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Conserved domains on  [gi|37590644|gb|AAH58933|]
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IKK interacting protein [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-348 4.22e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     83 TNEFQQLQSKISLISEKLESTESILQEATSSMSLM----TQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDF 158
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    159 WKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLED------STLRNIRTVKRQEEEDLLRVEEQLG 232
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAeltllnEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    233 SDTKAIEKLEEEqhalfardedltnkLSDYEPKVEECKTHLPTIESAIHSVL----RVSQDLIETEKKMEDLTMQMFNME 308
Cdd:TIGR02168  842 DLEEQIEELSED--------------IESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRELE 907

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 37590644    309 DDMLKAVSEIMEMQKTLEgiQYDNSILKMQNELDILKEKV 348
Cdd:TIGR02168  908 SKRSELRRELEELREKLA--QLELRLEGLEVRIDNLQERL 945
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-348 4.22e-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: 51.98  E-value: 4.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     83 TNEFQQLQSKISLISEKLESTESILQEATSSMSLM----TQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDF 158
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    159 WKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLED------STLRNIRTVKRQEEEDLLRVEEQLG 232
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAeltllnEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    233 SDTKAIEKLEEEqhalfardedltnkLSDYEPKVEECKTHLPTIESAIHSVL----RVSQDLIETEKKMEDLTMQMFNME 308
Cdd:TIGR02168  842 DLEEQIEELSED--------------IESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRELE 907

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 37590644    309 DDMLKAVSEIMEMQKTLEgiQYDNSILKMQNELDILKEKV 348
Cdd:TIGR02168  908 SKRSELRRELEELREKLA--QLELRLEGLEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-326 2.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  67 EKFAKVENQYQLLKLE--TNEFQQLQSKISLISEKLESTESILQEATSSMSLMtqfEQEVSNLQDIMHDIQNNEEVLTQR 144
Cdd:COG1196 213 ERYRELKEELKELEAEllLLKLRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLELEELELELEEAQAE 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644 145 MQSLNEkfqnitdfwkrsleemnintdifkseakhihsqvtvQINSAEQEIKLLTERLKDLEDSTLRN---IRTVKRQEE 221
Cdd:COG1196 290 EYELLA------------------------------------ELARLEQDIARLEERRRELEERLEELeeeLAELEEELE 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644 222 EDLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEEckthlptIESAIHSVLRVSQDLIETEKKMEDLT 301
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-------LEELAEELLEALRAAAELAAQLEELE 406

                       250       260
                ....*....|....*....|....*
gi 37590644 302 MQMFNMEDDMLKAVSEIMEMQKTLE 326
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALA 431
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 43-231 3.59e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.26  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    43 PRTCLSLLSLGTclglawFVFQQ---------SEKFAKVENQYQLLKLetnefQQLQSKISLISEKlestESILQEATSs 113
Cdd:pfam10168 530 PQECLQLLSRAT------QVFREeylkkhdlaREEIQKRVKLLKLQKE-----QQLQELQSLEEER----KSLSERAEK- 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   114 msLMTQFEqevsnlqdimhDIQNNEEVLTQR----MQSLNEKFQNITDF---WKRSLEEMNINTDIFKS---EAKHIHSQ 183
Cdd:pfam10168 594 --LAEKYE-----------EIKDKQEKLMRRckkvLQRLNSQLPVLSDAereMKKELETINEQLKHLANaikQAKKKMNY 660

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 37590644   184 VTVQINSAEQEIKLLTERLKDLEDSTLRNIRTvkrQEEEDLLRVEEQL 231
Cdd:pfam10168 661 QRYQIAKSQSIRKKSSLSLSEKQRKTIKEILK---QLGSEIDELIKQV 705
46 PHA02562
endonuclease subunit; Provisional
 163-350 4.70e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  163 LEEMNIntdIFKSEAKHIHSQ---VTVQINSAEQEIKLLT--------------ERLKDLEDSTLRNIRTVKRQEEE--- 222
Cdd:PHA02562 165 LSEMDK---LNKDKIRELNQQiqtLDMKIDHIQQQIKTYNknieeqrkkngeniARKQNKYDELVEEAKTIKAEIEEltd 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  223 DLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEpKVEECKThlptiesaihsvlrVSQDLIETEKKMEDLTM 302
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYE-KGGVCPT--------------CTQQISEGPDRITKIKD 306

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  303 QMFNME----------DDMLKAVSEIMEMQKTLEGIQ------------YDNSILKMQNELDILKEKVHD 350
Cdd:PHA02562 307 KLKELQhslekldtaiDELEEIMDEFNEQSKKLLELKnkistnkqslitLVDKAKKVKAAIEELQAEFVD 376
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 83-348 4.22e-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: 51.98  E-value: 4.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     83 TNEFQQLQSKISLISEKLESTESILQEATSSMSLM----TQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDF 158
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    159 WKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLED------STLRNIRTVKRQEEEDLLRVEEQLG 232
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAeltllnEEAANLRERLESLERRIAATERRLE 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    233 SDTKAIEKLEEEqhalfardedltnkLSDYEPKVEECKTHLPTIESAIHSVL----RVSQDLIETEKKMEDLTMQMFNME 308
Cdd:TIGR02168  842 DLEEQIEELSED--------------IESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRELE 907

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 37590644    309 DDMLKAVSEIMEMQKTLEgiQYDNSILKMQNELDILKEKV 348
Cdd:TIGR02168  908 SKRSELRRELEELREKLA--QLELRLEGLEVRIDNLQERL 945
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 70-342 1.26e-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: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     70 AKVENQYQllKLETNEFQQLQSKISLISEKLESTESILQEatssmsLMTQFEQEVSN-LQDIMHDIQNNEEVLTQrmqsl 148
Cdd:TIGR01612  703 SKIDKEYD--KIQNMETATVELHLSNIENKKNELLDIIVE------IKKHIHGEINKdLNKILEDFKNKEKELSN----- 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    149 nekfqNITDFWKRSlEEMNIntdiFKSEAKHIHSQVTVQI---NSAEQEIKLLTERLKDL-------EDSTLRNIRTVKR 218
Cdd:TIGR01612  770 -----KINDYAKEK-DELNK----YKSKISEIKNHYNDQInidNIKDEDAKQNYDKSKEYiktisikEDEIFKIINEMKF 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    219 QEEEDLLRVEEQLGSDTKAIEKLEEEqHALFA------RDEDLTNKLSDYEPKVEECKTHLPTIESAIHS---------- 282
Cdd:TIGR01612  840 MKDDFLNKVDKFINFENNCKEKIDSE-HEQFAeltnkiKAEISDDKLNDYEKKFNDSKSLINEINKSIEEeyqnintlkk 918

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590644    283 ---VLRVSQDLIETEKKMEDLTMQMFNMEDDMLKAVSEIMEMQKTLEGiQYDNSILKMQNELD 342
Cdd:TIGR01612  919 vdeYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKD-KFDNTLIDKINELD 980
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 64-349 4.42e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     64 QQSEKFAKVENQYQLLKLE--TNEFQQLQSKISLISEKLESTESILQEATSsmsLMTQFEQEVSNLQDIMHDIQNNEEVL 141
Cdd:TIGR02168  210 EKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTA---ELQELEEKLEELRLEVSELEEEIEEL 286

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    142 TQRMQSLNEKfqnitdfwkrsleemnintdifkseakhihsqvtvqINSAEQEIKLLTERLKDLEDSTLR---NIRTVKR 218
Cdd:TIGR02168  287 QKELYALANE------------------------------------ISRLEQQKQILRERLANLERQLEEleaQLEELES 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    219 QEEED---LLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHL------------------PTIE 277
Cdd:TIGR02168  331 KLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlelqiaslnneierleARLE 410

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37590644    278 SAIHSVLRVSQDLIETEKKMEDLTMQMFNMEDDMLKAvsEIMEMQKTLEGIQ-----YDNSILKMQNELDILKEKVH 349
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE--ELEELQEELERLEealeeLREELEEAEQALDAAERELA 485
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 64-341 6.45e-04

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


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.96  E-value: 6.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     64 QQSEKFAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQEATSSMSLMTQFEQEVSNLQDimhDIQNNEEV--- 140
Cdd:TIGR01612 1518 QYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIED---DAAKNDKSnka 1594

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    141 ---LTQRMQSLNEKFQNITDFWKRSleemninTDIFKsEAKHIHSQV-TVQINSAEQEIKLLTERLKDLEdSTLRNIRTV 216
Cdd:TIGR01612 1595 aidIQLSLENFENKFLKISDIKKKI-------NDCLK-ETESIEKKIsSFSIDSQDTELKENGDNLNSLQ-EFLESLKDQ 1665

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    217 KRQEEEDLLRVEEqLGSDTKAIEkLEEEQHAL---FARDEDLTNKLSDYEPKVEECKTHL-PTIESAIHSVLRVSQDLIE 292
Cdd:TIGR01612 1666 KKNIEDKKKELDE-LDSEIEKIE-IDVDQHKKnyeIGIIEKIKEIAIANKEEIESIKELIePTIENLISSFNTNDLEGID 1743

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 37590644    293 TEKKMEDLTMQMFNMEDDMLKAVSEIMEMQKTL--EGIQYD---NSILKMQNEL 341
Cdd:TIGR01612 1744 PNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVskEPITYDeikNTRINAQNEF 1797
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 64-348 8.03e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     64 QQSEKFAKVENQYQLLK--LETNEFQQLQSKISLISEKLESTESILQE---ATSSMSLMTQF-EQEVSNLQDIMHDIQNN 137
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYlEKEIQELQEQRIDLKEQ 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    138 EEVLTQRMQSLNEKfqnitdfwKRSLEEmnintdifkseakhihsqvtvQINSAEQEIKLLTERLKDLEdstlRNIRTVK 217
Cdd:TIGR02169  849 IKSIEKEIENLNGK--------KEELEE---------------------ELEELEAALRDLESRLGDLK----KERDELE 895

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    218 RQEEEDLLRVEEQlgsdTKAIEKLEEEQHALFARDEDLTNKLSDYEPKV---EECKTHLPTIESAIHSVLRVSQDLiete 294
Cdd:TIGR02169  896 AQLRELERKIEEL----EAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedEEIPEEELSLEDVQAELQRVEEEI---- 967

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 37590644    295 KKMEDLTMQMFNMEDDMLKAVSEIMEMQKTLEgiQYDNSILKMQNELDILKEKV 348
Cdd:TIGR02169  968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLE--EERKAILERIEEYEKKKREV 1019
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 71-367 8.63e-04

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: 41.54  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    71 KVENQYQLLKLETNEFQQLQSKISLISEKLEStesILQEATSSMSLMTQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNE 150
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIER---LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   151 KFQNITDFWKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLE------DSTLRNIRTVKRQEEEDL 224
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSLKEKIEKLEsekkekESKISDLEDELNKDDFEL 554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   225 LR--VEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHlptIESAIHSVLRVSQDLIETEKKMEDLTM 302
Cdd:TIGR04523 555 KKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---IEEKEKKISSLEKELEKAKKENEKLSS 631

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37590644   303 QMFNMEDDMLKAVSEIMEMQKTLEGIQYDNSILKMQNEldILKEKVHDFIAYSSTGEKGTLKEYN 367
Cdd:TIGR04523 632 IIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK--ESKTKIDDIIELMKDWLKELSLHYK 694
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 88-248 1.07e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     88 QLQSKISLISEKLESTESILQEATSSMSLMTQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKF---QNITDFWKRSLE 164
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyREKLEKLKREIN 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    165 EMNINTDIFKSEAKHIHSQVT---VQINSAEQEIKLLTERLKDLEDStLRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKL 241
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELAdlnAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481


                   ....*..
gi 37590644    242 EEEQHAL 248
Cdd:TIGR02169  482 EKELSKL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-290 1.08e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     62 VFQQSEKFAKVENQYQLLKletNEFQQLQSKISLISEKLESTESILQEatssmslmtqfeqevsnLQDIMHDIQNNEEVL 141
Cdd:TIGR02168  290 LYALANEISRLEQQKQILR---ERLANLERQLEELEAQLEELESKLDE-----------------LAEELAELEEKLEEL 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    142 TQRMQSLNEKFQNITDFW---KRSLEEMNINTDIFKSEAKhihsQVTVQINSAEQEIKLLTERLKDLEDSTLRNIRTV-- 216
Cdd:TIGR02168  350 KEELESLEAELEELEAELeelESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARLERLEDRRERLQQEIee 425

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37590644    217 --KRQEEEDLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDL 290
Cdd:TIGR02168  426 llKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-326 2.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  67 EKFAKVENQYQLLKLE--TNEFQQLQSKISLISEKLESTESILQEATSSMSLMtqfEQEVSNLQDIMHDIQNNEEVLTQR 144
Cdd:COG1196 213 ERYRELKEELKELEAEllLLKLRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLELEELELELEEAQAE 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644 145 MQSLNEkfqnitdfwkrsleemnintdifkseakhihsqvtvQINSAEQEIKLLTERLKDLEDSTLRN---IRTVKRQEE 221
Cdd:COG1196 290 EYELLA------------------------------------ELARLEQDIARLEERRRELEERLEELeeeLAELEEELE 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644 222 EDLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEEckthlptIESAIHSVLRVSQDLIETEKKMEDLT 301
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-------LEELAEELLEALRAAAELAAQLEELE 406

                       250       260
                ....*....|....*....|....*
gi 37590644 302 MQMFNMEDDMLKAVSEIMEMQKTLE 326
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALA 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 64-327 2.36e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  64 QQSEKFAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQEAtssmslmtqfEQEVSNLQDIMHDIQNNEEVLTQ 143
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL----------EERRRELEERLEELEEELAELEE 330

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644 144 RMQSLNEKfqnitdfwKRSLEEMNINTDIFKSEAKHIHSQVTVQINSAEQEIKLLTERLKDLEDSTLRNIRTvKRQEEED 223
Cdd:COG1196 331 ELEELEEE--------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQ 401

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644 224 LLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDLIETEKKMEDLTMQ 303
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                       250       260
                ....*....|....*....|....
gi 37590644 304 MFNMEDDMLKAVSEIMEMQKTLEG 327
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEG 505
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 104-352 2.59e-03

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: 40.03  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    104 ESILQEATSSMSLMTQFEQEVSN--LQDIMHDIQNNEEVLTQRMQSLNEKFQNITdfwkrSLEEMNINTDIFKSEAKHI- 180
Cdd:TIGR01612  860 EKIDSEHEQFAELTNKIKAEISDdkLNDYEKKFNDSKSLINEINKSIEEEYQNIN-----TLKKVDEYIKICENTKESIe 934

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    181 --HSQVTVQINSAEQEIKLLTE------RLKDLEDSTLRNIRTV--KRQEEEDLLRVEEQLGSDTKAIEKLEE-----EQ 245
Cdd:TIGR01612  935 kfHNKQNILKEILNKNIDTIKEsnliekSYKDKFDNTLIDKINEldKAFKDASLNDYEAKNNELIKYFNDLKAnlgknKE 1014

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    246 HALFARDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDLIETE--KKMEDLTMQMFNMEDDMLKAVSEIMEMQK 323
Cdd:TIGR01612 1015 NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINITNFNEIKEKLK 1094

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 37590644    324 TL--------EGIQYDNSILKMQNELDILKEKVHDFI 352
Cdd:TIGR01612 1095 HYnfddfgkeENIKYADEINKIKDDIKNLDQKIDHHI 1131
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
92-267 3.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  92 KISLISEKLESTESILQEATSSMSLMTQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLnEKFQNITDFWKRsLEEMNINTD 171
Cdd:COG4717  65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQE-LEALEAELA 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644 172 IFKSEAKHIHSQVTvQINSAEQEIKLLTERLKDLEDSTLRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKLEEEQHALFAR 251
Cdd:COG4717 143 ELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221

                       170
                ....*....|....*.
gi 37590644 252 DEDLTNKLSDYEPKVE 267
Cdd:COG4717 222 LEELEEELEQLENELE 237
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 43-231 3.59e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.26  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    43 PRTCLSLLSLGTclglawFVFQQ---------SEKFAKVENQYQLLKLetnefQQLQSKISLISEKlestESILQEATSs 113
Cdd:pfam10168 530 PQECLQLLSRAT------QVFREeylkkhdlaREEIQKRVKLLKLQKE-----QQLQELQSLEEER----KSLSERAEK- 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   114 msLMTQFEqevsnlqdimhDIQNNEEVLTQR----MQSLNEKFQNITDF---WKRSLEEMNINTDIFKS---EAKHIHSQ 183
Cdd:pfam10168 594 --LAEKYE-----------EIKDKQEKLMRRckkvLQRLNSQLPVLSDAereMKKELETINEQLKHLANaikQAKKKMNY 660

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 37590644   184 VTVQINSAEQEIKLLTERLKDLEDSTLRNIRTvkrQEEEDLLRVEEQL 231
Cdd:pfam10168 661 QRYQIAKSQSIRKKSSLSLSEKQRKTIKEILK---QLGSEIDELIKQV 705
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 61-340 3.97e-03

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: 39.32  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    61 FVFQQSEKFAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQEATSsmslmtqfeqEVSNLQDIMHDIQNNEEV 140
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK----------ELEDIKMSLQRSMSTQKA 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   141 LTQRMQSLNEKFQNITDFWKRSLEEMNintdifksEAKHIHSQVTVQINSA------------------EQEIKLLTERL 202
Cdd:pfam05483 315 LEEDLQIATKTICQLTEEKEAQMEELN--------KAKAAHSFVVTEFEATtcsleellrteqqrleknEDQLKIITMEL 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   203 K----DLEDST-LRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKLEEEqhaLFARDEDLTNKLSDYEPKVEECKTHLPTIE 277
Cdd:pfam05483 387 QkkssELEEMTkFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIK 463

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 37590644   278 SAIHSVLRVSQDLiETEKKMEDLTMQMFNMEDDML-----KAVSEIMEMQKTLEGIQYDNSILKMQNE 340
Cdd:pfam05483 464 TSEEHYLKEVEDL-KTELEKEKLKNIELTAHCDKLllenkELTQEASDMTLELKKHQEDIINCKKQEE 530
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 64-348 4.13e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.23  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    64 QQSEKFAKVENQYQLLKLETNEFQQLQSKIS-LISEKLESTESILQEatssmslmtQFEQEVSNLQDIMHDIQNNEEVLT 142
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQDWNKELKS---------ELKNQEKKLEEIQNQISQNNKIIS 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   143 QrmqsLNEKFQNItdfwKRSLEEMNINTDIFKSEAKHIHSQVTV---QINSAEQEIKLLTERLKDLEdSTLRNIRTVKRQ 219
Cdd:TIGR04523 339 Q----LNEQISQL----KKELTNSESENSEKQRELEEKQNEIEKlkkENQSYKQEIKNLESQINDLE-SKIQNQEKLNQQ 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644   220 EEEDLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLR-----------VSQ 288
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqnleqKQK 489

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37590644   289 DLIETEKKMEDLTMQMFNME---DDMLKAVSEIMEMQKTLEgiqydNSILKMQNELDILKEKV 348
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEekvKDLTKKISSLKEKIEKLE-----SEKKEKESKISDLEDEL 547
46 PHA02562
endonuclease subunit; Provisional
 163-350 4.70e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 38.84  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  163 LEEMNIntdIFKSEAKHIHSQ---VTVQINSAEQEIKLLT--------------ERLKDLEDSTLRNIRTVKRQEEE--- 222
Cdd:PHA02562 165 LSEMDK---LNKDKIRELNQQiqtLDMKIDHIQQQIKTYNknieeqrkkngeniARKQNKYDELVEEAKTIKAEIEEltd 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  223 DLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEpKVEECKThlptiesaihsvlrVSQDLIETEKKMEDLTM 302
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYE-KGGVCPT--------------CTQQISEGPDRITKIKD 306

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  303 QMFNME----------DDMLKAVSEIMEMQKTLEGIQ------------YDNSILKMQNELDILKEKVHD 350
Cdd:PHA02562 307 KLKELQhslekldtaiDELEEIMDEFNEQSKKLLELKnkistnkqslitLVDKAKKVKAAIEELQAEFVD 376
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
191-303 5.13e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644  191 AEQEIKLLTERLKDLEDST------LRNIRTVKRQEEEDLLRVEEQL-GSDTKAIEKLEEEQHALFARDEDLTNKLSDYE 263
Cdd:COG4913  286 AQRRLELLEAELEELRAELarleaeLERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLE 365

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 37590644  264 PKVEECKTHLPTIESAIHSVLRVSQDLIETEKKMEDLTMQ 303
Cdd:COG4913  366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 87-354 5.34e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.05  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     87 QQLQSKISLISEKLESTESILQEATSSMSLMT-QFEQEVSNLQDIMHDIQNNEEvltqRMQSLNEKFQNITDFWKRSLEE 165
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAAAEEQLVQANgELEKASREETFARTALKNARL----DLRRLFDEKQSEKDKKNKALAE 675

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    166 mnintdifkseakHIHSQVTvQINSAEQEIKLLTERLKDLEDSTLRNIRTVKRQEEEDLLRVEE----QLGSDTKAIEKL 241
Cdd:pfam12128  676 -------------RKDSANE-RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGaldaQLALLKAAIAAR 741

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    242 EEEQHA-LFARDEDLTNKL----------SDYEPKVEECKTHLPTIESAIHSVLRVSQ---------------DLIETEK 295
Cdd:pfam12128  742 RSGAKAeLKALETWYKRDLaslgvdpdviAKLKREIRTLERKIERIAVRRQEVLRYFDwyqetwlqrrprlatQLSNIER 821

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 37590644    296 KMEDLTMQMFNMEDDMLKAVSEIMEMQKTLEgiqydnsilKMQNELDILKEKVHDFIAY 354
Cdd:pfam12128  822 AISELQQQLARLIADTKLRRAKLEMERKASE---------KQQVRLSENLRGLRCEMSK 871
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 65-343 5.41e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 38.95  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     65 QSEKfAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQeaTSSMSLMTQFEQEVSNLQDIMHDI-QNNEEVLTQ 143
Cdd:pfam15921  589 QVEK-AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--LEKVKLVNAGSERLRAVKDIKQERdQLLNEVKTS 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    144 R--MQSLNEKFQNITDFWKRSLEEMNINTDIFKseakhihsqvtVQINSAEQEIKLLTERLKDLEDSTLRNIRtVKRQEE 221
Cdd:pfam15921  666 RneLNSLSEDYEVLKRNFRNKSEEMETTTNKLK-----------MQLKSAQSELEQTRNTLKSMEGSDGHAMK-VAMGMQ 733

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    222 EDLLRVEEQLGSDTKAIEKLEE-------EQHALFARDEDLTNKLSDYEPKVEECKTHLPTIESaihsvlrvsqdlieTE 294
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLEEamtnankEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS--------------QE 799

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 37590644    295 KKMEDltmQMFNMEDDMLKAVSEIMEMQKTLEGIQYDNSILKMQNELDI 343
Cdd:pfam15921  800 RRLKE---KVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDV 845
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-261 7.83e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 7.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644     62 VFQQSEKFAKVENQYQLLKLE----TNEFQQLQSKISLISEKLESTESILQEATSSMSL----MTQFEQEVSNLQDIMHD 133
Cdd:TIGR02168  798 LKALREALDELRAELTLLNEEaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeIEELEELIEELESELEA 877

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37590644    134 IQNNEEVLTQRMQSLNEKFQNITDFWKRSLEEMNINTDIfKSEAKHIHSQVTVQINSAEQEIKLLTERLKDLEDSTLRNI 213
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRE-LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 37590644    214 RTVKRQEEEDLLRVEEQLGSDTKAIEKL-------EEEQHALFARDEDLTNKLSD 261
Cdd:TIGR02168  957 EALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKED 1011
 
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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