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Conserved domains on  [gi|24233517|ref|NP_710154|]
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inhibitor of nuclear factor kappa-B kinase-interacting protein isoform 1 [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 24233517     83 TNEFQQLQSKISLISEKLESTESILQEATSSMSLM----TQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDF 158
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    159 WKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLED------STLRNIRTVKRQEEEDLLRVEEQLG 232
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAeltllnEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    233 SDTKAIEKLEEEqhalfardedltnkLSDYEPKVEECKTHLPTIESAIHSVL----RVSQDLIETEKKMEDLTMQMFNME 308
Cdd:TIGR02168  842 DLEEQIEELSED--------------IESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRELE 907
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 24233517    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 24233517     83 TNEFQQLQSKISLISEKLESTESILQEATSSMSLM----TQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDF 158
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    159 WKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLED------STLRNIRTVKRQEEEDLLRVEEQLG 232
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAeltllnEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    233 SDTKAIEKLEEEqhalfardedltnkLSDYEPKVEECKTHLPTIESAIHSVL----RVSQDLIETEKKMEDLTMQMFNME 308
Cdd:TIGR02168  842 DLEEQIEELSED--------------IESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRELE 907
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 24233517    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 24233517  67 EKFAKVENQYQLLKLE--TNEFQQLQSKISLISEKLESTESILQEATSSMSLMtqfEQEVSNLQDIMHDIQNNEEVLTQR 144
Cdd:COG1196 213 ERYRELKEELKELEAEllLLKLRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517 145 MQSLNEkfqnitdfwkrsleemnintdifkseakhihsqvtvQINSAEQEIKLLTERLKDLEDSTLRN---IRTVKRQEE 221
Cdd:COG1196 290 EYELLA------------------------------------ELARLEQDIARLEERRRELEERLEELeeeLAELEEELE 333
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517 222 EDLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEEckthlptIESAIHSVLRVSQDLIETEKKMEDLT 301
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-------LEELAEELLEALRAAAELAAQLEELE 406
                       250       260
                ....*....|....*....|....*
gi 24233517 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 24233517    43 PRTCLSLLSLGTclglawFVFQQ---------SEKFAKVENQYQLLKLetnefQQLQSKISLISEKlestESILQEATSs 113
Cdd:pfam10168 530 PQECLQLLSRAT------QVFREeylkkhdlaREEIQKRVKLLKLQKE-----QQLQELQSLEEER----KSLSERAEK- 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   114 msLMTQFEqevsnlqdimhDIQNNEEVLTQR----MQSLNEKFQNITDF---WKRSLEEMNINTDIFKS---EAKHIHSQ 183
Cdd:pfam10168 594 --LAEKYE-----------EIKDKQEKLMRRckkvLQRLNSQLPVLSDAereMKKELETINEQLKHLANaikQAKKKMNY 660
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 24233517   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 24233517  163 LEEMNIntdIFKSEAKHIHSQ---VTVQINSAEQEIKLLT--------------ERLKDLEDSTLRNIRTVKRQEEE--- 222
Cdd:PHA02562 165 LSEMDK---LNKDKIRELNQQiqtLDMKIDHIQQQIKTYNknieeqrkkngeniARKQNKYDELVEEAKTIKAEIEEltd 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517  223 DLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEpKVEECKThlptiesaihsvlrVSQDLIETEKKMEDLTM 302
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYE-KGGVCPT--------------CTQQISEGPDRITKIKD 306
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517  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 24233517     83 TNEFQQLQSKISLISEKLESTESILQEATSSMSLM----TQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKFQNITDF 158
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    159 WKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLED------STLRNIRTVKRQEEEDLLRVEEQLG 232
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAeltllnEEAANLRERLESLERRIAATERRLE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    233 SDTKAIEKLEEEqhalfardedltnkLSDYEPKVEECKTHLPTIESAIHSVL----RVSQDLIETEKKMEDLTMQMFNME 308
Cdd:TIGR02168  842 DLEEQIEELSED--------------IESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRELE 907
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 24233517    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 24233517     70 AKVENQYQllKLETNEFQQLQSKISLISEKLESTESILQEatssmsLMTQFEQEVSN-LQDIMHDIQNNEEVLTQrmqsl 148
Cdd:TIGR01612  703 SKIDKEYD--KIQNMETATVELHLSNIENKKNELLDIIVE------IKKHIHGEINKdLNKILEDFKNKEKELSN----- 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    149 nekfqNITDFWKRSlEEMNIntdiFKSEAKHIHSQVTVQI---NSAEQEIKLLTERLKDL-------EDSTLRNIRTVKR 218
Cdd:TIGR01612  770 -----KINDYAKEK-DELNK----YKSKISEIKNHYNDQInidNIKDEDAKQNYDKSKEYiktisikEDEIFKIINEMKF 839
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    219 QEEEDLLRVEEQLGSDTKAIEKLEEEqHALFA------RDEDLTNKLSDYEPKVEECKTHLPTIESAIHS---------- 282
Cdd:TIGR01612  840 MKDDFLNKVDKFINFENNCKEKIDSE-HEQFAeltnkiKAEISDDKLNDYEKKFNDSKSLINEINKSIEEeyqnintlkk 918
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24233517    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 24233517     64 QQSEKFAKVENQYQLLKLE--TNEFQQLQSKISLISEKLESTESILQEATSsmsLMTQFEQEVSNLQDIMHDIQNNEEVL 141
Cdd:TIGR02168  210 EKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTA---ELQELEEKLEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    142 TQRMQSLNEKfqnitdfwkrsleemnintdifkseakhihsqvtvqINSAEQEIKLLTERLKDLEDSTLR---NIRTVKR 218
Cdd:TIGR02168  287 QKELYALANE------------------------------------ISRLEQQKQILRERLANLERQLEEleaQLEELES 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    219 QEEED---LLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHL------------------PTIE 277
Cdd:TIGR02168  331 KLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaqlelqiaslnneierleARLE 410
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24233517    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 24233517     64 QQSEKFAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQEATSSMSLMTQFEQEVSNLQDimhDIQNNEEV--- 140
Cdd:TIGR01612 1518 QYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIED---DAAKNDKSnka 1594
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    141 ---LTQRMQSLNEKFQNITDFWKRSleemninTDIFKsEAKHIHSQV-TVQINSAEQEIKLLTERLKDLEdSTLRNIRTV 216
Cdd:TIGR01612 1595 aidIQLSLENFENKFLKISDIKKKI-------NDCLK-ETESIEKKIsSFSIDSQDTELKENGDNLNSLQ-EFLESLKDQ 1665
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    217 KRQEEEDLLRVEEqLGSDTKAIEkLEEEQHAL---FARDEDLTNKLSDYEPKVEECKTHL-PTIESAIHSVLRVSQDLIE 292
Cdd:TIGR01612 1666 KKNIEDKKKELDE-LDSEIEKIE-IDVDQHKKnyeIGIIEKIKEIAIANKEEIESIKELIePTIENLISSFNTNDLEGID 1743
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24233517    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 24233517     64 QQSEKFAKVENQYQLLK--LETNEFQQLQSKISLISEKLESTESILQE---ATSSMSLMTQF-EQEVSNLQDIMHDIQNN 137
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYlEKEIQELQEQRIDLKEQ 848
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    138 EEVLTQRMQSLNEKfqnitdfwKRSLEEmnintdifkseakhihsqvtvQINSAEQEIKLLTERLKDLEdstlRNIRTVK 217
Cdd:TIGR02169  849 IKSIEKEIENLNGK--------KEELEE---------------------ELEELEAALRDLESRLGDLK----KERDELE 895
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    218 RQEEEDLLRVEEQlgsdTKAIEKLEEEQHALFARDEDLTNKLSDYEPKV---EECKTHLPTIESAIHSVLRVSQDLiete 294
Cdd:TIGR02169  896 AQLRELERKIEEL----EAQIEKKRKRLSELKAKLEALEEELSEIEDPKgedEEIPEEELSLEDVQAELQRVEEEI---- 967
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24233517    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 24233517    71 KVENQYQLLKLETNEFQQLQSKISLISEKLEStesILQEATSSMSLMTQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNE 150
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIER---LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   151 KFQNITDFWKRSLEEMNINTDIFKSEAKHIhSQVTVQINSAEQEIKLLTERLKDLE------DSTLRNIRTVKRQEEEDL 224
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSLKEKIEKLEsekkekESKISDLEDELNKDDFEL 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   225 LR--VEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHlptIESAIHSVLRVSQDLIETEKKMEDLTM 302
Cdd:TIGR04523 555 KKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE---IEEKEKKISSLEKELEKAKKENEKLSS 631
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24233517   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 24233517     88 QLQSKISLISEKLESTESILQEATSSMSLMTQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLNEKF---QNITDFWKRSLE 164
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyREKLEKLKREIN 402
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    165 EMNINTDIFKSEAKHIHSQVT---VQINSAEQEIKLLTERLKDLEDStLRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKL 241
Cdd:TIGR02169  403 ELKRELDRLQEELQRLSEELAdlnAAIAGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481

                   ....*..
gi 24233517    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 24233517     62 VFQQSEKFAKVENQYQLLKletNEFQQLQSKISLISEKLESTESILQEatssmslmtqfeqevsnLQDIMHDIQNNEEVL 141
Cdd:TIGR02168  290 LYALANEISRLEQQKQILR---ERLANLERQLEELEAQLEELESKLDE-----------------LAEELAELEEKLEEL 349
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    142 TQRMQSLNEKFQNITDFW---KRSLEEMNINTDIFKSEAKhihsQVTVQINSAEQEIKLLTERLKDLEDSTLRNIRTV-- 216
Cdd:TIGR02168  350 KEELESLEAELEELEAELeelESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARLERLEDRRERLQQEIee 425
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24233517    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 24233517  67 EKFAKVENQYQLLKLE--TNEFQQLQSKISLISEKLESTESILQEATSSMSLMtqfEQEVSNLQDIMHDIQNNEEVLTQR 144
Cdd:COG1196 213 ERYRELKEELKELEAEllLLKLRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517 145 MQSLNEkfqnitdfwkrsleemnintdifkseakhihsqvtvQINSAEQEIKLLTERLKDLEDSTLRN---IRTVKRQEE 221
Cdd:COG1196 290 EYELLA------------------------------------ELARLEQDIARLEERRRELEERLEELeeeLAELEEELE 333
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517 222 EDLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEEckthlptIESAIHSVLRVSQDLIETEKKMEDLT 301
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-------LEELAEELLEALRAAAELAAQLEELE 406
                       250       260
                ....*....|....*....|....*
gi 24233517 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 24233517  64 QQSEKFAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQEAtssmslmtqfEQEVSNLQDIMHDIQNNEEVLTQ 143
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL----------EERRRELEERLEELEEELAELEE 330
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517 144 RMQSLNEKfqnitdfwKRSLEEMNINTDIFKSEAKHIHSQVTVQINSAEQEIKLLTERLKDLEDSTLRNIRTvKRQEEED 223
Cdd:COG1196 331 ELEELEEE--------LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQ 401
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517 224 LLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDLIETEKKMEDLTMQ 303
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                       250       260
                ....*....|....*....|....
gi 24233517 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 24233517    104 ESILQEATSSMSLMTQFEQEVSN--LQDIMHDIQNNEEVLTQRMQSLNEKFQNITdfwkrSLEEMNINTDIFKSEAKHI- 180
Cdd:TIGR01612  860 EKIDSEHEQFAELTNKIKAEISDdkLNDYEKKFNDSKSLINEINKSIEEEYQNIN-----TLKKVDEYIKICENTKESIe 934
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    181 --HSQVTVQINSAEQEIKLLTE------RLKDLEDSTLRNIRTV--KRQEEEDLLRVEEQLGSDTKAIEKLEE-----EQ 245
Cdd:TIGR01612  935 kfHNKQNILKEILNKNIDTIKEsnliekSYKDKFDNTLIDKINEldKAFKDASLNDYEAKNNELIKYFNDLKAnlgknKE 1014
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    246 HALFARDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLRVSQDLIETE--KKMEDLTMQMFNMEDDMLKAVSEIMEMQK 323
Cdd:TIGR01612 1015 NMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINITNFNEIKEKLK 1094
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 24233517    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 24233517  92 KISLISEKLESTESILQEATSSMSLMTQFEQEVSNLQDIMHDIQNNEEVLTQRMQSLnEKFQNITDFWKRsLEEMNINTD 171
Cdd:COG4717  65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQE-LEALEAELA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517 172 IFKSEAKHIHSQVTvQINSAEQEIKLLTERLKDLEDSTLRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKLEEEQHALFAR 251
Cdd:COG4717 143 ELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
                       170
                ....*....|....*.
gi 24233517 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 24233517    43 PRTCLSLLSLGTclglawFVFQQ---------SEKFAKVENQYQLLKLetnefQQLQSKISLISEKlestESILQEATSs 113
Cdd:pfam10168 530 PQECLQLLSRAT------QVFREeylkkhdlaREEIQKRVKLLKLQKE-----QQLQELQSLEEER----KSLSERAEK- 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   114 msLMTQFEqevsnlqdimhDIQNNEEVLTQR----MQSLNEKFQNITDF---WKRSLEEMNINTDIFKS---EAKHIHSQ 183
Cdd:pfam10168 594 --LAEKYE-----------EIKDKQEKLMRRckkvLQRLNSQLPVLSDAereMKKELETINEQLKHLANaikQAKKKMNY 660
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 24233517   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 24233517    61 FVFQQSEKFAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQEATSsmslmtqfeqEVSNLQDIMHDIQNNEEV 140
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK----------ELEDIKMSLQRSMSTQKA 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   141 LTQRMQSLNEKFQNITDFWKRSLEEMNintdifksEAKHIHSQVTVQINSA------------------EQEIKLLTERL 202
Cdd:pfam05483 315 LEEDLQIATKTICQLTEEKEAQMEELN--------KAKAAHSFVVTEFEATtcsleellrteqqrleknEDQLKIITMEL 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   203 K----DLEDST-LRNIRTVKRQEEEDLLRVEEQLGSDTKAIEKLEEEqhaLFARDEDLTNKLSDYEPKVEECKTHLPTIE 277
Cdd:pfam05483 387 QkkssELEEMTkFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE---LKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24233517   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 24233517    64 QQSEKFAKVENQYQLLKLETNEFQQLQSKIS-LISEKLESTESILQEatssmslmtQFEQEVSNLQDIMHDIQNNEEVLT 142
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISdLNNQKEQDWNKELKS---------ELKNQEKKLEEIQNQISQNNKIIS 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   143 QrmqsLNEKFQNItdfwKRSLEEMNINTDIFKSEAKHIHSQVTV---QINSAEQEIKLLTERLKDLEdSTLRNIRTVKRQ 219
Cdd:TIGR04523 339 Q----LNEQISQL----KKELTNSESENSEKQRELEEKQNEIEKlkkENQSYKQEIKNLESQINDLE-SKIQNQEKLNQQ 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517   220 EEEDLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEPKVEECKTHLPTIESAIHSVLR-----------VSQ 288
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqnleqKQK 489
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24233517   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 24233517  163 LEEMNIntdIFKSEAKHIHSQ---VTVQINSAEQEIKLLT--------------ERLKDLEDSTLRNIRTVKRQEEE--- 222
Cdd:PHA02562 165 LSEMDK---LNKDKIRELNQQiqtLDMKIDHIQQQIKTYNknieeqrkkngeniARKQNKYDELVEEAKTIKAEIEEltd 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517  223 DLLRVEEQLGSDTKAIEKLEEEQHALFARDEDLTNKLSDYEpKVEECKThlptiesaihsvlrVSQDLIETEKKMEDLTM 302
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYE-KGGVCPT--------------CTQQISEGPDRITKIKD 306
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517  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 24233517  191 AEQEIKLLTERLKDLEDST------LRNIRTVKRQEEEDLLRVEEQL-GSDTKAIEKLEEEQHALFARDEDLTNKLSDYE 263
Cdd:COG4913  286 AQRRLELLEAELEELRAELarleaeLERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLE 365
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 24233517  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 24233517     87 QQLQSKISLISEKLESTESILQEATSSMSLMT-QFEQEVSNLQDIMHDIQNNEEvltqRMQSLNEKFQNITDFWKRSLEE 165
Cdd:pfam12128  600 EELRERLDKAEEALQSAREKQAAAEEQLVQANgELEKASREETFARTALKNARL----DLRRLFDEKQSEKDKKNKALAE 675
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    166 mnintdifkseakHIHSQVTvQINSAEQEIKLLTERLKDLEDSTLRNIRTVKRQEEEDLLRVEE----QLGSDTKAIEKL 241
Cdd:pfam12128  676 -------------RKDSANE-RLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGaldaQLALLKAAIAAR 741
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    242 EEEQHA-LFARDEDLTNKL----------SDYEPKVEECKTHLPTIESAIHSVLRVSQ---------------DLIETEK 295
Cdd:pfam12128  742 RSGAKAeLKALETWYKRDLaslgvdpdviAKLKREIRTLERKIERIAVRRQEVLRYFDwyqetwlqrrprlatQLSNIER 821
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 24233517    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 24233517     65 QSEKfAKVENQYQLLKLETNEFQQLQSKISLISEKLESTESILQeaTSSMSLMTQFEQEVSNLQDIMHDI-QNNEEVLTQ 143
Cdd:pfam15921  589 QVEK-AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE--LEKVKLVNAGSERLRAVKDIKQERdQLLNEVKTS 665
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    144 R--MQSLNEKFQNITDFWKRSLEEMNINTDIFKseakhihsqvtVQINSAEQEIKLLTERLKDLEDSTLRNIRtVKRQEE 221
Cdd:pfam15921  666 RneLNSLSEDYEVLKRNFRNKSEEMETTTNKLK-----------MQLKSAQSELEQTRNTLKSMEGSDGHAMK-VAMGMQ 733
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    222 EDLLRVEEQLGSDTKAIEKLEE-------EQHALFARDEDLTNKLSDYEPKVEECKTHLPTIESaihsvlrvsqdlieTE 294
Cdd:pfam15921  734 KQITAKRGQIDALQSKIQFLEEamtnankEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS--------------QE 799
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 24233517    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 24233517     62 VFQQSEKFAKVENQYQLLKLE----TNEFQQLQSKISLISEKLESTESILQEATSSMSL----MTQFEQEVSNLQDIMHD 133
Cdd:TIGR02168  798 LKALREALDELRAELTLLNEEaanlRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeIEELEELIEELESELEA 877
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24233517    134 IQNNEEVLTQRMQSLNEKFQNITDFWKRSLEEMNINTDIfKSEAKHIHSQVTVQINSAEQEIKLLTERLKDLEDSTLRNI 213
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRE-LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 24233517    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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