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Conserved domains on  [gi|1723267|sp|Q10198|]
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RecName: Full=Kinetochore protein ndc80; AltName: Full=NMS complex subunit ndc80

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ndc80_HEC pfam03801
HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been ...
73-221 2.41e-62

HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been shown that Ndc80/HEC from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle.


:

Pssm-ID: 461058  Cd Length: 159  Bit Score: 203.67  E-value: 2.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     73 RRSSV--------RVSNASFISQTPNITSI-KDPRPLSDRRYQQECATQVVNYLLESGFSQPLGLNNRFMPSTREFAAIF 143
Cdd:pfam03801   2 RRSSVyggrgggpRSSHQSFFSSSPMPASVpRDPRPLRDKSFQQQCIQELLEYLTENNFEHPLSPKLLKSPTQKDFNSIF 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267    144 KHLYNKLDPNFRFGARYEEDVTTCLKALNYPFLDSISRSRLVAIGSPHVWPAILGMLHWVVSLIQCTEKAVAMVYTVE 221
Cdd:pfam03801  82 KFLYHRLDPSYEFQKKIEEEVPMILKQLRYPFLDSISKSQLSAVGGPHTWPTFLGLLHWLVELAKFLEALEQNLYDDD 159
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
333-548 3.76e-10

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 62.09  E-value: 3.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  333 MKQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQldrNLNMIGSKISELRKEVFDtdllIQASIDS 412
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELEKEIAE----LRAELEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  413 LEKKVQKFNSLAYRIGIVPIAAirsanndfeLEINPEGPN--YINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEH 490
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLA---------LLLSPEDFLdaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267  491 VDTVNDLIAELQDELRgiesRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLK 548
Cdd:COG4942 173 RAELEALLAELEEERA----ALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
259-398 5.21e-05

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     259 LKATFNQQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQV 338
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     339 NIEEKESQLQLLKEKRDSLKYQVENQDisisefekmvSEREQLDRNLNMIGSKISELRKE 398
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLR----------SELEELSEELRELESKRSELRRE 916
 
Name Accession Description Interval E-value
Ndc80_HEC pfam03801
HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been ...
73-221 2.41e-62

HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been shown that Ndc80/HEC from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle.


Pssm-ID: 461058  Cd Length: 159  Bit Score: 203.67  E-value: 2.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     73 RRSSV--------RVSNASFISQTPNITSI-KDPRPLSDRRYQQECATQVVNYLLESGFSQPLGLNNRFMPSTREFAAIF 143
Cdd:pfam03801   2 RRSSVyggrgggpRSSHQSFFSSSPMPASVpRDPRPLRDKSFQQQCIQELLEYLTENNFEHPLSPKLLKSPTQKDFNSIF 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267    144 KHLYNKLDPNFRFGARYEEDVTTCLKALNYPFLDSISRSRLVAIGSPHVWPAILGMLHWVVSLIQCTEKAVAMVYTVE 221
Cdd:pfam03801  82 KFLYHRLDPSYEFQKKIEEEVPMILKQLRYPFLDSISKSQLSAVGGPHTWPTFLGLLHWLVELAKFLEALEQNLYDDD 159
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
333-548 3.76e-10

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 62.09  E-value: 3.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  333 MKQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQldrNLNMIGSKISELRKEVFDtdllIQASIDS 412
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELEKEIAE----LRAELEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  413 LEKKVQKFNSLAYRIGIVPIAAirsanndfeLEINPEGPN--YINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEH 490
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLA---------LLLSPEDFLdaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267  491 VDTVNDLIAELQDELRgiesRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLK 548
Cdd:COG4942 173 RAELEALLAELEEERA----ALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
260-586 6.40e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.80  E-value: 6.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    260 KATFNQQNQDLYNQTEALKStneELINQIKSAEELDSAIQVLEERYRTMQRDEVKfqsamsgMKSKMESRTNLMKQLQVN 339
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLES---KIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-------LKETIIKNNSEIKDLTNQ 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    340 IEEKESQLQLLKEKRDSLKYQVENQDISI----SEFEKMVSEREQLDRNLNMIGSKISELRKEVFDtdllIQASIDSLEK 415
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSInkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD----LTKKISSLKE 524
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    416 KVQKFNSLayrigivpIAAIRSANNDFELEINPEGPNYINLDLKNKVRPFINEVRrsitlEFHEEQNKSLKLQEHVDtvn 495
Cdd:TIGR04523 525 KIEKLESE--------KKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE-----ELKQTQKSLKKKQEEKQ--- 588
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    496 DLIAELQDELrgieSRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNsmlqLDQRIQSINIEADQIaha 575
Cdd:TIGR04523 589 ELIDQKEKEK----KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK----LKQEVKQIKETIKEI--- 657
                         330
                  ....*....|.
gi 1723267    576 cMEYKNNIYKE 586
Cdd:TIGR04523 658 -RNKWPEIIKK 667
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
271-548 1.98e-06

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: 51.27  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     271 YNQTEALKSTNEELINQIKSAEE-LDSAIQVLEERYRTMQRDEVKFQSAMSGMKskMEsrtnlmKQLQVNIEEKESQLQl 349
Cdd:pfam15921   70 YPGKEHIERVLEEYSHQVKDLQRrLNESNELHEKQKFYLRQSVIDLQTKLQEMQ--ME------RDAMADIRRRESQSQ- 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     350 lkekrDSLKYQVENqdiSISEFEKMVSEREQLDRNLNmigSKISELRKEVFDTDLLIQA--SI-----DSLEKKVQKFNS 422
Cdd:pfam15921  141 -----EDLRNQLQN---TVHELEAAKCLKEDMLEDSN---TQIEQLRKMMLSHEGVLQEirSIlvdfeEASGKKIYEHDS 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     423 LAyrigIVPIAAIRSANNDFELEINPEgpnyINLdLKNKVRPFINEVRrsiTLEfHEEQNK-SLKLQEHVDTVNDLIAEL 501
Cdd:pfam15921  210 MS----TMHFRSLGSAISKILRELDTE----ISY-LKGRIFPVEDQLE---ALK-SESQNKiELLLQQHQDRIEQLISEH 276
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1723267     502 QDELRGIESRLTSVLSECN-------MLRETASEEKNAFDAESDKLERELQQLK 548
Cdd:pfam15921  277 EVEITGLTEKASSARSQANsiqsqleIIQEQARNQNSMYMRQLSDLESTVSQLR 330
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
259-398 5.21e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     259 LKATFNQQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQV 338
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     339 NIEEKESQLQLLKEKRDSLKYQVENQDisisefekmvSEREQLDRNLNMIGSKISELRKE 398
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLR----------SELEELSEELRELESKRSELRRE 916
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
336-551 5.40e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   336 LQVNIEEKESQLQLLKEKRDSLKY-QVENQDISISEFEKMVSER-EQLDRNLNMIGSKISELRKEVFDTDLLIQA----- 408
Cdd:PRK05771  51 LLTKLSEALDKLRSYLPKLNPLREeKKKVSVKSLEELIKDVEEElEKIEKEIKELEEEISELENEIKELEQEIERlepwg 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   409 SIDSLEKKVQKFNSLAYRIGIVPIAAIrsanNDFELEINPEGPNYINlDLKNKV-------RPFINEVRRsiTLEFHEEQ 481
Cdd:PRK05771 131 NFDLDLSLLLGFKYVSVFVGTVPEDKL----EELKLESDVENVEYIS-TDKGYVyvvvvvlKELSDEVEE--ELKKLGFE 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   482 NKSLklqEHVDTVNDLIAELQDELRGIESRLTSVLSEcnmLRETASEEKNAFDAESDKLERELQQLKLSS 551
Cdd:PRK05771 204 RLEL---EEEGTPSELIREIKEELEEIEKERESLLEE---LKELAKKYLEELLALYEYLEIELERAEALS 267
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
268-358 8.58e-04

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 39.10  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    268 QDLYNQTEALKSTNEELINQIKSAEEL-DSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNIEEKESQ 346
Cdd:pfam14931  14 PEVADQTEELKEECKEFVNKISEFQKIvGGFIEIVDTLAKKVEKEKLKAIGARNLLKSEAKQREAEQQQLQALILEKKVE 93
                          90
                  ....*....|..
gi 1723267    347 LQLLKEKRDSLK 358
Cdd:pfam14931  94 LERLRVEYQSLQ 105
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
259-376 1.60e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  259 LKATFNQQN-QDLYNQTEALKSTNEELINQIKS----AEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLM 333
Cdd:COG4942 122 LALLLSPEDfLDAVRRLQYLKYLAPARREQAEElradLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 1723267  334 KQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVS 376
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
 
Name Accession Description Interval E-value
Ndc80_HEC pfam03801
HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been ...
73-221 2.41e-62

HEC/Ndc80p family; Members of this family are components of the mitotic spindle. It has been shown that Ndc80/HEC from yeast is part of a complex called the Ndc80p complex. This complex is thought to bind to the microtubules of the spindle.


Pssm-ID: 461058  Cd Length: 159  Bit Score: 203.67  E-value: 2.41e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     73 RRSSV--------RVSNASFISQTPNITSI-KDPRPLSDRRYQQECATQVVNYLLESGFSQPLGLNNRFMPSTREFAAIF 143
Cdd:pfam03801   2 RRSSVyggrgggpRSSHQSFFSSSPMPASVpRDPRPLRDKSFQQQCIQELLEYLTENNFEHPLSPKLLKSPTQKDFNSIF 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267    144 KHLYNKLDPNFRFGARYEEDVTTCLKALNYPFLDSISRSRLVAIGSPHVWPAILGMLHWVVSLIQCTEKAVAMVYTVE 221
Cdd:pfam03801  82 KFLYHRLDPSYEFQKKIEEEVPMILKQLRYPFLDSISKSQLSAVGGPHTWPTFLGLLHWLVELAKFLEALEQNLYDDD 159
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
333-548 3.76e-10

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 62.09  E-value: 3.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  333 MKQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQldrNLNMIGSKISELRKEVFDtdllIQASIDS 412
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELEKEIAE----LRAELEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  413 LEKKVQKFNSLAYRIGIVPIAAirsanndfeLEINPEGPN--YINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEH 490
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLA---------LLLSPEDFLdaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267  491 VDTVNDLIAELQDELRgiesRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLK 548
Cdd:COG4942 173 RAELEALLAELEEERA----ALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
260-586 6.40e-08

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.80  E-value: 6.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    260 KATFNQQNQDLYNQTEALKStneELINQIKSAEELDSAIQVLEERYRTMQRDEVKfqsamsgMKSKMESRTNLMKQLQVN 339
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLES---KIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-------LKETIIKNNSEIKDLTNQ 448
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    340 IEEKESQLQLLKEKRDSLKYQVENQDISI----SEFEKMVSEREQLDRNLNMIGSKISELRKEVFDtdllIQASIDSLEK 415
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSInkikQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD----LTKKISSLKE 524
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    416 KVQKFNSLayrigivpIAAIRSANNDFELEINPEGPNYINLDLKNKVRPFINEVRrsitlEFHEEQNKSLKLQEHVDtvn 495
Cdd:TIGR04523 525 KIEKLESE--------KKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE-----ELKQTQKSLKKKQEEKQ--- 588
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    496 DLIAELQDELrgieSRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNsmlqLDQRIQSINIEADQIaha 575
Cdd:TIGR04523 589 ELIDQKEKEK----KDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK----LKQEVKQIKETIKEI--- 657
                         330
                  ....*....|.
gi 1723267    576 cMEYKNNIYKE 586
Cdd:TIGR04523 658 -RNKWPEIIKK 667
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
333-623 2.82e-07

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: 53.92  E-value: 2.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     333 MKQLQVNIEEKESQLQLL-KEKRDSLKYQV---ENQDIsisEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDLLIQA 408
Cdd:TIGR02169  186 IERLDLIIDEKRQQLERLrREREKAERYQAllkEKREY---EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     409 SIDSLEKKVQKFNSLAYRI---GIVPIAAIRSANNDFELEI-NPEGPNYINL----DLKNKVRpfINEVRRSITLEFHEE 480
Cdd:TIGR02169  263 LEKRLEEIEQLLEELNKKIkdlGEEEQLRVKEKIGELEAEIaSLERSIAEKEreleDAEERLA--KLEAEIDKLLAEIEE 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     481 QNKSLK-LQEHVDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLErELQQLKLSSHNSMLQLD 559
Cdd:TIGR02169  341 LEREIEeERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN-ELKRELDRLQEELQRLS 419
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     560 QRIQSIN-----IEADQIA-HACMEYKNNIYKEVAFVLGEIIHFKLHVQDSLEDLKMDYQKELDDLSRSE 623
Cdd:TIGR02169  420 EELADLNaaiagIEAKINElEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
265-548 1.51e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     265 QQNQDLYNQTEALKSTNEELINQI----KSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMEsrtnlmkQLQVNI 340
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQIsalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-------EAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     341 EEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEreqLDRNLNMIGSKISELRKEVFDTDLLIQASIDSLEKKVQKF 420
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     421 NSLAYRIgivpiAAIRSANNDFELEINpegpnyINLDLKNKVRPFINEVR----------RSITLEFHEEQNKSLKLQEH 490
Cdd:TIGR02168  855 ESLAAEI-----EELEELIEELESELE------ALLNERASLEEALALLRseleelseelRELESKRSELRRELEELREK 923
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267     491 VDTVNDLIAELQDELRGIESRLTSvlsECNMLRETASEEKNAFDAESDKLERELQQLK 548
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERLSE---EYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
271-548 1.98e-06

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: 51.27  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     271 YNQTEALKSTNEELINQIKSAEE-LDSAIQVLEERYRTMQRDEVKFQSAMSGMKskMEsrtnlmKQLQVNIEEKESQLQl 349
Cdd:pfam15921   70 YPGKEHIERVLEEYSHQVKDLQRrLNESNELHEKQKFYLRQSVIDLQTKLQEMQ--ME------RDAMADIRRRESQSQ- 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     350 lkekrDSLKYQVENqdiSISEFEKMVSEREQLDRNLNmigSKISELRKEVFDTDLLIQA--SI-----DSLEKKVQKFNS 422
Cdd:pfam15921  141 -----EDLRNQLQN---TVHELEAAKCLKEDMLEDSN---TQIEQLRKMMLSHEGVLQEirSIlvdfeEASGKKIYEHDS 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     423 LAyrigIVPIAAIRSANNDFELEINPEgpnyINLdLKNKVRPFINEVRrsiTLEfHEEQNK-SLKLQEHVDTVNDLIAEL 501
Cdd:pfam15921  210 MS----TMHFRSLGSAISKILRELDTE----ISY-LKGRIFPVEDQLE---ALK-SESQNKiELLLQQHQDRIEQLISEH 276
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1723267     502 QDELRGIESRLTSVLSECN-------MLRETASEEKNAFDAESDKLERELQQLK 548
Cdd:pfam15921  277 EVEITGLTEKASSARSQANsiqsqleIIQEQARNQNSMYMRQLSDLESTVSQLR 330
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
259-557 6.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 6.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     259 LKATFNQQNQDLYNQTEALKSTNEELinqiksaEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQV 338
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKL-------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     339 NIEEKESQLQLLKEKRDSLKYqvenqdisisEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDLLIQASIDSLEKKVQ 418
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAE----------ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     419 KFNSLAyrigivpiAAIRSANNDFE-LEINPEgpnyinlDLKNKVRPFINEVRrsiTLEFHEEQNKSLKLQEHVDTVNDL 497
Cdd:TIGR02168  387 KVAQLE--------LQIASLNNEIErLEARLE-------RLEDRRERLQQEIE---ELLKKLEEAELKELQAELEELEEE 448
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1723267     498 IAELQDELRGIESRLtsvlsecnmlrETASEEKNAFDAESDKLERELQQL--KLSSHNSMLQ 557
Cdd:TIGR02168  449 LEELQEELERLEEAL-----------EELREELEEAEQALDAAERELAQLqaRLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
327-608 8.03e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 8.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     327 ESRTNLmKQLQVNIEEKESQLQLLKEKRDS------LKYQVENQDISIS----------------EFEKMVSEREQLDRN 384
Cdd:TIGR02168  183 RTRENL-DRLEDILNELERQLKSLERQAEKaerykeLKAELRELELALLvlrleelreeleelqeELKEAEEELEELTAE 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     385 LNMIGSKISELRKEVFDTDlliqasiDSLEKKVQKFNSLAYRIgivpiaairsanNDFELEInpegpNYINLDLKNKVRp 464
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELE-------EEIEELQKELYALANEI------------SRLEQQK-----QILRERLANLER- 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     465 fiNEVRRSITLEfhEEQNKSLKLQEHVDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLEREL 544
Cdd:TIGR02168  317 --QLEELEAQLE--ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267     545 QQLKLSShNSMLQLDQRIQSIN----IEADQIAHACMEYKNNIYKEVAFVLGEIIHFKLHVQDSLEDL 608
Cdd:TIGR02168  393 LQIASLN-NEIERLEARLERLEdrreRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERL 459
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
264-574 3.90e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.94  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    264 NQQNQDLYNQTEALKSTNEELINQiKSAE---ELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMES----RTNLM--- 333
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQ-KEQDwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQlkkeLTNSEsen 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    334 KQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQLDRNLNmigSKISELRKEvfdtDLLIQASIDSL 413
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD---EQIKKLQQE----KELLEKEIERL 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    414 EKKVQKFNSlayrigivPIAAIRSANNDFELEINpegpnyiNLD-LKNKVRPFINEVRRSITLEFHEEQNKSLKLQEHVD 492
Cdd:TIGR04523 432 KETIIKNNS--------EIKDLTNQDSVKELIIK-------NLDnTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    493 TVNDLIAELQdELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLERELqqLKLSSHNSMLQLDQRIQSINIEADQI 572
Cdd:TIGR04523 497 ELKKLNEEKK-ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL--NKDDFELKKENLEKEIDEKNKEIEEL 573

                  ..
gi 1723267    573 AH 574
Cdd:TIGR04523 574 KQ 575
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
259-398 5.21e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     259 LKATFNQQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQV 338
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     339 NIEEKESQLQLLKEKRDSLKYQVENQDisisefekmvSEREQLDRNLNMIGSKISELRKE 398
Cdd:TIGR02168  867 LIEELESELEALLNERASLEEALALLR----------SELEELSEELRELESKRSELRRE 916
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
336-551 5.40e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.07  E-value: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   336 LQVNIEEKESQLQLLKEKRDSLKY-QVENQDISISEFEKMVSER-EQLDRNLNMIGSKISELRKEVFDTDLLIQA----- 408
Cdd:PRK05771  51 LLTKLSEALDKLRSYLPKLNPLREeKKKVSVKSLEELIKDVEEElEKIEKEIKELEEEISELENEIKELEQEIERlepwg 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   409 SIDSLEKKVQKFNSLAYRIGIVPIAAIrsanNDFELEINPEGPNYINlDLKNKV-------RPFINEVRRsiTLEFHEEQ 481
Cdd:PRK05771 131 NFDLDLSLLLGFKYVSVFVGTVPEDKL----EELKLESDVENVEYIS-TDKGYVyvvvvvlKELSDEVEE--ELKKLGFE 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   482 NKSLklqEHVDTVNDLIAELQDELRGIESRLTSVLSEcnmLRETASEEKNAFDAESDKLERELQQLKLSS 551
Cdd:PRK05771 204 RLEL---EEEGTPSELIREIKEELEEIEKERESLLEE---LKELAKKYLEELLALYEYLEIELERAEALS 267
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
275-548 1.46e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   275 EALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRdEVKFQSAMSGMKSKMESRTNLMKQLQV----NIEEKESQLQLL 350
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKL 530
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   351 KEKRDSLKYQVENQDISISEFEKMVSEREQLDRNLNMIGSKISELRKEV----FDTDLLIQASIDSLEKKVQKFNSLAYR 426
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELeelgFESVEELEERLKELEPFYNEYLELKDA 610
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   427 IGIVPIAAIRSANNDFELEINPEGPNYINLDLKnKVRPFINEVRRSITLEFHEE-QNKSLKLQEhvdtvndLIAELQDEL 505
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEKKYSEEEYEElREEYLELSR-------ELAGLRAEL 682
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 1723267   506 RGIESRLTSVLSECNMLRETASEEKNAfDAESDKLERELQQLK 548
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKA-KKELEKLEKALERVE 724
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
265-617 2.56e-04

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: 44.34  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     265 QQNQDlynQTEALKSTNEELINQI--------KSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQL 336
Cdd:pfam15921  263 QQHQD---RIEQLISEHEVEITGLtekassarSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRM 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     337 -QVNIEEKESQLQLL-------KEKRDSLKYQVENQDisiSEFEKMVSEREQLDRNLNMIgskiSELRKEVFDTDLLIQA 408
Cdd:pfam15921  340 yEDKIEELEKQLVLAnselteaRTERDQFSQESGNLD---DQLQKLLADLHKREKELSLE----KEQNKRLWDRDTGNSI 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     409 SIDSLEKKVQKFNSLAYRIGIVPIAAIRSANNDFELEINP-EGPNYiNLDLKNKVRPFINEVRRSITLEFHEEQNKSLKL 487
Cdd:pfam15921  413 TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAiQGKNE-SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     488 QEHVDTVNDLIAELQDELRGIE---SRLTSVLSECNMLRETASEEKNAFD-AESDKLERELQQLKLSSHNSMLQ-LDQRI 562
Cdd:pfam15921  492 ESSERTVSDLTASLQEKERAIEatnAEITKLRSRVDLKLQELQHLKNEGDhLRNVQTECEALKLQMAEKDKVIEiLRQQI 571
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267     563 QSINIEADQ---IAHACMEYKNNIYKEVAFVLGEIIHFKLhvqdsLEDLKMDYQKELD 617
Cdd:pfam15921  572 ENMTQLVGQhgrTAGAMQVEKAQLEKEINDRRLELQEFKI-----LKDKKDAKIRELE 624
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
265-571 4.41e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  265 QQNQDLYNQTEALKSTNEELINQIKSAEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNIEEKE 344
Cdd:COG4372  42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  345 SQLQLLKEKRDSLKYQVENQDISISEFEKmvsEREQLDRNLNMIGSKISELRKEvfdtdlLIQASIDSLEKKVQKFNSLA 424
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREE---ELKELEEQLESLQEELAALEQE------LQALSEAEAEQALDELLKEA 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  425 YRIGIVPIAAIRSANNDFELEINPEGPNYINLDLKNKVRPFINEVRRSITLEFHEEQNKSLKLQEHVDTVN-DLIAELQD 503
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELeLAILVEKD 272
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267  504 ELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNSMLQLDQRIQSINIEADQ 571
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
259-453 8.56e-04

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 42.36  E-value: 8.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    259 LKATFNQQNQDLYNQTEALK----STNEELINQIKSA--------------EELDSAIQVLEERYRTMQR---DEVKFQS 317
Cdd:pfam13166 273 LEAHFDDEFTEFQNRLQKLIekveSAISSLLAQLPAVsdlasllsafeldvEDIESEAEVLNSQLDGLRRaleAKRKDPF 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    318 AMSGMKS---KMESRTNLMKQLQVNIEEKESQLQLLKEKRDSLK-----YQVENQDISISEFEKMVS----EREQLDRNL 385
Cdd:pfam13166 353 KSIELDSvdaKIESINDLVASINELIAKHNEITDNFEEEKNKAKkklrlHLVEEFKSEIDEYKDKYAglekAINSLEKEI 432
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1723267    386 NMIGSKISELRKEVFDtdllIQASIDSLEKKVQKFNSLAYRIGIvpiaairsanNDFELEINPEGPNY 453
Cdd:pfam13166 433 KNLEAEIKKLREEIKE----LEAQLRDHKPGADEINKLLKAFGF----------GELELSFNEEGKGY 486
IFT20 pfam14931
Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar ...
268-358 8.58e-04

Intraflagellar transport complex B, subunit 20; IFT20 is subunit 20 of the intraflagellar transport complex B. The intraflagellar transport complex assembles and maintains eukaryotic cilia and flagella. IFT20 is localized to the Golgi complex and is anchored there by the Golgi polypeptide, GMAP210, whereas all other subunits except IFT172 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. IFT20 accompanies Golgi-derived vesicles to the point of exocytosis near the basal bodies where the other IFT polypeptides are present, and where the intact IFT particle is assembled in association with the inner surface of the cell membrane. Passage of the IFT complex then follows, through the flagellar pore recognition site at the transition region, into the ciliary compartment. There also appears to be a role of intraflagellar transport (IFT) polypeptides in the formation of the immune synapse in non ciliated cells. The flagellum, in addition to being a sensory and motile organelle, is also a secretory organelle. A number of IFT components are expressed in haematopoietic cells, which have no cilia, indicating an unexpected role of IFT proteins in immune synapse-assembly and intracellular membrane trafficking in T lymphocytes; this suggests that the immune synapse could represent the functional homolog of the primary cilium in these cells.


Pssm-ID: 464383 [Multi-domain]  Cd Length: 109  Bit Score: 39.10  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267    268 QDLYNQTEALKSTNEELINQIKSAEEL-DSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNIEEKESQ 346
Cdd:pfam14931  14 PEVADQTEELKEECKEFVNKISEFQKIvGGFIEIVDTLAKKVEKEKLKAIGARNLLKSEAKQREAEQQQLQALILEKKVE 93
                          90
                  ....*....|..
gi 1723267    347 LQLLKEKRDSLK 358
Cdd:pfam14931  94 LERLRVEYQSLQ 105
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
268-548 1.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   268 QDLYNQTEALKSTNEELINQIKSAEEldsaIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLMKQLQVNI---EEKE 344
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKE 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   345 SQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQLDR--------NLNMIGSKISELRK---EVFDTDLLIQASIDSL 413
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrltglTPEKLEKELEELEKakeEIEEEISKITARIGEL 417
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   414 EKKVQK----FNSLAYRIGIVPIAAiRSANNDFELEINPEgpnyINLDLKN--------------------KVRPFINEV 469
Cdd:PRK03918 418 KKEIKElkkaIEELKKAKGKCPVCG-RELTEEHRKELLEE----YTAELKRiekelkeieekerklrkelrELEKVLKKE 492
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   470 RRSITLEFHEEQNKSL--KLQEH----VDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASeEKNAFDAESDKLERE 543
Cdd:PRK03918 493 SELIKLKELAEQLKELeeKLKKYnleeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK-KLAELEKKLDELEEE 571

                 ....*
gi 1723267   544 LQQLK 548
Cdd:PRK03918 572 LAELL 576
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
259-376 1.60e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  259 LKATFNQQN-QDLYNQTEALKSTNEELINQIKS----AEELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNLM 333
Cdd:COG4942 122 LALLLSPEDfLDAVRRLQYLKYLAPARREQAEElradLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 1723267  334 KQLQVNIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVS 376
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
264-615 1.79e-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: 41.64  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     264 NQQNQDLYNQTEALKSTNEELInqiKSAEELDSAIQVLEERYRTMQRDEVKFQS------AMSGMKSKMESRTNLMKQLQ 337
Cdd:pfam15921  457 NESLEKVSSLTAQLESTKEMLR---KVVEELTAKKMTLESSERTVSDLTASLQEkeraieATNAEITKLRSRVDLKLQEL 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     338 VNIEEKESQLQLLKEKRDSLKYQVENQDISI----SEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDLLIQASIDSL 413
Cdd:pfam15921  534 QHLKNEGDHLRNVQTECEALKLQMAEKDKVIeilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILK 613
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     414 EKKVQKFNSLAYRIgivpiaairsanNDFELEinpegpnyinldlknKVRpFINEVrrsitlefheeqnkslklQEHVDT 493
Cdd:pfam15921  614 DKKDAKIRELEARV------------SDLELE---------------KVK-LVNAG------------------SERLRA 647
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     494 VNDLIAElQDELRgieSRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHNSMLQLDQRIQSINIEADQIA 573
Cdd:pfam15921  648 VKDIKQE-RDQLL---NEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDG 723
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1723267     574 HAcMEYKNNIYKEVAFVLGEIIHFKLHVQdSLEDLKMDYQKE 615
Cdd:pfam15921  724 HA-MKVAMGMQKQITAKRGQIDALQSKIQ-FLEEAMTNANKE 763
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
284-571 1.81e-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: 41.58  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     284 LINQIKSAEELDSAIQVL-----EERYRTMQRDEVKFQSAMSG----MKSKMESRTNLMKQLQVNIEEKESQLQLLKEKR 354
Cdd:TIGR02168  621 LLGGVLVVDDLDNALELAkklrpGYRIVTLDGDLVRPGGVITGgsakTNSSILERRREIEELEEKIEELEEKIAELEKAL 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     355 DSLKyqvenqdisiSEFEKMVSEREQLDRNLNMIGSKISELRKEvfdtdlliqasIDSLEKKVQKFNSLayrigivpIAA 434
Cdd:TIGR02168  701 AELR----------KELEELEEELEQLRKELEELSRQISALRKD-----------LARLEAEVEQLEER--------IAQ 751
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267     435 IRSANNDFELEINpegpnyINLDLKNKVRPFINEVRRSITlefhEEQNKSLKLQEHVDTVNDLIAELQDELRGIESRLTS 514
Cdd:TIGR02168  752 LSKELTELEAEIE------ELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1723267     515 VLSECNMLRETASEEKNAFDAESDKLERELQQLKLSSHnSMLQLDQRIQSINIEADQ 571
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-EIEELEELIEELESELEA 877
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
275-427 2.28e-03

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 41.21  E-value: 2.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267  275 EALKSTNEELINQIKSA-EELDSAIQVLEERYRTMQRDEVKFQSAMSGMKSKMESRTNlmKQLQVNIEEKESQLQLLKEK 353
Cdd:COG5244 122 EALKSTEKEEIVELRREnEELDKINLSLRERISSEEPELNKDGSKLSYDELKEFVEES--RVQVYDMVELVSDISETLNR 199
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1723267  354 RDSLKYQVENQDISISEFEKMVSEREQLDRNLNMIGSKISELRKEVfdTDLLIQASID-----SLEKKVQKFNSLAYRI 427
Cdd:COG5244 200 NGSIQRSSVRECERSNIHDVLFLVNGILDGVIDELNGELERLRRQL--VSLMSSHGIEveensRLKATLEKFQSLELKV 276
PRK01156 PRK01156
chromosome segregation protein; Provisional
259-568 2.35e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.04  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   259 LKATFNQQNQDLyNQTEALKSTNEELINQIKSAEE-----LDSAIQVLEER---YRTMQRDEVKFQSAMSGMKSKMESRT 330
Cdd:PRK01156 247 LEDMKNRYESEI-KTAESDLSMELEKNNYYKELEErhmkiINDPVYKNRNYindYFKYKNDIENKKQILSNIDAEINKYH 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   331 NLMKQLQV------NIEEKESQLQLLKEKRDSLKYQVENQDISISEFEKMVSEREQLDRNLNMIGSKISELRKEVFDTDL 404
Cdd:PRK01156 326 AIIKKLSVlqkdynDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   405 LIQASIDSLEKKVQKFNSLAYRIGiVPIAAIRSanNDFELEINPEGPNYINldlknkVRPFI-----NEVRRSITLEFHE 479
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLN-QRIRALRE--NLDELSRNMEMLNGQS------VCPVCgttlgEEKSNHIINHYNE 476
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723267   480 EQNkslKLQEHVDTVNDLIAELQDELRGIESRLTSVLSECNMLRETASEEKNAFDAESDKLERELQQLKlSSHNSMLQLD 559
Cdd:PRK01156 477 KKS---RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELK-DKHDKYEEIK 552

                 ....*....
gi 1723267   560 QRIQSINIE 568
Cdd:PRK01156 553 NRYKSLKLE 561
 
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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