 MKENTELVQKLSnyeqkiKESKKHVQETRKQNMILSdeaikfkdkIKTLEKNNEIlgdaaKNLRVMLESERE---QNVKN 178
Cdd:pfam05483 217 LKEDHEKIQHLE------EEYKKEINDKEKQVSLLL---------IQITEKENKM-----KDLTFLLEESRDkanQLEEK 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 179 QDLISENKKSIEKLKDAISmnaSEFSEVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHA----E 254
Cdd:pfam05483 277 TKLQDENLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvtE 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 255 LSEQIKSFEKSQKDLEVALTHKDDNINALTncitqLNRLECESESEGQNKGGNDSD-ELANGEVGGDQNEKMKNQIKQMM 333
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKNEDQLKIIT-----MELQKKSSELEEMTKFKNNKEvELEELKKILAEDEKLLDEKKQFE 428

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 334 DVS-----RTQTAISVV---EEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNEly 405
Cdd:pfam05483 429 KIAeelkgKEQELIFLLqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQ-- 506

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 406 QQKEMALQ-KKLSQEEYERQEREHRLSaadeKAVSAAEEVKTYKR-RIEEMEDELQKTERSFKNQIATHEKKAHENWLKA 483
Cdd:pfam05483 507 EASDMTLElKKHQEDIINCKKQEERML----KQIENLEEKEMNLRdELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1622828953 484 RAAERAIAEEKREAANLRHKLLELTQKMAMLQEEPVIVKPMPGRPNTQ 531
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
Filament pfam00038
Intermediate filament protein;
143-407 6.66e-04

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 42.60  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 143 FKDKIKTLEKNNeilgdaaKNLRVMLESEREQN---VKNQDLISEnkKSIEKLKDAISMNASEFSEVQIALNEAKLSEEK 219
Cdd:pfam00038  16 YIDKVRFLEQQN-------KLLETKISELRQKKgaePSRLYSLYE--KEIEDLRRQLDTLTVERARLQLELDNLRLAAED 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 220 VKSEC-----HRVQEEN----------------ARLKKKKEQLQQEIEDWSKLH-AELSEQIKSFEKSQKDLEVALTHKD 277
Cdd:pfam00038  87 FRQKYedelnLRTSAENdlvglrkdldeatlarVDLEAKIESLKEELAFLKKNHeEEVRELQAQVSDTQVNVEMDAARKL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 278 D------NINALTNCITQLNRLECESESEGQnkggndsdeLANGEVGGDQNEKMKNQIKQ-MMDVSRTqtaisvveedLK 350
Cdd:pfam00038 167 DltsalaEIRAQYEEIAAKNREEAEEWYQSK---------LEELQQAAARNGDALRSAKEeITELRRT----------IQ 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828953 351 LLQLKLRASVSTKCNLEDQIKKLED----DRNSLQAAKAGLEDECKTLRQKVEILNELYQQ 407
Cdd:pfam00038 228 SLEIELQSLKKQKASLERQLAETEEryelQLADYQELISELEAELQETRQEMARQLREYQE 288
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 77-251 7.65e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 42.49  E-value: 7.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  77 RTVLVVKSRVYQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMilsdeaikfkdkiKTLEKNNEI 156
Cdd:pfam15905 165 RNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE-------------KLLEYITEL 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 157 lgdaaKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEA-----KLSEEKVKSECHRVQEEN 231
Cdd:pfam15905 232 -----SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKcklleSEKEELLREYEEKEQTLN 306

                         170       180
                  ....*....|....*....|
gi 1622828953 232 ARLKKKKEQLQQEIEDWSKL 251
Cdd:pfam15905 307 AELEELKEKLTLEEQEHQKL 326
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 95-268 8.30e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.31  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   95 SEKLKIIMKENTELVQKLSNYEqkikeSKKHVQETRKQNMilsdeaikfKDKIKTLEKNNEILgdaaknlrvmlESEREQ 174
Cdd:smart00787 108 SPDVKLLMDKQFQLVKTFARLE-----AKKMWYEWRMKLL---------EGLKEGLDENLEGL-----------KEDYKL 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  175 NVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSE-----EKVKSECHRVQEEN---ARLKKKKEQLQQEIE 246
Cdd:smart00787 163 LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTEldrakEKLKKLLQEIMIKVkklEELEEELQELESKIE 242

                          170       180
                   ....*....|....*....|..
gi 1622828953  247 DWSKLHAELSEQIKSFEKSQKD 268
Cdd:smart00787 243 DLTNKKSELNTEIAEAEKKLEQ 264
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 93-466 1.18e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 42.90  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   93 QISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEK-NNEILG------DAAKNLR 165
Cdd:PTZ00440   474 DLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNNIVNNNFKNIEDYYITIEGlKNEIEGlielikYYLQSIE 553

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  166 VMLESERE-QNVKNQ-----DLISENkksIEKLKDAISMNAS---EFSEVQIALNEAKLSEEKVKSECHRVQEENARLKK 236
Cdd:PTZ00440   554 TLIKDEKLkRSMKNDiknkiKYIEEN---VDHIKDIISLNDEidnIIQQIEELINEALFNKEKFINEKNDLQEKVKYILN 630

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  237 K--KEQLQQEIEDWSKlhaelseqiksFEKSQKDLEVALTHKDDNINALTNCITQLNRLECESESEGQNKGGNDSDELAN 314
Cdd:PTZ00440   631 KfyKGDLQELLDELSH-----------FLDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQN 699

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  315 -GEVGGDQNEKMKNQIKQMMDVSRTQTAISVVEedlkllqlkLRASVStkcNLEDQIKKLEDDRNSLQAAK----AGLED 389
Cdd:PTZ00440   700 lLSLKENIIKKQLNNIEQDISNSLNQYTIKYND---------LKSSIE---EYKEEEEKLEVYKHQIINRKnefiLHLYE 767

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828953  390 ECKTLRQKVEILNELYQQKEMALQKKlsqeeyerQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFK 466
Cdd:PTZ00440   768 NDKDLPDGKNTYEEFLQYKDTILNKE--------NKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELK 836
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 513-809 1.39e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.45  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 513 MLQEEPVIVKPMPGRPNTQNPPRRGPlSQNGSFGPSPvsgGECSPPLTVEPPVRPLSATLSRRDMPRSEFGSvdGPLPHP 592
Cdd:pfam03154 166 ILQTQPPVLQAQSGAASPPSPPPPGT-TQAATAGPTP---SAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQ--TPTLHP 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 593 RwsaeasGKPSPSDPgsgtaamMNSSSRGSSPNRVIDEGKQTVLQEPEVPSVP----SITSLAEHPVAvnmapkgPPPFS 668
Cdd:pfam03154 240 Q------RLPSPHPP-------LQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPhslqTGPSHMQHPVP-------PQPFP 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 669 GVPLMSTPMGGPIPPPIRYGPPPQLCGPFGPRPLPPPFGPGMRPPLglrefapgvPPGKRDLP-LHPreflPGHTPFRPL 747
Cdd:pfam03154 300 LTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPL---------PPAPLSMPhIKP----PPTTPIPQL 366

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953 748 gPLGPREYFIPGARLPPPTHGPQDYPPPPAARDLPPSGSRDDP---PPASQSTSQdcSQALKQSP 809
Cdd:pfam03154 367 -PNPQSHKHPPHLSGPSPFQMNSNLPPPPALKPLSSLSTHHPPsahPPPLQLMPQ--SQQLPPPP 428
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
 745-804 2.41e-03

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 434857 [Multi-domain]  Cd Length: 668  Bit Score: 41.29  E-value: 2.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953 745 RPLGPLGPREYF----IPGARL-PPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQSTSQDCSQA 804
Cdd:pfam15685 143 RPLLPLLPRQLIekdpAPGAPApPPPTPLEPRKPPPLPPSDRQPPNRGITPALATSATSPTDSQA 207
46 PHA02562
endonuclease subunit; Provisional
 103-259 2.55e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 103 KENTELVQKLSNYEQKIKESKKH----VQETRKQNMILSDEAI-KFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVK 177
Cdd:PHA02562  259 KLNTAAAKIKSKIEQFQKVIKMYekggVCPTCTQQISEGPDRItKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKK 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 178 nqdlISENKKSIEKLKDAISmnasefSEVqialNEAKlseeKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSE 257
Cdd:PHA02562  339 ----LLELKNKISTNKQSLI------TLV----DKAK----KVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVK 400


                  ..
gi 1622828953 258 QI 259
Cdd:PHA02562  401 EK 402
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 107-221 2.71e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 107 ELVQKLSN----YEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTL-----EKNNEILGDA----AKNLRVMLESERE 173
Cdd:PRK00409  520 ELIASLEElereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLleeaeKEAQQAIKEAkkeaDEIIKELRQLQKG 599

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622828953 174 Q--NVKNQDLIsENKKSIEKLKDAISMNASEFSEVQIALNEAklseEKVK 221
Cdd:PRK00409  600 GyaSVKAHELI-EARKRLNKANEKKEKKKKKQKEKQEELKVG----DEVK 644
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
58-407 3.12e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  58 KPVLITAFLGIVSFAVFFwrtvLVVKSRVYQVTEQ-QI-SEKLKIIMKENTELVQKLSNYEQKIKeskkhvqetrkqnMI 135
Cdd:COG3206    28 KWLILLVFLLVLALALLY----ALLLPPVYEASATlLVePQSSDVLLSGLSSLSASDSPLETQIE-------------IL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 136 LSDE----AIK----FKDKIKTLEKNNEILGDAAKNLRVmlesereQNVKNQDLI-----SENKKSIEKLKDAIsmnASE 202
Cdd:COG3206    91 KSRPvlerVVDklnlDEDPLGEEASREAAIERLRKNLTV-------EPVKGSNVIeisytSPDPELAAAVANAL---AEA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 203 FSEVQIALNEAKLSEEKVksechRVQEENARLKKKKEQLQQEIEDWSKLH--AELSEQIKSFEKSQKDLEVALTHKDDNI 280
Cdd:COG3206   161 YLEQNLELRREEARKALE-----FLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAEL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 281 NALTNCITQLNRLECESESEGQNKGGNDS-----DELANGEV--------GGDQNEKMKNQIKQMMDV-----SRTQTAI 342
Cdd:COG3206   236 AEAEARLAALRAQLGSGPDALPELLQSPViqqlrAQLAELEAelaelsarYTPNHPDVIALRAQIAALraqlqQEAQRIL 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622828953 343 SVVEEDLKLLQLKLRAsvstkcnLEDQIKKLEDDRNSLQAAKAGLEDecktLRQKVEILNELYQQ 407
Cdd:COG3206   316 ASLEAELEALQAREAS-------LQAQLAQLEARLAELPELEAELRR----LEREVEVARELYES 369
mS26_Tt cd23695
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ...
 60-354 3.35e-03

Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.


Pssm-ID: 467909 [Multi-domain]  Cd Length: 496  Bit Score: 40.96  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  60 VLITAFLGIVSFAVFFWRTVLVVKSRVYQVTEQQISEKLKIIMKENTELVQKLS--------NYEQKIKESKKHVQETRK 131
Cdd:cd23695   173 LLMPIYQDLKSLIKHLKYTELFKLLKEYQDAKAIIIEDFRESSEEGAEKLEKLEkafatllkNYKEELEEPEKQLEFMQK 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 132 QNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEklkdaismnASEFSEVQIALN 211
Cdd:cd23695   253 RLLDLYNLLRLWGQYITIVKMPDSVVRDIMNKTQARPEVAKLNSKQELEDAKNRKRDTE---------ENEFDDDYESAD 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 212 EAKLSEEKVKSECHRVQEENArlKKKKEQLQQEIEDWSKLHAELSEQ-----IKSFEK-SQKDLEVALTHKD-DNINALT 284
Cdd:cd23695   324 EGETSDEEDEIEEENFQLQKE--KKKEEELNAEFNIAKNSLYKFSPQndknvVDDRDFySGVDLENVFPRALlNNLNDFT 401

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622828953 285 NCITQlNRLECESESEGQ---NKGGNDSDELANGEVGGDQN----EKMKNQIKQMMDVSRTQTAISVVEEDLKLLQL 354
Cdd:cd23695   402 GLDFQ-NVKEILNNEEKLkiiQGEDDQNDQEDFNNPRKFQTslivQTYKQKINNLDAESLTRATQEKKNDIQKLLDL 477
Prefoldin_4 cd23165
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ...
 179-276 3.58e-03

prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467481 [Multi-domain]  Cd Length: 103  Bit Score: 37.52  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 179 QDLISENKKSIEKLKDA---ISMnASEFSEVQIALNEA--KLSEEKVKSechrvqeenaRLKKKKEQLQQEIEdwsklha 253
Cdd:cd23165    19 KEELKAKKKELENLEDAsdeLEL-ADDDEPVPYKIGEVfvHLSLEEAQE----------RLEKAKEELEEEIE------- 80

                          90       100
                  ....*....|....*....|...
gi 1622828953 254 ELSEQIKSFEKSQKDLEVALTHK 276
Cdd:cd23165    81 KLEEEIDEIEEEMKELKVQLYAK 103
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 155-294 3.85e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.05  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 155 EILGDAAKNLRVMLESEREQNVKN--------QDLISENKKSIEKLKDAISMNASEFSEVQIALNE------AKLSEEKV 220
Cdd:cd22656    95 EILELIDDLADATDDEELEEAKKTikallddlLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETlekalkDLLTDEGG 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622828953 221 KSECHRVQEENARLKKKKE----QLQQEIEDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQLNRLE 294
Cdd:cd22656   175 AIARKEIKDLQKELEKLNEeyaaKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQ 252
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 367-468 4.02e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 367 EDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMalqkklsqeeyerqerehRLSAADEKAVSAAEEVKT 446
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA------------------ELEALQAEIDKLQAEIAE 76

                          90       100
                  ....*....|....*....|..
gi 1622828953 447 YKRRIEEMEDELQKTERSFKNQ 468
Cdd:COG3883    77 AEAEIEERREELGERARALYRS 98
SF-assemblin pfam06705
SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related ...
 88-262 4.09e-03

SF-assemblin/beta giardin; This family consists of several eukaryotic SF-assemblin and related beta giardin proteins. During mitosis the SF-assemblin-based cytoskeleton is reorganized; it divides in prophase and is reduced to two dot-like structures at each spindle pole in metaphase. During anaphase, the two dots present at each pole are connected again. In telophase there is an asymmetrical outgrowth of new fibres. It has been suggested that SF-assemblin is involved in re-establishing the microtubular root system characteriztic of interphase cells after mitosis.


Pssm-ID: 284187 [Multi-domain]  Cd Length: 247  Bit Score: 39.92  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  88 QVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIK--FKDKIKTLEKNNEILGDAAKNLR 165
Cdd:pfam06705  26 EVKRVDEDTRVKMIKEAIAHLEKLIQTESKKRQESFEDIQEEFKKEIDNMQETIKeeIDDMAANFRKALAELNDTINNVE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 166 VMLESEREqnVKNQDLISENK---KSIEKLKDAISMNASEFSEVQIALNEaKLSEEKVKSECHRVQEENARlKKKKEQLQ 242
Cdd:pfam06705 106 TNLQNEIA--IHNDAIEALRKealKSLNDLETGIATENAERKKMYDQLNK-KVAEGFARISAAIDTEKNAR-DSAVSAAT 181

                         170       180
                  ....*....|....*....|
gi 1622828953 243 QEIEDWSKLHAELSEQIKSF 262
Cdd:pfam06705 182 TELTNTKLVEKCVNEQFENA 201
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 116-200 4.25e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.16  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 116 EQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGDAAKNLRV---MLESereqnvKNQDLISENKKSIE-- 190
Cdd:cd22887     3 ESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIennLLEE------KLRKLQEENDELVErw 76

                          90
                  ....*....|...
gi 1622828953 191 ---KLKDAISMNA 200
Cdd:cd22887    77 makKQQEADKMNE 89
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
 724-795 5.00e-03

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 38.18  E-value: 5.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622828953 724 PPGKRDLPLHPREFLPGHTPFRPLGPLGPREYFIPGARLPPPTHGPQDYPPPPAArdLPPSGSRDDPPPASQ 795
Cdd:pfam12868  62 PPSPAGPYASQGQYYPETNYFPPPPGSTPQPPVDPQPNAPPPPYNPADYPPPPGA--APPPQPYQYPPPPGP 131
PROL5-SMR pfam15621
Proline-rich submaxillary gland androgen-regulated family; SMR is a family of proteins found ...
 737-809 5.16e-03

Proline-rich submaxillary gland androgen-regulated family; SMR is a family of proteins found in eukaryotes. The family of SMR proteins is expressed in the submaxillary gland. SMR members may play a role in protection or detoxification.


Pssm-ID: 434817 [Multi-domain]  Cd Length: 103  Bit Score: 37.10  E-value: 5.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828953 737 FLPGHTPFRPLGPLGPREYFIP-GARLPPPTHGPQDYPPPPAARDLPPSGSRDDPPPASQSTSQDCSQALKQSP 809
Cdd:pfam15621  25 GPRGHDPRRPLPPSQPPPNGPQiGPPPPPPPYGPGRIPPPPPPPFGPGRIPPPPPPPYGPGRILSQSFPPPPDP 98
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 86-462 5.89e-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: 40.44  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   86 VYQVTEQQISEklkiIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIktLEKNNEILGDAAKNLR 165
Cdd:TIGR02169  365 ELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL--ADLNAAIAGIEAKINE 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  166 vmLESEREqnvknqDLISENKKSIEKLKDAISMNASEfsEVQIALNEAKLseEKVKSECHRVQEENARLKKKKEQLQQEI 245
Cdd:TIGR02169  439 --LEEEKE------DKALEIKKQEWKLEQLAADLSKY--EQELYDLKEEY--DRVEKELSKLQRELAEAEAQARASEERV 506

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  246 -----------EDWSKLHAELSEQIKSFEKSQKDLEVALTHKDDNINALTN-----CITQLNRlecesESEGQ------N 303
Cdd:TIGR02169  507 rggraveevlkASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDavakeAIELLKR-----RKAGRatflplN 581

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  304 K---GGNDSDELA-NGEVGG-----DQNEKMKNQIKQM---------MDVSRTQ--------------------TAISVV 345
Cdd:TIGR02169  582 KmrdERRDLSILSeDGVIGFavdlvEFDPKYEPAFKYVfgdtlvvedIEAARRLmgkyrmvtlegelfeksgamTGGSRA 661

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  346 EEDLKLLQLKLRASVStkcNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEI----LNELYQQKEMaLQKKLSQEEY 421
Cdd:TIGR02169  662 PRGGILFSRSEPAELQ---RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDasrkIGEIEKEIEQ-LEQEEEKLKE 737

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 1622828953  422 ERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTE 462
Cdd:TIGR02169  738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
 87-486 6.82e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 40.20  E-value: 6.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953   87 YQVTEQQISEklkIIMKENTELVQKLsnyEQKIKESKKHVQETRKQNMILSDEAikfKDKIKTLEKNNEIlgdaaknlrv 166
Cdd:PTZ00440  1007 YNILNKKIDD---LIKKQHDDIIELI---DKLIKEKGKEIEEKVDQYISLLEKM---KTKLSSFHFNIDI---------- 1067

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  167 mlesEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALNEAKLSEEKVKsechrvQEENARLKKKKEQLQQEIE 246
Cdd:PTZ00440  1068 ----KKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEK------NKQTEHYNKKKKSLEKIYK 1137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  247 DWSKLHAELS----EQIKSFEKSQKDLEVALTHKDDNINALTNCITQLN--RLECES-----ESEGQNKGGNDSDELANG 315
Cdd:PTZ00440  1138 QMEKTLKELEnmnlEDITLNEVNEIEIEYERILIDHIVEQINNEAKKSKtiMEEIESykkdiDQVKKNMSKERNDHLTTF 1217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  316 EVGGDQNE--KMKNQIKQMMDVSRTQTAISVVEEDLKLLQlklrasvSTKCNLEDQIKKLEDDRNSLQAAKAGLEDeCKT 393
Cdd:PTZ00440  1218 EYNAYYDKatASYENIEELTTEAKGLKGEANRSTNVDELK-------EIKLQVFSYLQQVIKENNKMENALHEIKN-MYE 1289

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  394 LRQKV-------EILNELYQQKEMALQ--KKLSQEEYERQEREHRLSAADE--KAVSAAEE---VKTYKRRIEEMEDELQ 459
Cdd:PTZ00440  1290 FLISIdsekilkEILNSTKKAEEFSNDakKELEKTDNLIKQVEAKIEQAKEhkNKIYGSLEdkqIDDEIKKIEQIKEEIS 1369

                          410       420
                   ....*....|....*....|....*..
gi 1622828953  460 KTERSFKNQIATHEKKAHENWLKARAA 486
Cdd:PTZ00440  1370 NKRKEINKYLSNIKSNKEKCDLHVRNA 1396
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 87-259 7.08e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  87 YQVTE------QQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNneilgda 160
Cdd:PRK04778  340 YTLNEselesvRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKD------- 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 161 aknlrvmlESEREQNVKN-QDLISENKKSIEKL------KDAISM--NAS-EFSEVQIALNEAKLSEEKVKSECHRVQEE 230
Cdd:PRK04778  413 --------ELEAREKLERyRNKLHEIKRYLEKSnlpglpEDYLEMffEVSdEIEALAEELEEKPINMEAVNRLLEEATED 484

                         170       180
                  ....*....|....*....|....*....
gi 1622828953 231 NARLKKKKEQLQQeiedwsklHAELSEQI 259
Cdd:PRK04778  485 VETLEEETEELVE--------NATLTEQL 505
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 106-468 7.30e-03

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: 40.03  E-value: 7.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  106 TELVQKLSNYEQKIKESKKHVQETRKQNMIL---SDEAIKFKDKIKTLEKNNEilgdAAKNLRVMLESEREQNVKNQDLI 182
Cdd:TIGR00606  182 TRYIKALETLRQVRQTQGQKVQEHQMELKYLkqyKEKACEIRDQITSKEAQLE----SSREIVKSYENELDPLKNRLKEI 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  183 SENKKSIEKLKDAISMNASEFSEVQIALNEAKL--------SEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAE 254
Cdd:TIGR00606  258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkmekvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  255 LSEQIKSFEKSQKDLEVALTHKDDNINALTNCITQlnrLECESESEGQNKGGNDSDELANGE--VGGDQNEKMKNQIKQM 332
Cdd:TIGR00606  338 LNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFERGPFSERQIKNFHtlVIERQEDEAKTAAQLC 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  333 MDVSR----TQTAISVVEEDLKLLQLKLRasvSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQK 408
Cdd:TIGR00606  415 ADLQSkerlKQEQADEIRDEKKGLGRTIE---LKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAE 491

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828953  409 EMA----LQKKLSQEEYERQEREHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQ 468
Cdd:TIGR00606  492 KNSltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIK 555
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 130-472 7.33e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 130 RKQNMILSDEAIKFKDKIKTLEKNNEIlgDAAKNLRVMLESE---REQNVKNQDLISENKKSIEK-LKDAISMNAS-EFS 204
Cdd:PRK04778   24 RKRNYKRIDELEERKQELENLPVNDEL--EKVKKLNLTGQSEekfEEWRQKWDEIVTNSLPDIEEqLFEAEELNDKfRFR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 205 EVQIALNEAKLSEEKVKSECHRVQEENARLKKKKEQLQQEIEDWSKLHAELSEQIK----SFEKSQKDLEVALthkdDNI 280
Cdd:PRK04778  102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLanrfSFGPALDELEKQL----ENL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 281 NALTNCITQLNrleceseSEGqnkggndsDELANGEVGGDQNEKMkNQIKQMMD-----VSRTQTAISVVEEDLK--LLQ 353
Cdd:PRK04778  178 EEEFSQFVELT-------ESG--------DYVEAREILDQLEEEL-AALEQIMEeipelLKELQTELPDQLQELKagYRE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 354 LKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLedECKTLRQKVEILNE----LYQ--QKEMA-------LQKKLSQEE 420
Cdd:PRK04778  242 LVEEGYHLDHLDIEKEIQDLKEQIDENLALLEEL--DLDEAEEKNEEIQEridqLYDilEREVKarkyvekNSDTLPDFL 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622828953 421 YERQEREHRLSA------------ADEkavsaAEEVKTYKRRIEEMEDELQKTERSFKNQIATH 472
Cdd:PRK04778  320 EHAKEQNKELKEeidrvkqsytlnESE-----LESVRQLEKQLESLEKQYDEITERIAEQEIAY 378
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 101-275 8.34e-03

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


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 38.49  E-value: 8.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 101 IMKENTELVQKLSNYEQKIKE-SK------KHVQETRKQNMILSDEAIKF----KDKIKTLEKNNEILGDAAKNLRVMLE 169
Cdd:cd07596     2 EDQEFEEAKDYILKLEEQLKKlSKqaqrlvKRRRELGSALGEFGKALIKLakceEEVGGELGEALSKLGKAAEELSSLSE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 170 SE-REQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIA---LNEAKLSEEKVK----SECHRVQEENARLKKKKEQL 241
Cdd:cd07596    82 AQaNQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLkkdLASKKAQLEKLKaapgIKPAKVEELEEELEEAESAL 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622828953 242 QQEIEDWSKLHAELSEQIKSFEKS-QKDLEVALTH 275
Cdd:cd07596   162 EEARKRYEEISERLKEELKRFHEErARDLKAALKE 196
PLN02939 PLN02939
transferase, transferring glycosyl groups
 171-478 8.62e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 39.89  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 171 EREQNVKnqdliSENKKSIEKLKDAISMNASEFSEVqIALNEAKLseekvksechRVQEENARLKKKKEQLQQEIEDWSK 250
Cdd:PLN02939  114 EQQTNSK-----DGEQLSDFQLEDLVGMIQNAEKNI-LLLNQARL----------QALEDLEKILTEKEALQGKINILEM 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 251 LHAELSEQIKSFEKSQKDLEVALThkddninaltncitQLNRLECESESEGQNKGGNDSDELANGEVGGDQNEKMKNQIK 330
Cdd:PLN02939  178 RLSETDARIKLAAQEKIHVEILEE--------------QLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQ 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 331 ----QMMDVSRTQTAISVVEEDLKLLQLKLR----------ASVSTKCNLE-----DQIKKLED--DRNSLQAAKAGLE- 388
Cdd:PLN02939  244 flkaELIEVAETEERVFKLEKERSLLDASLReleskfivaqEDVSKLSPLQydcwwEKVENLQDllDRATNQVEKAALVl 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 389 DECKTLRQKVEILNElyqQKEMALQKKLSQEEYERQEreHRLSAADEKAVSAAEEVKTYKRRIEEMEDELQKTERSFKNQ 468
Cdd:PLN02939  324 DQNQDLRDKVDKLEA---SLKEANVSKFSSYKVELLQ--QKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEE 398

                         330
                  ....*....|
gi 1622828953 469 iatHEKKAHE 478
Cdd:PLN02939  399 ---SKKRSLE 405
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 80-267 8.76e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 38.57  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  80 LVVKSRVYQVTEQQISEKLKIIMKENTELVQKLSNYEQKIKESKKHVQETRKQNMILSDEAIKFKDKIKTLEKNNEILGD 159
Cdd:pfam17078  29 LLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953 160 AAKNLRV----MLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQIALN---EAKLSE--EKVKSECHRVQEE 230
Cdd:pfam17078 109 ELERLQIqydaLVDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRISSNDkdiDTKLDSynNKFKNLDNIYVNK 188

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622828953 231 NARLKKKKEQLQQE--IEDWSKLHAELseQIKSFEKSQK 267
Cdd:pfam17078 189 NNKLLTKLDSLAQLldLPSWLNLYPES--RNKILEYAEK 225
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 200-271 8.81e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 38.07  E-value: 8.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622828953 200 ASEFSEVQIALNEAKLSEEKVKSECHRVQEENARL----KKKKEQLQQEIEDWSKlhAELSEQIKSFEkSQKDLEV 271
Cdd:PRK08475   59 SKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIvetaKKEAYILTQKIEKQTK--DDIENLIKSFE-ELMEFEV 131
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 210-415 9.40e-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: 39.77  E-value: 9.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  210 LNEAKLSEEKVKSECHRVQEENARLKKKK----EQLQQEIEDWSK---LHAELSEQIKSFEKSQKDLEVALTHKDDNINA 282
Cdd:pfam01576   14 LQKVKERQQKAESELKELEKKHQQLCEEKnalqEQLQAETELCAEaeeMRARLAARKQELEEILHELESRLEEEEERSQQ 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  283 LTN----CITQLNRLECESESE-------------GQNKGGNDSDELANGEvggDQNEKMKNQIKQMMD-VSRTQTAISV 344
Cdd:pfam01576   94 LQNekkkMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLE---DQNSKLSKERKLLEErISEFTSNLAE 170

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622828953  345 VEEDLKLLQLKLRASVSTKCNLEDQIKKLEDDRNSLQAAKAGLEDECKTLRQKVEILNELYQQKEMALQKK 415
Cdd:pfam01576  171 EEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKK 241
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 128-515 9.49e-03

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: 39.64  E-value: 9.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  128 ETRKQNMILSDeaikFKDKIKTLEKNNEILGDAAKNLRVMLESEREQNVKNQDLISENKKSIEKLKDAISMNASEFSEVQ 207
Cdd:TIGR00606  406 EAKTAAQLCAD----LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  208 IALNEAKLSEEKVKSECHR-----VQEENARLKKKKEQLQQEIEDWSKlHAELSEQIKSFEKSQKDlevalthKDDNINa 282
Cdd:TIGR00606  482 KAERELSKAEKNSLTETLKkevksLQNEKADLDRKLRKLDQEMEQLNH-HTTTRTQMEMLTKDKMD-------KDEQIR- 552

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  283 ltncitqlnrlecESESEGQNKGGNDSDELANGEVGGDQNEKMKNQIKQMmdvsrtqtaisvvEEDLKLLQLKLRASVST 362
Cdd:TIGR00606  553 -------------KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQT-------------RDRLAKLNKELASLEQN 606

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  363 KCNLEDQIKKLEDDRNSLQAA---KAGLEDECKTLRQKVEILNELYQQKEMalqkkLSQEEYERQEREHRLSAADEKAVS 439
Cdd:TIGR00606  607 KNHINNELESKEEQLSSYEDKlfdVCGSQDEESDLERLKEEIEKSSKQRAM-----LAGATAVYSQFITQLTDENQSCCP 681

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622828953  440 AAEEVKTYKRRIEEMEDELQKTERSF-------KNQIATHEKKAHENWLKARAAERAIAEEKREAANLRHKLLELTQKMA 512
Cdd:TIGR00606  682 VCQRVFQTEAELQEFISDLQSKLRLApdklkstESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761


                   ...
gi 1622828953  513 MLQ 515
Cdd:TIGR00606  762 RLK 764
 
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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