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Conserved domains on  [gi|392896894|ref|NP_001022956|]
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C2H2-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00121 super family cl31754
MAEBL; Provisional
 866-993 9.40e-11

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 9.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  866 EERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL---RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 942
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896894  943 RLQFAKENA-AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:PTZ00121 1419 KADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
 866-993 9.40e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 9.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  866 EERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL---RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 942
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896894  943 RLQFAKENA-AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:PTZ00121 1419 KADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 865-993 1.11e-09

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 61.40  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidKEKLRLKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAER 940
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAE--AEAERKAKEEAAKQAEEEAKakaaAEAKKKAEEAKKKAEAEAKAKAEA 185

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896894   941 DARlqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKidvqQAKLEAER 993
Cdd:TIGR02794  186 EAK---AKAEEAKAKAEAAKA----KAAAEAAAKAEAEAAA----AAAAEAER 227
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 865-999 2.02e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKK---MDDEERHREKERQKKAERD 941
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEealLEAEAELAEAEEELEELAE 386

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894  942 ARLQFAKEnAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 999
Cdd:COG1196   387 ELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 866-980 9.48e-09

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 55.43  E-value: 9.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   866 EERKQFAILAKiQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE-----ERHREKERQKKAER 940
Cdd:pfam05672   17 AEKRRQAREQR-EREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEErqrkaEEEAEEREQREQEE 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896894   941 DARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 980
Cdd:pfam05672   96 QERLQKQKEEAEAKAREEAE-----RQRQEREKIMQQEEQ 130
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 864-991 6.88e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  864 GEEERKQFaiLAKIQAEEKQ-RRLDEAKEKLAIDKEKLRLKKEAL---QRELEERNKAERQKKMDDEERHREKERQKKAE 939
Cdd:cd16269   168 AEEVLQEF--LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAAeqeRKLLEEQQRELEQKLEDQERSYEEHLRQLKEK 245

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896894  940 RDARlqfakenaAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEA 991
Cdd:cd16269   246 MEEE--------RENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
 866-993 9.40e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.70  E-value: 9.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  866 EERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL---RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 942
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896894  943 RLQFAKENA-AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:PTZ00121 1419 KADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
PTZ00121 PTZ00121
MAEBL; Provisional
 865-993 1.21e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.32  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQR--RLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE--- 939
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelk 1708

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896894  940 -------RDARLQFAKENAAKLAAQEAKKDISL-KSRLEQASMQQRERQKIdvQQAKLEAER 993
Cdd:PTZ00121 1709 kkeaeekKKAEELKKAEEENKIKAEEAKKEAEEdKKKAEEAKKDEEEKKKI--AHLKKEEEK 1768
PTZ00121 PTZ00121
MAEBL; Provisional
 861-993 5.68e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.01  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  861 DPIGEEERKQFAILAKIQAEEKqRRLDEAKEKLAIDKEK---LRLKKEALQRELEERNKAERQKKMDD-----EERHREK 932
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEK-KKADEAKKKAEEDKKKadeLKKAAAAKKKADEAKKKAEEKKKADEakkkaEEAKKAD 1447

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896894  933 ERQKKAERDARLQFAKENA--------AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAeeakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 865-993 1.11e-09

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 61.40  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidKEKLRLKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAER 940
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAE--AEAERKAKEEAAKQAEEEAKakaaAEAKKKAEEAKKKAEAEAKAKAEA 185

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896894   941 DARlqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKidvqQAKLEAER 993
Cdd:TIGR02794  186 EAK---AKAEEAKAKAEAAKA----KAAAEAAAKAEAEAAA----AAAAEAER 227
PTZ00121 PTZ00121
MAEBL; Provisional
 834-993 1.25e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.85  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  834 KGKELRKflssiLKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQ----- 908
Cdd:PTZ00121 1291 KADEAKK-----AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaeek 1365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  909 RELEERNKAERQKKMDD-----EERHREKERQKKAERDARL--QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK 981
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAakkkaEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445

                         170
                  ....*....|..
gi 392896894  982 IDVQQAKLEAER 993
Cdd:PTZ00121 1446 ADEAKKKAEEAK 1457
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 865-999 2.02e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKK---MDDEERHREKERQKKAERD 941
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEealLEAEAELAEAEEELEELAE 386

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894  942 ARLQFAKEnAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 999
Cdd:COG1196   387 ELLEALRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
PTZ00121 PTZ00121
MAEBL; Provisional
 813-993 8.06e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 8.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  813 QKYRQAQVRELFEHLANQTADKGKELRKflssiLKEIHPPEDycIKVYDPIGEEERKQFAILAKIQAEEKqRRLDEAKEK 892
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARK-----ADELKKAEE--KKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKK 1323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  893 laidKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARLqfaKENAAKLAAQEAKKDISLKSRLEQA 972
Cdd:PTZ00121 1324 ----AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK---KKEEAKKKADAAKKKAEEKKKADEA 1396

                         170       180
                  ....*....|....*....|.
gi 392896894  973 SMQQRERQKIDVQQAKLEAER 993
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAK 1417
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 866-980 9.48e-09

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 55.43  E-value: 9.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   866 EERKQFAILAKiQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE-----ERHREKERQKKAER 940
Cdd:pfam05672   17 AEKRRQAREQR-EREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEErqrkaEEEAEEREQREQEE 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896894   941 DARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 980
Cdd:pfam05672   96 QERLQKQKEEAEAKAREEAE-----RQRQEREKIMQQEEQ 130
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 865-981 1.25e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 58.28  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAE---RQKKMDDEERHREKERQKKAERD 941
Cdd:PRK09510  135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAKKKAEAEAKKKAAAE 214

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 392896894  942 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK 981
Cdd:PRK09510  215 AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 865-997 1.46e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKM---DDEERHREKERQKKAERD 941
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelaEAEEALLEAEAELAEAEE 379

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392896894  942 ARLQFAKENAAKL-AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLL 997
Cdd:COG1196   380 ELEELAEELLEALrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
PTZ00121 PTZ00121
MAEBL; Provisional
 813-994 2.13e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  813 QKYRQAQVRELFEHLANQTADKGKELRKflSSILKEIhppedycikvydpigeeERKQFAILAKIQAEEKQRRLDEAKEK 892
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRK--AEEAKKA-----------------EEARIEEVMKLYEEEKKMKAEEAKKA 1615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  893 laidkEKLRLKKEALQRELEERNKAERQKKMDDEERhREKERQKKAERDARLQFA----KENAAKLAAQEAKKDISLKSR 968
Cdd:PTZ00121 1616 -----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK-KKAEELKKAEEENKIKAAeeakKAEEDKKKAEEAKKAEEDEKK 1689

                         170       180
                  ....*....|....*....|....*.
gi 392896894  969 LEQASMQQRERQKIDVQQAKLEAERI 994
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEK 1715
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 865-992 2.60e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 57.16  E-value: 2.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHR--EKERQKKAERDA 942
Cdd:TIGR02794   61 PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAkqAAEAKAKAEAEA 140

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 392896894   943 RLQfAKENAAKLAAQEAKKDislksRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:TIGR02794  141 ERK-AKEEAAKQAEEEAKAK-----AAAEAKKKAEEAKKKAEAEAKAKAE 184
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 890-992 3.14e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  890 KEKLAIDKEKLRLKKEALQ-RELEERNKAERQK-KMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKS 967
Cdd:PRK09510   70 QQKSAKRAEEQRKKKEQQQaEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149

                          90       100       110
                  ....*....|....*....|....*....|...
gi 392896894  968 -----RLEQASMQQRE---RQKIDVQQAKLEAE 992
Cdd:PRK09510  150 eaeakRAAAAAKKAAAeakKKAEAEAAKKAAAE 182
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 865-997 3.51e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQfAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 944
Cdd:COG1196   350 EEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896894  945 QFAKENAAKLAAQEAKKDI-SLKSRLEQASMQQRERQKIDVQQAKLEAERILLL 997
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAaEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
PTZ00121 PTZ00121
MAEBL; Provisional
 866-988 3.72e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  866 EERKQFAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEAlqrelEERNKAERQKKMDDEERHREkERQKKAERDARLQ 945
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKA-----EEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKAD 1486

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392896894  946 FAKENA--AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAK 988
Cdd:PTZ00121 1487 EAKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
PTZ00121 PTZ00121
MAEBL; Provisional
 813-992 3.91e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  813 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILKEIHP--PEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAK 890
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  891 EKLAIDKEKLRLKKEALQ---RELEERNKAERQKKMDDEERHREKERQKKAERDARlqfaKENAAKLAAQEAKKDISLKS 967
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK----EAEEAKKAEELKKKEAEEKK 1716

                         170       180
                  ....*....|....*....|....*
gi 392896894  968 RLEQASMQQRERqKIDVQQAKLEAE 992
Cdd:PTZ00121 1717 KAEELKKAEEEN-KIKAEEAKKEAE 1740
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 865-992 4.04e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 56.39  E-value: 4.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDE--AKEKLAIDKEKLRLKKEALQRELEE---RNKAERQKKMDDE-ERHREKERQKKA 938
Cdd:TIGR02794   73 LEQQAEEAEKQRAAEQARQKELEQraAAEKAAKQAEQAAKQAEEKQKQAEEakaKQAAEAKAKAEAEaERKAKEEAAKQA 152

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392896894   939 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:TIGR02794  153 EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA 206
PTZ00121 PTZ00121
MAEBL; Provisional
 865-992 5.57e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDK--EKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQ----KKA 938
Cdd:PTZ00121 1454 EEAKK--AEEAKKKAEEA-KKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeaKKA 1530

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896894  939 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 865-992 7.09e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.97  E-value: 7.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEAlQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 944
Cdd:PRK09510   91 ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQK-QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKK 169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896894  945 QfAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:PRK09510  170 K-AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
PTZ00121 PTZ00121
MAEBL; Provisional
 865-992 7.62e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.07  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKqfAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREK---------ERQ 935
Cdd:PTZ00121 1480 EEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadelkkaEEL 1557

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896894  936 KKAERDARLQFAK-----ENAAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:PTZ00121 1558 KKAEEKKKAEEAKkaeedKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 865-996 7.80e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 7.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKI------------QAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEERNKAERQKKMDDEE-- 927
Cdd:COG1196   222 LKELEAELLLLKLreleaeleeleaELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARle 301

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896894  928 ---RHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK--IDVQQAKLEAERILL 996
Cdd:COG1196   302 qdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELA 375
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 866-992 8.82e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.58  E-value: 8.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  866 EERKQFaiLAKIQAEEKQRRLDEAKEKL-AIDKEKLRLKKEALQRElEERNKAERQKKMDDEERHREKERQK-KAERDAR 943
Cdd:PRK09510   78 EEQRKK--KEQQQAEELQQKQAAEQERLkQLEKERLAAQEQKKQAE-EAAKQAALKQKQAEEAAAKAAAAAKaKAEAEAK 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 392896894  944 lqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:PRK09510  155 ---RAAAAAKKAAAEAKK----KAEAEAAKKAAAEAKKKAEAEAAAKAA 196
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
 876-1001 8.93e-08

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 53.78  E-value: 8.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   876 KIQAEEKQRRLDEAKE--KLAIDKEKLRLKKEalQRELEERNKAERQKKMD--DEERHREKERQKKAERDAR-----LQF 946
Cdd:pfam06391   60 GIDVEETEKKIEQYEKenKDLILKNKMKLSQE--EEELEELLELEKREKEErrKEEKQEEEEEKEKKEKAKQelideLMT 137

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896894   947 AKENAAKLAAQEAKKDISLKSRLEQASM-------QQRERQKIDVQQAKLEAERILLLSKYP 1001
Cdd:pfam06391  138 SNKDAEEIIAQHKKTAKKRKSERRRKLEelnrvleQKPTQFSTGIKFGQLPVPKIEEGPLYP 199
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 863-993 1.63e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  863 IGEEERKQFAILAKIQAEEKQrrLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD- 941
Cdd:COG1196   248 LEELEAELEELEAELAELEAE--LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEl 325

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896894  942 ARLQFAKENAAKLAAQEAKKDISLKSRLE--QASMQQRERQKIDVQQAKLEAER 993
Cdd:COG1196   326 AELEEELEELEEELEELEEELEEAEEELEeaEAELAEAEEALLEAEAELAEAEE 379
PTZ00121 PTZ00121
MAEBL; Provisional
 865-993 3.45e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEALQ-RELEE-RNKAERQKKMDDEERHREKERQK-----K 937
Cdd:PTZ00121 1441 EEAKK--ADEAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEEaKKADEaKKKAEEAKKKADEAKKAAEAKKKadeakK 1517

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894  938 AERDARLQFAKENAAKLAAQEAKK--DISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
PTZ00121 PTZ00121
MAEBL; Provisional
 865-988 4.34e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.38  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEA--------LQRELEERNKAERQKKMDDEERHREKERQK 936
Cdd:PTZ00121 1428 EEKKK--ADEAKKKAEEA-KKADEAKKKAEEAKKAEEAKKKAeeakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896894  937 KAERDARLQFAKENAAKLAAQEAKKdISLKSRLEQASMQQRERQKIDVQQAK 988
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEKKKADELKKAE 1555
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 813-992 4.71e-07

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 53.97  E-value: 4.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   813 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILKEIhppedycikvyDPIGEEE---RKQFAILAKIQAEEKQRRLDEA 889
Cdd:pfam17380  412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM-----------ERVRLEEqerQQQVERLRQQEEERKRKKLELE 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   890 KEKLAiDKEKLRLKKEALQRELEERNKA----ERQKKM---DDEERHR---EKERQKKAERDARLQFAKENAAKLAaQEA 959
Cdd:pfam17380  481 KEKRD-RKRAEEQRRKILEKELEERKQAmieeERKRKLlekEMEERQKaiyEEERRREAEEERRKQQEMEERRRIQ-EQM 558

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 392896894   960 KKDISLKSRLEqASMQQRE--RQKIDVQQAKLEAE 992
Cdd:pfam17380  559 RKATEERSRLE-AMEREREmmRQIVESEKARAEYE 592
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
865-1090 4.88e-07

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 53.50  E-value: 4.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQfailAKIQAEeKQRRLDEAKEKLAIDKEKLRLKKEALQRELEErnKAERQKKMDDEERHREKERQKKAERDARL 944
Cdd:COG3064    63 EAEQRA----AELAAE-AAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEA--AAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  945 QfaKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPL 1024
Cdd:COG3064   136 K--AEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896894 1025 NPYGVSSFGVAQAIIVPDNNAQRFGVLQQQCVAKEPLKSWTPSKFRATLVRVFKTLRMRLELIMWL 1090
Cdd:COG3064   214 AALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLV 279
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 863-996 6.68e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 6.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  863 IGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 942
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896894  943 RLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILL 996
Cdd:COG1196   413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 876-992 9.11e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 52.50  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  876 KIQAEEK-QRRLDEAKEKLAIDK-EKLRLKKEALQREL----EERNKAERQKKMDDEERHREKERQKKAERDARLQFAK- 948
Cdd:PRK09510   66 RQQQQQKsAKRAEEQRKKKEQQQaEELQQKQAAEQERLkqleKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAa 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896894  949 ----ENAAKLAAQEAKKDISLKSRLEQASMQQRERQKidvQQAKLEAE 992
Cdd:PRK09510  146 kakaEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAE 190
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 833-992 9.53e-07

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 52.70  E-value: 9.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   833 DKGKELRKFLSSiLKEIHPPEDycikvydpigeEERKQfaiLAKIQAEEKQRRLDEAKEKLAIDKEKL-RLKKEALQREL 911
Cdd:pfam05262  191 EKGVNFRRDMTD-LKERESQED-----------AKRAQ---QLKEELDKKQIDADKAQQKADFAQDNAdKQRDEVRQKQQ 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   912 EERN---KAERQKKMDD----EERHREKER-QKKAER-DARLQFAKENAAKLAAQEAKkdiSLKSRLEQASMQ-QRERQK 981
Cdd:pfam05262  256 EAKNlpkPADTSSPKEDkqvaENQKREIEKaQIEIKKnDEEALKAKDHKAFDLKQESK---ASEKEAEDKELEaQKKREP 332

                          170
                   ....*....|...
gi 392896894   982 I--DVQQAKLEAE 992
Cdd:pfam05262  333 VaeDLQKTKPQVE 345
PTZ00121 PTZ00121
MAEBL; Provisional
 830-994 1.00e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  830 QTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQfailAKIQAEEKQRRLDEAKeklaidKEKLRLKKEALQR 909
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA----DELKKAEEKKKADEAK------KAEEKKKADEAKK 1309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  910 ELEERNKAERQKKMDDEERHREKERQKKAERDARlqfaKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKL 989
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK----AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385


                  ....*
gi 392896894  990 EAERI 994
Cdd:PTZ00121 1386 KAEEK 1390
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 865-983 1.63e-06

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 51.53  E-value: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKqfailaKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQreleERNKAErqkkmddeeRHREKERQKKAERDARL 944
Cdd:pfam07767  206 EAEKK------RLKEEEKLERVLEKIAESAATAEAREEKRKTKA----QRNKEK---------RRKEEEREAKEEKALKK 266

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896894   945 QFAK-ENAAKLAAQEAKKDISLKSRLEQASMQQRERQKID 983
Cdd:pfam07767  267 KLAQlERLKEIAKEIAEKEKEREEKAEARKREKRKKKKEE 306
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
878-993 1.73e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.96  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  878 QAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKaERQKKMDDEERHREKERQKKAERDARLQFAKENAAK--LA 955
Cdd:COG3064     3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEE-ERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAE 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 392896894  956 AQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:COG3064    82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEK 119
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 863-1006 1.99e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 52.14  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  863 IGEEERKQFAILAKiqAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 942
Cdd:PRK00409  511 IGEDKEKLNELIAS--LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADE 588

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894  943 RLQFAKE-NAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKL--EAERIlllsKYPNFG-KG 1006
Cdd:PRK00409  589 IIKELRQlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkVGDEV----KYLSLGqKG 652
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 865-993 3.43e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 51.28  E-value: 3.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQfailaKIQAEEKQRRLDEAK-EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDAR 943
Cdd:pfam17380  399 EAARKV-----KILEEERQRKIQQQKvEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK 473

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896894   944 ---LQFAKENAAKLAAQEAKKDI---SLKSRlEQASMQQRERQKI------DVQQAKLEAER 993
Cdd:pfam17380  474 rkkLELEKEKRDRKRAEEQRRKIlekELEER-KQAMIEEERKRKLlekemeERQKAIYEEER 534
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 865-968 3.88e-06

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 50.72  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAIL------AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnKAERQKK---MDDEERHREKERQ 935
Cdd:pfam15709  405 EEERKQRLQLqaaqerARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ-LAEEQKRlmeMAEEERLEYQRQK 483

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 392896894   936 KKAERDARLQFAK-----ENAAKLAAQEAKKDISLKSR 968
Cdd:pfam15709  484 QEAEEKARLEAEErrqkeEEAARLALEEAMKQAQEQAR 521
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 875-1041 4.53e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.21  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  875 AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQREleernKAERQKKMDDEERHREKERQKKAERDARLQfAKENAAKL 954
Cdd:COG3883   141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ-----QAEQEALLAQLSAEEAAAEAQLAELEAELA-AAEAAAAA 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  955 AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPLNPYGVSSFGV 1034
Cdd:COG3883   215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294


                  ....*..
gi 392896894 1035 AQAIIVP 1041
Cdd:COG3883   295 GGGAASG 301
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
875-1047 8.02e-06

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 49.65  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  875 AKIQAEEKQRRLD----EAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDArlqfakEN 950
Cdd:COG3064    58 REAKAEAEQRAAElaaeAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKA------EE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  951 AAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPLNPYGVS 1030
Cdd:COG3064   132 EAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAA 211

                         170
                  ....*....|....*..
gi 392896894 1031 SFGVAQAIIVPDNNAQR 1047
Cdd:COG3064   212 ADAALLALAVAARAAAA 228
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
878-992 9.95e-06

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.49  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  878 QAEEKQRRLDEAKEKLAIDKEKlRLKKEALQRElEERNKAERQKKMDDEERHREKERQK-----KAERDARLQfakENAA 952
Cdd:COG2268   225 EAELEQEREIETARIAEAEAEL-AKKKAEERRE-AETARAEAEAAYEIAEANAEREVQRqleiaEREREIELQ---EKEA 299

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 392896894  953 KLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:COG2268   300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
PTZ00121 PTZ00121
MAEBL; Provisional
 865-993 1.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKiQAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD 941
Cdd:PTZ00121 1670 AEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392896894  942 ARLQFAKEN-AAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDvQQAKLEAER 993
Cdd:PTZ00121 1749 AKKDEEEKKkIAHLKKEEEKK--AEEIRKEKEAVIEEELDEED-EKRRMEVDK 1798
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 864-1001 1.30e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 46.61  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   864 GEEERKQFAILAKIQAEEKQRRLDEAKEklaidkEKLRLKKEAlqRELEERNKAERQKKMDDEERHREKERQKKAERDAr 943
Cdd:pfam11600    9 SQEEKEKQRLEKDKERLRRQLKLEAEKE------EKERLKEEA--KAEKERAKEEARRKKEEEKELKEKERREKKEKDE- 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896894   944 lqfaKENAAKLAAQEAK---KDISLKSRLEQASMQQRER----QKIDVQQAKLEAERILLLSKYP 1001
Cdd:pfam11600   80 ----KEKAEKLRLKEEKrkeKQEALEAKLEEKRKKEEEKrlkeEEKRIKAEKAEITRFLQKPKTQ 140
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 865-993 1.43e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidkEKLRLKKEALQRELEERNKA-----ERQKKMDDEERHREKERQKKAE 939
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL---EAEAELAEAEEELEELAEELlealrAAAELAAQLEELEEAEEALLER 415

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896894  940 RDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
874-991 1.54e-05

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 47.13  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  874 LAKIQAEEKQ--RRLDEAKE---------KLAIDKEKLRLKKEALQRELEERNKAERQKKmddeerhrEKERQKKAERDA 942
Cdd:COG1842    46 LAQVIANQKRleRQLEELEAeaekweekaRLALEKGREDLAREALERKAELEAQAEALEA--------QLAQLEEQVEKL 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894  943 RLQfAKENAAKLAAQEAKKDIsLKSRLEQASMQQR-----------------ER--QKIDVQQAKLEA 991
Cdd:COG1842   118 KEA-LRQLESKLEELKAKKDT-LKARAKAAKAQEKvnealsgidsddatsalERmeEKIEEMEARAEA 183
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
865-1046 1.57e-05

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.88  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLD-EAKEKLAIDKEKLRLKKEALQRELEE---RNKAERQKKMDDEERHREKERQKKAER 940
Cdd:COG3064     6 EEKAAEAAAQERLEQAEAEKRAAaEAEQKAKEEAEEERLAELEAKRQAEEearEAKAEAEQRAAELAAEAAKKLAEAEKA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  941 DARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQ-AKLEAERILLLSKYPNFGKGPTAAAATRPQVTA 1019
Cdd:COG3064    86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165

                         170       180
                  ....*....|....*....|....*..
gi 392896894 1020 KQVPLNPYGVSSFGVAQAIIVPDNNAQ 1046
Cdd:COG3064   166 AAAAAAARAAAGAAAALVAAAAAAVEA 192
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 866-995 1.63e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 48.38  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   866 EERKQFaILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARLQ 945
Cdd:pfam13868  130 EEIDEF-NEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRA 208

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896894   946 ---------FAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERIL 995
Cdd:pfam13868  209 klyqeeqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 866-993 2.76e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.61  E-value: 2.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   866 EERKQFAILAKIQAEEK-QRRLDEAKEKLaIDKEKLRLKKEALQRE--LEERNKAERQKKMDDE--------ERHREKER 934
Cdd:pfam13868   69 EERKRYRQELEEQIEEReQKRQEEYEEKL-QEREQMDEIVERIQEEdqAEAEEKLEKQRQLREEidefneeqAEWKELEK 147

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   935 QKKAERDAR-LQFAKENAAKLAAQEAKkdislksRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:pfam13868  148 EEEREEDERiLEYLKEKAEREEEREAE-------REEIEEEKEREIARLRAQQEKAQDEK 200
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 875-992 3.41e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.15  E-value: 3.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   875 AKIQAEEKQRRLDEAKEKlaiDKEKLRLKKEALQ-RELEERNKAE--RQKKMDD-----------EERHREKERQKKAER 940
Cdd:TIGR02794   46 GAVAQQANRIQQQKKPAA---KKEQERQKKLEQQaEEAEKQRAAEqaRQKELEQraaaekaakqaEQAAKQAEEKQKQAE 122

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896894   941 DARLQFAKENAAKLAAQEAKKdislksRLEQASMQQRERQKIDVQ-QAKLEAE 992
Cdd:TIGR02794  123 EAKAKQAAEAKAKAEAEAERK------AKEEAAKQAEEEAKAKAAaEAKKKAE 169
MT pfam12777
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ...
 874-959 3.51e-05

Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This family is the region between D4 and D5 and is the two predicted alpha-helical coiled coil segments that form the stalk supporting the ATP-sensitive microtubule binding component.


Pssm-ID: 463699 [Multi-domain]  Cd Length: 344  Bit Score: 47.38  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   874 LAKIQAEEKQrrLDEAKEKLAIDKEKLRLKKEALQRELE----ERNKAERQKKMDDEERHRE-------KERQKKAERDa 942
Cdd:pfam12777    7 LLKLHSTAAQ--VDDLKAKLAAQEAELKQKNEDADKLIQvvgiEADKVSKEKAIADEEEQKVavimkevKEKQKACEED- 83

                           90
                   ....*....|....*..
gi 392896894   943 rlqFAKENAAKLAAQEA 959
Cdd:pfam12777   84 ---LAKAEPALLAAQAA 97
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 865-992 3.58e-05

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 47.64  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQfailakiqAEEKQRRLDEAKEKLAID----KEKLRLKK-----EALQRELEERNKAeRQKKMDDEERHREKERQ 935
Cdd:pfam15709  358 EEQRRL--------QQEQLERAEKMREELELEqqrrFEEIRLRKqrleeERQRQEEEERKQR-LQLQAAQERARQQQEEF 428

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896894   936 KKAERDARLQFAKENAAKLAAQEAK-KDISLKSRLEQAS-MQQRERQKIDVQQAKLEAE 992
Cdd:pfam15709  429 RRKLQELQRKKQQEEAERAEAEKQRqKELEMQLAEEQKRlMEMAEEERLEYQRQKQEAE 487
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 865-993 3.62e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 47.22  E-value: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFaiLAKIQAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEER---NKAERQKKMDDEERHREKERQKKA 938
Cdd:pfam13868   50 EEERERA--LEEEEEKEEERKEERKRYRQELEEqieEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAEAEEKLEKQRQ 127

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392896894   939 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:pfam13868  128 LREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK 182
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 865-975 4.75e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.11  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQR---ELEERNKAERQKKMDDEERhrekerqKKAERD 941
Cdd:PRK09510  150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAKKKAAAEAK-------KKAAAE 222

                          90       100       110
                  ....*....|....*....|....*....|....
gi 392896894  942 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQ 975
Cdd:PRK09510  223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 880-993 5.14e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  880 EEKQRRLDEAKEKLAidkeklRLkkEALQRELE--------ERNKAERQKKMDDEERHREKERQKKAERDARLQFAKENA 951
Cdd:COG1196   175 EEAERKLEATEENLE------RL--EDILGELErqleplerQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEA 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 392896894  952 AKLAAQEAKKDISLKSRLEQASMQQrERQKIDVQQAKLEAER 993
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQ 287
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 865-995 5.97e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 5.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnkaERQKKMDDEERHREKERQKKAERDARL 944
Cdd:pfam13868   36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER---EQKRQEEYEEKLQEREQMDEIVERIQE 112

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896894   945 QFAKENAAKLAAQEAKKDIslksrLEQASMQQRERQKIDVQQAKLEAERIL 995
Cdd:pfam13868  113 EDQAEAEEKLEKQRQLREE-----IDEFNEEQAEWKELEKEEEREEDERIL 158
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 876-999 6.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  876 KIQAEEKQRRLDEAKekLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARLqfakeNAAKLA 955
Cdd:COG1196   217 ELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAE 289

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392896894  956 AQEAKKDISlksRLEQASMQQRERQK-IDVQQAKLEAERILLLSK 999
Cdd:COG1196   290 EYELLAELA---RLEQDIARLEERRReLEERLEELEEELAELEEE 331
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
 868-967 7.21e-05

rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.


Pssm-ID: 461829 [Multi-domain]  Cd Length: 158  Bit Score: 44.09  E-value: 7.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   868 RKQFAILAKIQAEEKQrrldEAKEKLaiDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERqKKAERDARLQ-- 945
Cdd:pfam06102   48 RKNYGFLDEYRKKEIE----ELKKQL--KKTKDPEEKEELKRTLQSMESRLKAKKRKDREREVLKEH-KKEEKEKVKQgk 120

                           90       100
                   ....*....|....*....|....*
gi 392896894   946 ---FAKENAAKLAAQEAKKDiSLKS 967
Cdd:pfam06102  121 kpfYLKKSEKKKLLLKEKFE-ELKK 144
PTZ00121 PTZ00121
MAEBL; Provisional
 813-993 8.69e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 8.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  813 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILK--EIHPPEDYciKVYDPIGEEERKQFAILAKiQAEEKQRRlDEAK 890
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEA--KKADEAKKAEEAKKADEAK-KAEEKKKA-DELK 1552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  891 EklaidKEKLRLKKEalQRELEERNKAERQKKMddEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLE 970
Cdd:PTZ00121 1553 K-----AEELKKAEE--KKKAEEAKKAEEDKNM--ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623

                         170       180
                  ....*....|....*....|...
gi 392896894  971 QASMQQRERQKIDVQQAKLEAER 993
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEK 1646
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 821-991 9.74e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 9.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   821 RELFEHLAN-QTADKGKE-LRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQA--EEKQRRLDEAKEKLAID 896
Cdd:TIGR02169  223 YEGYELLKEkEALERQKEaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAE 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   897 KEKLRLKKEALQRELEErnkAERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDIS-LKSRLEQASMQ 975
Cdd:TIGR02169  303 IASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdLRAELEEVDKE 379

                          170
                   ....*....|....*..
gi 392896894   976 QRE-RQKIDVQQAKLEA 991
Cdd:TIGR02169  380 FAEtRDELKDYREKLEK 396
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 865-987 1.19e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.61  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKiQAEEKQRrldeAKEKLAIDKEKLRLKKealQRELEERNKAERQKKMDDEERHREKERQKK---AERD 941
Cdd:TIGR02794  139 EAERKAKEEAAK-QAEEEAK----AKAAAEAKKKAEEAKK---KAEAEAKAKAEAEAKAKAEEAKAKAEAAKAkaaAEAA 210

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 392896894   942 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQA 987
Cdd:TIGR02794  211 AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAA 256
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 865-996 1.25e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKkealQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 944
Cdd:pfam13868  111 QEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEE----EREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392896894   945 QFAKENAAKLAAQEAKKDiSLKSRLEQASMQQRERQKIDVQQAKLEAERILL 996
Cdd:pfam13868  187 ARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237
PTZ00121 PTZ00121
MAEBL; Provisional
 880-1002 1.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  880 EEKQRRLDEAKEKLAIDKEKLRLKKEALQRElEERNKAERQKKMDDEerhREKERQKKAERDARLQFAKENAAKLAAQEA 959
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKA-EDARKAEEARKAEDA---RKAEEARKAEDAKRVEIARKAEDARKAEEA 1169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 392896894  960 KKDISLKsRLEQASMQQRERQKIDVQQAKlEAERILLLSKYPN 1002
Cdd:PTZ00121 1170 RKAEDAK-KAEAARKAEEVRKAEELRKAE-DARKAEAARKAEE 1210
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 879-996 1.34e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.49  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   879 AEEKQRRLDEAKEKLAIDKEklRLKKEALQRELEERNKAERQKKMDDEERHR--EKERQKKAERdarlQFAKENAAKLAA 956
Cdd:pfam05672    9 AEEAARILAEKRRQAREQRE--REEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEER----RREEEERQRKAE 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896894   957 QEAKKDisLKSRLEQASMQQRERQKIDVqQAKLEAERILL 996
Cdd:pfam05672   83 EEAEER--EQREQEEQERLQKQKEEAEA-KAREEAERQRQ 119
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 865-1019 1.55e-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: 45.83  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRldeakEKLAIDKEKLrLKKEALQRELEER---------NKAERQKK-----MDDEERHR 930
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQL-----ERLRREREKA-ERYQALLKEKREYegyellkekEALERQKEaierqLASLEEEL 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   931 EK---ERQKKAER-DARLQFAKENAAKLAAQ------EAKKDI-SLKSRLEQA----SMQQRERQKIDVQQAKLEAERIL 995
Cdd:TIGR02169  254 EKlteEISELEKRlEEIEQLLEELNKKIKDLgeeeqlRVKEKIgELEAEIASLersiAEKERELEDAEERLAKLEAEIDK 333

                          170       180
                   ....*....|....*....|....
gi 392896894   996 LLSKYPNFGKGPTAAAATRPQVTA 1019
Cdd:TIGR02169  334 LLAEIEELEREIEEERKRRDKLTE 357
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 865-999 1.61e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKE-KLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKaerdAR 943
Cdd:pfam13868  213 EEQERKERQKEREEAEKKARQRQELQQAREEQIElKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM----KR 288

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896894   944 LQFAKENAAKLAAQEAKKdisLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 999
Cdd:pfam13868  289 LEHRRELEKQIEEREEQR---AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 876-996 1.85e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  876 KIQAEeKQRRLDEAKEKL-AIDKEKLRLKKEALQRELE---------ERNKAERQKKMDDEERHREKERQKKAERDARLQ 945
Cdd:COG1196   206 ERQAE-KAERYRELKEELkELEAELLLLKLRELEAELEeleaeleelEAELEELEAELAELEAELEELRLELEELELELE 284

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392896894  946 FAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILL 996
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 802-995 1.92e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.73  E-value: 1.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   802 VREMDHCIYWIQKY-RQAQVRELFEHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQF--AILAKIQ 878
Cdd:pfam02463  229 LDYLKLNEERIDLLqELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKseLLKLERR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   879 AEEKQRRLDEAKEKLA-IDKEKLRLKKEALQRELE----ERNKAERQKKMDDEERHREKERQKKAERDARL----QFAKE 949
Cdd:pfam02463  309 KVDDEEKLKESEKEKKkAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKklesERLSS 388

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 392896894   950 NAAKLAAQEAKKDISLKSRLEQasMQQRERQKIDVQQAKLEAERIL 995
Cdd:pfam02463  389 AAKLKEEELELKSEEEKEAQLL--LELARQLEDLLKEEKKEELEIL 432
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 895-981 2.10e-04

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 44.87  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   895 IDK--EKLRLKKEALQR-------ELEERNKAERQKKMddEERHREKERQKKAERDARLqfakenaAKLAAQEAKKdisl 965
Cdd:pfam07946  245 IDKlaKRAKLRPEALKKakktreeEIEKIKKAAEEERA--EEAQEKKEEAKKKEREEKL-------AKLSPEEQRK---- 311

                           90
                   ....*....|....*.
gi 392896894   966 ksrleqasMQQRERQK 981
Cdd:pfam07946  312 --------YEEKERKK 319
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 865-991 2.23e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 45.33  E-value: 2.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAI-LAKIQAEEKQRRLDEAKEK----LAIDKEKLRLKKEALQRELEERNKAERQKKMD----DEERHREKERQ 935
Cdd:pfam15709  381 EQQRRFEEIrLRKQRLEEERQRQEEEERKqrlqLQAAQERARQQQEEFRRKLQELQRKKQQEEAEraeaEKQRQKELEMQ 460

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896894   936 KKAERDARLQFAKENaaKLAAQEAKKDISLKSRLEQASMQQRERQKIDV------QQAKLEA 991
Cdd:pfam15709  461 LAEEQKRLMEMAEEE--RLEYQRQKQEAEEKARLEAEERRQKEEEAARLaleeamKQAQEQA 520
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
875-996 2.31e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  875 AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQkkMDDEERHREKERQKKAERDARLQFAKENAAKL 954
Cdd:COG4372    57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--LESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 392896894  955 AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILL 996
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
PTZ00121 PTZ00121
MAEBL; Provisional
 865-992 2.33e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAI--LAKIQAEEKQRRLDEAKEKLAIDK-EKLRLKKEAlqRELEERNKAERQKKMDDEERHREKERQKKAER- 940
Cdd:PTZ00121 1179 EAARKAEEVrkAEELRKAEDARKAEAARKAEEERKaEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRk 1256

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896894  941 --DARLQFAKENAAKLAAQEAKKDISLKSRLE--QASMQQRERQKIDVQQAKLEAE 992
Cdd:PTZ00121 1257 feEARMAHFARRQAAIKAEEARKADELKKAEEkkKADEAKKAEEKKKADEAKKKAE 1312
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 865-990 3.02e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 44.14  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRR--LDEAKEKLAIDkeklRLKKEALQRELEERNKAERQKKM-----DDEERHREKERQKK 937
Cdd:pfam13868  180 EEKEREIARLRAQQEKAQDEKaeRDELRAKLYQE----EQERKERQKEREEAEKKARQRQElqqarEEQIELKERRLAEE 255

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896894   938 AERD--------ARLQFAKENAAKLAAQEAKKDISLKSRLEQAsMQQRERQKIDVQQAKLE 990
Cdd:pfam13868  256 AEREeeefermlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ-IEEREEQRAAEREEELE 315
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 865-1000 3.11e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.96  E-value: 3.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKI-QAEEKQRRLDEAK-----EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEER-----HREKE 933
Cdd:pfam02463  219 LELEEEYLLYLDYlKLNEERIDLLQELlrdeqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELkllakEEEEL 298

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896894   934 RQKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKY 1000
Cdd:pfam02463  299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
865-992 3.57e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAE--EKQRRLDEAKEKLAIDKEKLRLKK---EALQRELEERNK--AERQKKMDDEERHREKERQKK 937
Cdd:COG4372    31 EQLRKALFELDKLQEEleQLREELEQAREELEQLEEELEQARselEQLEEELEELNEqlQAAQAELAQAQEELESLQEEA 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392896894  938 AERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
889-999 3.74e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.26  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  889 AKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE---ERHREKERQKKAERDARLQFA--KENAAKLAAQEAKKdi 963
Cdd:COG3064     1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEaeeERLAELEAKRQAEEEAREAKAeaEQRAAELAAEAAKK-- 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 392896894  964 slKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 999
Cdd:COG3064    79 --LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEK 112
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 825-999 3.98e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 3.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   825 EHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEE----RKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL 900
Cdd:pfam02463  317 KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEelekLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   901 RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDaRLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQ 980
Cdd:pfam02463  397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475

                          170
                   ....*....|....*....
gi 392896894   981 KIDVQQAKLEAERILLLSK 999
Cdd:pfam02463  476 ETQLVKLQEQLELLLSRQK 494
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 876-993 4.13e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.17  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   876 KIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQR--------ELEERNKAE--RQKKMDDEErhrEKERQKKAERDARLQ 945
Cdd:pfam15709  337 RLRAERAEMRRLEVERKRREQEEQRRLQQEQLERaekmreelELEQQRRFEeiRLRKQRLEE---ERQRQEEEERKQRLQ 413

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392896894   946 FAkenaaklAAQEakkdislKSRLEQASMQ------QRERQKIDVQQAKLEAER 993
Cdd:pfam15709  414 LQ-------AAQE-------RARQQQEEFRrklqelQRKKQQEEAERAEAEKQR 453
PRK12704 PRK12704
phosphodiesterase; Provisional
 865-998 4.23e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEE-KQRRLDEAKEKlaIDKEKLRLKKEA--------------LQRE---------LEERNKAERQ 920
Cdd:PRK12704   37 EEEAKRILEEAKKEAEAiKKEALLEAKEE--IHKLRNEFEKELrerrnelqklekrlLQKEenldrklelLEKREEELEK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  921 KKMDDEERHRE-KERQKKAERDARLQFAK-ENAAKLAAQEAKKDI--SLKSRLE-QASMQQRERQKIDVQQAKLEAERIL 995
Cdd:PRK12704  115 KEKELEQKQQElEKKEEELEELIEEQLQElERISGLTAEEAKEILleKVEEEARhEAAVLIKEIEEEAKEEADKKAKEIL 194


                  ...
gi 392896894  996 LLS 998
Cdd:PRK12704  195 AQA 197
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 874-994 4.29e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 42.74  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   874 LAKIQAEEKQ--RRLDEAKEKLAIDKEK----LRLKKEALQRE-LEERNKAERQKkmddEERHREKERQKKAERDARLQF 946
Cdd:pfam04012   45 LAQTIARQKQleRRLEQQTEQAKKLEEKaqaaLTKGNEELAREaLAEKKSLEKQA----EALETQLAQQRSAVEQLRKQL 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896894   947 AKeNAAKLAAQEAKKDIsLKSRLEQASMQ---QRERQKIDVQQAKLEAERI 994
Cdd:pfam04012  121 AA-LETKIQQLKAKKNL-LKARLKAAKAQeavQTSLGSLSTSSATDSFERI 169
PTZ00121 PTZ00121
MAEBL; Provisional
 865-992 4.32e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKqfaILAKIQAEEKQRRLDEAKEKlaidkEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 944
Cdd:PTZ00121 1221 EDAKK---AEAVKKAEEAKKDAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896894  945 QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKiDVQQAKLEAE 992
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAE 1339
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
862-1004 4.89e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 4.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  862 PIGEEERKQfaILAKIQAEEKqrRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQK----K 937
Cdd:PRK03918  444 ELTEEHRKE--LLEEYTAELK--RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynleE 519

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896894  938 AERDAR-LQFAKENAAKLaaqeaKKDI-SLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFG 1004
Cdd:PRK03918  520 LEKKAEeYEKLKEKLIKL-----KGEIkSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 880-967 5.00e-04

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


Pssm-ID: 462530  Cd Length: 239  Bit Score: 43.05  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   880 EEKQRRLDEAKEKlaidKEKLRLKKEALQRELEERNK--AERQKKMDDEERHREKERQKKAERDARLqfakENAAKL--A 955
Cdd:pfam08597   47 KEKAAKAAAAKAK----KKKKSKKQKIAEKEAERKAEeeAEEEEELTPEDEAARKLRLRKAEEESDL----ENAADLfgG 118

                           90
                   ....*....|..
gi 392896894   956 AQEAKKDISLKS 967
Cdd:pfam08597  119 AGDPTKDTDLSS 130
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 863-958 5.68e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.96  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  863 IGEEERKQFAILAKIQAEEKQRRLdEAKEKLAIDKEKL-RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD 941
Cdd:PTZ00266  440 IEKENAHRKALEMKILEKKRIERL-EREERERLERERMeRIERERLERERLERERLERDRLERDRLDRLERERVDRLERD 518

                          90
                  ....*....|....*..
gi 392896894  942 aRLQFAKENAAKLAAQE 958
Cdd:PTZ00266  519 -RLEKARRNSYFLKGME 534
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
 868-931 6.18e-04

Transcription initiation factor TFIID component TAF4 family; This region of similarity is found in Transcription initiation factor TFIID component TAF4.


Pssm-ID: 461598 [Multi-domain]  Cd Length: 264  Bit Score: 43.03  E-value: 6.18e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896894   868 RKQFAILAKIQAEEKQRRLDEAKEKLA---------IDKEKLRLKKEAlqreleernkAERQKKMDDEERHRE 931
Cdd:pfam05236  113 RKQLKFLAQKDKEEEERRVAEEREGLLkaaksrsnqEDPEQLKLKQEA----------KEMQKEEDEKMRHRA 175
Caldesmon pfam02029
Caldesmon;
852-1000 6.72e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 43.70  E-value: 6.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   852 PEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEK-----LAIDKEKLRLKKEALQRELEERNKAERQKKMDDE 926
Cdd:pfam02029   45 EEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERqkefdPTIADEKESVAERKENNEEEENSSWEKEEKRDSR 124

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896894   927 ERHREKERQKKAERDARLQfAKENAAKLAAQEAKKDislksRLEQASMQQRERQKIDVQQAKLEAERILLLSKY 1000
Cdd:pfam02029  125 LGRYKEEETEIREKEYQEN-KWSTEVRQAEEEGEEE-----EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKY 192
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 864-991 6.88e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 6.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  864 GEEERKQFaiLAKIQAEEKQ-RRLDEAKEKLAIDKEKLRLKKEAL---QRELEERNKAERQKKMDDEERHREKERQKKAE 939
Cdd:cd16269   168 AEEVLQEF--LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAAeqeRKLLEEQQRELEQKLEDQERSYEEHLRQLKEK 245

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896894  940 RDARlqfakenaAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEA 991
Cdd:cd16269   246 MEEE--------RENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 865-1016 8.35e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 43.40  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQfAILAKIQAEEKQRRLD----EAKEKLAIDKEKLRLKKEALQRELEERNKAerqKKMDDEERHREKERQK---- 936
Cdd:PRK05035  442 EQEKKK-AEEAKARFEARQARLErekaAREARHKKAAEARAAKDKDAVAAALARVKA---KKAAATQPIVIKAGARpdns 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  937 --KAERDARLQFAKENAAKLAAQEAKKDislKSRLEQASMqQRERQKIDVQQAKLEAERILLLSKypnfgKGPTAAAATR 1014
Cdd:PRK05035  518 avIAAREARKAQARARQAEKQAAAAADP---KKAAVAAAI-ARAKAKKAAQQAANAEAEEEVDPK-----KAAVAAAIAR 588


                  ..
gi 392896894 1015 PQ 1016
Cdd:PRK05035  589 AK 590
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 890-980 8.37e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 41.56  E-value: 8.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   890 KEKLAIdKEKLRLKKEALQRELEERNK--AERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKS 967
Cdd:pfam09756    8 RAKLEL-KEAKRQQREAEEEEREEREKleEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKSQFVVEE 86

                           90
                   ....*....|...
gi 392896894   968 RLEQASMQQRERQ 980
Cdd:pfam09756   87 EGTDKLSAEDESQ 99
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 868-980 8.92e-04

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 40.93  E-value: 8.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   868 RKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKeaLQRELE-ERNKAERQKKMDDEERHREKErQKKAERDARLQF 946
Cdd:pfam15236   33 RGQNALLDPAQLEERERKRQKALEHQNAIKKQLEEKE--RQKKLEeERRRQEEQEEEERLRREREEE-QKQFEEERRKQK 109

                           90       100       110
                   ....*....|....*....|....*....|....
gi 392896894   947 AKENAAKLAAQEAKKDISLKSRLEQASMQQRERQ 980
Cdd:pfam15236  110 EKEEAMTRKTQALLQAMQKAQELAQRLKQEQRIR 143
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 875-992 9.25e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 43.40  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  875 AKIQA-EEKQRRLDEAKEKLAidkeklrLKKEALQREleernKAERqkkmddEERHREKERQKKAERDARLQFAKE--NA 951
Cdd:PRK05035  436 AEIRAiEQEKKKAEEAKARFE-------ARQARLERE-----KAAR------EARHKKAAEARAAKDKDAVAAALArvKA 497

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 392896894  952 AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:PRK05035  498 KKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQ 538
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 857-999 1.11e-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: 43.12  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   857 IKVYDPIGEEERKQFAIlaKIQAE--EKQRRLDEAKEKLAIDKEKLRLkkEALQRELEERNKAERQKkmddEERHREKER 934
Cdd:TIGR02168  189 DRLEDILNELERQLKSL--ERQAEkaERYKELKAELRELELALLVLRL--EELREELEELQEELKEA----EEELEELTA 260

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896894   935 QKKAER----DARLQFAKENAAKLAAQEAKKDIS-LKSRLEQASMQQRERQKIDVQQAK-LEAERILLLSK 999
Cdd:TIGR02168  261 ELQELEekleELRLEVSELEEEIEELQKELYALAnEISRLEQQKQILRERLANLERQLEeLEAQLEELESK 331
PTZ00121 PTZ00121
MAEBL; Provisional
 865-994 1.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAE--EKQRRLDEAKEKlaidKEKLRLKKEAlqRELEERNKAERQKKMDDEER---HREKERQKKAE 939
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGkaEEARKAEEAKKK----AEDARKAEEA--RKAEDARKAEEARKAEDAKRveiARKAEDARKAE 1167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  940 RDARLQFAKENAAKLAAQEAKKDISLKS-----RLEQASMQQRERQKIDVQQAKlEAERI 994
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKaedarKAEAARKAEEERKAEEARKAE-DAKKA 1226
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 870-1037 1.51e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  870 QFAILAKIqAEEKQRRLDEAKEklaiDKEKLrlkkEALQRELEErNKAERQKKMDDEERHREKERQKKAERDARLQFAKE 949
Cdd:COG3883   120 RLSALSKI-ADADADLLEELKA----DKAEL----EAKKAELEA-KLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  950 NAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPLNPYGV 1029
Cdd:COG3883   190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAA 269


                  ....*...
gi 392896894 1030 SSFGVAQA 1037
Cdd:COG3883   270 GAAGAGAA 277
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 876-993 1.54e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   876 KIQAEEKQ--RRLDEAKEKLAIDKEK------LRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD--ARLQ 945
Cdd:pfam01576  149 KLSKERKLleERISEFTSNLAEEEEKakslskLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiAELQ 228

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896894   946 fakENAAKLAAQEAKKDISLKS---RLEQASMQQRERQK--------IDVQQAKLEAER 993
Cdd:pfam01576  229 ---AQIAELRAQLAKKEEELQAalaRLEEETAQKNNALKkireleaqISELQEDLESER 284
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 863-964 1.85e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  863 IGEEERKQFAILAKIQAE--EKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAerQKKMDDEERHREKERQKKAER 940
Cdd:COG4942   144 LAPARREQAEELRADLAElaALRAELEAERAELEALLAELEEERAALEALKAERQKL--LARLEKELAELAAELAELQQE 221

                          90       100
                  ....*....|....*....|....
gi 392896894  941 DARLQFAKENAAKLAAQEAKKDIS 964
Cdd:COG4942   222 AEELEALIARLEAEAAAAAERTPA 245
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 822-989 2.18e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   822 ELFEHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAK--EKLAIDKEK 899
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltQKREAQEEQ 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   900 LRLKKEA--LQRELEE--------------RNKAERQKKMDDEERHREKERQKKAERDARLQ-----FAKENAAKLAAQE 958
Cdd:TIGR00618  256 LKKQQLLkqLRARIEElraqeavleetqerINRARKAAPLAAHIKAVTQIEQQAQRIHTELQskmrsRAKLLMKRAAHVK 335

                          170       180       190
                   ....*....|....*....|....*....|.
gi 392896894   959 AKKDISLKSRLEQASMQQRERQKIDVQQAKL 989
Cdd:TIGR00618  336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 865-945 2.33e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKIQAEEKQRRLDEAK-----EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE---------ERHR 930
Cdd:pfam05672   39 EEERLRKEELRRRAEEERARREEEARrleeeRRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEaeakareeaERQR 118

                           90
                   ....*....|....*.
gi 392896894   931 -EKERQKKAERDARLQ 945
Cdd:pfam05672  119 qEREKIMQQEEQERLE 134
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 895-993 2.36e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.37  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   895 IDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE----RDARLQFAKENAAKLAAQEAKKDISLKSRLE 970
Cdd:TIGR02794   43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEqarqKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122

                           90       100
                   ....*....|....*....|...
gi 392896894   971 QASMQQRERQKidvqqAKLEAER 993
Cdd:TIGR02794  123 EAKAKQAAEAK-----AKAEAEA 140
PRK12705 PRK12705
hypothetical protein; Provisional
 865-993 2.38e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.62  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  865 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKkmDDEERHREKERQKKAERDARL 944
Cdd:PRK12705   51 EAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARELELEELEKQL 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392896894  945 QFAKENAAKLAAQEAKKDI--SLKSRLEQasmQQRERQKIDVQQAKLEAER 993
Cdd:PRK12705  129 DNELYRVAGLTPEQARKLLlkLLDAELEE---EKAQRVKKIEEEADLEAER 176
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
793-993 2.63e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  793 KRAIALESHVREMDHciywiqkyrqaQVRELFEHLAN---QTADKGKELRKFLSSILKEIHPPEDYCIKVYDpigeeerk 869
Cdd:PRK03918  549 EKLEELKKKLAELEK-----------KLDELEEELAEllkELEELGFESVEELEERLKELEPFYNEYLELKD-------- 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  870 qfailAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALqRELeeRNKAERQKKMDDEERHREKERQ--KKAERDARLQFA 947
Cdd:PRK03918  610 -----AEKELEREEKELKKLEEELDKAFEELAETEKRL-EEL--RKELEELEKKYSEEEYEELREEylELSRELAGLRAE 681

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392896894  948 KENAAKLaAQEAKKDIS-LKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:PRK03918  682 LEELEKR-REEIKKTLEkLKEELEEREKAKKELEKLEKALERVEELR 727
NPIP pfam06409
Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate ...
 867-944 2.65e-03

Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate specific nuclear pore complex interacting protein (NPIP) sequences. The function of this family is unknown but is well conserved from African apes to humans.


Pssm-ID: 461900 [Multi-domain]  Cd Length: 267  Bit Score: 40.88  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   867 ERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRlKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAERDA 942
Cdd:pfam06409   93 ERKQEAIICKLEDIFKLNRHDEIKGKAKIAKEHLR-KKSMKEDEHGEKEKqakeAEEKGKLDEKEHGEKEEMFQEAEALG 171


                   ..
gi 392896894   943 RL 944
Cdd:pfam06409  172 KL 173
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 880-993 2.65e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   880 EEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHR-EKERQKKAERDARLQFAKENAAK----L 954
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERlEQKRQEAEEEKERLEESAEMEAEekeqL 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 392896894   955 AAQEAKKDiSLKSRLEQASmQQRERQKIDVQQAKLEAER 993
Cdd:pfam20492   82 EAELAEAQ-EEIARLEEEV-ERKEEEARRLQEELEEARE 118
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 865-951 2.68e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQfailakiqAEEKQRRLDEAKEKLAIDKEKLRLKKEalqRELEERNKAERQKKMDDEERHR-EKERQKKAERDAR 943
Cdd:pfam20492   40 EEERRQ--------AEEEAERLEQKRQEAEEEKERLEESAE---MEAEEKEQLEAELAEAQEEIARlEEEVERKEEEARR 108


                   ....*...
gi 392896894   944 LQFAKENA 951
Cdd:pfam20492  109 LQEELEEA 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 864-992 3.03e-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: 41.97  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   864 GEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEE-----RNKAER----QKKMDDEERHREKER 934
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERleslERRIAATERRLEDLE 844

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894   935 QKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 992
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 865-996 3.16e-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: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFAILAKiQAEEKQRRLDEAKEKLA---IDKEKLRLKKEALQRELEERNKA--ERQKKMDDEERHREKERQKKAE 939
Cdd:TIGR02168  221 ELRELELALLVL-RLEELREELEELQEELKeaeEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISR 299

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896894   940 RDARLQFAKENAAKLAAQEAKKDISL----KSRLEQASMQQRERQKIDVQQAKLEAERILL 996
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLeeleSKLDELAEELAELEEKLEELKEELESLEAEL 360
Caldesmon pfam02029
Caldesmon;
865-943 3.29e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQFaILAKIQAEEKQRRLDEAKEKlaiDKEKLRLKKEALQRELEERNKA--ERQKKMDDEERHR---EKERQKKAE 939
Cdd:pfam02029  237 EEEAEVF-LEAEQKLEELRRRRQEKESE---EFEKLRQKQQEAELELEELKKKreERRKLLEEEEQRRkqeEAERKLREE 312


                   ....
gi 392896894   940 RDAR 943
Cdd:pfam02029  313 EEKR 316
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 871-999 3.51e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   871 FAILAKIQAEEKQRRLDEAKEKLAIDK--EKLRLKKEALQRELEERNKAERQK-KMDDEERHREKERQKKAERDARLQFA 947
Cdd:pfam13868   21 NKERDAQIAEKKRIKAEEKEEERRLDEmmEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQER 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392896894   948 KENAAKLAAQEAKkdislksrlEQASMQQRERQKIDVQQAKLEAERILLLSK 999
Cdd:pfam13868  101 EQMDEIVERIQEE---------DQAEAEEKLEKQRQLREEIDEFNEEQAEWK 143
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 865-940 3.54e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 41.01  E-value: 3.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896894   865 EEERKQFAilaKIQAEEKQrrldeakEKLAIDKEKLRLKKEalqRELEERNKAERQKKMDdeerhrEKERQKKAER 940
Cdd:pfam07946  267 EEEIEKIK---KAAEEERA-------EEAQEKKEEAKKKER---EEKLAKLSPEEQRKYE------EKERKKEQRK 323
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 908-994 3.57e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 41.26  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   908 QRELEERNKAERQKKMDDEERHREKErQKKAERDARLQFAKENAAKLAAQEakKDISLKSRLEQASMQ-QRERQKIDVQQ 986
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQERMAMErERELERIRQEE 357


                   ....*...
gi 392896894   987 AKLEAERI 994
Cdd:pfam17380  358 RKRELERI 365
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
867-992 3.66e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  867 ERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQ--RELEERNKAERQKKMDDEERHREKERQKKAERDARL 944
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEelRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896894  945 QFAKENAAKLAAQEAKkdisLKSRLEQAsmqQRERQKIDVQQAKLEAE 992
Cdd:COG4717   195 QDLAEELEELQQRLAE----LEEELEEA---QEELEELEEELEQLENE 235
DUF4175 pfam13779
Domain of unknown function (DUF4175);
878-995 4.29e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.13  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   878 QAEEK----QRRLDEAKEKLAIDKEKLRLK---KEALQRELEERnkAERQKKMDDEERHREKERQKKAERDA------RL 944
Cdd:pfam13779  486 DAERRlraaQERLSEALERGASDEEIAKLMqelREALDDYMQAL--AEQAQQNPQDLQQPDDPNAQEMTQQDlqrmldRI 563

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896894   945 QFAKENAAKLAAQEAKKDisLKSRLEQASMQQRERQKidvQQAKLEAERIL 995
Cdd:pfam13779  564 EELARSGRRAEAQQMLSQ--LQQMLENLQAGQPQQQQ---QQGQSEMQQAM 609
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 861-978 4.78e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   861 DPIGEEERKQFA-----ILAKIQAEEKQRRLD-EAKEKLAIDKEKLRLKKEALQRELEERNKAER--QKKMDDEERHREK 932
Cdd:pfam01576  737 DEQGEEKRRQLVkqvreLEAELEDERKQRAQAvAAKKKLELDLKELEAQIDAANKGREEAVKQLKklQAQMKDLQRELEE 816

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896894   933 ERqkkAERDARLQFAKENAAKLAAQEA-----KKDISLKSRLEQASMQQRE 978
Cdd:pfam01576  817 AR---ASRDEILAQSKESEKKLKNLEAellqlQEDLAASERARRQAQQERD 864
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 865-981 4.88e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 39.69  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKQfailaKIQA--EEKQRRLDEAKEKLAIDKEKLrlkKEALQRELEERNKAERQKKMDDEERHREKER----QKKA 938
Cdd:pfam13904   65 QRQRQK-----ELQAqkEEREKEEQEAELRKRLAKEKY---QEWLQRKARQQTKKREESHKQKAAESASKSLakpeRKVS 136

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896894   939 ERDARLQFAKENAAKLAAQEAKKdisLKSRLEQASMQQRERQK 981
Cdd:pfam13904  137 QEEAKEVLQEWERKKLEQQQRKR---EEEQREQLKKEEEEQER 176
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 880-993 5.29e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 5.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   880 EEKQRRLDEAKE-KLAIDKEKLRLKKEALqrELEERNKAERQKKMDDEERHR----------------EKERQKKAERDA 942
Cdd:pfam01576  359 EELTEQLEQAKRnKANLEKAKQALESENA--ELQAELRTLQQAKQDSEHKRKklegqlqelqarlsesERQRAELAEKLS 436

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896894   943 RLQFAKENAAKLAAQEAKKDI-------SLKSRLE--QASMQQRERQKIDV--QQAKLEAER 993
Cdd:pfam01576  437 KLQSELESVSSLLNEAEGKNIklskdvsSLESQLQdtQELLQEETRQKLNLstRLRQLEDER 498
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
 816-971 5.37e-03

CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129661 [Multi-domain]  Cd Length: 309  Bit Score: 40.17  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   816 RQAQVR-ELFEhlaNQTADKGKELRKflsSILKEIHPPED--YCIKVYDPIGEE-ERKQFAILAKIQAEEKQRRLD---- 887
Cdd:TIGR00570   54 RKNNFRvQLFE---DPTVEKEVDIRK---RVLKIYNKREEdfPSLREYNDYLEEvEDIVYNLTNNIDLENTKKKIEtyqk 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   888 EAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA---RLQFAKENAAKLAAQEAKKDIS 964
Cdd:TIGR00570  128 ENKDVIQKNKEKSTREQEELEEALEFEKEEEEQRRLLLQKEEEEQQMNKRKNKQAlldELETSTLPAAELIAQHKKNSVK 207


                   ....*..
gi 392896894   965 LKSRLEQ 971
Cdd:TIGR00570  208 LEMQVEK 214
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
863-993 5.37e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  863 IGEEERKQFAILAKIQA-EEKQRRLDEAKEKLA-IDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKK--A 938
Cdd:COG4717    80 LKEAEEKEEEYAELQEElEELEEELEELEAELEeLREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEelR 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896894  939 ERDARLQFAKENAAKLAAQ--EAKKDIS------LKSRLEQASMQQRERQKIDVQQAKLEAER 993
Cdd:COG4717   160 ELEEELEELEAELAELQEEleELLEQLSlateeeLQDLAEELEELQQRLAELEEELEEAQEEL 222
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 878-996 5.48e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.41  E-value: 5.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   878 QAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDD------------EERHREKERQKKAERDarlQ 945
Cdd:pfam15558   66 EKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERarqeaeqrkqcqEQRLKEKEEELQALRE---Q 142

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894   946 FAKENAAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDVQQAKL-------EAERILL 996
Cdd:pfam15558  143 NSLQLQERLEEACHKR--QLKEREEQKKVQENNLSELLNHQARKvlvdcqaKAEELLR 198
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 880-961 5.74e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 38.49  E-value: 5.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   880 EEKQRRLDEAKEKL------AIDKEKLRLKKEALQRELEERNK--------AERQKKMDDEERHREKERQKKAERDARLq 945
Cdd:pfam15346   37 AEVERRVEEARKIMekqvleELEREREAELEEERRKEEEERKKreelerilEENNRKIEEAQRKEAEERLAMLEEQRRM- 115

                           90
                   ....*....|....*.
gi 392896894   946 faKENAAKLAAQEAKK 961
Cdd:pfam15346  116 --KEERQRREKEEEER 129
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 905-996 5.81e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.71  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  905 EALQRELEeRNKAERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDiSLKSRLEQASMQQRERQKIDV 984
Cdd:PRK11448  145 HALQQEVL-TLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE-QLQEKAAETSQERKQKRKEIT 222

                          90
                  ....*....|..
gi 392896894  985 QQAkleAERILL 996
Cdd:PRK11448  223 DQA---AKRLEL 231
PRK01294 PRK01294
lipase secretion chaperone;
864-993 7.11e-03

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 40.05  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894  864 GEEERKQFAILAKIQ--------AEEKQRRLDEAKEKLAIDkEKLRLKKEALQRELEERNKAERQKKMDDEERhrekerq 935
Cdd:PRK01294  182 GEENQYQRYALERLRiaqdpslsDAQKAARLAALEAQLPED-LRAALQESQRQQALLQQLAQLQASGASPQEL------- 253

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896894  936 kkaeRDARLQFAKENAAKLAAQEAKKDISLKSRLEQasmQQRERQKIDVQQAKLEAER 993
Cdd:PRK01294  254 ----RLMRAQLVGPEAAQRLEQLDQQRAAWQQRYDD---YLAQRAQILNAAGLSPQDR 304
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 865-987 7.13e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.83  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   865 EEERKqfailAKIQAEEKQRRlDEAKEKLAIDKEKLRLKKEALQRElEERNKAERQKKmddeerHREKERQKKAERDARL 944
Cdd:TIGR02794  153 EEEAK-----AKAAAEAKKKA-EEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKA------KAAAEAAAKAEAEAAA 219

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896894   945 QFAKEnaAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQA 987
Cdd:TIGR02794  220 AAAAE--AERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 901-984 7.56e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.02  E-value: 7.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   901 RLKKEALQRELeeRNKAERQKkmdDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 980
Cdd:pfam15558   16 RHKEEQRMREL--QQQAALAW---EELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQR-----KARLGREERRRADRR 85


                   ....
gi 392896894   981 KIDV 984
Cdd:pfam15558   86 EKQV 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 881-992 7.69e-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: 40.43  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   881 EKQRRLDEAKEKLAIDKEKLRLKKEAL------QRELEERNKAERQKKMDDEERHR---------EKERQKKAERDARLQ 945
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALaelrkeLEELEEELEQLRKELEELSRQISalrkdlarlEAEVEQLEERIAQLS 753

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 392896894   946 FAKENAAKLAAQEAKKDISLKSRLEQASmQQRERQKIDVQQAKLEAE 992
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELK 799
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 876-996 9.19e-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: 40.04  E-value: 9.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   876 KIQAEEKQRRLDEAKEKLA----IDKEkLRLKKEALQRELEernKAERQKKMDDEERHREKE------RQKKAERDARLQ 945
Cdd:TIGR02168  171 KERRKETERKLERTRENLDrledILNE-LERQLKSLERQAE---KAERYKELKAELRELELAllvlrlEELREELEELQE 246

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392896894   946 FAKENA---AKLAAQEAKKDISL-KSRLEQASMQqrerQKIDVQQAKLEAERILL 996
Cdd:TIGR02168  247 ELKEAEeelEELTAELQELEEKLeELRLEVSELE----EEIEELQKELYALANEI 297
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
 882-994 9.81e-03

YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. The family includes Chlamydia trachomatis CT670 which is found in a type III secretion gene cluster. CT670 interacts with CT671, a putative YscP homolog and CT670 and CT671 may form a chaperone-effector pair.


Pssm-ID: 435583 [Multi-domain]  Cd Length: 160  Bit Score: 37.89  E-value: 9.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896894   882 KQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKK---------MDD-----------EERHREKERQKKAERD 941
Cdd:pfam16789   12 KKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVRKHKKakmqqlrdeMDRgttsdkilqmkRYIKVVKERLKQEEKK 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896894   942 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQkidVQQAKLEAERI 994
Cdd:pfam16789   92 VQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEW---VKEMKKEEEDQ 141
 
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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